|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-225 |
1.65e-82 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 248.83 E-value: 1.65e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGYMTQ 87
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 88 RFTYWEDLTVRENLDFVARLYEVRRRRERV--DRMLDELRLGSRAKQLAGSLSGGWKQRlalaaallqepelllldepTA 165
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEAREriDELLELFGLTDAADRKVGTLSGGMKQRlglalallhdpellildepTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1422354951 166 GVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQ 225
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
8-213 |
3.15e-60 |
|
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: 189.53 E-value: 3.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGYMTQ 87
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 88 RFTYWEDLTVRENLDfvarlyevrrrrervdrmldelrlgsrakqlagsLSGGWKQRlalaaallqepelllldepTAGV 167
Cdd:cd03230 81 EPSLYENLTVRENLK----------------------------------LSGGMKQRlalaqallhdpellildepTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1422354951 168 DPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVL 213
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
15-299 |
4.41e-55 |
|
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: 181.05 E-value: 4.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 15 KRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGYMTQRFTYWED 94
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 95 LTVRENLDFVARLY--EVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSAR 172
Cdd:TIGR01188 81 LTGRENLEMMGRLYglPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 173 REFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQG---EARDLIRQQALHTWAVSGANLVGLNDRLQGQ 248
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHYMEEADKlCDRIAIIDHGRIIAEGtpeELKRRLGKDTLESRPRDIQSLKVEVSMLIAE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 249 PGVEQI------VAFGRSLHVSGGDPERLESSLNELKAEGAVIEKIDT---SLEHVFLHL 299
Cdd:TIGR01188 241 LGETGLgllavtVDSDRIKILVPDGDETVPEIVEAAIRNGIRIRSISTerpSLDDVFLKL 300
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-222 |
2.94e-53 |
|
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: 173.71 E-value: 2.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGYMTQ 87
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 88 RFTYWEDLTVRENLDFVARLY--EVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTA 165
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYgvPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1422354951 166 GVDPSARREFWEELHRLAAR-GISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDL 222
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-225 |
2.08e-51 |
|
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: 169.65 E-value: 2.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGYMT 86
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 87 QRFTYWEDLTVRENLDFVARLYEVRRRRERVD--RMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPT 164
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRieELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 165 AGVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQ 225
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREE 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-302 |
1.61e-50 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 169.22 E-value: 1.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGYMTQ 87
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 88 RFTYWEDLTVRENLDFVARLYEVRRRRERVD--RMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTA 165
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALvpPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 166 GVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQQ-ALHTWAVSGANLVGLND 243
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIESEiGCDVIEIYGPDPVALRD 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1422354951 244 RLqgQPGVEQIVAFGRSLHVSGGDPERLESSLNElkAEGAVIEKIDTSLEHVFLHL----MKD 302
Cdd:PRK13537 248 EL--APLAERTEISGETLFCYVRDPEPLHARLKG--RAGLRYLHRPANLEDVFLRLtgreMQD 306
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
8-222 |
7.07e-48 |
|
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: 159.59 E-value: 7.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGD--RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGYM 85
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 86 TQRFTYWEDLTVRENLDFVARL--YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEP 163
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLkgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 164 TAGVDPSARREFWEELHRLaARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDL 222
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-230 |
1.32e-47 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 170.69 E-value: 1.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 3 ADDLLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRV 82
Cdd:NF033858 262 DDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 83 GYMTQRFTYWEDLTVRENLDFVARLYE--VRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRlalaaallqepellll 160
Cdd:NF033858 342 GYMSQAFSLYGELTVRQNLELHARLFHlpAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRlslavavihkpellil 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1422354951 161 depTAGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEAERCHKLAYISYGVLLAQGEARDLIRQQALHT 230
Cdd:NF033858 422 depTSGVDPVARDMFWRLLIELSREdGVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVAARGAAT 492
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-286 |
8.05e-47 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 159.50 E-value: 8.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITkqsREIKRRVGYMTQ 87
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 88 -RFTYwEDLTVRENLDFVARL--YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRlalaaallqepelllldept 164
Cdd:COG4152 79 eRGLY-PKMKVGEQLVYLARLkgLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQK-------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 165 A--------------------GVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLI 223
Cdd:COG4152 138 VqliaallhdpellildepfsGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIR 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1422354951 224 RQQALHTWAVSGANLVGLndrLQGQPGVEQIVAFGRSLHV---SGGDPERLessLNELKAEGAVIE 286
Cdd:COG4152 218 RQFGRNTLRLEADGDAGW---LRALPGVTVVEEDGDGAELkleDGADAQEL---LRALLARGPVRE 277
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-299 |
4.63e-44 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 153.45 E-value: 4.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 1 MNADDLLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKR 80
Cdd:PRK13536 35 GSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 81 RVGYMTQRFTYWEDLTVRENLDFVARLYEVRRRRERVD--RMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELL 158
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVipSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 159 LLDEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQQ-ALHTWAVSGA 236
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDEHiGCQVIEIYGG 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1422354951 237 NLVGLndRLQGQPGVEQIVAFGRSLHVSGGDPERLESSLNELKaeGAVIEKIDTSLEHVFLHL 299
Cdd:PRK13536 275 DPHEL--SSLVKPYARRIEVSGETLFCYAPDPEQVRVQLRGRA--GLRLLQRPPNLEDVFLRL 333
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
8-217 |
2.42e-42 |
|
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: 145.03 E-value: 2.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGeIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGYMTQ 87
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 88 RFTYWEDLTVRENLDFVARLY--EVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTA 165
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKgiPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1422354951 166 GVDPSARREFWEELHRLAARGIsVLVSTHYM-DEAERCHKLAYISYGVLLAQG 217
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRI-VILSTHIVeDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-217 |
2.55e-38 |
|
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: 134.65 E-value: 2.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSrEIKRRVGYMTQ 87
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 88 RFTYWEDLTVRENLDFVARLYEVRRRRERVdrMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGV 167
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKKRIDE--VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1422354951 168 DPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQG 217
Cdd:cd03268 158 DPDGIKELRELILSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-223 |
4.95e-38 |
|
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: 134.59 E-value: 4.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 13 LNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQsrEIKRR----VGYMTQR 88
Cdd:cd03218 6 LSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL--PMHKRarlgIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 89 FTYWEDLTVRENLDFVARL--YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAG 166
Cdd:cd03218 84 ASIFRKLTVEENILAVLEIrgLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1422354951 167 VDPSARREFWEELHRLAARGISVLVSTHYMDEA-ERCHKlAYISY-GVLLAQGEARDLI 223
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDRGIGVLITDHNVRETlSITDR-AYIIYeGKVLAEGTPEEIA 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
10-223 |
5.08e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 132.08 E-value: 5.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 10 VHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSreIKRR----VGYM 85
Cdd:COG1137 6 AENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP--MHKRarlgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 86 TQRFTYWEDLTVRENLDFVARL--YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRlalaaallqepelllldep 163
Cdd:COG1137 84 PQEASIFRKLTVEDNILAVLELrkLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRR------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 164 T-------------------AGVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKlAYISY-GVLLAQGEARDL 222
Cdd:COG1137 145 VeiaralatnpkfilldepfAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGiCDR-AYIISeGKVLAEGTPEEI 223
|
.
gi 1422354951 223 I 223
Cdd:COG1137 224 L 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-217 |
1.02e-36 |
|
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: 130.57 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDR----HVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRV 82
Cdd:cd03266 1 MITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 83 GYMTQRFTYWEDLTVRENLDFVARLY--EVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLL 160
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYglKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1422354951 161 DEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQG 217
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-205 |
1.86e-36 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 129.52 E-value: 1.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGYMT 86
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 87 QRFTYWEDLTVRENLDFVARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRlalaaallqepelllldepTAG 166
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRvalarlllspaplwlldepFTA 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1422354951 167 VDPSARREFWEELHRLAARGISVLVSTHYMDEAERCHKL 205
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
13-223 |
1.52e-32 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 120.46 E-value: 1.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 13 LNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRR--VGYMTQRFT 90
Cdd:TIGR04406 7 LIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARlgIGYLPQEAS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 91 YWEDLTVRENLDFVARL---YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGV 167
Cdd:TIGR04406 87 IFRKLTVEENIMAVLEIrkdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1422354951 168 DPSARREFWEELHRLAARGISVLVSTHYMDEAERCHKLAYISY-GVLLAQGEARDLI 223
Cdd:TIGR04406 167 DPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISdGKVLAEGTPAEIV 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
8-217 |
2.09e-32 |
|
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: 119.31 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHgtcLGYDITKQSREIKRRVGYMTQ 87
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGE---VLFDGKPLDIAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 88 RFTYWEDLTVRENLDFVARL--YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTA 165
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLkgLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1422354951 166 GVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQG 217
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-202 |
3.22e-32 |
|
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: 117.67 E-value: 3.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDIT---KQSREIKRRVGY 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdleDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 85 MTQRFTYWEDLTVRENLDFvarlyevrrrrervdrmldelrlgsrakqlagSLSGGWKQRLALAAALLQEPELLLLDEPT 164
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL--------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190
....*....|....*....|....*....|....*....
gi 1422354951 165 AGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEAERC 202
Cdd:cd03229 129 SALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARL 167
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-222 |
3.67e-30 |
|
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: 113.92 E-value: 3.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 3 ADDLLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSR----EI 78
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelyEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 79 KRRVGYMTQR---FTyweDLTVRENLDFVARLYEVRRRRERV---DRMLDELRLGSRAKQLAGSLSGGWKQRlalaaall 152
Cdd:COG1127 81 RRRIGMLFQGgalFD---SLTVFENVAFPLREHTDLSEAEIRelvLEKLELVGLPGAADKMPSELSGGMRKRvalarala 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 153 qepelllldepTAGVDPSARREFWEELHRL-AARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDL 222
Cdd:COG1127 158 ldpeillydepTAGLDPITSAVIDELIRELrDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-226 |
6.75e-30 |
|
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: 113.37 E-value: 6.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSR----EIKRRVG 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 84 YMTQRFTYWEDLTVRENLDFVARLYEVRRRRERVDRMLDELR---LGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLL 160
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEavgLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1422354951 161 DEPTAGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQQ 226
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-217 |
7.89e-30 |
|
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: 113.20 E-value: 7.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 11 HRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGY-MTQRF 89
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVvFGQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 90 TYWEDLTVRENLDFVARLYE--VRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGV 167
Cdd:cd03267 105 QLWWDLPVIDSFYLLAAIYDlpPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 168 DPSARREFWEELHRLAA-RGISVLVSTHYMDEAER-CHKLAYISYGVLLAQG 217
Cdd:cd03267 185 DVVAQENIRNFLKEYNReRGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
8-218 |
2.60e-28 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 108.64 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHgtcLGYDITKQSREIKRRVGYMTQ 87
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGE---IIFDGHPWTRKDLHKIGSLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 88 RFTYWEDLTVRENLDFVARLyeVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGV 167
Cdd:TIGR03740 78 SPPLYENLTARENLKVHTTL--LGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 168 DPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGE 218
Cdd:TIGR03740 156 DPIGIQELRELIRSFPEQGITVILSSHILSEVQQlADHIGIISEGVLGYQGK 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-249 |
2.68e-28 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 109.36 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-REIKRRVGYM 85
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSrRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 86 TQRFTYWEDLTVRenlDFVA--RL-YEVRRRRERV------DRMLDELRLGSRAKQLAGSLSGGWKQRlalaaallqepe 156
Cdd:COG1120 81 PQEPPAPFGLTVR---ELVAlgRYpHLGLFGRPSAedreavEEALERTGLEHLADRPVDELSGGERQRvliaralaqepp 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 157 lllldepTAGVDPSARREFWEELHRLAA-RGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQQALHtwAVS 234
Cdd:COG1120 158 lllldepTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVLTPELLE--EVY 235
|
250
....*....|....*
gi 1422354951 235 GANLVGLNDRLQGQP 249
Cdd:COG1120 236 GVEARVIEDPVTGRP 250
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
18-228 |
3.37e-28 |
|
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: 108.57 E-value: 3.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-REIKRRVGYMtqrFTYWED-- 94
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNlRELRRKVGLV---FQNPDDql 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 95 --LTVRENLDF------------VARLyevrrrrervDRMLDELRLGSRAKQLAGSLSGGWKQRlalaaallqepellll 160
Cdd:COG1122 89 faPTVEEDVAFgpenlglpreeiRERV----------EEALELVGLEHLADRPPHELSGGQKQRvaiagvlamepevlvl 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1422354951 161 DEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQQAL 228
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-229 |
4.10e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 108.64 E-value: 4.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 3 ADDLLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQsreiKRRV 82
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 83 GYMTQRFTYWED--LTVRenlDFVA--RLYEVRRRRERV-------DRMLDELRLGSRAKQLAGSLSGGWKQRlalaaal 151
Cdd:COG1121 78 GYVPQRAEVDWDfpITVR---DVVLmgRYGRRGLFRRPSradreavDEALERVGLEDLADRPIGELSGGQQQRvllaral 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1422354951 152 lqepelllldepTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVlLAQGEARDLIRQQALH 229
Cdd:COG1121 155 aqdpdlllldepFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREyFDRVLLLNRGL-VAHGPPEEVLTPENLS 232
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-144 |
7.17e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 107.88 E-value: 7.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREiKRRVGYMT 86
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE-KRNVGMVF 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1422354951 87 QRFTYWEDLTVRENLDF---------------VARlyevrrrrervdrMLDELRLGSRAKQLAGSLSGGWKQR 144
Cdd:COG3842 84 QDYALFPHLTVAENVAFglrmrgvpkaeirarVAE-------------LLELVGLEGLADRYPHQLSGGQQQR 143
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-144 |
2.08e-26 |
|
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: 103.37 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREiKRRVGYMTQ 87
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNIGMVFQ 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1422354951 88 RFTYWEDLTVRENLDF--VARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQR 144
Cdd:cd03259 80 DYALFPHLTVAENIAFglKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQR 138
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-144 |
2.72e-26 |
|
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: 101.19 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 23 VKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREI-KRRVGYMTQRFTYWEDLTVRENL 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1422354951 102 DFVARLYEVRRRRERV--DRMLDELRLGSRAKQLAG----SLSGGWKQR 144
Cdd:pfam00005 81 RLGLLLKGLSKREKDAraEEALEKLGLGDLADRPVGerpgTLSGGQRQR 129
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-213 |
5.27e-26 |
|
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: 102.57 E-value: 5.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGD----RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITK-----QSREI 78
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 79 KRRVGYMTQRFTYWEDLTVRENLDFVARLYEVRRRRERV--DRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPE 156
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERREraEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1422354951 157 LLLLDEPTAGVDPSARREFWEELHRLAA-RGISVLVSTHYMDEAERCHKLAYISYGVL 213
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-218 |
7.40e-26 |
|
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: 101.77 E-value: 7.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-REIKRRVGYM-----TQRFTy 91
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlKELRRKVGLVfqnpdDQFFG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 92 wedLTVRENLDFVARLYEVRRRRERV--DRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDP 169
Cdd:cd03225 91 ---PTVEEEVAFGLENLGLPEEEIEErvEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1422354951 170 SARREFWEELHRLAARGISVLVSTHYMDEAerchkLAYISYGVLLAQGE 218
Cdd:cd03225 168 AGRRELLELLKKLKAEGKTIIIVTHDLDLL-----LELADRVIVLEDGK 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-225 |
9.39e-26 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 102.27 E-value: 9.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDR----HVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS----REI 78
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 79 KRRVGYMTQRFTYWEDLTVRENLDFVARL--YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPE 156
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIagVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1422354951 157 LLLLDEPTAGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQ 225
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-224 |
1.56e-25 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 101.74 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDIT-KQSREIKRR-VGYM 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITgLPPHEIARLgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 86 TQRFTYWEDLTVRENLDFVARLYEVRRRRERVDR------------MLDELRLGSRAKQLAGSLSGGWKQRlalaaallq 153
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLLARARreereareraeeLLERVGLADLADRPAGELSYGQQRRleiaralat 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 154 epelllldePTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIR 224
Cdd:cd03219 161 dpklllldePAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-108 |
8.75e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 101.70 E-value: 8.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 11 HRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGY-MTQRF 89
Cdd:COG4586 26 GLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVvFGQRS 105
|
90
....*....|....*....
