|
Name |
Accession |
Description |
Interval |
E-value |
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-251 |
8.91e-106 |
|
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: 306.63 E-value: 8.91e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 1 MLFSIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAG-EIQLFGMVPGqrGYSAHHVREH 79
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRG--GEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 80 IGYVSGLLRDRFSAGEIVRDVVLSGIFKSIGLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMN 159
Cdd:COG1119 80 IGLVSPALQLRFPRDETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 160 EPSLLILDEPANGLDFVGREQLMATLSQIRQHfPQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNHTLSQ 239
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAE-GAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSE 238
|
250
....*....|..
gi 505962082 240 LFDIPVALYQHH 251
Cdd:COG1119 239 AFGLPVEVERRD 250
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
14-251 |
2.88e-57 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 182.98 E-value: 2.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMInaydfL-----TAGEIQLFGMvpgqrgySAHHVREHIGYV--SGL 86
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAI-----LgllppTSGTVRLFGK-------PPRRARRRIGYVpqRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 87 LRDRFSAgeIVRDVVLSGIFKSIGLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLIL 166
Cdd:COG1121 86 VDWDFPI--TVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 167 DEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQnQGRIEAVLTNHTLSQLFDIPVA 246
Cdd:COG1121 164 DEPFAGVDAATEEALYELLRELRRE--GKTILVVTHDLGAVREYFDRVLLLNRGLVA-HGPPEEVLTPENLSRAYGGPVA 240
|
....*
gi 505962082 247 LYQHH 251
Cdd:COG1121 241 LLAHG 245
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
10-253 |
1.85e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.84 E-value: 1.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGEcwlVYGL---NGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRgysAHHVREHIGYV--S 84
Cdd:COG1131 8 KRYGDKTALDGVSLTVEPGE---IFGLlgpNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARD---PAEVRRRIGYVpqE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 85 GLLRDRFSAGEIVRdvvlsgIFKsiGLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLL 164
Cdd:COG1131 82 PALYPDLTVRENLR------FFA--RLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 165 ILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAvLTNHTLSQLFdip 244
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAE--GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE-LKARLLEDVF--- 227
|
....*....
gi 505962082 245 VALYQHHGR 253
Cdd:COG1131 228 LELTGEEAR 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
14-257 |
1.02e-46 |
|
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: 155.97 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGmvpgQ--RGYSAHHVREHIGYV--SGLLRD 89
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG----RdlASLSRRELARRIAYVpqEPPAPF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 RFSageiVRDVVLSGIFKSIGLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEP 169
Cdd:COG1120 89 GLT----VRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 170 ANGLDFVGREQLMATLSQIRQHfPQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNHTLSQLFDIPVALYQ 249
Cdd:COG1120 165 TSHLDLAHQLEVLELLRRLARE-RGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEARVIE 243
|
250
....*....|
gi 505962082 250 HH--GRYQIV 257
Cdd:COG1120 244 DPvtGRPLVL 253
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-220 |
4.30e-44 |
|
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: 148.07 E-value: 4.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 13 SGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGmvpgqrgYSAHHVREHIGYV---SGLLRD 89
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-------KPLEKERKRIGYVpqrRSIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 rFSAGeiVRDVVLSGIFKSIGLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEP 169
Cdd:cd03235 83 -FPIS--VRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505962082 170 ANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQG 220
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRRE--GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-237 |
2.92e-41 |
|
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: 141.32 E-value: 2.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRgySAHHVREHIGYVsgllrdrFS- 92
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKK--NLRELRRKVGLV-------FQn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 93 -----AGEIVRDVVlsgIF--KSIGLyeqPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLI 165
Cdd:COG1122 84 pddqlFAPTVEEDV---AFgpENLGL---PREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505962082 166 LDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNHTL 237
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKE--GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-251 |
2.91e-40 |
|
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: 139.22 E-value: 2.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYsahHVREHIGYVSGL--L 87
Cdd:COG4555 9 KKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR---EARRQIGVLPDErgL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 88 RDRFSAGEIVRdvvlsgIFKSigLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILD 167
Cdd:COG4555 86 YDRLTVRENIR------YFAE--LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 168 EPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNHTLSQLFDIPVAL 247
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKE--GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVAL 235
|
....
gi 505962082 248 YQHH 251
Cdd:COG4555 236 IGSE 239
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-215 |
1.45e-39 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 142.85 E-value: 1.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMI-----NAYdfltAGEIQLFGMVPGQrGYSAHHVREHIGYVSGLLRD 89
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpQGY----SNDLTLFGRRRGS-GETIWDIKKHIGYVSSSLHL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 RFSAGEIVRDVVLSGIFKSIGLYEQPTETQVALAREMLALLNMQAFEA-QYFGLLSTGEQQRVLFARALMNEPSLLILDE 168
Cdd:PRK10938 348 DYRVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKRTAdAPFHSLSWGQQRLALIVRALVKHPTLLILDE 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505962082 169 PANGLDFVGReQLMATLSQIRQHFPQTAVIYVSHFIEEVTEDFTHAL 215
Cdd:PRK10938 428 PLQGLDPLNR-QLVRRFVDVLISEGETQLLFVSHHAEDAPACITHRL 473
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
10-222 |
1.19e-38 |
|
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: 132.91 E-value: 1.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGysaHHVREHIGYVSGllrd 89
Cdd:cd03230 8 KRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP---EEVKRRIGYLPE---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 rfsageivrdvvlsgifkSIGLYEQPTetqvalAREMLallnmqafeaqyfgLLSTGEQQRVLFARALMNEPSLLILDEP 169
Cdd:cd03230 81 ------------------EPSLYENLT------VRENL--------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505962082 170 ANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTI 222
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKE--GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-221 |
5.44e-37 |
|
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: 129.51 E-value: 5.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 12 KSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPgqRGYSAHHVREHIGYV-----SGL 86
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL--TKLSLKELRRKVGLVfqnpdDQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 87 LRDRfsageiVRDVVLSGiFKSIGLyeqPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLIL 166
Cdd:cd03225 89 FGPT------VEEEVAFG-LENLGL---PEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 167 DEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGT 221
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAE--GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-221 |
2.75e-34 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 121.20 E-value: 2.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 4 SIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQrgYSAHHVREHIGYV 83
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK--LPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 84 SGllrdrfsageivrdvvlsgifksiglyeqptetqvalaremlallnmqafeaqyfglLSTGEQQRVLFARALMNEPSL 163
Cdd:cd00267 79 PQ---------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505962082 164 LILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGT 221
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE--GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-222 |
1.69e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 120.69 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 3 FSIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVpgQRGYSAHHVREHIGY 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKP--LSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 83 V---SGLLRDRfsageiVRDVvLSGIFKSIGLYEQPTEtqvalAREMLALLNMQA-FEAQYFGLLSTGEQQRVLFARALM 158
Cdd:COG4619 79 VpqePALWGGT------VRDN-LPFPFQLRERKFDRER-----ALELLERLGLPPdILDKPVERLSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505962082 159 NEPSLLILDEPANGLDFVGREQLMATLSQIRQHfPQTAVIYVSHFIEEVTEDFTHALLLKQGTI 222
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLAE-EGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-219 |
2.55e-32 |
|
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: 117.58 E-value: 2.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 1 MLFSIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRgysAHHVREHI 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA---REDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 81 GYVSGL--LRDRFSAGEIVRdvVLSGIFksiglyeqPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALM 158
Cdd:COG4133 78 AYLGHAdgLKPELTVRENLR--FWAALY--------GLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505962082 159 NEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHfiEEVTEDFTHALLLKQ 219
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLAR--GGAVLLTTH--QPLELAAARVLDLGD 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
18-222 |
6.01e-31 |
|
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: 114.12 E-value: 6.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-----MVPGQRgysAHHVREHIGYV--SGLLRDR 90
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdiskLSEKEL---AAFRRRHIGFVfqSFNLLPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 91 FSAGEivrDVVLSGIFKSIglyeqPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPA 170
Cdd:cd03255 97 LTALE---NVELPLLLAGV-----PKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505962082 171 NGLDFVGREQLMATLSQIRQHFpQTAVIYVSHfIEEVTEDFTHALLLKQGTI 222