gi 1422354951 90 TYWEDLTVRENLDFVARLY 108
Cdd:COG4586 106 QLWWDLPAIDSFRLLKAIY 124
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-225 |
1.62e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 103.67 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 10 VHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS--REIKRRVGYMTQ 87
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARhrRAVCPRIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 88 ---RFTYwEDLTVRENLDFVARLYEVRRRRERV--DRMLDELRLGSRAKQLAGSLSGGWKQRlalaaallqepellllde 162
Cdd:NF033858 84 glgKNLY-PTLSVFENLDFFGRLFGQDAAERRRriDELLRATGLAPFADRPAGKLSGGMKQKlglccalihdpdllilde 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 163 pTAGVDPSARREFWEELHRLAAR--GISVLVSTHYMDEAERCHKLAYISYGVLLAQGEARDLIRQ 225
Cdd:NF033858 163 pTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLAR 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-211 |
2.01e-24 |
|
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: 96.55 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 10 VHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITK-QSREIKRRVGYMTQr 88
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 89 ftywedltvrenldfvarlyevrrrrervdrmldelrlgsrakqlagsLSGGWKQRLALAAALLQEPELLLLDEPTAGVD 168
Cdd:cd00267 81 ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1422354951 169 PSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYG 211
Cdd:cd00267 113 PASRERLLELLRELAEEGRTVIIVTHDPELAELaADRVIVLKDG 156
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-199 |
2.04e-24 |
|
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: 97.99 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDIT---KQSREIKRRVGY 84
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 85 MTQRFTYWEDLTVRENLDF---VARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLD 161
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLapiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1422354951 162 EPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEA 199
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFA 198
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
7-217 |
2.09e-24 |
|
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: 98.96 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-REIKRR-VGY 84
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPpHRIARLgIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 85 MTQRFTYWEDLTVRENLDfVARLYEVRRRRERVDR------------------MLDELRLGSRAKQLAGSLSGGWKQRla 146
Cdd:COG0411 84 TFQNPRLFPELTVLENVL-VAAHARLGRGLLAALLrlprarreereareraeeLLERVGLADRADEPAGNLSYGQQRRle 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1422354951 147 laaallqepelllldePTAGVDPSARREFWEELHRLAA-RGISVLVSTHYMDEAER-CHKLAYISYGVLLAQG 217
Cdd:COG0411 163 iaralatepklllldePAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGlADRIVVLDFGRVIAEG 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-222 |
4.38e-24 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 97.50 E-value: 4.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQ-SREIKRR-VGYM 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 86 TQR---FTyweDLTVRENLDFVARLYEVRRRRERVDRMLDEL-RLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLD 161
Cdd:cd03224 81 PEGrriFP---ELTVEENLLLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 162 EPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEA-ERCHKLAYISYGVLLAQGEARDL 222
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAEL 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-269 |
9.71e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 99.07 E-value: 9.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSG----HGTCLgyDITKQSREikRRVG 83
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGrivlNGRDL--FTNLPPRE--RRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 84 YMTQRFTYWEDLTVRENLDFV--ARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRlalaaallqepelllld 161
Cdd:COG1118 79 FVFQHYALFPHMTVAENIAFGlrVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQR----------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 162 epTA-----GVDP---------SA-----RREFWEELHRL--AARGISVLVsTHYMDEA-ERCHKLAYISYGVLLAQGEA 219
Cdd:COG1118 142 --VAlaralAVEPevllldepfGAldakvRKELRRWLRRLhdELGGTTVFV-THDQEEAlELADRVVVMNQGRIEQVGTP 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1422354951 220 RDLIRQQAlhTWAVsgANLVGLNDRLQGQPGVEQIVAFGRSLHVSGGDPE 269
Cdd:COG1118 219 DEVYDRPA--TPFV--ARFLGCVNVLRGRVIGGQLEADGLTLPVAEPLPD 264
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-217 |
1.33e-23 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 94.81 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 9 DVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-REIKRRVGYMTQ 87
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSpKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 88 rftywedltvrenldfvarlyevrrrrervdrMLDELRLGSRAKQLAGSLSGGWKQRlalaaallqepelllldepTAGV 167
Cdd:cd03214 81 --------------------------------ALELLGLAHLADRPFNELSGGERQRvllaralaqeppillldepTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 168 DPSARREFWEELHRLAA-RGISVLVSTHYMDEAER-CHKLAYISYGVLLAQG 217
Cdd:cd03214 129 DIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-222 |
3.54e-23 |
|
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: 94.94 E-value: 3.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLL-----TPDSGHGTCLGYDITKQSR---EIK 79
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVdvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 80 RRVGYMTQR---FtyweDLTVRENLDFVARLYEVRRRRERVDRMLDELR---LGSRAK--QLAGSLSGGWKQRLALAAAL 151
Cdd:cd03260 81 RRVGMVFQKpnpF----PGSIYDNVAYGLRLHGIKLKEELDERVEEALRkaaLWDEVKdrLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 152 LQEPELLLLDEPTAGVDPSARREFWEELHRLAARgISVLVSTHYMDEAERC-HKLAYISYGVLLAQGEARDL 222
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-225 |
3.57e-23 |
|
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: 99.21 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 3 ADDLLIDVHRLNKRF-----GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-- 75
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrr 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 76 --REIKRRVGYMTQrftyweD--------LTVRENLDFVARLYEVRRRRERV---DRMLDELRLGSRAKQ-LAGSLSGGW 141
Cdd:COG1123 336 slRELRRRVQMVFQ------DpysslnprMTVGDIIAEPLRLHGLLSRAERRervAELLERVGLPPDLADrYPHELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 142 KQRlalaaallqepelllldepTAGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEA 219
Cdd:COG1123 410 RQRvaiaralalepkllildepTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
....*.
gi 1422354951 220 RDLIRQ 225
Cdd:COG1123 490 EEVFAN 495
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-194 |
3.60e-23 |
|
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: 94.91 E-value: 3.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 10 VHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSReikrRVGYMTQRF 89
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK----RIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 90 TY-WE-DLTVRenlDFVA-RLYEVRRRRERV--------DRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELL 158
Cdd:cd03235 78 SIdRDfPISVR---DVVLmGLYGHKGLFRRLskadkakvDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1422354951 159 LLDEPTAGVDPSARREFWEELHRLAARGISVLVSTH 194
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTH 190
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-218 |
2.05e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 93.12 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-REIKRR-VGY 84
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 85 MTQR---FTyweDLTVRENLDFVARLYEVRRRRERVDRMLDEL--RLGSRAKQLAGSLSGGWKQrlalaaallqepelll 159
Cdd:COG0410 83 VPEGrriFP---SLTVEENLLLGAYARRDRAEVRADLERVYELfpRLKERRRQRAGTLSGGEQQmlaigralmsrpklll 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1422354951 160 LDEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAerchkLAYISYGVLLAQGE 218
Cdd:COG0410 160 LDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFA-----LEIADRAYVLERGR 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
7-216 |
2.07e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 93.18 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGD----RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-REI--- 78
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSeRELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 79 -KRRVGYMTQRFTYWEDLTVRENLDFVARL--YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRlalaaallqep 155
Cdd:COG1136 84 rRRHIGFVFQFFNLLPELTALENVALPLLLagVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRvaiaralvnrp 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 156 ellllDEPTAGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEAERCHKLAYISYGVLLAQ 216
Cdd:COG1136 164 klilaDEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-213 |
2.77e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 92.19 E-value: 2.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-REIKRRVGYMT 86
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPpPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 87 QRFTYWEDlTVRENLDFVARLYEVRRRRERVDRMLDELRLGSRA-KQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTA 165
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1422354951 166 GVDPSARREFWEELHRLAAR-GISVLVSTHYMDEAER-CHKLAYISYGVL 213
Cdd:COG4619 160 ALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-204 |
6.46e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 91.65 E-value: 6.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRF-GDRHVVKDLSMQVRRGEiFGFL-GPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSRE----IKRR 81
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGE-FVFLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 82 VGYMTQRFTYWEDLTVRENLDFVARL--YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRlalaaallqepelll 159
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVtgKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRvaiaralvnrpelll 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1422354951 160 LDEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAERCHK 204
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPK 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-227 |
1.02e-21 |
|
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: 94.97 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRF--GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLtPDSGH--GTCL--GYDITKQSREIK- 79
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRisGEVLldGRDLLELSEALRg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 80 RRVGYMTQRF-TYWEDLTVRENLDFVARLYEVRRRRERV--DRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPE 156
Cdd:COG1123 83 RRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARArvLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1422354951 157 LLLLDEPTAGVDPSARREFWEELHRLAA-RGISVLVSTHYMDE-AERCHKLAYISYGVLLAQGEARDLIRQQA 227
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-144 |
1.50e-21 |
|
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: 90.76 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREiKRRVGYMTQ 87
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-KRPVNTVFQ 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1422354951 88 RFTYWEDLTVRENLDFVARLYEVRRRRERV--DRMLDELRLGSRAKQLAGSLSGGWKQR 144
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKErvAEALDLVQLEGYANRKPSQLSGGQQQR 138
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-227 |
3.22e-21 |
|
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: 90.05 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRH-VVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSR-EIKRRVGYM 85
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPvELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 86 TQRFTYWEDLTVRENLDFVARL--YEVRRRRERVDRMLDELRLGSR--AKQLAGSLSGGWKQRLALAAALLQEPELLLLD 161
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLlkWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1422354951 162 EPTAGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQQA 227
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILRSPA 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-222 |
4.13e-21 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 93.92 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 2 NADDLLiDVHRLNKRFG--DRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIK 79
Cdd:TIGR01257 1933 NKTDIL-RLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 80 RRVGYMTQRFTYWEDLTVRENLDFVARLYEVRRRRERVDR--MLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPEL 157
Cdd:TIGR01257 2012 QNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVAnwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1422354951 158 LLLDEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDL 222
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
8-144 |
4.66e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 91.67 E-value: 4.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGH---GtclGYDITKQSREiKRRVGY 84
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEiliG---GRDVTDLPPK-DRNIAM 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 85 MTQRFTYWEDLTVRENLDF---------------VARlyevrrrrervdrMLDELRLGSRAKQLAGSLSGGWKQR 144
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFplklrkvpkaeidrrVRE-------------AAELLGLEDLLDRKPKQLSGGQRQR 141
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
12-217 |
5.66e-21 |
|
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: 88.89 E-value: 5.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 12 RLNKRFGDRHVvkDLSMQVRrGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGH----GTCLgyDITKQSREI---KRRVGY 84
Cdd:cd03297 5 DIEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTivlnGTVL--FDSRKKINLppqQRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 85 MTQRFTYWEDLTVRENLDFVARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPT 164
Cdd:cd03297 80 VFQQYALFPHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 165 AGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEAER-CHKLAYISYGVLLAQG 217
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-295 |
6.35e-21 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 93.54 E-value: 6.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 20 RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGYMTQRFTYWEDLTVRE 99
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 100 NLDFVARL--YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSARREFWE 177
Cdd:TIGR01257 1023 HILFYAQLkgRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 178 ELHRLAArGISVLVSTHYMDEAERC-HKLAYISYGVLLAQGEArdLIRQQALHTWAVsgANLVGLNDRLQGQPGVEQIVA 256
Cdd:TIGR01257 1103 LLLKYRS-GRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGTP--LFLKNCFGTGFY--LTLVRKMKNIQSQRGGCEGTC 1177
|
250 260 270
....*....|....*....|....*....|....*....
gi 1422354951 257 FGRSLHVSGGDPERLESSLNELKAEGAVIEKIDTSLEHV 295
Cdd:TIGR01257 1178 SCTSKGFSTRCPARVDEITPEQVLDGDVNELMDLVYHHV 1216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-199 |
2.19e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 88.22 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 1 MNADDLLIDVHRLNKRF----GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSR 76
Cdd:COG1116 1 MSAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 77 eikrRVGYMTQRFTY--WedLTVRENLDFVARL--YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRlalaaall 152
Cdd:COG1116 81 ----DRGVVFQEPALlpW--LTVLDNVALGLELrgVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRvaiarala 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1422354951 153 qepelllldeptAGVDPSARREFWEELHRL-AARGISVLVSTHYMDEA 199
Cdd:COG1116 155 ndpevllmdepfGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEA 202
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-201 |
3.44e-20 |
|
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: 87.24 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGD-RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS----REIKRRV 82
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkalRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 83 GYMTQRFTYWEDLTVRENLdFVARL-----------YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAAL 151
Cdd:cd03256 81 GMIFQQFNLIERLSVLENV-LSGRLgrrstwrslfgLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1422354951 152 LQEPELLLLDEPTAGVDPSARREFWEELHRLA-ARGISVLVSTHYMDEAER 201
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLARE 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-223 |
7.68e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.49 E-value: 7.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 13 LNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDIT--KQSREIKRRVGYMTQRFT 90
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 91 YWEDLTVRENLDFVARL---YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGV 167
Cdd:PRK10895 89 IFRRLSVYDNLMAVLQIrddLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1422354951 168 DPSARREFWEELHRLAARGISVLVSTHYMDEA-ERCHKLAYISYGVLLAQGEARDLI 223
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDSGLGVLITDHNVRETlAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-224 |
9.22e-20 |
|
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: 86.40 E-value: 9.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFG----DRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDIT-KQSREIKRR 81
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTrRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 82 VGYMTQ--------RFTywedltVRENLDFVARLYEVRRRRERVDRMLDELRLGSR-AKQLAGSLSGGWKQRLALAAALL 152
Cdd:COG1124 81 VQMVFQdpyaslhpRHT------VDRILAEPLRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1422354951 153 QEPELLLLDEPTAGVDPSARREFWEELHRL-AARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIR 224
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
8-254 |
1.01e-19 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 87.87 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMrMMCGLLTPDSGHGTCLGYDITKQSREIKRRVG-YMT 86
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 87 QRFTYWEDLTVRENLDFVARLY--EVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPT 164
Cdd:NF000106 93 VR*GRRESFSGRENLYMIGR*LdlSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 165 AGVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQQALHTWAVSGANLVGLnD 243
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAHAAEL-D 251
|
250
....*....|....
gi 1422354951 244 RLQG---QPGVEQI 254
Cdd:NF000106 252 RMVGaiaQAGLDGI 265
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-223 |
3.63e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 84.37 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDIT---KQSREIKRRVG 83
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 84 YMTQRFTYWEDLTVRENLDF---VARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLL 160
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFgplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1422354951 161 DEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAERC-HKLAYISYGVLLAQGEARDLI 223
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLI 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
8-268 |
9.74e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.66 E-value: 9.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-REIKRRVGYMT 86
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSaRAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 87 QRFTYWEDLTVRENLDF-----VARLYEVRRRRERV-DRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLL 160
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMgrtphRSRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 161 DEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQQALHTwAVSGANLV 239
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTADTLRA-AFDARTAV 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 1422354951 240 GlNDRLQGQPGVEQI-------VAFGRSLHVSG-GDP 268
Cdd:PRK09536 243 G-TDPATGAPTVTPLpdpdrteAAADTRVHVVGgGQP 278
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-199 |
1.14e-18 |
|
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: 83.16 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREiKRRVGYMTQ 87
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-ERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 88 RFTYWEDLTVRENLDF------VARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLD 161
Cdd:cd03296 82 HYALFRHMTVFDNVAFglrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1422354951 162 EPTAGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEA 199
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEA 200
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-199 |
1.70e-18 |
|
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: 82.13 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDR----HVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSReikrRVG 83
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP----DRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 84 YMTQRFTYWEDLTVREN--LDFVARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLD 161
Cdd:cd03293 77 YVFQQDALLPWLTVLDNvaLGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1422354951 162 EPTAGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEA 199
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEA 195
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
7-225 |
3.12e-18 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 81.96 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDIT---KQSREIKRRVG 83
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 84 YMTQRFTYWEDLTVRENL-------------DFVARlyevrrrrerVDRMLDELRLGSRAKQLAGSLSGGWKQRlalaaa 150
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVtlapikvkkmskaEAEER----------AMELLERVGLADKADAYPAQLSGGQQQRvaiara 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1422354951 151 llqepelllLDEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQ 225
Cdd:COG1126 151 lamepkvmlFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-144 |
4.93e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.96 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 5 DLLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGhgtclgyditkqsrEIKR---- 80
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG--------------TVKLgetv 378
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1422354951 81 RVGYMTQRFTYW-EDLTVRENLdfvaRLYEVRRRRERVDRMLDELRL-GSRAKQLAGSLSGGWKQR 144
Cdd:COG0488 379 KIGYFDQHQEELdPDKTVLDEL----RDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKAR 440
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
18-199 |
2.10e-17 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 78.62 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSG----HGTCLGYDiTKQSREIKRRVGYMTQR----- 88
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGavliDGEPLDYS-RKGLLERRQRVGLVFQDpddql 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 89 --FTYWEDLT----------------VRENLdfvarlyevrrrrervdRMLDELRLGSRAKQLagsLSGGWKQRLALAAA 150
Cdd:TIGR01166 82 faADVDQDVAfgplnlglseaeverrVREAL-----------------TAVGASGLRERPTHC---LSGGEKKRVAIAGA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1422354951 151 LLQEPELLLLDEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEA 199
Cdd:TIGR01166 142 VAMRPDVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
7-144 |
4.89e-17 |
|
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: 78.32 E-value: 4.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRF----GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIK--- 79
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkir 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 80 -RRVGYMTQ--------RFTYWEdlTVRENLDFVARLYEVRRRRERVDRMLDELRLGS-RAKQLAGSLSGGWKQR 144
Cdd:cd03257 81 rKEIQMVFQdpmsslnpRMTIGE--QIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQR 153
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-226 |
5.56e-17 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 79.01 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSR--EIKRRVGYMTQRftywED- 94
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENlwEIRKKVGMVFQN----PDn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 95 ----LTVRENLDF------------VARLYEVrrrrervdrmLDELRLGSRAKQLAGSLSGGWKQRLALaaallqepell 158
Cdd:TIGR04520 89 qfvgATVEDDVAFglenlgvpreemRKRVDEA----------LKLVGMEDFRDREPHLLSGGQKQRVAI----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 159 lldeptAGV-----------------DPSARREFWEELHRLAA-RGISVLVSTHYMDEAERCHKLAYISYGVLLAQGEAR 220
Cdd:TIGR04520 148 ------AGVlamrpdiiildeatsmlDPKGRKEVLETIRKLNKeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPR 221
|
....*.
gi 1422354951 221 DLIRQQ 226
Cdd:TIGR04520 222 EIFSQV 227
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-144 |
5.93e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 78.62 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 1 MNAD---DLLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSR- 76
Cdd:COG4674 1 MSLDtmhGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 77 EIKRR-VGYMTQRFTYWEDLTVRENLD------------FVARLyeVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQ 143
Cdd:COG4674 81 EIARLgIGRKFQKPTVFEELTVFENLElalkgdrgvfasLFARL--TAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQ 158
|
.
gi 1422354951 144 R 144
Cdd:COG4674 159 W 159
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-289 |
1.01e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 79.35 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRF----GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS----REIK 79
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSerelRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 80 RRVGYMTQRFTYWEDLTVRENLDF---------------VARLyevrrrrervdrmLDELRLGSRAKQLAGSLSGGWKQR 144
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALpleiagvpkaeirkrVAEL-------------LELVGLSDKADAYPSQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 145 lalaaallqepelllLDEPTAGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEAER-CHKLAYISYGVLLAQGE---- 218
Cdd:COG1135 149 vgiaralannpkvllCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPvldv 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 219 --------ARDLIRQ-----------QALHTWAVSGANL-VGLNDRLQGQP------------------GVEQI--VAFG 258
Cdd:COG1135 229 fanpqselTRRFLPTvlndelpeellARLREAAGGGRLVrLTFVGESADEPllselarrfgvdvnilsgGIEEIqgTPVG 308
|
330 340 350
....*....|....*....|....*....|..
gi 1422354951 259 R-SLHVSgGDPERLESSLNELKAEGAVIEKID 289
Cdd:COG1135 309 RlIVELE-GDDAAIDAALAYLREQGVVVEVLG 339
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-144 |
1.06e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 10 VHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGhgtclgyDITKQSREikrRVGYMTQRF 89
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSG-------EVSIPKGL---RIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 90 TYWEDLTVREN-----------LDFVARLYEVRRRRERVDRMLDEL-----RLG-----SRAKQLA-------------- 134
Cdd:COG0488 71 PLDDDLTVLDTvldgdaelralEAELEELEAKLAEPDEDLERLAELqeefeALGgweaeARAEEILsglgfpeedldrpv 150
|
170
....*....|
gi 1422354951 135 GSLSGGWKQR 144
Cdd:COG0488 151 SELSGGWRRR 160
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
8-219 |
1.16e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 77.75 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDI-------TKQSREIKR 80
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 81 RVGYMTQRFTYWEDLTVRENLD----FVARLyEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPE 156
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIeapcKVLGL-SKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1422354951 157 LLLLDEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEA 219
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDA 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
12-228 |
2.16e-16 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 78.62 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 12 RLNKRFGDRHVvkDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGH----GTCL-----GYDITKQsreiKRRV 82
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEivlnGRTLfdsrkGIFLPPE----KRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 83 GYMTQRFTYWEDLTVRENLDFVARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDE 162
Cdd:TIGR02142 78 GYVFQEARLFPHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1422354951 163 PTAGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQQAL 228
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-144 |
3.70e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 77.82 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITK-QSREikRRVGYMT 86
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlHARD--RKVGFVF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1422354951 87 QRFTYWEDLTVRENLDFVARLY------EVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQR 144
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTVLprrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQR 144
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-144 |
3.70e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 78.07 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 1 MNADDLLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREiKR 80
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-NR 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1422354951 81 RVGYMTQRFTYWEDLTVRENLDFVARLYEVRRRRERVDRM--LDELRLGSRAKQLAGSLSGGWKQR 144
Cdd:PRK09452 87 HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMeaLRMVQLEEFAQRKPHQLSGGQQQR 152
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-108 |
3.93e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.27 E-value: 3.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 10 VHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGhgtclgyditkqsrEIKRR-------- 81
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG--------------RVEVNgrvsalle 94
|
90 100
....*....|....*....|....*....
gi 1422354951 82 --VGYMtqrftywEDLTVRENLDFVARLY 108
Cdd:COG1134 95 lgAGFH-------PELTGRENIYLNGRLL 116
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-144 |
4.22e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.35 E-value: 4.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITK-QSREIKRRVGYM 85
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRAVL 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 86 TQRFTYWEDLTVREnldfVARL--YEVRRRRERVDRMLDELRLGSRAKQLAG----SLSGGWKQR 144
Cdd:PRK13548 82 PQHSSLSFPFTVEE----VVAMgrAPHGLSRAEDDALVAAALAQVDLAHLAGrdypQLSGGEQQR 142
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
8-144 |
6.01e-16 |
|
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: 74.98 E-value: 6.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREiKRRVGYMTQ 87
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRDIAMVFQ 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1422354951 88 RFTYWEDLTVRENLDFVARLYEVRRRR-----ERVDRMLD-ELRLGSRAKQlagsLSGGWKQR 144
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEidervREVAELLQiEHLLDRKPKQ----LSGGQRQR 138
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-217 |
6.84e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.21 E-value: 6.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGD--RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSR-EIKRRVG 83
Cdd:PRK13635 5 IIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 84 YMTQ----RFTyweDLTVRENLDF------------VARLyevrrrrervDRMLDELRLGSRAKQLAGSLSGGWKQRLAL 147
Cdd:PRK13635 85 MVFQnpdnQFV---GATVQDDVAFglenigvpreemVERV----------DQALRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1422354951 148 AAALLQEPELLLLDEPTAGVDPSARREFWEELHRL-AARGISVLVSTHYMDEAERCHKLAYISYGVLLAQG 217
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-219 |
1.43e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 74.67 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLG--YDIT-----KQSREIKR 80
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSktpsdKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 81 RVGYMTQRFTYWEDLTVRENLD----FVARLyEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPE 156
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIeapcRVLGL-SKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1422354951 157 LLLLDEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEA 219
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDA 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-227 |
1.54e-15 |
|
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: 74.99 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 15 KRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS----REIKR-RVGYMTQRF 89
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelRELRRkKISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 90 TYWEDLTVRENLDFVARLYEVRRRRERVDRM--LDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGV 167
Cdd:cd03294 112 ALLPHRTVLENVAFGLEVQGVPRAEREERAAeaLELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 168 DPSARREFWEELHRLAA-RGISVLVSTHYMDEAERC-HKLAYISYGVLLAQGEARDLIRQQA 227
Cdd:cd03294 192 DPLIRREMQDELLRLQAeLQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTNPA 253
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
12-217 |
1.74e-15 |
|
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: 73.68 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 12 RLNK-RFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITkQSREIKRRVGYMTQRFT 90
Cdd:cd03298 2 RLDKiRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT-AAPPADRPVSMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 91 YWEDLTVRENLDF--VARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVD 168
Cdd:cd03298 81 LFAHLTVEQNVGLglSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1422354951 169 PSARREFWE---ELHRlaARGISVLVSTHYMDEAERC-HKLAYISYGVLLAQG 217
Cdd:cd03298 161 PALRAEMLDlvlDLHA--ETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
7-220 |
1.85e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.66 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDS---GHGTCLGYDITKQ---SREIKR 80
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREgrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 81 ---RVGYMTQRFTYWEDLTVRENLdFVARL-----------YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLA 146
Cdd:PRK09984 84 sraNTGYIFQQFNLVNRLSVLENV-LIGALgstpfwrtcfsWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1422354951 147 LAAALLQEPELLLLDEPTAGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEAR 220
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQ 238
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-108 |
2.25e-15 |
|
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: 73.72 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 11 HRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGhgtclgyditkqsrEIKRR--------- 81
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG--------------TVTVRgrvssllgl 91
|
90 100
....*....|....*....|....*...
gi 1422354951 82 -VGYMtqrftywEDLTVRENLDFVARLY 108
Cdd:cd03220 92 gGGFN-------PELTGRENIYLNGRLL 112
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-230 |
6.02e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.12 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-REIKRRVGYMT 86
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSsRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 87 QRFTYWEDLTVRE--------NLDFVARLyeVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELL 158
Cdd:PRK11231 83 QHHLTPEGITVRElvaygrspWLSLWGRL--SAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1422354951 159 LLDEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQQALHT 230
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTPGLLRT 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-62 |
8.78e-15 |
|
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: 70.54 E-value: 8.78e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSG 62
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSG 55
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
18-101 |
1.12e-14 |
|
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: 70.49 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITK-QSREIKRRVGYMTQRFTYWEDlT 96
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAYVPQDPFLFSG-T 91
|
....*
gi 1422354951 97 VRENL 101
Cdd:cd03228 92 IRENI 96
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-194 |
1.13e-14 |
|
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: 71.67 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRF-GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSRE----IKRRV 82
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 83 GYMTQRFTYWEDLTVRENLDFVARLYEVRRRRERVDRM--LDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLL 160
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPaaLELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190
....*....|....*....|....*....|....