Cdd:cd03255 169 GNLDSETGKEVMELLRELNKEA-GTTIVVVTH-DPELAEYADRIIELRDGKI 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-226 |
7.50e-30 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 110.22 E-value: 7.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQrgYSAHHVREHIGYVSgllrdrfsa 93
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS--LSPKELARKIAYVP--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 94 geivrdvvlsgifksiglyeqptetQValaremLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGL 173
Cdd:cd03214 80 -------------------------QA------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505962082 174 DFVGREQLMATLSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQG 226
Cdd:cd03214 129 DIAHQIELLELLRRLARER-GKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-222 |
9.62e-29 |
|
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: 109.19 E-value: 9.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 12 KSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGM-VPGQRGYSAHHVREHIGYV--SGLLR 88
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdINKLKGKALRQLRRQIGMIfqQFNLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 89 DRFSAGEivrdVVLSGIFKSI----GLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLL 164
Cdd:cd03256 91 ERLSVLE----NVLSGRLGRRstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505962082 165 ILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGTI 222
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKRINREE-GITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-250 |
1.43e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 109.05 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGmvpgqRGYSAHHVREhigyvsgLLRDR--- 90
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNG-----RPLAAWSPWE-------LARRRavl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 91 ---------FSAGEIVRdvvlsgifksIGLYEQPTETQ--VALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARAL-- 157
Cdd:COG4559 81 pqhsslafpFTVEEVVA----------LGRAPHGSSAAqdRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 158 -----MNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHfieevteDFT-------HALLLKQGTIQNQ 225
Cdd:COG4559 151 lwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR--GGGVVAVLH-------DLNlaaqyadRILLLHQGRLVAQ 221
|
250 260
....*....|....*....|....*
gi 505962082 226 GRIEAVLTNHTLSQLFDIPVALYQH 250
Cdd:COG4559 222 GTPEEVLTDELLERVYGADLRVLAH 246
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
18-227 |
3.09e-28 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 107.44 E-value: 3.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-----MVPGQRgysAHHVREHIGYV---SGLLrD 89
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdissLSEREL---ARLRRRHIGFVfqfFNLL-P 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 RFSAGEivrDVVLSGIFKSIGLYEQPtetqvALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEP 169
Cdd:COG1136 100 ELTALE---NVALPLLLAGVSRKERR-----ERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505962082 170 -ANgLDFVGREQLMATLSQIRQHFPQTAVIyVSHfIEEVTEDFTHALLLKQGTIQNQGR 227
Cdd:COG1136 172 tGN-LDSKTGEEVLELLRELNRELGTTIVM-VTH-DPELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-234 |
6.16e-28 |
|
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: 107.00 E-value: 6.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIqlfgMVPGQ--RGYSAHHVREHIGYV---S 84
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEI----FIDGEdiREQDPVELRRKIGYViqqI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 85 GLLRDRFSAGEIVrdVVLSgifksigLYEQPTETQVALAREMLALLNM--QAFEAQYFGLLSTGEQQRVLFARALMNEPS 162
Cdd:cd03295 85 GLFPHMTVEENIA--LVPK-------LLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505962082 163 LLILDEPANGLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTN 234
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKT-IVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
13-222 |
8.01e-28 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 106.68 E-value: 8.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 13 SGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSA-HHVREHIGYV--SGLLRD 89
Cdd:COG3638 14 GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlRRLRRRIGMIfqQFNLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 RFSageiVRDVVLSG------IFKSI-GLYeqpTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPS 162
Cdd:COG3638 94 RLS----VLTNVLAGrlgrtsTWRSLlGLF---PPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 163 LLILDEPANGLDFVGREQLMATLSQIRQHFPQTAVIyVSHFIEEVTEDFTHALLLKQGTI 222
Cdd:COG3638 167 LILADEPVASLDPKTARQVMDLLRRIAREDGITVVV-NLHQVDLARRYADRIIGLRDGRV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-235 |
9.01e-28 |
|
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: 110.76 E-value: 9.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 11 RKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAY---DFLTAGEIQLFGMVPgqRGYSAHHVREHIGYVSGLL 87
Cdd:COG1123 15 PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDL--LELSEALRGRRIGMVFQDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 88 RDRFSAGEIVRDVVLSgifksIGLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILD 167
Cdd:COG1123 93 MTQLNPVTVGDQIAEA-----LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIAD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505962082 168 EPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNH 235
Cdd:COG1123 168 EPTTALDVTTQAEILDLLRELQRER-GTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-171 |
1.74e-27 |
|
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: 103.11 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPgqRGYSAHHVREHIGYVS--GLLRDRFSAGE 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL--TDDERKSLRKEIGYVFqdPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505962082 96 IVRDVVLSGifksiGLYEQPTETQVALAREMLALLNMQAFEA-QYFGLLSTGEQQRVLFARALMNEPSLLILDEPAN 171
Cdd:pfam00005 79 NLRLGLLLK-----GLSKREKDARAEEALEKLGLGDLADRPVgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
10-226 |
2.93e-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: 107.49 E-value: 2.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-----MVPGQRG-------YSA--HH 75
Cdd:COG3842 13 KRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtgLPPEKRNvgmvfqdYALfpHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 76 -VREHIGYvsGLLRDRFSAGEIVRDVvlsgifksiglyeqptetqvalaREMLALLNMQAFEAQYFGLLSTGEQQRVLFA 154
Cdd:COG3842 93 tVAENVAF--GLRMRGVPKAEIRARV-----------------------AELLELVGLEGLADRYPHQLSGGQQQRVALA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505962082 155 RALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHfieevteDFTHAL-------LLKQGTIQNQG 226
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRLQREL-GITFIYVTH-------DQEEALaladriaVMNDGRIEQVG 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-226 |
5.25e-27 |
|
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: 103.75 E-value: 5.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 5 IQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEI-----QLFGMVPGQRGYSA------ 73
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrDVTGVPPERRNIGMvfqdya 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 74 --HH--VREHIGYvsGLLRDRFSAGEIVRDVvlsgifksiglyeqptetqvalaREMLALLNMQAFEAQYFGLLSTGEQQ 149
Cdd:cd03259 83 lfPHltVAENIAF--GLKLRGVPKAEIRARV-----------------------RELLELVGLEGLLNRYPHELSGGQQQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505962082 150 RVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIrQHFPQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQG 226
Cdd:cd03259 138 RVALARALAREPSLLLLDEPLSALDAKLREELREELKEL-QRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
13-242 |
9.57e-27 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 103.92 E-value: 9.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 13 SGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQ-RGYSAHHVREHIGYVSGL--LRD 89
Cdd:TIGR02315 13 NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlRGKKLRKLRRRIGMIFQHynLIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 RFSAGEivrdVVLSGIFKSI----GLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLI 165
Cdd:TIGR02315 93 RLTVLE----NVLHGRLGYKptwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLIL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505962082 166 LDEPANGLDFVGREQLMATLSQIRQHFPQTAVIYVsHFIEEVTEDFTHALLLKQGTIQNQGRIEAvLTNHTLSQLFD 242
Cdd:TIGR02315 169 ADEPIASLDPKTSKQVMDYLKRINKEDGITVIINL-HQVDLAKKYADRIVGLKAGEIVFDGAPSE-LDDEVLRHIYG 243
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-234 |
2.95e-26 |
|
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: 106.53 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 8 GAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGM-VPGQRGYSAHHVREHIGYV--- 83
Cdd:COG1123 271 PVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdLTKLSRRSLRELRRRVQMVfqd 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 84 -SGLLRDRFSAGEIVRD-VVLSGIFksiglyeqPTETQVALAREMLALLNMQA-FEAQYFGLLSTGEQQRVLFARALMNE 160
Cdd:COG1123 351 pYSSLNPRMTVGDIIAEpLRLHGLL--------SRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALALE 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505962082 161 PSLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTN 234
Cdd:COG1123 423 PKLLILDEPTSALDVSVQAQILNLLRDLQREL-GLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-250 |
4.31e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.54 E-value: 4.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 1 MLFSIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQrgYSAHHVREHI 80
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAD--WSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 81 GyvsgLLRDR------FSageiVRDVVLSGIfksIGLYEQPTETQvALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFA 154
Cdd:PRK13548 79 A----VLPQHsslsfpFT----VEEVVAMGR---APHGLSRAEDD-ALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 155 RALM------NEPSLLILDEPANGLDFVGREQLMATLSQI-RQHfpQTAVIYVSHfieevteDFTHA-------LLLKQG 220
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHER--GLAVIVVLH-------DLNLAaryadriVLLHQG 217
|
250 260 270
....*....|....*....|....*....|
gi 505962082 221 TIQNQGRIEAVLTNHTLSQLFDIPVALYQH 250
Cdd:PRK13548 218 RLVADGTPAEVLTPETLRRVYGADVLVQPH 247
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-221 |
1.59e-25 |
|
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: 98.80 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 9 AKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSAHHVREHIGYVsgllr 88
Cdd:cd03229 7 SKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGMV----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 89 drfsageivrdvvlsgiFKSIGLYEQPTetqvalAREMLALLnmqafeaqyfglLSTGEQQRVLFARALMNEPSLLILDE 168
Cdd:cd03229 82 -----------------FQDFALFPHLT------VLENIALG------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505962082 169 PANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGT 221
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQL-GITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
11-226 |
2.70e-25 |
|
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: 99.50 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 11 RKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLfgmvpgqRGYS----AHHVREHIGYV--S 84
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYI-------NGYSirtdRKAARQSLGYCpqF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 85 GLLRDRFSAGEIVRdvvLSGIFKSIglyeqPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLL 164
Cdd:cd03263 84 DALFDELTVREHLR---FYARLKGL-----PKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505962082 165 ILDEPANGLDFVGREQLMATLSQIRQHfpqTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQG 226
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRKG---RSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-202 |
4.37e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 98.97 E-value: 4.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGE-CWLVyGLNGAGKTTLLNMINAYDFLTAGEIQLFGM-VPGQRGYSAHHVREHIGYV---SGLLR 88
Cdd:COG2884 14 GREALSDVSLEIEKGEfVFLT-GPSGAGKSTLLKLLYGEERPTSGQVLVNGQdLSRLKRREIPYLRRRIGVVfqdFRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 89 DR--------------FSAGEIVRDVvlsgifksiglyeqptetqvalaREMLALLNMQAFEAQYFGLLSTGEQQRVLFA 154
Cdd:COG2884 93 DRtvyenvalplrvtgKSRKEIRRRV-----------------------REVLDLVGLSDKAKALPHELSGGEQQRVAIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505962082 155 RALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSH 202
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR--GTTVLIATH 195
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
11-217 |
4.56e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 99.78 E-value: 4.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 11 RKSGRTLLSDINWQVNEGE--CwLVyGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGysahhvrEHIGYV---SG 85
Cdd:COG1116 20 GGGGVTALDDVSLTVAAGEfvA-LV-GPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-------PDRGVVfqePA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 86 LL--RDrfsageiVRDVVLSGiFKSIGLyeqPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSL 163
Cdd:COG1116 91 LLpwLT-------VLDNVALG-LELRGV---PKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505962082 164 LILDEPANGLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEvtedfthALLL 217
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQETGKT-VLFVTHDVDE-------AVFL 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
11-234 |
4.71e-25 |
|
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: 99.19 E-value: 4.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 11 RKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGM-VPGQRGYSAHHVREHIGYVS---GL 86
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdLTLLSGKELRKARRRIGMIFqhfNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 87 LRDRFSAGEIVRDVVLSGIFKSiglyEQPTEtqvalAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLIL 166
Cdd:cd03258 94 LSSRTVFENVALPLEIAGVPKA----EIEER-----VLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505962082 167 DEPANGLDFVGREQLMATLSQIRQHFPQTAVIyVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTN 234
Cdd:cd03258 165 DEATSALDPETTQSILALLRDINRELGLTIVL-ITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
16-244 |
5.34e-25 |
|
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: 98.70 E-value: 5.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 16 TLLSDINWQVNEGE-CWLVyGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGysahhvrEHIGYV---SGLL--RD 89
Cdd:cd03293 18 TALEDISLSVEEGEfVALV-GPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-------PDRGYVfqqDALLpwLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 rfsageiVRDVVLSGIfKSIGLyeqPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEP 169
Cdd:cd03293 90 -------VLDNVALGL-ELQGV---PKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505962082 170 ANGLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEvtedfthALLLKQgtiqnqgRIeAVLTNH--TLSQLFDIP 244
Cdd:cd03293 159 FSALDALTREQLQEELLDIWRETGKT-VLLVTHDIDE-------AVFLAD-------RV-VVLSARpgRIVAEVEVD 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
33-254 |
1.07e-24 |
|
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: 100.57 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 33 VYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMV---PGQRGYSAHHVREhIGYVsgllrdrFSAGEI-----VRDVVLSG 104
Cdd:TIGR02142 28 IFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdSRKGIFLPPEKRR-IGYV-------FQEARLfphlsVRGNLRYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 105 IFKSiglyeQPTETQVALAReMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMAT 184
Cdd:TIGR02142 100 MKRA-----RPSERRISFER-VIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505962082 185 LSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNHTLSQLFD------IPVALYQHHGRY 254
Cdd:TIGR02142 174 LERLHAEF-GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLARedqgslIEGVVAEHDQHY 248
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
14-220 |
1.14e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 98.62 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMV---PG-QRGYSAHHvrehigyvSGLLRD 89
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegPGaERGVVFQN--------EGLLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 RFSAGEIVRDVVLSGIfksiglyeqPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEP 169
Cdd:PRK11248 85 RNVQDNVAFGLQLAGV---------EKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505962082 170 ANGLDFVGREQLMATLSQIRQhfpQTA--VIYVSHFIEEVTEDFTHALLLKQG 220
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQ---ETGkqVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-222 |
2.01e-24 |
|
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: 96.90 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 4 SIQQGAKRKSGRTLLSDINWQVNEGEcwlVYGL---NGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRgysaHHVREHI 80
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGE---IYGFlgpNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN----IEALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 81 GYV--SGLLRDRFSAGE-IVRDVVLSGIFKSIglyeqptetqvalAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARAL 157
Cdd:cd03268 75 GALieAPGFYPNLTAREnLRLLARLLGIRKKR-------------IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 158 MNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTI 222
Cdd:cd03268 142 LGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ--GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
14-202 |
1.30e-23 |
|
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: 95.88 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGEcwlVYGL---NGAGKTTLLNMINAYDFLTAGEIQLFGmvpgQR--GYSAHHVREHigyvsGLLR 88
Cdd:COG0411 16 GLVAVDDVSLEVERGE---IVGLigpNGAGKTTLFNLITGFYRPTSGRILFDG----RDitGLPPHRIARL-----GIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 89 --------DRFSAGEIV--------RDVVLSGIFKSIGLYEQPTETQvALAREMLALLNMQAFEAQYFGLLSTGEQQRVL 152
Cdd:COG0411 84 tfqnprlfPELTVLENVlvaaharlGRGLLAALLRLPRARREEREAR-ERAEELLERVGLADRADEPAGNLSYGQQRRLE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505962082 153 FARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSH 202
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDER-GITILLIEH 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
11-226 |
1.37e-23 |
|
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: 95.27 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 11 RKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGM-VPGQRGYSAHHVREHIGYV----SG 85
Cdd:cd03257 14 GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdLLKLSRRLRKIRRKEIQMVfqdpMS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 86 LLRDRFSAGEIVRDVVLsgiFKSIGLYEQPTETQVALAREML----ALLNMQAFEaqyfglLSTGEQQRVLFARALMNEP 161
Cdd:cd03257 94 SLNPRMTIGEQIAEPLR---IHGKLSKKEARKEAVLLLLVGVglpeEVLNRYPHE------LSGGQRQRVAIARALALNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 162 SLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQG 226
Cdd:cd03257 165 KLLIADEPTSALDVSVQAQILDLLKKLQEEL-GLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
33-259 |
1.63e-23 |
|
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: 97.48 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 33 VYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMV--PGQRGYS--AHhvREHIGYV--SGLLRDRFSageiVRDVVLSGIF 106
Cdd:COG4148 30 LFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqDSARGIFlpPH--RRRIGYVfqEARLFPHLS----VRGNLLYGRK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 107 KSiglyeQPTETQVALArEMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLS 186
Cdd:COG4148 104 RA-----PRAERRISFD-EVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 187 QIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNHTLSQLFD-------IPVALYQHHGRYQIVKV 259
Cdd:COG4148 178 RLRDEL-DIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGgeeagsvLEATVAAHDPDYGLTRL 256
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-226 |
1.80e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 94.27 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 9 AKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGmvpgqRGYSAHHvREHIGYV---SG 85
Cdd:cd03269 7 TKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-----KPLDIAA-RNRIGYLpeeRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 86 LLRDrfsagEIVRDVVLsgIFKSigLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLI 165
Cdd:cd03269 81 LYPK-----MKVIDQLV--YLAQ--LKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505962082 166 LDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQG 226
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARA--GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-223 |
2.38e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.21 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECW-LVyGLNGAGKTTLLNMINAYDFLTAGEIQLfgmvpgQRGYSahhvrehIGYVSGllR 88
Cdd:COG0488 6 KSFGGRPLLDDVSLSINPGDRIgLV-GRNGAGKSTLLKILAGELEPDSGEVSI------PKGLR-------IGYLPQ--E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 89 DRFSAGEIVRDVVLSGiFKSIG--------LYEQPTETQVALAR-----EMLALLNMQAFEAQY------FGL------- 142
Cdd:COG0488 70 PPLDDDLTVLDTVLDG-DAELRaleaeleeLEAKLAEPDEDLERlaelqEEFEALGGWEAEARAeeilsgLGFpeedldr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 143 ----LSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLsqirQHFPqTAVIYVSH---FIEEVTedfTHAL 215
Cdd:COG0488 149 pvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYP-GTVLVVSHdryFLDRVA---TRIL 220
|
....*...