gi 1422354951 161 DEPTAGVDPSARREFWEELHRLAARGISVLVSTH 194
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
10-194 |
2.26e-14 |
|
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: 70.47 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 10 VHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGYMTQRF 89
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 90 TYWEDLTVRENLDFVARLYEVRRRRERVDrmLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDP 169
Cdd:TIGR01189 83 GLKPELSALENLHFWAAIHGGAQRTIEDA--LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*
gi 1422354951 170 SARREFWEELHRLAARGISVLVSTH 194
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
8-222 |
3.55e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.93 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDI---------TKQSREI 78
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqqKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 79 KRRVGYMTQRFTYWEDLTVRENL---DFVARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEP 155
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIiegPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1422354951 156 ELLLLDEPTAGVDPSARREFWEELHRLAARGISVLVSTHYM----DEAERChklAYISYGVLLAQGEARDL 222
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMsfarDVADRA---IFMDQGRIVEQGPAKAL 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-62 |
4.79e-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: 72.28 E-value: 4.79e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1422354951 5 DLLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSG 62
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSG 377
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
18-226 |
5.89e-14 |
|
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: 72.10 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSRE-IKRRVGYMTQRfTYWEDLT 96
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAsWRRQIAWVPQN-PYLFAGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 97 VRENL----------------------DFVARLyevrrrrervDRMLDElRLGSRAKQLagslSGGWKQRlalaaallqe 154
Cdd:COG4988 427 IRENLrlgrpdasdeeleaaleaagldEFVAAL----------PDGLDT-PLGEGGRGL----SGGQAQRlalarallrd 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 155 pelllldepTAGVDPSARREFWEELHRLaARGISVLVSTHYMDEAERCHKLAYISYGVLLAQGEARDLIRQQ 226
Cdd:COG4988 492 aplllldepTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-144 |
5.91e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.40 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITkQSREIKRRVGYMT 86
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-HVPPYQRPINMMF 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 87 QRFTYWEDLTVRENLDFVARL--YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQR 144
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFGLKQdkLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQR 157
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
8-199 |
6.39e-14 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 69.67 E-value: 6.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVvKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREiKRRVGYMTQ 87
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-KRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 88 RFTYWEDLTVRENLDFVARLyevrrrrervdRMLDELRLGSRAKQLA-------------GSLSGGWKQRLALAAALLQE 154
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKK-----------RKVDKKEIERKVLEIAemlgidhllnrkpETLSGGEQQRVAIARALVVN 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1422354951 155 PELLLLDEPTAGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEA 199
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEA 193
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-228 |
1.31e-13 |
|
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: 68.96 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 5 DLLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCL------GYDItkqsREI 78
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLfgerrgGEDV----WEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 79 KRRVGY----MTQRFTywEDLTVRenlDFVA-------RLYEVRRRRERV--DRMLDELRLGSRAKQLAGSLSGGWKQRl 145
Cdd:COG1119 77 RKRIGLvspaLQLRFP--RDETVL---DVVLsgffdsiGLYREPTDEQREraRELLELLGLAHLADRPFGTLSQGEQRRv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 146 alaaallqepellllDEPTAGVDPSARREFWEELHRLAARGI--SVLVsTHYMDEAERC--HKLAyISYGVLLAQGEARD 221
Cdd:COG1119 152 liaralvkdpellilDEPTAGLDLGARELLLALLDKLAAEGAptLVLV-THHVEEIPPGitHVLL-LKDGRVVAAGPKEE 229
|
....*..
gi 1422354951 222 LIRQQAL 228
Cdd:COG1119 230 VLTSENL 236
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-62 |
2.08e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 2.08e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1422354951 5 DLLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSG 62
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSG 379
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-144 |
3.64e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.25 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSR----EIKRRV 82
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRsrlyTVRKRM 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 83 GYMTQRFTYWEDLTVRENLDFVARLYEVRRRRERVDRMLDELR-LGSR--AKQLAGSLSGGWKQR 144
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEaVGLRgaAKLMPSELSGGMARR 151
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-101 |
5.67e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.90 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 5 DLLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDIT-KQSRE-IKRRV 82
Cdd:COG3845 3 PPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDaIALGI 82
|
90
....*....|....*....
gi 1422354951 83 GYMTQRFTYWEDLTVRENL 101
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENI 101
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-218 |
5.67e-13 |
|
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: 69.06 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGL--LTPDSGH-----GTC-------------- 66
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRiiyhvALCekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 67 ----LGYDITKQ-----------SREIKRRVGYMTQR-FTYWEDLTVREN-LDFVARL-YEVRRRRERVDRMLDELRLGS 128
Cdd:TIGR03269 81 pcpvCGGTLEPEevdfwnlsdklRRRIRKRIAIMLQRtFALYGDDTVLDNvLEALEEIgYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 129 RAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSARREFWEELHRLA-ARGISVLVSTHYmdeAERCHKLAy 207
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHW---PEVIEDLS- 236
|
250
....*....|.
gi 1422354951 208 iSYGVLLAQGE 218
Cdd:TIGR03269 237 -DKAIWLENGE 246
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-227 |
5.80e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 68.52 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 23 VKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS----REIKRR-VGYMTQRFTYWEDLTV 97
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelREVRRKkIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 98 RENLDFVARLyEVRRRRERVDRMLDELR---LGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSARRE 174
Cdd:PRK10070 124 LDNTAFGMEL-AGINAEERREKALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 175 FWEELHRLAAR-GISVLVSTHYMDEAERC-HKLAYISYGVLLAQGEARDLIRQQA 227
Cdd:PRK10070 203 MQDELVKLQAKhQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNPA 257
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-87 |
6.18e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 65.16 E-value: 6.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGhgtclgyDITKQSREikrRVGYMTQ 87
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-------IVTWGSTV---KIGYFEQ 70
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-198 |
7.67e-13 |
|
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: 65.53 E-value: 7.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 20 RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSRE--IKRRVGYMTqrftywED--- 94
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdaIRAGIAYVP------EDrkr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 95 ------LTVRENLdfvarlyevrrrrervdrmldelrlgsrakQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVD 168
Cdd:cd03215 87 eglvldLSVAENI------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190
....*....|....*....|....*....|
gi 1422354951 169 PSARREFWEELHRLAARGISVLVSTHYMDE 198
Cdd:cd03215 137 VGAKAEIYRLIRELADAGKAVLLISSELDE 166
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-194 |
8.28e-13 |
|
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: 66.13 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 9 DVHRLNKRFGD-RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLtpDSGHGTCLGYDITKQSREIKRRVGYMTQ 87
Cdd:cd03226 1 RIENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLI--KESSGSILLNGKPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 88 RFTY--WEDlTVRENLDFVARLYEVRRRRERVdrMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTA 165
Cdd:cd03226 79 DVDYqlFTD-SVREELLLGLKELDAGNEQAET--VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180
....*....|....*....|....*....
gi 1422354951 166 GVDPSARREFWEELHRLAARGISVLVSTH 194
Cdd:cd03226 156 GLDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-205 |
8.83e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.28 E-value: 8.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 1 MNADDLLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKR 80
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 81 R-VGYMTQRFTYWEDlTVRENLDFVarlYEVRRRRERVDRMLDEL-RLG---SRAKQLAGSLSGGWKQRLALAAALLQEP 155
Cdd:PRK10247 81 QqVSYCAQTPTLFGD-TVYDNLIFP---WQIRNQQPDPAIFLDDLeRFAlpdTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1422354951 156 ELLLLDEPTAGVDPSARREFWEELHRLAA-RGISVLVSTHYMDEAERCHKL 205
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVReQNIAVLWVTHDKDEINHADKV 207
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-225 |
9.15e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 67.03 E-value: 9.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 22 VVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSR--EIKRRVGYMTQR-------FTYW 92
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAGMVFQNpdnqivaTIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 93 EDLTV-RENLDFVARLYEVRRRRERVDRMLDELRlgSRAKQLagsLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSA 171
Cdd:PRK13633 105 EDVAFgPENLGIPPEEIRERVDESLKKVGMYEYR--RHAPHL---LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 172 RREFWEELHRLAAR-GISVLVSTHYMDEAERCHKLAYISYGVLLAQGEARDLIRQ 225
Cdd:PRK13633 180 RREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-259 |
1.04e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.93 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 17 FGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITK-QSREIKRRVGYMTQRFTYWEDL 95
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 96 TVREnldFVARLYEVRRRRERVDRMLDE------LR---LGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAG 166
Cdd:PRK10253 97 TVQE---LVARGRYPHQPLFTRWRKEDEeavtkaMQatgITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 167 VDPSARREFWEELHRL-AARGISVLVSTHYMDEAER--CHKLAyISYGVLLAQGEARDLIRQQALHTwaVSGANLVGLND 243
Cdd:PRK10253 174 LDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRyaSHLIA-LREGKIVAQGAPKEIVTAELIER--IYGLRCMIIDD 250
|
250
....*....|....*.
gi 1422354951 244 RLQGQPGVeqiVAFGR 259
Cdd:PRK10253 251 PVAGTPLV---VPLGR 263
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-226 |
1.48e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 66.68 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 5 DLLIDVHRLNKRFGD-RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-REIKRRV 82
Cdd:PRK13647 2 DNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENeKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 83 GYMTQ-------RFTYWEDLT---VRENLDfvarlyeVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALL 152
Cdd:PRK13647 82 GLVFQdpddqvfSSTVWDDVAfgpVNMGLD-------KDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 153 QEPELLLLDEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMD-EAERCHKLAYISYGVLLAQGEARDLIRQQ 226
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-201 |
1.58e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 64.95 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 16 RFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGhgTClgyditkqSREIKRRVGYMTQRFTYWEDL 95
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG--TV--------RRAGGARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 96 --TVRE--NLDFVARL----YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGV 167
Cdd:NF040873 71 plTVRDlvAMGRWARRglwrRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|....
gi 1422354951 168 DPSARREFWEELHRLAARGISVLVSTHYMDEAER 201
Cdd:NF040873 151 DAESRERIIALLAEEHARGATVVVVTHDLELVRR 184
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
18-234 |
2.41e-12 |
|
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: 67.10 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSRE-IKRRVGYMTQRfTYWEDLT 96
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDdLRRRIAVVPQR-PHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 97 VRENLDFV------ARLYEvrrrrervdrMLDELRLGSRAKQL----------AGS-LSGGWKQRlalaaallqepelll 159
Cdd:COG4987 425 LRENLRLArpdatdEELWA----------ALERVGLGDWLAALpdgldtwlgeGGRrLSGGERRRlalarallrdapill 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 160 ldepTAGVDPSARREFWEELHRlAARGISVLVSTHYMDEAERCHKLAYISYGVLLAQGEARDLIRQQALHTWAVS 234
Cdd:COG4987 495 ldepTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
7-219 |
4.41e-12 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 64.38 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDR----HVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSRE----- 77
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDararl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 78 IKRRVGYMTQRFTYWEDLTVRENLDFVARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPEL 157
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1422354951 158 LLLDEPTAGVDPSARREFWEELHRL-AARGISVLVSTHYMDEAERCHKLAYISYGVLLAQGEA 219
Cdd:COG4181 168 LFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAA 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-246 |
5.71e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.01 E-value: 5.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 23 VKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSR--EIKRRVGYMTQR-FTYWEDLTVRE 99
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlqGIRKLVGIVFQNpETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 100 NLDFVAR--LYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSARREFWE 177
Cdd:PRK13644 98 DLAFGPEnlCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1422354951 178 ELHRLAARGISVLVSTHYMDEAERCHKLAYISYGVLLAQGEARDLIRQQALHTWAVSGANLVGLNDRLQ 246
Cdd:PRK13644 178 RIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPSLIELAENLK 246
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
15-198 |
9.42e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.42 E-value: 9.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 15 KRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLG--YDITKQSREIKRRVGYMTqrftyw 92
Cdd:COG1129 260 EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDAIRAGIAYVP------ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 93 ED---------LTVREN-----LDFVAR--LYEVRRRRERVDRMLDELRL-GSRAKQLAGSLSGGWKQRlalaaallqep 155
Cdd:COG1129 334 EDrkgeglvldLSIRENitlasLDRLSRggLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKvvlakwlatdp 413
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1422354951 156 elllldepTAGVDPSARREFWEELHRLAARGISVLVSTHYMDE 198
Cdd:COG1129 414 kvlildepTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPE 456
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-107 |
1.29e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.65 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 4 DDLLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-RE-IKRR 81
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDaQAAG 80
|
90 100
....*....|....*....|....*.
gi 1422354951 82 VGYMTQRFTYWEDLTVRENLdFVARL 107
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENI-FLGRE 105
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
8-222 |
1.45e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.45 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDIT--------------K 73
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 74 QSREIKRRVGYMTQRFTYWEDLTVRENL--DFVARL-YEVRRRRERVDRMLDELRLGSRAKQ-LAGSLSGGWKQRLALAA 149
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVmeAPIQVLgLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1422354951 150 ALLQEPELLLLDEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAERCHK-LAYISYGVLLAQGEARDL 222
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQL 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
12-227 |
1.63e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 62.85 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 12 RLNKRFGDRHvvKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREiKRRVGYMTQRFTY 91
Cdd:COG3840 6 DLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERPVSMLFQENNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 92 WEDLTVREN--LDFVARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRlalaaallqepelllldepTA---- 165
Cdd:COG3840 83 FPHLTVAQNigLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQR-------------------VAlarc 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1422354951 166 ---------------GVDPSARREFWEELHRLAA-RGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQQA 227
Cdd:COG3840 144 lvrkrpillldepfsALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEP 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-100 |
1.83e-11 |
|
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: 61.46 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRR-VGYMTQRFTYWEDlT 96
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDhVGYLPQDDELFSG-S 91
|
....
gi 1422354951 97 VREN 100
Cdd:cd03246 92 IAEN 95
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-144 |
5.11e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.04 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITkqSREIKRRVGYMTQRFTYWEDLTV 97
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID--DPDVAEACHYLGHRNAMKPALTV 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1422354951 98 RENLDFVARLYEVRRRRERVDrmLDELRLGSRAKQLAGSLSGGWKQR 144
Cdd:PRK13539 91 AENLEFWAAFLGGEELDIAAA--LEAVGLAPLAHLPFGYLSAGQKRR 135
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-107 |
6.65e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.88 E-value: 6.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREI--KRRVGY 84
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaaQLGIGI 84
|
90 100
....*....|....*....|...
gi 1422354951 85 MTQRFTYWEDLTVRENLdFVARL 107
Cdd:PRK09700 85 IYQELSVIDELTVLENL-YIGRH 106
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
6.83e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 61.55 E-value: 6.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 1 MNADDLLIDVHRLNKRFGDRH--VVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-RE 77
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 78 IKRRVGYMTQ----RFTyweDLTVRENLDF------VAR--LYEVRRRRERVDRMLDELrlgsraKQLAGSLSGGWKQRL 145
Cdd:PRK13632 81 IRKKIGIIFQnpdnQFI---GATVEDDIAFglenkkVPPkkMKDIIDDLAKKVGMEDYL------DKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1422354951 146 ALAAALLQEPELLLLDEPTAGVDPSARREFWEELHRLAARGISVLVS-THYMDEAERCHKLAYISYGVLLAQGE 218
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
7-88 |
1.02e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.90 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGhgtclgyditKQSREIKRRVGYMT 86
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIKRNGKLRIGYVP 73
|
..
gi 1422354951 87 QR 88
Cdd:PRK09544 74 QK 75
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-279 |
1.09e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 61.30 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 25 DLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-----REIKRRVGYMtqrFTYWE----DL 95
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdiKQIRKKVGLV---FQFPEsqlfEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 96 TVRENLDFVARLYEVRRRRERVDRmLDELRLGSRAKQLAG----SLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSA 171
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEEAEALA-REKLALVGISESLFEknpfELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 172 RREFWEELHRLAARGISVLVSTHYMDEAERCHKLAYI-SYGVLLAQGEARDLIRQQALhtwavsganlvgLNDRlqgQPG 250
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVlEKGKLVLSGKPKDIFQDVDF------------LEEK---QLG 245
|
250 260
....*....|....*....|....*....