gi 505962082 216 LLKQGTIQ 223
Cdd:COG0488 221 ELDRGKLT 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
10-226 |
2.43e-23 |
|
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: 94.18 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGecwlVYGL---NGAGKTTLLNMINAYDFLTAGEIQLFGM-VPGQRGYsahhVREHIGYVSG 85
Cdd:cd03264 8 KRYGKKRALDGVSLTLGPG----MYGLlgpNGAGKTTLMRILATLTPPSSGTIRIDGQdVLKQPQK----LRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 86 --LLRDRFSAGEIVRDV-VLSGIFKSiglyeqpteTQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPS 162
Cdd:cd03264 80 efGVYPNFTVREFLDYIaWLKGIPSK---------EVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505962082 163 LLILDEPANGLDFVGREQLMATLSQIRQhfpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQG 226
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGE---DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-231 |
2.80e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.56 E-value: 2.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGEcwlVYGL---NGAGKTTLLNMINayDFL--TAGEIQLFGmvpgqRGYSAHHvREHIGYvs 84
Cdd:COG4152 9 KRFGDKTAVDDVSFTVPKGE---IFGLlgpNGAGKTTTIRIIL--GILapDSGEVLWDG-----EPLDPED-RRRIGY-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 85 gLLRDRfsageivrdvvlsGIFKSIGLYEQptetQVALARemlaLLNMQAFEAQ--------YFGL----------LSTG 146
Cdd:COG4152 76 -LPEER-------------GLYPKMKVGEQ----LVYLAR----LKGLSKAEAKrradewleRLGLgdrankkveeLSKG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 147 EQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQhfPQTAVIYVSHFIEEVtEDF-THALLLKQGTIQNQ 225
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAA--KGTTVIFSSHQMELV-EELcDRIVIINKGRKVLS 210
|
....*.
gi 505962082 226 GRIEAV 231
Cdd:COG4152 211 GSVDEI 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-226 |
4.16e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 95.08 E-value: 4.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGEcWL-VYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRgySAHHVREHIGYVSGLLRDRFsAGEI 96
Cdd:PRK13635 23 LKDVSFSVYEGE-WVaIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEE--TVWDVRRQVGMVFQNPDNQF-VGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 97 VRDVVLSGIfKSIGLyeqPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFV 176
Cdd:PRK13635 99 VQDDVAFGL-ENIGV---PREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505962082 177 GREQLMATLSQIRQHFPQTaVIYVSHFIEEVTEDfTHALLLKQGTIQNQG 226
Cdd:PRK13635 175 GRREVLETVRQLKEQKGIT-VLSITHDLDEAAQA-DRVIVMNKGEILEEG 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
10-231 |
5.39e-23 |
|
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: 93.46 E-value: 5.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-----MVPGQRGYSA---------H- 74
Cdd:cd03300 8 KFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkditnLPPHKRPVNTvfqnyalfpHl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 75 HVREHIGYvsGLLRDRFSAGEIVRDVvlsgifksiglyeqptetqvalaREMLALLNMQAFEAQYFGLLSTGEQQRVLFA 154
Cdd:cd03300 88 TVFENIAF--GLRLKKLPKAEIKERV-----------------------AEALDLVQLEGYANRKPSQLSGGQQQRVAIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505962082 155 RALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEvtedfthALLLKQG-TIQNQGRIEAV 231
Cdd:cd03300 143 RALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGIT-FVFVTHDQEE-------ALTMSDRiAVMNKGKIQQI 212
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-250 |
5.65e-23 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 95.87 E-value: 5.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 4 SIQQGAKRKSGRTLLSDINWQVNEGE--CWLvyGLNGAGKTTLLNMINAYDFLTAGEIQLFG-----MVPGQRGYS---- 72
Cdd:TIGR03265 6 SIDNIRKRFGAFTALKDISLSVKKGEfvCLL--GPSGCGKTTLLRIIAGLERQTAGTIYQGGrditrLPPQKRDYGivfq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 73 ------AHHVREHIGYvsGLLRDRFSAGEIVRDVvlsgifksiglyeqptetqvalaREMLALLNMQAFEAQYFGLLSTG 146
Cdd:TIGR03265 84 syalfpNLTVADNIAY--GLKNRGMGRAEVAERV-----------------------AELLDLVGLPGSERKYPGQLSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 147 EQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTAvIYVSHFIEEvtedfthALLLKQG-TIQNQ 225
Cdd:TIGR03265 139 QQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTT-IMVTHDQEE-------ALSMADRiVVMNH 210
|
250 260
....*....|....*....|....*
gi 505962082 226 GRIEAVLTnhtlsqlfdiPVALYQH 250
Cdd:TIGR03265 211 GVIEQVGT----------PQEIYRH 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-244 |
6.57e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 95.60 E-value: 6.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 1 MLFSIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIqLFGmvpGQRGYSAHHVRE-H 79
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRI-VLN---GRDLFTNLPPRErR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 80 IGYVS-----------------GLLRDRFSAGEIVRDVvlsgifksiglyeqptetqvalaREMLALLNMQAFEAQYFGL 142
Cdd:COG1118 77 VGFVFqhyalfphmtvaeniafGLRVRPPSKAEIRARV-----------------------EELLELVQLEGLADRYPSQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 143 LSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEVTE--DftHALLLkqg 220
Cdd:COG1118 134 LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGT-TVFVTHDQEEALElaD--RVVVM--- 207
|
250 260
....*....|....*....|....