gi 1422354951 251 VEQIVAFGRSLHVSGGDPERLESSLNELK 279
Cdd:PRK13649 246 VPKITKFAQRLADRGISFSSLPITIEEFR 274
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
8-229 |
1.13e-10 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 62.16 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRH--VVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGH---GtclGYDITKQS-REIKRR 81
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRiliD---GIDLRQIDpASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 82 VGYMTQRFTYWEDlTVRENL----------------------DFVARL---YevrrrrervdrmldELRLGSRAkqlaGS 136
Cdd:COG2274 551 IGVVLQDVFLFSG-TIRENItlgdpdatdeeiieaarlaglhDFIEALpmgY--------------DTVVGEGG----SN 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 137 LSGGWKQRlalaaallqepellllDEPTAGVDPSARREFWEELHRLaARGISVLVSTHYMDEAERCHKLAYISYGVLLAQ 216
Cdd:COG2274 612 LSGGQRQRlaiarallrnprililDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
250
....*....|...
gi 1422354951 217 GEARDLIRQQALH 229
Cdd:COG2274 691 GTHEELLARKGLY 703
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-194 |
1.24e-10 |
|
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: 59.81 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGYMTQRFTYWEDLTV 97
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 98 RENLDFVARLYEVRRRRERvdrmLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSARREFWE 177
Cdd:cd03231 91 LENLRFWHADHSDEQVEEA----LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
170
....*....|....*..
gi 1422354951 178 ELHRLAARGISVLVSTH 194
Cdd:cd03231 167 AMAGHCARGGMVVLTTH 183
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
12-232 |
1.24e-10 |
|
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: 61.27 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 12 RLNKRFGDRHVvkDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGH----GTCLgYDitkQSREI-----KRRV 82
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRirlgGEVL-QD---SARGIflpphRRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 83 GYMTQrftywED-----LTVRENLDFVARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRlalaaallqepel 157
Cdd:COG4148 80 GYVFQ-----EArlfphLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRvaigrallssprl 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1422354951 158 lllDEPTAGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQQALHTWA 232
Cdd:COG4148 155 llmDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRPDLLPLA 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-144 |
1.48e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 61.72 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSRE-IKRRVGYMTQ---RFtywe 93
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLEsLRRQIGVVPQdtfLF---- 426
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1422354951 94 DLTVRENL----------------------DFVARL---YevrrrrervdrmldELRLGSRAkqlaGSLSGGWKQR 144
Cdd:COG1132 427 SGTIRENIrygrpdatdeeveeaakaaqahEFIEALpdgY--------------DTVVGERG----VNLSGGQRQR 484
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-222 |
1.84e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.31 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGL--LTPD---SGHGTCLGYDITKQS-REIKRR 81
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMDvIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 82 VGYMTQ------RFTYWEDLTVRENLDFVAR----LYEVRRRRERVDRMLDELRlgSRAKQLAGSLSGGWKQRLALAAAL 151
Cdd:PRK14247 84 VQMVFQipnpipNLSIFENVALGLKLNRLVKskkeLQERVRWALEKAQLWDEVK--DRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 152 LQEPELLLLDEPTAGVDPSARREFwEELHRLAARGISVLVSTHYMDEAERCHK-LAYISYGVLLAQGEARDL 222
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKI-ESLFLELKKDMTIVLVTHFPQQAARISDyVAFLYKGQIVEWGPTREV 232
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-228 |
2.05e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.95 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 26 LSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLtPDSGH----GTCLGydiTKQSREIKRRVGYMTQR---------FTYW 92
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSiqfaGQPLE---AWSAAELARHRAYLSQQqtppfampvFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 93 E----DLT----VRENLDFVARLyevrrrrervdrmldeLRLGSRAKQLAGSLSGGWKQRLALaaallqepelllldept 164
Cdd:PRK03695 91 TlhqpDKTrteaVASALNEVAEA----------------LGLDDKLGRSVNQLSGGEWQRVRL----------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 165 AGV--------DPSARREFWEE----------------LHRLAARGISVLVSTHYMDE-AERCHKLAYISYGVLLAQGEA 219
Cdd:PRK03695 138 AAVvlqvwpdiNPAGQLLLLDEpmnsldvaqqaaldrlLSELCQQGIAVVMSSHDLNHtLRHADRVWLLKQGKLLASGRR 217
|
....*....
gi 1422354951 220 RDLIRQQAL 228
Cdd:PRK03695 218 DEVLTPENL 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-78 |
2.38e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.50 E-value: 2.38e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1422354951 13 LNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITK---QSREI 78
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHrsiQQRDI 80
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-228 |
2.57e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 59.82 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-REIKRRVGYMTQR-------F 89
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENiREVRKFVGLVFQNpddqifsP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 90 TYWEDLTVRE-NLDFVARLYEVRRRRERVDRMLDELRlgsraKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVD 168
Cdd:PRK13652 95 TVEQDIAFGPiNLGLDEETVAHRVSSALHMLGLEELR-----DRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 169 PSARREFWEELHRLAAR-GISVLVSTHYMD-EAERCHKLAYISYGVLLAQGEARDLIRQQAL 228
Cdd:PRK13652 170 PQGVKELIDFLNDLPETyGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-194 |
2.74e-10 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 59.21 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 14 NKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLtpdSGHGTCLGyDITKQSREIKR-----RVGYMTQR 88
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV---EGGGTTSG-QILFNGQPRKPdqfqkCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 89 FTYWEDLTVRENLDFVARLYEVRRRRERVDRMLDE------LRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDE 162
Cdd:cd03234 90 DILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEdvllrdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|..
gi 1422354951 163 PTAGVDPSARREFWEELHRLAARGISVLVSTH 194
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-144 |
2.79e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.41 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 1 MNADDLLiDVHRLNKRFGD-RHVVKDLS---MQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSR 76
Cdd:PRK10584 1 MPAENIV-EVHHLKKSVGQgEHELSILTgveLVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDE 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 77 EIK-----RRVGYMTQRFTYWEDLTVRENLDFVARLY--EVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQR 144
Cdd:PRK10584 80 EARaklraKHVGFVFQSFMLIPTLNALENVELPALLRgeSSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQR 154
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-229 |
3.33e-10 |
|
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: 59.04 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 20 RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDI-TKQSREIKRRVGYMTQRFTYWeDLTVR 98
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGVVLQENVLF-NRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 99 ENLDF------------VARLyevrrrrERVDRMLDELRLGSraKQLAG----SLSGGWKQRLALAAALLQEPELLLLDE 162
Cdd:cd03252 94 DNIALadpgmsmervieAAKL-------AGAHDFISELPEGY--DTIVGeqgaGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1422354951 163 PTAGVDPSARREFWEELHRLAArGISVLVSTHYMDEAERCHKLAYISYGVLLAQGEARDLIRQQALH 229
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLY 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-194 |
3.34e-10 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 58.33 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCL--GYDITKQSreIKRRVGYMTQRFTYWEDL 95
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLinGRPLDKRS--FRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 96 TVRENLDFVArlyevrrrrervdrmldELRlgsrakqlagSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSARREF 175
Cdd:cd03213 98 TVRETLMFAA-----------------KLR----------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170
....*....|....*....
gi 1422354951 176 WEELHRLAARGISVLVSTH 194
Cdd:cd03213 151 MSLLRRLADTGRTIICSIH 169
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-220 |
4.04e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.09 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGL--LTPDS---GHGTCLGYDITKQSR---EIK 79
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEArveGEVRLFGRNIYSPDVdpiEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 80 RRVGYMTQRFTYWEDLTVRENLDFVARLYEVRRRRE----------RVDRMLDELRlgSRAKQLAGSLSGGWKQRLALAA 149
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKeldervewalKKAALWDEVK--DRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 150 ALLQEPELLLLDEPTAGVDPSARREFWEELHRLAARGISVLVsTHYMDEAERCHK-LAYISYGVLLAQGEAR 220
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLV-THSPAQAARVSDyVAFLYLGKLIEVGPTR 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-228 |
4.55e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.43 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 20 RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHG---TCLGYDITKQSR-EIKRRVGYMTQ----RFTy 91
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNskiTVDGITLTAKTVwDIREKVGIVFQnpdnQFV- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 92 weDLTVRENLDF--VARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDP 169
Cdd:PRK13640 99 --GATVGDDVAFglENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 170 SARREFWEELHRLAA-RGISVLVSTHYMDEAERCHKLAYISYGVLLAQGEARDLIRQQAL 228
Cdd:PRK13640 177 AGKEQILKLIRKLKKkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-107 |
4.76e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.28 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGYMTQRFTYWEDLTV 97
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTA 91
|
90
....*....|
gi 1422354951 98 RENLDFVARL 107
Cdd:PRK13538 92 LENLRFYQRL 101
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-217 |
6.28e-10 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 57.32 E-value: 6.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 19 DRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGYMTQRfTYWEDLTVR 98
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQR-PYLFDTTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 99 ENLdfvarlyevrrrrervdrmldelrlGSRakqlagsLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSARREFWEE 178
Cdd:cd03247 93 NNL-------------------------GRR-------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSL 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 1422354951 179 LHRlAARGISVLVSTHYMDEAERCHKLAYISYGVLLAQG 217
Cdd:cd03247 141 IFE-VLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-194 |
7.77e-10 |
|
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: 57.98 E-value: 7.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 19 DRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-REIKRRVGYMTQRFTYWEDlTV 97
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDpADLRRNIGYVPQDVTLFYG-TL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 98 RENLDF------------VARLYEVRRRRERVDRMLDeLRLGSRAKqlagSLSGGWKQRLALAAALLQEPELLLLDEPTA 165
Cdd:cd03245 95 RDNITLgapladderilrAAELAGVTDFVNKHPNGLD-LQIGERGR----GLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180
....*....|....*....|....*....
gi 1422354951 166 GVDPSARREFWEELHRLaARGISVLVSTH 194
Cdd:cd03245 170 AMDMNSEERLKERLRQL-LGDKTLIIITH 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-101 |
8.98e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 8.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 6 LLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGH---GTclgyditkqsreiKRRV 82
Cdd:PRK11147 318 IVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRihcGT-------------KLEV 384
|
90 100
....*....|....*....|...
gi 1422354951 83 GYMTQrftYWEDL----TVRENL 101
Cdd:PRK11147 385 AYFDQ---HRAELdpekTVMDNL 404
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-194 |
9.52e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.51 E-value: 9.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 15 KRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDiTKQSREIKRRVGYMTQRFTYWED 94
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN-RKPTKQILKRTGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 95 LTVRENLDFVARL-----YEVRRRRERVDRMLDELRLGSRAKQLAGS-----LSGGWKQRLALAAALLQEPELLLLDEPT 164
Cdd:PLN03211 155 LTVRETLVFCSLLrlpksLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190
....*....|....*....|....*....|
gi 1422354951 165 AGVDPSARREFWEELHRLAARGISVLVSTH 194
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-217 |
1.05e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 58.66 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRF----GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS----REIK 79
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekelRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 80 RRVGYMTQRFTYWEDLTVRENLDF---------------VARLyevrrrrervdrmLDELRLGSRAKQLAGSLSGGWKQR 144
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALplelagtpkaeikarVTEL-------------LELVGLSDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 145 LALAAALLQEPELLLLDEPTAGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEAER-CHKLAYISYGVLLAQG 217
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-228 |
1.80e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.49 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 16 RFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITK-QSREIKRRVGYMTQRFTYWED 94
Cdd:PRK10575 20 RVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 95 LTVREnLDFVARL-------YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGV 167
Cdd:PRK10575 100 MTVRE-LVAIGRYpwhgalgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1422354951 168 DPSARREFWEELHRLA-ARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQQAL 228
Cdd:PRK10575 179 DIAHQVDVLALVHRLSqERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMRGETL 241
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-194 |
2.17e-09 |
|
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: 58.14 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSR-EIKRRVGYMTQR---Ftywe 93
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVSVCAQDahlF---- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 94 DLTVRENLdfvaRLYEVRRRRERVDRMLDELRLGSRAKQL-----------AGSLSGGWKQRLALAAALLQEPELLLLDE 162
Cdd:TIGR02868 422 DTTVRENL----RLARPDATDEELWAALERVGLADWLRALpdgldtvlgegGARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|..
gi 1422354951 163 PTAGVDPSARREFWEELhRLAARGISVLVSTH 194
Cdd:TIGR02868 498 PTEHLDAETADELLEDL-LAALSGRTVVLITH 528
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-99 |
5.90e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGhgtclgyditkqsrEIK----RRVG 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG--------------TVKwsenANIG 385
|
90
....*....|....*...
gi 1422354951 84 YMTQRFTYW--EDLTVRE 99
Cdd:PRK15064 386 YYAQDHAYDfeNDLTLFD 403
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-201 |
7.37e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 54.88 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 17 FGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITK-QSREI---KRRVGYMTQRFTYW 92
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlKNREVpflRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 93 EDLTVREN--LDFVARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPS 170
Cdd:PRK10908 92 MDRTVYDNvaIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190
....*....|....*....|....*....|....
gi 1422354951 171 ARR---EFWEELHRLaarGISVLVSTHYMDEAER 201
Cdd:PRK10908 172 LSEgilRLFEEFNRV---GVTVLMATHDIGLISR 202
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
9.66e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 55.04 E-value: 9.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 1 MNADDLLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGL--LTPD---SGHGTCLGYDITKQS 75
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 76 R---EIKRRVGYMTQR---FTywedLTVRENLDFVARLYEVRRRRErvdrmLDEL----------------RLgsraKQL 133
Cdd:COG1117 85 VdvvELRRRVGMVFQKpnpFP----KSIYDNVAYGLRLHGIKSKSE-----LDEIveeslrkaalwdevkdRL----KKS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 134 AGSLSGGWKQRlalaaallqepelllLDEPTAGVDP-SARRefWEEL-HRLAARgISVLVSTHYMDEAERC-HKLAYISY 210
Cdd:COG1117 152 ALGLSGGQQQRlciaralavepevllMDEPTSALDPiSTAK--IEELiLELKKD-YTIVIVTHNMQQAARVsDYTAFFYL 228
|
250
....*....|..
gi 1422354951 211 GVLLAQGEARDL 222
Cdd:COG1117 229 GELVEFGPTEQI 240
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-236 |
1.00e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 19 DRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS--REIKRRVGYMTQ--RFT-YWE 93
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSplDAVKKGMAYITEsrRDNgFFP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 94 DLTVRENLDFVARLYEVRRRRER-VDRMLDELRLGSRAKQL-----------AGSLSGGWKQRLALAAALLQEPELLLLD 161
Cdd:PRK09700 355 NFSIAQNMAISRSLKDGGYKGAMgLFHEVDEQRTAENQRELlalkchsvnqnITELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1422354951 162 EPTAGVDPSARREFWEELHRLAARGISVL-VSTHYMDEAERCHKLAYISYGVLLAQGEARDLIRQQALHTWAVSGA 236
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADDGKVILmVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIMAWALPQE 510
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-228 |
1.00e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.82 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 4 DDLLIDVHRLNKRFGD----RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIK 79
Cdd:PRK11629 2 NKILLQCDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 80 -----RRVGYMTQRFTYWEDLTVREN--LDFVARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALL 152
Cdd:PRK11629 82 aelrnQKLGFIYQFHHLLPDFTALENvaMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1422354951 153 QEPELLLLDEPTAGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEAERCHKlayisygvllaQGEARDLIRQQAL 228
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRMSR-----------QLEMRDGRLTAEL 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-144 |
1.07e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.08 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRF---------GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSRE 77
Cdd:PRK10419 3 LLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 78 IK---RR---------VGYMTQRFTYWEdlTVRENLDFVARLyEVRRRRERVDRMLDELRLG-SRAKQLAGSLSGGWKQR 144
Cdd:PRK10419 83 QRkafRRdiqmvfqdsISAVNPRKTVRE--IIREPLRHLLSL-DKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQR 159
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-101 |
1.12e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.95 E-value: 1.12e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1422354951 29 QVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGhgtclgyditkqSREIKRRVGYMTQRFTYWEDLTVRENL 101
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG------------EVDEDLKISYKPQYISPDYDGTVEEFL 422
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-199 |
1.22e-08 |
|
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: 54.39 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 23 VKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREikRRVGYMTQRFTYWedLTVRENL- 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD--RMVVFQNYSLLPW--LTVRENIa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 102 ---DFVARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSARREFWEE 178
Cdd:TIGR01184 77 lavDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180
....*....|....*....|..
gi 1422354951 179 LHRLAAR-GISVLVSTHYMDEA 199
Cdd:TIGR01184 157 LMQIWEEhRVTVLMVTHDVDEA 178
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
7-87 |
1.98e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 54.35 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFG---DRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSR-EIKRRV 82
Cdd:PRK13650 4 IIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKI 83
|
....*
gi 1422354951 83 GYMTQ 87
Cdd:PRK13650 84 GMVFQ 88
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-144 |
2.14e-08 |
|
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: 53.95 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 30 VRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRvgymtqrftywEDLTVRENL-DFVARLY 108
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKAD-----------YEGTVRDLLsSITKDFY 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 1422354951 109 evrRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQR 144
Cdd:cd03237 91 ---THPYFKTEIAKPLQIEQILDREVPELSGGELQR 123
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-108 |
2.26e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 29 QVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGhgtclgyditkqSREIKRRVGYMTQRFTYWEDLTVRENLDFVARLY 108
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG------------EVDPELKISYKPQYIKPDYDGTVEDLLRSITDDL 428
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-225 |
2.48e-08 |
|
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: 54.81 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFG--DRHVVK---DLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGH-GTCLG---YDITKQSRE 77
Cdd:TIGR03269 279 IIKVRNVSKRYIsvDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvNVRVGdewVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 78 ----IKRRVGYMTQRFTYWEDLTVRENL------DFVARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLAL 147
Cdd:TIGR03269 359 grgrAKRYIGILHQEYDLYPHRTVLDNLteaiglELPDELARMKAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVAL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 148 AAALLQEPELLLLDEPTAGVDPSARREFWEELHRlaAR---GISVLVSTHYMDEA-ERCHKLAYISYGVLLAQGEARDLI 223
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILK--AReemEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIV 516
|
..
gi 1422354951 224 RQ 225
Cdd:TIGR03269 517 EE 518
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-144 |
2.79e-08 |
|
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: 54.75 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSRE-IKRRVGYMTQR---Ftywe 93
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREeLGRHIGYLPQDvelF---- 418
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 94 DLTVRENldfVARLyevrrrrervdRMLDELRLgSRAKQLAG---------------------SLSGGWKQR 144
Cdd:COG4618 419 DGTIAEN---IARF-----------GDADPEKV-VAAAKLAGvhemilrlpdgydtrigeggaRLSGGQRQR 475
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-249 |
3.64e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.47 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 16 RFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSG----HGTCLGYDiTKQSREIKRRVGYMTQ---R 88
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGavlwQGKPLDYS-KRGLLALRQQVATVFQdpeQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 89 FTYWEDLtvreNLDFVARLYEVRRRRERVDRMLDELRLGSRAK----QLAGSLSGGWKQRLALAAALLQEPELLLLDEPT 164
Cdd:PRK13638 89 QIFYTDI----DSDIAFSLRNLGVPEAEITRRVDEALTLVDAQhfrhQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 165 AGVDPSARREFWEELHRLAARGISVLVSTHYMDEAERCHKLAYI-SYGVLLAQGEARDLI-RQQALHTWAVSGANLVGLN 242
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVlRQGQILTHGAPGEVFaCTEAMEQAGLTQPWLVKLH 244
|
....*..
gi 1422354951 243 DRLqGQP 249
Cdd:PRK13638 245 TQL-GLP 250
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
14-217 |
4.26e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.58 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 14 NKRFGDRHVVkDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGH---GTCLGYDITKQS--REIKRRVGYMTQ- 87
Cdd:PRK13643 14 NSPFASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKvtvGDIVVSSTSKQKeiKPVRKKVGVVFQf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 88 -RFTYWEDlTVRENLDFVARLYEVRRRRERVDRMlDELRLGSRAKQL----AGSLSGGWKQRLALAAALLQEPELLLLDE 162
Cdd:PRK13643 93 pESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAA-EKLEMVGLADEFweksPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 163 PTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAERchklaYISYGVLLAQG 217
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVAD-----YADYVYLLEKG 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-100 |
4.28e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.17 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 11 HRLNKRF-GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHgtclgydiTKQSREIKrrVGYMTQRF 89
Cdd:TIGR03719 8 NRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE--------ARPQPGIK--VGYLPQEP 77
|
90
....*....|.
gi 1422354951 90 TYWEDLTVREN 100
Cdd:TIGR03719 78 QLDPTKTVREN 88
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
7-136 |
4.38e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.54 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSReiKRRVGYMT 86
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR--SRFMAYLG 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1422354951 87 QRFTYWEDLTVRENLDFVARLYevrrrrervdrmldelrlGSRAKQLAGS 136
Cdd:PRK13543 89 HLPGLKADLSTLENLHFLCGLH------------------GRRAKQMPGS 120
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
22-238 |
6.65e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.77 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 22 VVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGH----GTCLGYDiTKQSREIKRRVGYMTQR-----FTyw 92
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEvlikGEPIKYD-KKSLLEVRKTVGIVFQNpddqlFA-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 93 edLTVRENLDFvARLYEVRRRRERVDRMLDELR---LGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDP 169
Cdd:PRK13639 94 --PTVEEDVAF-GPLNLGLSKEEVEKRVKEALKavgMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 170 SARREFWEELHRLAARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIRQQALhtwaVSGANL 238
Cdd:PRK13639 171 MGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSDIET----IRKANL 236
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
7-208 |
9.25e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.19 E-value: 9.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDIT--KQSREIKRRVGY 84
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 85 MTQRFTYWEDLTVRENLDFVARLYEVRRRRERVDRMLDEL-RLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEP 163
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1422354951 164 TAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAERCHKLAYI 208
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYV 209
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4-144 |
9.81e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 51.89 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 4 DDLLIDVHRLNKRFgdrhvvkdlSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREiKRRVG 83
Cdd:PRK10771 5 TDITWLYHHLPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-RRPVS 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1422354951 84 YMTQRFTYWEDLTVREN--LDFVARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQR 144
Cdd:PRK10771 75 MLFQENNLFSHLTVAQNigLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQR 137
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-103 |
1.05e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.49 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGYMT 86
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
|
90
....*....|....*..
gi 1422354951 87 QRFTYWEDLTVRENLDF 103
Cdd:PRK13540 81 HRSGINPYLTLRENCLY 97
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-201 |
1.09e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.09 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 1 MNADDLLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGL--LTPDSG-------HGTCLgYDI 71
Cdd:PRK14243 4 LNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFRvegkvtfHGKNL-YAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 72 TKQSREIKRRVGYMTQRFTYWEDlTVRENLDFVAR-------LYEVRRRRERVDRMLDELRlgSRAKQLAGSLSGGWKQR 144
Cdd:PRK14243 83 DVDPVEVRRRIGMVFQKPNPFPK-SIYDNIAYGARingykgdMDELVERSLRQAALWDEVK--DKLKQSGLSLSGGQQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1422354951 145 LALAAALLQEPELLLLDEPTAGVDPSARREFWEELHRLAARGISVLVsTHYMDEAER 201
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIV-THNMQQAAR 215
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
18-200 |
1.10e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 51.33 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPD-SGHGTCL--GYDITKQSREiKRRVGYMTQRFTYWED 94
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfSASGEVLlnGRRLTALPAE-QRRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 95 LTVRENLDF-VARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSARR 173
Cdd:COG4136 91 LSVGENLAFaLPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180 190
....*....|....*....|....*....|.
gi 1422354951 174 EF----WEELHrlaARGISVLVSTHYMDEAE 200
Cdd:COG4136 171 QFrefvFEQIR---QRGIPALLVTHDEEDAP 198
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-198 |
1.12e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.14 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 25 DLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-----REIKRRVGYMTQ--RFTYWEDlTV 97
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknlKKLRKKVSLVFQfpEAQLFEN-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 98 RENLDFVARLYEVRRRRERVDRMLDELRLGSRAKQLAGS---LSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSARRE 174
Cdd:PRK13641 104 LKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSpfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180
....*....|....*....|....
gi 1422354951 175 FWEELHRLAARGISVLVSTHYMDE 198
Cdd:PRK13641 184 MMQLFKDYQKAGHTVILVTHNMDD 207
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-199 |
1.36e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 51.62 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREikRRVGYMT 86
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE--RGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 87 QRFTYWEDltVRENLDFVARL--YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPT 164
Cdd:PRK11248 79 EGLLPWRN--VQDNVAFGLQLagVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1422354951 165 AGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEA 199
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEA 192
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-100 |
1.45e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 11 HRLNKRFG-DRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCL-GYditkqsreikrRVGYMTQR 88
Cdd:PRK11819 10 NRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGI-----------KVGYLPQE 78
|
90
....*....|..
gi 1422354951 89 FTYWEDLTVREN 100
Cdd:PRK11819 79 PQLDPEKTVREN 90
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-103 |
1.55e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.36 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVG-YM 85
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiYL 90
|
90
....*....|....*....
gi 1422354951 86 T-QRFTYWEDLTVRENLDF 103
Cdd:PRK15439 91 VpQEPLLFPNLSVKENILF 109
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
23-225 |
1.63e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 51.59 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 23 VKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS---REIKRRVGYMTQRFTY--WEDlTV 97
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklSDIRKKVGLVFQYPEYqlFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 98 RENLDFVARlyevrrrrervDRMLDELRLGSRAKQ---LAG------------SLSGGWKQRLALAAALLQEPELLLLDE 162
Cdd:PRK13637 102 EKDIAFGPI-----------NLGLSEEEIENRVKRamnIVGldyedykdkspfELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 163 PTAGVDPSARREFWEELHRLAAR-GISVLVSTHYM-DEAERCHKLAYISYGVLLAQGEARDLIRQ 225
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMeDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
22-194 |
1.93e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.42 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 22 VVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSRE---IKRR--VGYMTQRFTYWEDLT 96
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADalaQLRRehFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 97 VRENLDFVArLY---EVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSARR 173
Cdd:PRK10535 103 AAQNVEVPA-VYaglERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE 181
|
170 180
....*....|....*....|.
gi 1422354951 174 EFWEELHRLAARGISVLVSTH 194
Cdd:PRK10535 182 EVMAILHQLRDRGHTVIIVTH 202
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-225 |
1.95e-07 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 52.43 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 20 RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRR-VGYMTQRfTYWEDLTVR 98
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQfINYLPQE-PYIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 99 ENLDFVARLYEVRRRRERVDRMLD--------ELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPS 170
Cdd:TIGR01193 566 ENLLLGAKENVSQDEIWAACEIAEikddienmPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 171 ARREFWEELHRLAARGIsVLVStHYMDEAERCHKLAYISYGVLLAQGEARDLIRQ 225
Cdd:TIGR01193 646 TEKKIVNNLLNLQDKTI-IFVA-HRLSVAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
12-62 |
1.97e-07 |
|
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: 50.26 E-value: 1.97e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1422354951 12 RLNKRFGDRHVVKDLSmQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSG 62
Cdd:cd03222 5 DCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD 54
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-158 |
2.09e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 50.85 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQ-SREIKRRVGYMT 86
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTpSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 87 Q------RftywedLTVRENLDF-----------------VARlyevrrrrervdrMLDELRLGSRAKQLAGSLSGGWKQ 143
Cdd:COG4604 82 QenhinsR------LTVRELVAFgrfpyskgrltaedreiIDE-------------AIAYLDLEDLADRYLDELSGGQRQ 142
|
170
....*....|....*
gi 1422354951 144 RLALAAALLQEPELL 158
Cdd:COG4604 143 RAFIAMVLAQDTDYV 157
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-63 |
2.35e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.08 E-value: 2.35e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGH 63
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGE 62
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-222 |
2.97e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.82 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 2 NADDLLiDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLL-TPDS-----GHGTCLGYDITK-Q 74
Cdd:PRK14246 6 SAEDVF-NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeIYDSkikvdGKVLYFGKDIFQiD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 75 SREIKRRVGYMTQRFTYWEDLTVRENLDFVARLYEVRRRRERVDRMLDELR-------LGSRAKQLAGSLSGGWKQRLAL 147
Cdd:PRK14246 85 AIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRkvglwkeVYDRLNSPASQLSGGQQQRLTI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 148 AAALLQEPELLLLDEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAERCHKLAYISYGVLLAQGEARDL 222
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-194 |
3.48e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.59 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 20 RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDS-GHGTCL--GYDITKqsREIKRRVGYMTQRFTYWEDLT 96
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkGSGSVLlnGMPIDA--KEMRAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 97 VRENLDFVARL-----YEVRRRRERVDRMLDELRLGSRAKQLAG------SLSGGWKQRLALAAALLQEPELLLLDEPTA 165
Cdd:TIGR00955 116 VREHLMFQAHLrmprrVTKKEKRERVDEVLQALGLRKCANTRIGvpgrvkGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180
....*....|....*....|....*....
gi 1422354951 166 GVDPSARREFWEELHRLAARGISVLVSTH 194
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-101 |
3.52e-07 |
|
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: 51.36 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTpdsgHGTCLGyDITKQSREIKRR----- 81
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYP----HGTWDG-EIYWSGSPLKASnirdt 75
|
90 100
....*....|....*....|....
gi 1422354951 82 ----VGYMTQRFTYWEDLTVRENL 101
Cdd:TIGR02633 76 eragIVIIHQELTLVPELSVAENI 99
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-205 |
4.85e-07 |
|
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: 50.75 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 3 ADDLLIDVHRLNKRFGDR-HVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSRE-IKR 80
Cdd:TIGR02857 317 APASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADsWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 81 RVGYMTQRFTYWEDlTVRENLDF------------VARLYEVRRRRERVDRMLDeLRLGSRAkqlAGsLSGGWKQRLALA 148
Cdd:TIGR02857 397 QIAWVPQHPFLFAG-TIAENIRLarpdasdaeireALERAGLDEFVAALPQGLD-TPIGEGG---AG-LSGGQAQRLALA 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1422354951 149 AALLQEPELLLLDEPTAGVDPSARREFWEELHRLaARGISVLVSTHYMDEAERCHKL 205
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALADRI 526
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-238 |
9.86e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.46 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 4 DDLLIDVHRLNKRFGD-RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGH----GTCLGYDiTKQSREI 78
Cdd:PRK13636 2 EDYILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRilfdGKPIDYS-RKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 79 KRRVGYMTQRftywedltvRENLDFVARLYEVRRRRERVDRM-LDELRLG-SRAKQLAG----------SLSGGWKQRLA 146
Cdd:PRK13636 81 RESVGMVFQD---------PDNQLFSASVYQDVSFGAVNLKLpEDEVRKRvDNALKRTGiehlkdkpthCLSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 147 LAAALLQEPELLLLDEPTAGVDPSARREFWEELHRLAAR-GISVLVSTHYMDE-AERCHKLAYISYGVLLAQGEARDLIR 224
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
250
....*....|....