gi 505962082 221 tiqNQGRIEAVltnHTLSQLFDIP 244
Cdd:COG1118 208 ---NQGRIEQV---GTPDEVYDRP 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-226 |
1.44e-22 |
|
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: 91.97 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 33 VYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMV--PGQRGYSAHHVREHIGYV--SGLLRDRFSageiVRDVVLSGIFKs 108
Cdd:cd03297 28 IFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfDSRKKINLPPQQRKIGLVfqQYALFPHLN----VRENLAFGLKR- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 109 iglyEQPTETQVaLAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQI 188
Cdd:cd03297 103 ----KRNREDRI-SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 505962082 189 RQHFPQTaVIYVSHFIEEVTEDFTHALLLKQGTIQNQG 226
Cdd:cd03297 178 KKNLNIP-VIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
10-233 |
1.52e-22 |
|
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: 92.56 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-----MVPGQRGysahHVREHIGYV- 83
Cdd:cd03261 8 KSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisgLSEAELY----RLRRRMGMLf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 84 -SGLLRDRFSAGEIVrdvvlsgifkSIGLYEQ---PTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMN 159
Cdd:cd03261 84 qSGALFDSLTVFENV----------AFPLREHtrlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505962082 160 EPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTAVIyVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLT 233
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIM-VTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
14-224 |
1.59e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMInaydfltAGEIQLF-GMVpgQRGysaHHVRehIGYVSgLLRDRFS 92
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL-------AGELEPDsGTV--KLG---ETVK--IGYFD-QHQEELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 93 AGEIVRDVVLSGifksiglYEQPTETQValaREMLALLNMQAFEAQ-YFGLLSTGEQQRVLFARALMNEPSLLILDEPAN 171
Cdd:COG0488 392 PDKTVLDELRDG-------APGGTEQEV---RGYLGRFLFSGDDAFkPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTN 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505962082 172 GLDFVGREQLMATLsqirQHFPQTaVIYVSH---FIEEVTedfTHALLLKQGTIQN 224
Cdd:COG0488 462 HLDIETLEALEEAL----DDFPGT-VLLVSHdryFLDRVA---TRILEFEDGGVRE 509
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
13-257 |
3.43e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 91.83 E-value: 3.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 13 SGRtlLSDINWQVNEGECWLVYGLNGAGKTTLLNMINaydfltageiqlfGMVPGQ----------RGYSAHHVREHIGY 82
Cdd:COG4138 9 AGR--LGPISAQVNAGELIHLIGPNGAGKSTLLARMA-------------GLLPGQgeillngrplSDWSAAELARHRAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 83 VSGLLRDRFsageivrdvvLSGIFKSIGLYEQPTETQVALAREMLALlnmqafeAQYFGL----------LSTGEQQRVL 152
Cdd:COG4138 74 LSQQQSPPF----------AMPVFQYLALHQPAGASSEAVEQLLAQL-------AEALGLedklsrpltqLSGGEWQRVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 153 FARALMN-------EPSLLILDEPANGLDFVgreQLMATLSQIRQhFPQT--AVIYVSHfieevteDFTHAL-------L 216
Cdd:COG4138 137 LAAVLLQvwptinpEGQLLLLDEPMNSLDVA---QQAALDRLLRE-LCQQgiTVVMSSH-------DLNHTLrhadrvwL 205
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 505962082 217 LKQGTIQNQGRIEAVLTNHTLSQLFDIPVALYQHHGRYQIV 257
Cdd:COG4138 206 LKQGKLVASGETAEVMTPENLSEVFGVKFRRLEVEGHRWLI 246
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-235 |
3.57e-22 |
|
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: 95.22 E-value: 3.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 13 SGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMIN-AYDfLTAGEIQLFGmVPgQRGYSAHHVREHIGYVSgllrDR- 90
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLrFLD-PQSGSITLGG-VD-LRDLDEDDLRRRIAVVP----QRp 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 91 --FSAGeiVRDVVLSGifksiglYEQPTETQValaREMLALLNMQAF-EAQYFGL----------LSTGEQQRVLFARAL 157
Cdd:COG4987 419 hlFDTT--LRENLRLA-------RPDATDEEL---WAALERVGLGDWlAALPDGLdtwlgeggrrLSGGERRRLALARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505962082 158 MNEPSLLILDEPANGLDFVGREQLMATLsqiRQHFPQTAVIYVSHFIEEVtEDFTHALLLKQGTIQNQGRIEAVLTNH 235
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLADL---LEALAGRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
10-234 |
4.38e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 91.74 E-value: 4.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-MVPGQRGYSAH-----HVREHIGYV 83
Cdd:PRK11264 11 KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDiTIDTARSLSQQkglirQLRQHVGFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 84 S---GLLRDRFSAGEIVRD-VVLSGifksiglyeQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMN 159
Cdd:PRK11264 91 FqnfNLFPHRTVLENIIEGpVIVKG---------EPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 160 EPSLLILDEPANGLD--FVGreQLMATLSQIRQHfPQTAVIyVSH---FIEEVTEdftHALLLKQGTIQNQGRIEAVLTN 234
Cdd:PRK11264 162 RPEVILFDEPTSALDpeLVG--EVLNTIRQLAQE-KRTMVI-VTHemsFARDVAD---RAIFMDQGRIVEQGPAKALFAD 234
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
18-205 |
4.95e-22 |
|
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: 90.17 E-value: 4.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG--MVPGQRGYSAHhvREHIGYVSGLLRDRFSAGE 95
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGepLDYSRKGLLER--RQRVGLVFQDPDDQLFAAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 96 IVRDVVLSGIfkSIGLYEQPTETQValaREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDF 175
Cdd:TIGR01166 86 VDQDVAFGPL--NLGLSEAEVERRV---REALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180 190
....*....|....*....|....*....|
gi 505962082 176 VGREQLMATLSQIRQHfpQTAVIYVSHFIE 205
Cdd:TIGR01166 161 AGREQMLAILRRLRAE--GMTVVISTHDVD 188
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-236 |
7.10e-22 |
|
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: 91.02 E-value: 7.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECwlvYGL---NGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSAHhvREHIGYVS-- 84
Cdd:COG1124 13 QGGRRVPVLKDVSLEVAPGES---FGLvgeSGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF--RRRVQMVFqd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 85 --GLLRDRFSAGEIVRDVvlsgiFKSIGLYEQPTEtqvalAREMLALLNM-QAFEAQYFGLLSTGEQQRVLFARALMNEP 161
Cdd:COG1124 88 pyASLHPRHTVDRILAEP-----LRIHGLPDREER-----IAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 162 SLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNHT 236
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREER-GLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
10-210 |
8.75e-22 |
|
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: 87.89 E-value: 8.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQlfgmvpgqrgysaHHVREHIGYvsgllrd 89
Cdd:cd03221 8 KTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-------------WGSTVKIGY------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 rfsageivrdvvlsgifksiglYEQptetqvalaremlallnmqafeaqyfglLSTGEQQRVLFARALMNEPSLLILDEP 169
Cdd:cd03221 68 ----------------------FEQ----------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505962082 170 ANGLDFVGREQLMATLsqirQHFPQTaVIYVSH---FIEEVTED 210
Cdd:cd03221 98 TNHLDLESIEALEEAL----KEYPGT-VILVSHdryFLDQVATK 136
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
12-241 |
2.09e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 90.33 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 12 KSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMvPGQRGYSahhvREHIGYVSGLLRDRF 91
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ-PTRQALQ----KNLVAYVPQSEEVDW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SAGEIVRDVVLSGIFKSIGLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPAN 171
Cdd:PRK15056 92 SFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 172 GLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKqGTIQNQGRIEAVLTNHTLSQLF 241
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDE--GKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLELAF 238
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-234 |
2.30e-21 |
|
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: 90.01 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 11 RKSGRTL-LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIqlfgMVPGQ--RGYSAHHVREhigyvsgLL 87
Cdd:cd03294 32 KKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKV----LIDGQdiAAMSRKELRE-------LR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 88 RDRFSAgeivrdvvlsgIFKSIGLYEQ----------------PTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRV 151
Cdd:cd03294 101 RKKISM-----------VFQSFALLPHrtvlenvafglevqgvPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 152 LFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTaVIYVSHfieevteDFTHAL-------LLKQGTIQN 224
Cdd:cd03294 170 GLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKT-IVFITH-------DLDEALrlgdriaIMKDGRLVQ 241
|
250
....*....|
gi 505962082 225 QGRIEAVLTN 234
Cdd:cd03294 242 VGTPEEILTN 251
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-234 |
3.74e-21 |
|
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: 88.65 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-MVPG-------QRG----------YSAHHVRE- 78
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeDITGlppheiaRLGigrtfqiprlFPELTVLEn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 79 -----HIGYVSGLLRDRFSAGEivrdvvlsgifksiglyeqptETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLF 153
Cdd:cd03219 96 vmvaaQARTGSGLLLARARREE---------------------REARERAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 154 ARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLT 233
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER--GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
.
gi 505962082 234 N 234
Cdd:cd03219 233 N 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
21-235 |
3.81e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 88.66 E-value: 3.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 21 INWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-----MVPGQRGysahhvrehigyVSGLLRDR--FSA 93
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltaLPPAERP------------VSMLFQENnlFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 94 geivrdvvLSgIFKSIGLYEQP----TETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEP 169
Cdd:COG3840 86 --------LT-VAQNIGLGLRPglklTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505962082 170 ANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNH 235
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCRER-GLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
14-247 |
4.27e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.44 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGmvpgqRGYSAHHVREHIGYVSGLLRDRFSA 93
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG-----DDVEALSARAASRRVASVPQDTSLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 94 GEI-VRDVVLSGIFKSIGLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANG 172
Cdd:PRK09536 90 FEFdVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505962082 173 LDfVGREqlMATLSQIRQHFPQ-TAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNHTLSQLFDIPVAL 247
Cdd:PRK09536 170 LD-INHQ--VRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTAV 242
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-174 |
5.10e-21 |
|
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: 88.26 E-value: 5.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 6 QQGAKRKSGrtlLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQL---FGMV------PGQrgysAHHV 76
Cdd:COG4778 18 LQGGKRLPV---LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWVdlaqasPRE----ILAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 77 REH-IGYVSGLLR--DRFSAgeivRDVVLSGifksigLYEQPTETQVAL--AREMLALLNM-----QAFEAQYfgllSTG 146
Cdd:COG4778 91 RRRtIGYVSQFLRviPRVSA----LDVVAEP------LLERGVDREEARarARELLARLNLperlwDLPPATF----SGG 156
|
170 180
....*....|....*....|....*...