gi 1422354951 225 QQALhtwaVSGANL 238
Cdd:PRK13636 232 EKEM----LRKVNL 241
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-226 |
1.07e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 50.11 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 19 DRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITK-QSREIKRRVGYMTQRFTYWEDlTV 97
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLFSG-SV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 98 RENLDFVARLYEVRRRRERVDR-------MLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPS 170
Cdd:TIGR00958 572 RENIAYGLTDTPDEEIMAAAKAanahdfiMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1422354951 171 ARREFWEELHRlaaRGISVLVSTHYMDEAERCHKLAYISYGVLLAQGEARDLIRQQ 226
Cdd:TIGR00958 652 CEQLLQESRSR---ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-191 |
1.38e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.25 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 20 RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSRE--IKRRVGYMTqrftywED--- 94
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRerRRLGVAYIP------EDrlg 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 95 ------LTVRENLdfVARLYEVRRRRERVdrMLDELRLGSRAKQL--------------AGSLSGGWKQRlalaaallqe 154
Cdd:COG3845 345 rglvpdMSVAENL--ILGRYRRPPFSRGG--FLDRKAIRAFAEELieefdvrtpgpdtpARSLSGGNQQKvilarelsrd 420
|
170 180 190
....*....|....*....|....*....|....*..
gi 1422354951 155 pelllldepTAGVDPSARREFWEELHRLAARGISVLV 191
Cdd:COG3845 421 pklliaaqpTRGLDVGAIEFIHQRLLELRDAGAAVLL 457
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-199 |
1.45e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.93 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 22 VVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSG--------------HGTCLGYDIT-----------KQSR 76
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkkTKEKEKVLEKlviqktrfkkiKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 77 EIKRRVGYMTQRFTY--WEDlTVRENLDFVARLYEVRRRRERVDRM-------LDELRLgsraKQLAGSLSGGWKQRLAL 147
Cdd:PRK13651 102 EIRRRVGVVFQFAEYqlFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAkyielvgLDESYL----QRSPFELSGGQKRRVAL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 148 AAALLQEPELLLLDEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEA 199
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNV 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-63 |
1.70e-06 |
|
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: 49.30 E-value: 1.70e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1422354951 1 MNADDLLiDVHRLNKRFGD----RHVVKDLSMQVRRGEIFGFLGPNGSGKT-TSMRMMcGLLTPDSGH 63
Cdd:COG4172 1 MMSMPLL-SVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDPAAH 66
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
15-101 |
1.97e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 15 KRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLtPdsgHGTCLGyDI-----TKQSREIK--RRVG--YM 85
Cdd:PRK13549 13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-P---HGTYEG-EIifegeELQASNIRdtERAGiaII 87
|
90
....*....|....*.
gi 1422354951 86 TQRFTYWEDLTVRENL 101
Cdd:PRK13549 88 HQELALVKELSVLENI 103
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-55 |
2.06e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.10 E-value: 2.06e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 1 MNADDLLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCG 55
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-230 |
2.26e-06 |
|
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: 48.94 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 19 DRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-REIKRRVGYMTQRFTYWEDlTV 97
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTlASLRRQVALVSQDVVLFND-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 98 RENLDFVARLYEVRRRRERVDRM------LDELRLG--SRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDP 169
Cdd:TIGR02203 423 ANNIAYGRTEQADRAEIERALAAayaqdfVDKLPLGldTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDN 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1422354951 170 SARREFWEELHRLaARGISVLVSTHYMDEAERCHKLAYISYGVLLAQGEARDLIRQQALHT 230
Cdd:TIGR02203 503 ESERLVQAALERL-MQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYA 562
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
10-144 |
3.43e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 47.36 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 10 VHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGH---GTCLGYDITKQSReikrrvgYMT 86
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEllaGTAPLAEAREDTR-------LMF 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 87 Q--RFTYWEdlTVRENLDfvarLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQR 144
Cdd:PRK11247 88 QdaRLLPWK--KVIDNVG----LGLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQR 141
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-222 |
3.55e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 47.78 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 19 DRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSR-EIKRRVGYMTQR-FTYWEDLT 96
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 97 VRENLDFvaRLYEVRRRRERVDRMLDELRLGSRAKQLA----GSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSAR 172
Cdd:PRK13642 99 VEDDVAF--GMENQGIPREEMIKRVDEALLAVNMLDFKtrepARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1422354951 173 REFWEELHRLAAR-GISVLVSTHYMDEAERCHKLAYISYGVLLAQGEARDL 222
Cdd:PRK13642 177 QEIMRVIHEIKEKyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
7-196 |
4.83e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.91 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGhgtclgyDITKQSREIKRRVGYMT 86
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGG-------TILLRGQHIEGLPGHQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 87 QRF----TY-----WEDLTVRENL----------DFVARLY-------EVRRRRERVDRMLDELRLGSRAKQLAGSLSGG 140
Cdd:PRK11300 78 ARMgvvrTFqhvrlFREMTVIENLlvaqhqqlktGLFSGLLktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1422354951 141 WKQRLALAAALLQEPELLLLDEPTAGVDPSARREFWEELHRLAAR-GISVLVSTHYM 196
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDM 214
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
11-216 |
1.04e-05 |
|
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: 45.95 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 11 HRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRV-------- 82
Cdd:TIGR02769 15 GGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFrrdvqlvf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 83 --------GYMTQRFTYWEDLTVRENLDFVARLyevrrrrERVDRMLDELRLGSR-AKQLAGSLSGGWKQRLALAAALLQ 153
Cdd:TIGR02769 95 qdspsavnPRMTVRQIIGEPLRHLTSLDESEQK-------ARIAELLDMVGLRSEdADKLPRQLSGGQLQRINIARALAV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 154 EPELLLLDEPTAGVDPSARREFWEELHRLAAR-GISVLVSTHYMDEAER-CHKLAYISYGVLLAQ 216
Cdd:TIGR02769 168 KPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
27-201 |
1.41e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 45.77 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 27 SMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDI------TKQSREIKRRVGYMTQ--RFTYWEDlTVR 98
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkkIKEVKRLRKEIGLVFQfpEYQLFQE-TIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 99 ENLDF--VARLYEVRRRRERVDRMLDELRLGSR-AKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSARREF 175
Cdd:PRK13645 110 KDIAFgpVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDF 189
|
170 180
....*....|....*....|....*..
gi 1422354951 176 WEELHRL-AARGISVLVSTHYMDEAER 201
Cdd:PRK13645 190 INLFERLnKEYKKRIIMVTHNMDQVLR 216
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-48 |
1.42e-05 |
|
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: 45.21 E-value: 1.42e-05
10 20 30
....*....|....*....|....*....|.
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTT 48
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKST 41
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-191 |
1.60e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.06 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 27 SMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVGYMTQRftywED---------LTV 97
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCP----EDrkaegiipvHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 98 RENLDFVAR--------LYEVRRRRERVDRMLDELRLGSR-AKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVD 168
Cdd:PRK11288 349 ADNINISARrhhlragcLINNRWEAENADRFIRSLNIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180
....*....|....*....|...
gi 1422354951 169 PSARREFWEELHRLAARGISVLV 191
Cdd:PRK11288 429 VGAKHEIYNVIYELAAQGVAVLF 451
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-144 |
1.74e-05 |
|
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: 45.30 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 19 DRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-REIKRRVGYMTQRfTYWEDLTV 97
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlASLRRQIGLVSQD-VFLFNDTV 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1422354951 98 RENLDF------------VARLYEVRRRRERVDRMLDElRLGSRAkqlaGSLSGGWKQR 144
Cdd:cd03251 93 AENIAYgrpgatreeveeAARAANAHEFIMELPEGYDT-VIGERG----VKLSGGQRQR 146
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-226 |
2.81e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 44.74 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 23 VKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-REIKRRVGYMTQ----RFTyweDLTV 97
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNfEKLRKHIGIVFQnpdnQFV---GSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 98 RENLDF--VARLYEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSARREF 175
Cdd:PRK13648 102 KYDVAFglENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 176 WEELHRLAA-RGISVLVSTHYMDEAERCHKLAYISYGVLLAQGEARDLIRQQ 226
Cdd:PRK13648 182 LDLVRKVKSeHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-144 |
4.23e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 44.34 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 1 MNADDLLIDVHRLNKRF---------GDRHV--VKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGY 69
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 70 DITKQS----REIKRRVGYMTQ--------RFTYWEdlTVRENLDfVARLYEVRRRRERVDRMLDELRLGSR-AKQLAGS 136
Cdd:COG4608 81 DITGLSgrelRPLRRRMQMVFQdpyaslnpRMTVGD--IIAEPLR-IHGLASKAERRERVAELLELVGLRPEhADRYPHE 157
|
....*...
gi 1422354951 137 LSGGWKQR 144
Cdd:COG4608 158 FSGGQRQR 165
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
5-62 |
4.45e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.04 E-value: 4.45e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1422354951 5 DLLIDVHRlNKRFgdrHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSG 62
Cdd:PRK13546 26 DALIPKHK-NKTF---FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG 79
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-62 |
5.32e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 44.01 E-value: 5.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1422354951 5 DLLIDVHRLNKRFGDR-------HV--VKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSG 62
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRtgwfrrqTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSG 68
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-218 |
5.43e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.07 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 4 DDLLIDVHRLNKRFGDRH-----VVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSG-----------HGTCL 67
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 68 GYDITKQSREIK------RRVGYMTQ--RFTYWEDlTVRENLDF--VARLYEVRRRRERVDRMLDELRLGSRAKQLAG-S 136
Cdd:PRK13631 98 ELITNPYSKKIKnfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFgpVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPfG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 137 LSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDeaercHKLAYISYGVLLAQ 216
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME-----HVLEVADEVIVMDK 251
|
..
gi 1422354951 217 GE 218
Cdd:PRK13631 252 GK 253
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-144 |
5.46e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 44.57 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRR-VGYMTQR---Ftywe 93
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRnIAVVFQDaglF---- 421
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1422354951 94 DLTVRENL----------------------DFVARlyevrrrrervdrmlDELRLGSRAKQLAGSLSGGWKQR 144
Cdd:PRK13657 422 NRSIEDNIrvgrpdatdeemraaaeraqahDFIER---------------KPDGYDTVVGERGRQLSGGERQR 479
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-107 |
6.37e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.71 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSM-----RMMCGLLTPD----SGHGTclgyDITKQsreikRRVGYMTQR 88
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGVITGGdrlvNGRPL----DSSFQ-----RSIGYVQQQ 844
|
90
....*....|....*....
gi 1422354951 89 FTYWEDLTVRENLDFVARL 107
Cdd:TIGR00956 845 DLHLPTSTVRESLRFSAYL 863
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-95 |
6.46e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 6.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1422354951 30 VRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDsghgtcLGYDITKQSRE--IKRRVGymTQRFTYWEDL 95
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPN------LGDYEEEPSWDevLKRFRG--TELQNYFKKL 155
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-62 |
7.45e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.00 E-value: 7.45e-05
10 20 30
....*....|....*....|....*....|..
gi 1422354951 31 RRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSG 62
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLG 128
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-144 |
8.37e-05 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 43.30 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 19 DRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQS-REIKRRVGYMTQR---FtyweD 94
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNlRWLRSQIGLVSQEpvlF----D 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 95 LTVRENLDF------------VARLYEVRRRRERVDRMLDELrLGSRAKQLagslSGGWKQR 144
Cdd:cd03249 91 GTIAENIRYgkpdatdeeveeAAKKANIHDFIMSLPDGYDTL-VGERGSQL----SGGQKQR 147
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-169 |
8.49e-05 |
|
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: 42.98 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKR-RVGYMTQRFTYWEDlT 96
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRsMIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 97 VRENLDFvARLYEVRRRRERVDRMLDELRLGSR--------AKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVD 168
Cdd:cd03254 93 IMENIRL-GRPNATDEEVIEAAKEAGAHDFIMKlpngydtvLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
.
gi 1422354951 169 P 169
Cdd:cd03254 172 T 172
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-107 |
1.36e-04 |
|
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: 41.85 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCL--GYDITKqsrEIKRRVGYMTQRFTYWEDL 95
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILinGRPLDK---NFQRSTGYVEQQDVHSPNL 94
|
90
....*....|..
gi 1422354951 96 TVRENLDFVARL 107
Cdd:cd03232 95 TVREALRFSALL 106
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-144 |
2.00e-04 |
|
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: 41.83 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 14 NKRFG---DRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSRE-IKRRVGYMTQRF 89
Cdd:cd03253 5 NVTFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDsLRRAIGVVPQDT 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1422354951 90 TYWEDlTVRENLDFvARLYEVRrrrervdrmlDELRLGSRAKQLAGS------------------LSGGWKQR 144
Cdd:cd03253 85 VLFND-TIGYNIRY-GRPDATD----------EEVIEAAKAAQIHDKimrfpdgydtivgerglkLSGGEKQR 145
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-222 |
2.66e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 42.01 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 17 FGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGH---GTCL--GYDI--TKQSREIKRRVGYMTQRF 89
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysGDVLlgGRSIfnYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 90 TYWEdLTVRENLDFVAR---LYEVRRRRERVDRMLDELRLGSRAK-QLAGS---LSGGWKQRLALAAALLQEPELLLLDE 162
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRahkLVPRKEFRGVAQARLTEVGLWDAVKdRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1422354951 163 PTAGVDPSARREFWEELHRLAARgISVLVSTHYMDEAERCHKLAYISY-GVLLAQGEARDL 222
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFdGRLVEEGPTEQL 249
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-62 |
2.71e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 41.48 E-value: 2.71e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1422354951 20 RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLL--TPDSG 62
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAG 87
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-56 |
2.86e-04 |
|
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: 40.60 E-value: 2.86e-04
10 20 30
....*....|....*....|....*....|....*
gi 1422354951 22 VVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGL 56
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL 50
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-62 |
2.99e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 2.99e-04
10 20 30
....*....|....*....|....*....|.
gi 1422354951 32 RGEIFGFLGPNGSGKTTSMRMMCGLLTPDSG 62
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG 31
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-232 |
3.04e-04 |
|
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: 41.96 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRF----GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTP---DSGHGTCLGYDITKQS-REI 78
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSeKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 79 K----RRVGYMTQrftyweD--------LTVRENLDFVARLYEVRRRRERV---DRMLDELRL---GSRAKQLAGSLSGG 140
Cdd:COG0444 81 RkirgREIQMIFQ------DpmtslnpvMTVGDQIAEPLRIHGGLSKAEAReraIELLERVGLpdpERRLDRYPHELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 141 WKQRlalaaallqepelllLDEPTAGVDPSARREFWEELHRLAA-RGISVLVSTHYMDE-AERCHKLAyisygVLLA--- 215
Cdd:COG0444 155 MRQRvmiaralalepklliADEPTTALDVTIQAQILNLLKDLQReLGLAILFITHDLGVvAEIADRVA-----VMYAgri 229
|
250 260
....*....|....*....|.
gi 1422354951 216 --QGEARDLIRqQALH--TWA 232
Cdd:COG0444 230 veEGPVEELFE-NPRHpyTRA 249
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
13-195 |
3.07e-04 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 41.48 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 13 LNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGllTPD----SGHGTCLGYDITKQSREIKRRVGyMTQR 88
Cdd:TIGR01978 6 LHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFKGQDLLELEPDERARAG-LFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 89 FTYWEDLTVRENLDFV-----ARLYEVRRRRERVDRMLDELRLGSRAKQLAGSL---------SGGWKQRLALAAALLQE 154
Cdd:TIGR01978 83 FQYPEEIPGVSNLEFLrsalnARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFlnrsvnegfSGGEKKRNEILQMALLE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1422354951 155 PELLLLDEPTAGVDPSARREFWEELHRLAARGISVLVSTHY 195
Cdd:TIGR01978 163 PKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHY 203
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-48 |
3.15e-04 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 41.59 E-value: 3.15e-04
10 20 30
....*....|....*....|....*....|.
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTT 48
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKST 41
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-101 |
3.25e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.21 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 25 DLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSG----HGTCLGYDITKQSreIKRRVGYMTQRFTYWEDLTVREN 100
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGsiliDGQEMRFASTTAA--LAAGVAIIYQELHLVPEMTVAEN 99
|
.
gi 1422354951 101 L 101
Cdd:PRK11288 100 L 100
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
18-63 |
3.76e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 41.75 E-value: 3.76e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGH 63
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE 60
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
15-199 |
3.86e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 41.55 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 15 KRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGH---GTCLGYDITKQsreiKRRVGYMTQRFTY 91
Cdd:PRK11000 11 KAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDlfiGEKRMNDVPPA----ERGVGMVFQSYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 92 WEDLTVRENLDFVARLYEVRRRRERV--DRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDP 169
Cdd:PRK11000 87 YPHLSVAENMSFGLKLAGAKKEEINQrvNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
170 180 190
....*....|....*....|....*....|.
gi 1422354951 170 SARREFWEELHRLAAR-GISVLVSTHYMDEA 199
Cdd:PRK11000 167 ALRVQMRIEISRLHKRlGRTMIYVTHDQVEA 197
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-84 |
4.51e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 3 ADDLLIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTsmrmMCGLLTPDsgHGTCLGYDITKQSR------ 76
Cdd:PRK10938 256 ANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKST----LLSLITGD--HPQGYSNDLTLFGRrrgsge 329
|
90
....*....|.
gi 1422354951 77 ---EIKRRVGY 84
Cdd:PRK10938 330 tiwDIKKHIGY 340
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-213 |
4.62e-04 |
|
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: 40.92 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 19 DRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITK-QSREIKRRVGYMTQRFTYWEDlTV 97
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 98 RENLDF-----VARLYEVRRRRERVDRMLDELRLG--SRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPS 170
Cdd:cd03248 105 QDNIAYglqscSFECVKEAAQKAHAHSFISELASGydTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1422354951 171 ARREFwEELHRLAARGISVLVSTHYMDEAERCHKLAYISYGVL 213
Cdd:cd03248 185 SEQQV-QQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-193 |
4.63e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 23 VKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSRE--IKRRVGYMTqrftywED------ 94
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdgLANGIVYIS------EDrkrdgl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 95 ---LTVREN-----LDFVARLYEVRRRRERVDRMLDELRL-----GSRaKQLAGSLSGGWKQRLALAAALLQEPELLLLD 161
Cdd:PRK10762 342 vlgMSVKENmsltaLRYFSRAGGSLKHADEQQAVSDFIRLfniktPSM-EQAIGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190
....*....|....*....|....*....|...
gi 1422354951 162 EPTAGVDPSARREFWEELHRLAARGIS-VLVST 193
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFKAEGLSiILVSS 453
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-224 |
4.67e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 41.16 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 20 RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDIT-----KQSREIKRRVGYMtqrFTYWE- 93
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknKKLKPLRKKVGIV---FQFPEh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 94 ---DLTVRENLDF------VARlyevRRRRERVDRMLDELRLGsrAKQLAGS---LSGGWKQRLALAAALLQEPELLLLD 161
Cdd:PRK13634 97 qlfEETVEKDICFgpmnfgVSE----EDAKQKAREMIELVGLP--EELLARSpfeLSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1422354951 162 EPTAGVDPSARREFWE---ELHRlaARGISVLVSTHYMDEAER-CHKLAYISYGVLLAQGEARDLIR 224
Cdd:PRK13634 171 EPTAGLDPKGRKEMMEmfyKLHK--EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFA 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-49 |
5.75e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 41.23 E-value: 5.75e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1422354951 13 LNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTS 49
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTT 328
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-199 |
6.38e-04 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 40.62 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 18 GDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREikRRVGYMTQRFTYWedLTV 97
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--RGVVFQKDALLPW--LNV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 98 RENLDFVARL--YEVRRRRERVDRMLDELRLGSRAKQLAGSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSARREF 175
Cdd:COG4525 94 LDNVAFGLRLrgVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQM 173
|
170 180
....*....|....*....|....*
gi 1422354951 176 WEELHRLAAR-GISVLVSTHYMDEA 199
Cdd:COG4525 174 QELLLDVWQRtGKGVFLITHSVEEA 198
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-62 |
6.42e-04 |
|
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: 40.43 E-value: 6.42e-04
10 20 30
....*....|....*....|....*....|...
gi 1422354951 30 VRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSG 62
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLG 55
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-218 |
6.68e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 40.45 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 8 IDVHRLNKRFG-----DRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREikRRV 82
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEY--KRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 83 GYMTQRF------TYwEDLTVRENLDFVA--------RLYEVRRRRERVDRMLDELRLG--SRAKQLAGSLSGGwkQRla 146
Cdd:COG1101 80 KYIGRVFqdpmmgTA-PSMTIEENLALAYrrgkrrglRRGLTKKRRELFRELLATLGLGleNRLDTKVGLLSGG--QRqa 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1422354951 147 laaall--qepellllDEPTAGVDPsARREFWEEL-HRLAAR-GISVLVSTHYMDEAerchklayISYG---VLLAQGE 218
Cdd:COG1101 157 lsllmatltkpkllllDEHTAALDP-KTAALVLELtEKIVEEnNLTTLMVTHNMEQA--------LDYGnrlIMMHEGR 226
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
25-108 |
6.96e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.85 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 25 DLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHgtcLGYDITKQSREIKRRVGYMTQRFTYWEDLTVRENLDFV 104
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGN---IYYKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKFW 94
|
....
gi 1422354951 105 ARLY 108
Cdd:PRK13541 95 SEIY 98
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-143 |
7.53e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.76 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 23 VKDLS---MQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDIT----KQSREIKrrVGYMTQRFTYWEDL 95
Cdd:PRK10762 17 VKALSgaaLNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQEAG--IGIIHQELNLIPQL 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 96 TVRENLdFVARLYEVRRRRERVDRMLDEL-----RLGSR--AKQLAGSLSGGWKQ 143
Cdd:PRK10762 95 TIAENI-FLGREFVNRFGRIDWKKMYAEAdkllaRLNLRfsSDKLVGELSIGEQQ 148
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-253 |
8.14e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 40.53 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 23 VKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDIT-----KQSREIKRRVGYM-----TQRFtyw 92
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdKYIRPVRKRIGMVfqfpeSQLF--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 93 EDLTVRE----------NLDFV-ARLYEvrrrrervdrMLDELRLGSRAKQLAG-SLSGGWKQRLALAAALLQEPELLLL 160
Cdd:PRK13646 100 EDTVEREiifgpknfkmNLDEVkNYAHR----------LLMDLGFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 161 DEPTAGVDPSARREFWEELHRLAA-RGISVLVSTHYMDE-AERCHKLAYISYGVLLAQGEARDLIRQ-QALHTWAvsgan 237
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQTdENKTIILVSHDMNEvARYADEVIVMKEGSIVSQTSPKELFKDkKKLADWH----- 244
|
250
....*....|....*.
gi 1422354951 238 lVGLNDRLQGQPGVEQ 253
Cdd:PRK13646 245 -IGLPEIVQLQYDFEQ 259
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-201 |
9.40e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.80 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 24 KDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRRVG-------------------- 83
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvylpedrqssglyldapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 84 -----YMTQRFTYWEDlTVRENldfvarlyevrrrrervdRMLDELR--LG---SRAKQLAGSLSGGWKQRLALAAALLQ 153
Cdd:PRK15439 360 wnvcaLTHNRRGFWIK-PAREN------------------AVLERYRraLNikfNHAEQAARTLSGGNQQKVLIAKCLEA 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1422354951 154 EPELLLLDEPTAGVDPSARREFWEELHRLAARGISVLVSTHYMDEAER 201
Cdd:PRK15439 421 SPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQ 468
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-190 |
1.01e-03 |
|
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: 39.72 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 1 MNAddlLIDVHRLNKRF-----GDR--HVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGH------GTCL 67
Cdd:COG4778 1 MTT---LLEVENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilvrhdGGWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 68 gyDITK-QSREI----KRRVGYMTQrFtywedLTVREN---LDFVA-----RLYEVRRRRERVDRMLDELRLGSRAKQLA 134
Cdd:COG4778 78 --DLAQaSPREIlalrRRTIGYVSQ-F-----LRVIPRvsaLDVVAeplleRGVDREEARARARELLARLNLPERLWDLP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1422354951 135 -GSLSGGWKQRLALAAALLQEPELLLLDEPTAGVDPSARREFWEELHRLAARGISVL 190
Cdd:COG4778 150 pATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-103 |
1.15e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 39.84 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 22 VVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGhgtclgydITKQSreikRRVGYMTQrFTYWEDLTVRENL 101
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG--------KIKHS----GRISFSSQ-FSWIMPGTIKENI 118
|
..
gi 1422354951 102 DF 103
Cdd:cd03291 119 IF 120
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-57 |
1.30e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.09 E-value: 1.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1422354951 1 MNADDLLIDVHRLNKRF----GDRHVVKDLSMQVRRGEIFGFLGPNGSGKT-TSMRMMcGLL 57
Cdd:PRK09473 6 QQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALM-GLL 66
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
7-201 |
1.35e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 39.37 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMM--CGLLTPD---------SGHGTclgYDITKQS 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtitgsivyNGHNI---YSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 76 REIKRRVGYMTQR-----FTYWEDLTVRENLDFV---ARLYEVRRRRERVDRMLDELRlgSRAKQLAGSLSGGWKQRLAL 147
Cdd:PRK14239 82 VDLRKEIGMVFQQpnpfpMSIYENVVYGLRLKGIkdkQVLDEAVEKSLKGASIWDEVK--DRLHDSALGLSGGQQQRVCI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1422354951 148 AAALLQEPELLLLDEPTAGVDPSARREFWEELHRLAARgISVLVSTHYMDEAER 201
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASR 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
17-104 |
1.41e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 17 FGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHgtclgyditkQSREIKRRVGYMTQ-RFTYwEDL 95
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGN----------VSLDPNERLGKLRQdQFAF-EEF 79
|
....*....
gi 1422354951 96 TVrenLDFV 104
Cdd:PRK15064 80 TV---LDTV 85
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-207 |
1.59e-03 |
|
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: 39.78 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 26 LSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGHGTCLGYDITKQSREIKRrvgymtQRFT-----YW--EDLTVR 98
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR------QLFSavfsdFHlfDRLLGL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 99 ENLDFVARLyevrrrrervDRMLDELRLGSRAKQLAG-----SLSGGWKQRLALAAallqepelllldeptAGV------ 167
Cdd:COG4615 425 DGEADPARA----------RELLERLELDHKVSVEDGrfsttDLSQGQRKRLALLV---------------ALLedrpil 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1422354951 168 ---------DPSARREFWEE-LHRLAARGISVLVSTH---YMDEAERCHKLAY 207
Cdd:COG4615 480 vfdewaadqDPEFRRVFYTElLPELKARGKTVIAISHddrYFDLADRVLKMDY 532
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-144 |
1.70e-03 |
|
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: 38.99 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 22 VVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGhgtclgyditkqSREIKRRVGYMTQrfTYW-EDLTVREN 100
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSG------------SVSVPGSIAYVSQ--EPWiQNGTIREN 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1422354951 101 LDFVARLyevrrrrervdrmlDELRLGS--RA-------KQLAG-----------SLSGGWKQR 144
Cdd:cd03250 86 ILFGKPF--------------DEERYEKviKAcalepdlEILPDgdlteigekgiNLSGGQKQR 135
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
22-106 |
2.08e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.83 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 22 VVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPD---SGHGTCLGYditKQSREIKRRV-GYMTQRFTYWEDLTV 97
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGY---RLNEFVPRKTsAYISQNDVHVGVMTV 256
|
....*....
gi 1422354951 98 RENLDFVAR 106
Cdd:PLN03140 257 KETLDFSAR 265
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
7-48 |
2.46e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 38.62 E-value: 2.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTT 48
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKST 42
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-62 |
2.57e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.18 E-value: 2.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1422354951 23 VKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSG 62
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSG 378
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-103 |
3.39e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 39.12 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1422354951 22 VVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGhgtclgyditkqsrEIKR--RVGYMTQrFTYWEDLTVRE 99
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG--------------KIKHsgRISFSPQ-TSWIMPGTIKD 505
|
....
gi 1422354951 100 NLDF 103
Cdd:TIGR01271 506 NIIF 509
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-72 |
3.89e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 38.27 E-value: 3.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1422354951 20 RHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLT-PDSGHGTCLGYDIT 72
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgGGAPRGARVTGDVT 67
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
14-62 |
4.00e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 38.72 E-value: 4.00e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1422354951 14 NKRFGDRH-VVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSG 62
Cdd:PRK13545 30 RSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKG 79
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
7-57 |
4.66e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 38.18 E-value: 4.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1422354951 7 LIDVHRLNKRFGDRHV----VKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLL 57
Cdd:PRK11022 3 LLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLI 57
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
7-69 |
5.89e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 38.23 E-value: 5.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1422354951 7 LIDVHRLNKRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTPDSGH-----GTCLGY 69
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEiglakGIKLGY 379
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-55 |
6.84e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.85 E-value: 6.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1422354951 15 KRFGDRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCG 55
Cdd:NF040905 9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-59 |
7.25e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 37.37 E-value: 7.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1422354951 19 DRHVVKDLSMQVRRGEIFGFLGPNGSGKTTSMRMMCGLLTP 59
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA 55
|
|
|