gi 505962082 147 EQQRVLFARALMNEPSLLILDEPANGLD 174
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
10-202 |
6.98e-21 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 87.29 E-value: 6.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSAHHV--REHIGYV---S 84
Cdd:TIGR03608 6 KKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKfrREKLGYLfqnF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 85 GLLRDrfsagEIVR---DVVLSGIFKSIGLYEQptetqvaLAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEP 161
Cdd:TIGR03608 86 ALIEN-----ETVEenlDLGLKYKKLSKKEKRE-------KKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505962082 162 SLLILDEPANGLDFVGREQLMATLSQIRQhfPQTAVIYVSH 202
Cdd:TIGR03608 154 PLILADEPTGSLDPKNRDEVLDLLLELND--EGKTIIIVTH 192
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-207 |
7.98e-21 |
|
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: 87.42 E-value: 7.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLfgmvpgqRGYSAHH----VREHIGYVSG--LLRDRF 91
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV-------DGFDVVKepaeARRRLGFVSDstGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SAGEIVRdvvlsgIFKsiGLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPAN 171
Cdd:cd03266 94 TARENLE------YFA--GLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 505962082 172 GLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEV 207
Cdd:cd03266 166 GLDVMATRALREFIRQLRAL--GKCILFSTHIMQEV 199
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
10-233 |
1.24e-20 |
|
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: 87.04 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRgysAHHVREHIGYVSG--LL 87
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRE---PREVRRRIGIVFQdlSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 88 RDRFSAGEivrDVVLSGifksiGLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILD 167
Cdd:cd03265 85 DDELTGWE---NLYIHA-----RLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505962082 168 EPANGLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEVTEdfthalLLKQGTIQNQGRIEAVLT 233
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMT-ILLTTHYMEEAEQ------LCDRVAIIDHGRIIAEGT 215
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
14-220 |
1.72e-20 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 86.53 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGM-VPGQRGYSAHHVREHIGYV---SGLLRD 89
Cdd:TIGR02673 14 GVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEdVNRLRGRQLPLLRRRIGVVfqdFRLLPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 RfsagEIVRDVVLSgiFKSIGLYEQPTETQVALAREMLALLN-MQAFEAQyfglLSTGEQQRVLFARALMNEPSLLILDE 168
Cdd:TIGR02673 94 R----TVYENVALP--LEVRGKKEREIQRRVGAALRQVGLEHkADAFPEQ----LSGGEQQRVAIARAIVNSPPLLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505962082 169 PANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHfIEEVTEDFTHALL-LKQG 220
Cdd:TIGR02673 164 PTGNLDPDLSERILDLLKRLNKR--GTTVIVATH-DLSLVDRVAHRVIiLDDG 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-245 |
2.25e-20 |
|
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: 86.75 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG----------MVPGQRgYSA---HHVREHIGY-V 83
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqitepgpdrMVVFQN-YSLlpwLTVRENIALaV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 84 SGLLRDRfsageivrdvvlsgifksiglyeqPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSL 163
Cdd:TIGR01184 80 DRVLPDL------------------------SKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 164 LILDEPANGLDFVGREQLMATLSQIRQHFPQTAVIyvshfieeVTEDFTHALLLKQgtiqnqgRIeAVLTN---HTLSQL 240
Cdd:TIGR01184 136 LLLDEPFGALDALTRGNLQEELMQIWEEHRVTVLM--------VTHDVDEALLLSD-------RV-VMLTNgpaANIGQI 199
|
....*
gi 505962082 241 FDIPV 245
Cdd:TIGR01184 200 LEVPF 204
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-217 |
2.87e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.84 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMV---PG-QRGYSAHHvrehigyvSGLL--RDrf 91
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgPGaDRGVVFQK--------DALLpwLN-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 sageiVRDVVlsgifkSIGLYEQ--PTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEP 169
Cdd:COG4525 93 -----VLDNV------AFGLRLRgvPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505962082 170 ANGLDFVGREQLMATLSQIRQHfPQTAVIYVSHFIEEvtedfthALLL 217
Cdd:COG4525 162 FGALDALTREQMQELLLDVWQR-TGKGVFLITHSVEE-------ALFL 201
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-234 |
4.57e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.03 E-value: 4.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSAHHVREHIGYVsgllrdrFSAGE-- 95
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLV-------FQYPEyq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 96 -----IVRDVVLSGifKSIGLYEQPTETQVALAREMLAL-----LNMQAFEaqyfglLSTGEQQRVLFARALMNEPSLLI 165
Cdd:PRK13637 96 lfeetIEKDIAFGP--INLGLSEEEIENRVKRAMNIVGLdyedyKDKSPFE------LSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505962082 166 LDEPANGLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTN 234
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKEYNMT-IILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
13-220 |
5.60e-20 |
|
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: 83.97 E-value: 5.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 13 SGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGmVPGqRGYSAHHVREHIGYVSgllrdrfs 92
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG-VDL-RDLDLESLRKNIAYVP-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 93 ageivRDVVL-SGifkSIglyeqptetqvalaREmlallNmqafeaqyfgLLSTGEQQRVLFARALMNEPSLLILDEPAN 171
Cdd:cd03228 83 -----QDPFLfSG---TI--------------RE-----N----------ILSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505962082 172 GLDFVGREQLMATLSQIRQHfpqTAVIYVSHFIEEVtEDFTHALLLKQG 220
Cdd:cd03228 126 ALDPETEALILEALRALAKG---KTVIVIAHRLSTI-RDADRIIVLDDG 170
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-231 |
6.23e-20 |
|
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: 85.47 E-value: 6.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 7 QGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-----MVPGQRGYS--------- 72
Cdd:cd03299 4 ENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnLPPEKRDISyvpqnyalf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 73 AH-HVREHIGYvsGLLRDRFSAGEIVRDVvlsgifksiglyeqptetqvalaREMLALLNMQAFEAQYFGLLSTGEQQRV 151
Cdd:cd03299 84 PHmTVYKNIAY--GLKKRKVDKKEIERKV-----------------------LEIAEMLGIDHLLNRKPETLSGGEQQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 152 LFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHfieevteDFTHALLL-KQGTIQNQGRIEA 230
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEF-GVTVLHVTH-------DFEEAWALaDKVAIMLNGKLIQ 210
|
.
gi 505962082 231 V 231
Cdd:cd03299 211 V 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-206 |
7.13e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.78 E-value: 7.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 4 SIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGM-VPGQrgysAHHVREHIGY 82
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpVPSR----ARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 83 VSGLlrDRFSAGEIVRDVVLsgIF-KSIGLYEQPTETQVALAREmLALLNMQAfEAQyFGLLSTGEQQRVLFARALMNEP 161
Cdd:PRK13537 85 VPQF--DNLDPDFTVRENLL--VFgRYFGLSAAAARALVPPLLE-FAKLENKA-DAK-VGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505962082 162 SLLILDEPANGLDFVGR----EQLMATLSQIRqhfpqtAVIYVSHFIEE 206
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARhlmwERLRSLLARGK------TILLTTHFMEE 200
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-226 |
8.77e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.05 E-value: 8.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 9 AKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-----MVPGQRG----------YSa 73
Cdd:COG3839 10 SKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvtdLPPKDRNiamvfqsyalYP- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 74 hH--VREHIGYvsGLLRDRFSAGEIVRDVvlsgifksiglyeqptetqvalaREMLALLNMQAFEAQYFGLLSTGEQQRV 151
Cdd:COG3839 89 -HmtVYENIAF--PLKLRKVPKAEIDRRV-----------------------REAAELLGLEDLLDRKPKQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 152 LFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTaVIYVSHfieevteDFTHAL-------LLKQGTIQN 224
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTT-TIYVTH-------DQVEAMtladriaVMNDGRIQQ 214
|
..
gi 505962082 225 QG 226
Cdd:COG3839 215 VG 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-234 |
1.45e-19 |
|
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: 84.02 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGM-VPGQrgySAHH-VREHIGYVS-GllRDRFsAG 94
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRdITGL---PPHErARAGIGYVPeG--RRIF-PE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 95 EIVRDVVLsgifksIGLYEQPTETQVALAREMLALL-NMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGL 173
Cdd:cd03224 90 LTVEENLL------LGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505962082 174 DFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTN 234
Cdd:cd03224 164 APKIVEEIFEAIRELRDE--GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-206 |
1.61e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.43 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 2 LFSIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-----MVPGQRG------ 70
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlshVPPYQRPinmmfq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 71 ----YSAHHVREHIGYvsGLLRDRFSAGEIVRDVvlsgifksiglyeqptetqvalaREMLALLNMQAFEAQYFGLLSTG 146
Cdd:PRK11607 99 syalFPHMTVEQNIAF--GLKQDKLPKAEIASRV-----------------------NEMLGLVHMQEFAKRKPHQLSGG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 147 EQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTAVIyVSHFIEE 206
Cdd:PRK11607 154 QRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVM-VTHDQEE 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-233 |
1.68e-19 |
|
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: 84.31 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 1 MLFSIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGmvpgqRGYSAHHVRE-H 79
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG-----EDATDVPVQErN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 80 IGYV---SGLLRDRfsageIVRDVVLSGIfKSIGLYEQPTETQV-ALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFAR 155
Cdd:cd03296 76 VGFVfqhYALFRHM-----TVFDNVAFGL-RVKPRSERPPEAEIrAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505962082 156 ALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTAViYVSHFIEEVTEDFTHALLLkqgtiqNQGRIEAVLT 233
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTV-FVTHDQEEALEVADRVVVM------NKGRIEQVGT 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-233 |
2.70e-19 |
|
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: 83.88 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMInaydfL-----TAGEIQLFGM-VPGQRGYSAHHVREHIGYV 83
Cdd:COG1127 13 KSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLI-----IgllrpDSGEILVDGQdITGLSEKELYELRRRIGML 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 84 --SGLLRDRFSAGEIVrdvvlsgifkSIGLYEQP--TETQV-ALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALM 158
Cdd:COG1127 88 fqGGALFDSLTVFENV----------AFPLREHTdlSEAEIrELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 159 NEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTAVIyVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLT 233
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVV-VTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-259 |
2.74e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.70 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 33 VYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMV-----------PGQRgysahhvreHIGYVsglLRD-RFSAGEIVRDV 100
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclpPEKR---------RIGYV---FQDaRLFPHYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 101 VLSGIfksiglyeqpTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQ 180
Cdd:PRK11144 97 LRYGM----------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 181 LMATLSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNH---------TLSQLFDIPVALyqHH 251
Cdd:PRK11144 167 LLPYLERLAREI-NIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSamrpwlpkeEQSSILKVTVLE--HH 243
|
....*...
gi 505962082 252 GRYQIVKV 259
Cdd:PRK11144 244 PHYAMTAL 251
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-240 |
3.89e-19 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 86.22 E-value: 3.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 5 IQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMInaydfltAGEIQLFGmvpGQRGYSAHH-VREHIGYV 83
Cdd:PRK10938 6 ISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARAL-------AGELPLLS---GERQSQFSHiTRLSFEQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 84 SGLLRDRF--------SAGE-----IVRDVVLSGIFKSiglyeqptetqvALAREMLALLNMQAFEAQYFGLLSTGEQQR 150
Cdd:PRK10938 76 QKLVSDEWqrnntdmlSPGEddtgrTTAEIIQDEVKDP------------ARCEQLAQQFGITALLDRRFKYLSTGETRK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 151 VLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfPQTAVIYVSHFiEEVTEDFTHALLLKQGTIQNQGRIEA 230
Cdd:PRK10938 144 TLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRF-DEIPDFVQFAGVLADCTLAETGEREE 221
|
250
....*....|
gi 505962082 231 VLTNHTLSQL 240
Cdd:PRK10938 222 ILQQALVAQL 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-202 |
4.32e-19 |
|
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: 82.84 E-value: 4.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGM-VPGQRGYSAHHVREHIGYV---SGLLRD 89
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdVSDLRGRAIPYLRRKIGVVfqdFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 RFSAGEIVRDVVLSGifksiglyEQPTETQVALArEMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEP 169
Cdd:cd03292 93 RNVYENVAFALEVTG--------VPPREIRKRVP-AALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190
....*....|....*....|....*....|...
gi 505962082 170 ANGLDFVGREQLMATLSQIrqHFPQTAVIYVSH 202
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKI--NKAGTTVVVATH 194
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-235 |
6.10e-19 |
|
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: 85.58 E-value: 6.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPgqRGYSAHHVREHIGYVSGllRDRFSA 93
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL--SDLDPASWRRQIAWVPQ--NPYLFA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 94 GEIvRDVVLsgifksigLYE-QPTETQVALAremLALLNMQAF-EAQYFGL----------LSTGEQQRVLFARALMNEP 161
Cdd:COG4988 425 GTI-RENLR--------LGRpDASDEELEAA---LEAAGLDEFvAALPDGLdtplgeggrgLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505962082 162 SLLILDEPANGLDFVGREQLMATLSQIRQHfpQTaVIYVSHFIEEVtEDFTHALLLKQGTIQNQGRIEAVLTNH 235
Cdd:COG4988 493 PLLLLDEPTAHLDAETEAEILQALRRLAKG--RT-VILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-223 |
1.97e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 82.09 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGEcWL-VYGLNGAGKTTLLNMINAYDFLTAGEIqlfgMVPGQRgYSAHHV---REHIGYVSGLLRDRFsA 93
Cdd:PRK13650 23 LNDVSFHVKQGE-WLsIIGHNGSGKSTTVRLIDGLLEAESGQI----IIDGDL-LTEENVwdiRHKIGMVFQNPDNQF-V 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 94 GEIVRDVVlsgifkSIGLYEQ--PTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPAN 171
Cdd:PRK13650 96 GATVEDDV------AFGLENKgiPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505962082 172 GLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIEEVTEDfTHALLLKQGTIQ 223
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDY-QMTVISITHDLDEVALS-DRVLVMKNGQVE 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-232 |
2.05e-18 |
|
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: 84.12 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 11 RKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMI-NAYDfLTAGEIqLFGMVPgQRGYSAHHVREHIGYV------ 83
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLlGLYE-PTSGRI-LIDGID-LRQIDPASLRRQIGVVlqdvfl 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 84 -SGLLRDRFSAGEivrdvvlsgifksiglyEQPTETQVALAREMLALLNM-QAFEAQYF-------GLLSTGEQQRVLFA 154
Cdd:COG2274 561 fSGTIRENITLGD-----------------PDATDEEIIEAARLAGLHDFiEALPMGYDtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 155 RALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQhfPQTAVIyVSH---FIEEVTEdfthALLLKQGTIQNQGRIEAV 231
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVII-IAHrlsTIRLADR----IIVLDKGRIVEDGTHEEL 696
|
.
gi 505962082 232 L 232
Cdd:COG2274 697 L 697
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
10-222 |
2.35e-18 |
|
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: 80.65 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSAHHVREHIGYVsgllrd 89
Cdd:cd03262 8 KSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGMV------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 rfsageivrdvvlsgiFKSIGLYE-----------------QPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVL 152
Cdd:cd03262 82 ----------------FQQFNLFPhltvlenitlapikvkgMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505962082 153 FARALMNEPSLLILDEPANGLD--FVGR-EQLMATLSQirqhfPQTAVIYVSH---FIEEVTEdftHALLLKQGTI 222
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDpeLVGEvLDVMKDLAE-----EGMTMVVVTHemgFAREVAD---RVIFMDDGRI 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-208 |
2.80e-18 |
|
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: 80.69 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFL-----TAGEIQLFGMVPGQRGYSAHHVREHIGYV----- 83
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLELRRRVGMVfqkpn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 84 --SGLLRDRFSAGEIVRDVVLSGIFKSIglyEQPTETQVALAREMLALLNMQAfeaqyfglLSTGEQQRVLFARALMNEP 161
Cdd:cd03260 92 pfPGSIYDNVAYGLRLHGIKLKEELDER---VEEALRKAALWDEVKDRLHALG--------LSGGQQQRLCLARALANEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505962082 162 SLLILDEPANGLDFVGR---EQLMATLSQirqhfpQTAVIYVSHFIEEVT 208
Cdd:cd03260 161 EVLLLDEPTSALDPISTakiEELIAELKK------EYTIVIVTHNMQQAA 204
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-207 |
2.92e-18 |
|
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: 79.78 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 13 SGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGmVPGQRGYSAHHVREHIGYVSGllrDRFS 92
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG-KPVTRRSPRDAIRAGIAYVPE---DRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 93 AGeivrdVVLsgifksiglyEQPTETQVALARemlallnmqafeaqyfgLLSTGEQQRVLFARALMNEPSLLILDEPANG 172
Cdd:cd03215 87 EG-----LVL----------DLSVAENIALSS-----------------LLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190
....*....|....*....|....*....|....*
gi 505962082 173 LDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEV 207
Cdd:cd03215 135 VDVGAKAEIYRLIRELADA--GKAVLLISSELDEL 167
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-231 |
3.21e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.82 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 4 SIQQGAKRKS-GRT-LLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGmvpgqRGYSAHHVRE-HI 80
Cdd:PRK10851 2 SIEIANIKKSfGRTqVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG-----TDVSRLHARDrKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 81 GYV---SGLLRDRfsageIVRDVVLSGIfKSIGLYEQPTetQVALAREMLALLNM-------QAFEAQyfglLSTGEQQR 150
Cdd:PRK10851 77 GFVfqhYALFRHM-----TVFDNIAFGL-TVLPRRERPN--AAAIKAKVTQLLEMvqlahlaDRYPAQ----LSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 151 VLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTAViYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEA 230
Cdd:PRK10851 145 VALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSV-FVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQ 223
|
.
gi 505962082 231 V 231
Cdd:PRK10851 224 V 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
10-231 |
4.47e-18 |
|
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: 79.99 E-value: 4.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMV-----PGQRG----------YSAH 74
Cdd:cd03301 8 KRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtdlpPKDRDiamvfqnyalYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 75 HVREHIGYvsGLLRDRFSAGEIVRDVvlsgifksiglyeqptetqvalaREMLALLNMQAFEAQYFGLLSTGEQQRVLFA 154
Cdd:cd03301 88 TVYDNIAF--GLKLRKVPKDEIDERV-----------------------REVAELLQIEHLLDRKPKQLSGGQRQRVALG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505962082 155 RALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHfieevteDFTHALLL-KQGTIQNQGRIEAV 231
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRL-GTTTIYVTH-------DQVEAMTMaDRIAVMNDGQIQQI 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-226 |
4.71e-18 |
|
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: 79.84 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 24 QVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-----MVPGQRGysahhvrehigyVSGLLRDR--FSAGEI 96
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaAPPADRP------------VSMLFQENnlFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 97 VRDVVLsGIFKSIGLYEQPTETQVALAREMlallNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFV 176
Cdd:cd03298 88 EQNVGL-GLSPGLKLTAEDRQAIEVALARV----GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505962082 177 GREQLMATLSQIRQHFPQTaVIYVSHFIEEVTEDFTHALLLKQGTIQNQG 226
Cdd:cd03298 163 LRAEMLDLVLDLHAETKMT-VLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-243 |
5.16e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.80 E-value: 5.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 11 RKS--GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGM-VPGQrgysAHHVREHIGYVSGLl 87
Cdd:PRK13536 48 SKSygDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpVPAR----ARLARARIGVVPQF- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 88 rDRFSAGEIVRDVVLsgIF-KSIGLYEQPTETQVAlaremlALLNMQAFEAQY---FGLLSTGEQQRVLFARALMNEPSL 163
Cdd:PRK13536 123 -DNLDLEFTVRENLL--VFgRYFGMSTREIEAVIP------SLLEFARLESKAdarVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 164 LILDEPANGLDFVGR----EQLMATLSQIRqhfpqtAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNHTLSQ 239
Cdd:PRK13536 194 LILDEPTTGLDPHARhliwERLRSLLARGK------TILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQ 267
|
....
gi 505962082 240 LFDI 243
Cdd:PRK13536 268 VIEI 271
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
15-231 |
5.22e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.22 E-value: 5.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLfG---MVPGQRGYSAHHVREHIGYVSgllrdRF 91
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GervITAGKKNKKLKPLRKKVGIVF-----QF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SAGEIVRDVVLSGI-F--KSIGLYEQPTEtqvALAREMLAL-------LNMQAFEaqyfglLSTGEQQRVLFARALMNEP 161
Cdd:PRK13634 94 PEHQLFEETVEKDIcFgpMNFGVSEEDAK---QKAREMIELvglpeelLARSPFE------LSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 162 SLLILDEPANGLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAV 231
Cdd:PRK13634 165 EVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLT-TVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
14-234 |
7.65e-18 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 80.91 E-value: 7.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGE-CWLVyGLNGAGKTTLLNMINAYDFLTAGEIqlfgMVPGQ--RGYSAHHVREHIGYV---SGLL 87
Cdd:COG1125 14 GTVAVDDLSLTIPAGEfTVLV-GPSGCGKTTTLRMINRLIEPTSGRI----LIDGEdiRDLDPVELRRRIGYViqqIGLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 88 RDRfsageIVRD---VVLsgifksiGLYEQPTETQVALAREMLALLNMQAfeAQYFGL----LSTGEQQRVLFARALMNE 160
Cdd:COG1125 89 PHM-----TVAEniaTVP-------RLLGWDKERIRARVDELLELVGLDP--EEYRDRypheLSGGQQQRVGVARALAAD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 161 PSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEvtedfthALLL-------KQGTIQNQGRIEAVLT 233
Cdd:COG1125 155 PPILLMDEPFGALDPITREQLQDELLRLQRELGKT-IVFVTHDIDE-------ALKLgdriavmREGRIVQYDTPEEILA 226
|
.
gi 505962082 234 N 234
Cdd:COG1125 227 N 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-202 |
8.63e-18 |
|
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: 79.07 E-value: 8.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 12 KSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSAHHVREHIGYVSGLlRDRF 91
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGI-KTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SAGEIVRdvvlsgIFKSIGLYEQPTEtqvALARemlalLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPAN 171
Cdd:cd03231 89 SVLENLR------FWHADHSDEQVEE---ALAR-----VGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|..
gi 505962082 172 GLDFVGREQLMatlSQIRQHFPQ-TAVIYVSH 202
Cdd:cd03231 155 ALDKAGVARFA---EAMAGHCARgGMVVLTTH 183
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-226 |
9.26e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.53 E-value: 9.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 2 LFSIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGM----VPGQR-------- 69
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithVPAENrhvntvfq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 70 GYS--AH-HVREHIGYvsGLLRDRFSAGEIVRDVvlsgifksiglyeqptetqvalaREMLALLNMQAFEAQYFGLLSTG 146
Cdd:PRK09452 94 SYAlfPHmTVFENVAF--GLRMQKTPAAEITPRV-----------------------MEALRMVQLEEFAQRKPHQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 147 EQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEVTEDFTHALLLKQGTIQNQG 226
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGIT-FVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-202 |
1.58e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.39 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 13 SGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMI----NAYDfltaGEIQ-------LFgmVPgQRGYsahhvrehig 81
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwPYGS----GRIArpagarvLF--LP-QRPY---------- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 82 YVSGLLRDrfsageivrdvVLsgifksigLY----EQPTETQValaREMLALLNMQAF------EAQYFGLLSTGEQQRV 151
Cdd:COG4178 437 LPLGTLRE-----------AL--------LYpataEAFSDAEL---REALEAVGLGHLaerldeEADWDQVLSLGEQQRL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505962082 152 LFARALMNEPSLLILDEPANGLDFVGREQLMATLsqiRQHFPQTAVIYVSH 202
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENEAALYQLL---REELPGTTVISVGH 542
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
18-253 |
4.04e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.05 E-value: 4.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMInAYDFLTAGEIQLFGMVPGQrgYSAHHVREHIGYVSgllrdrfsagEIV 97
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARM-AGLLPGSGSIQFAGQPLEA--WSAAELARHRAYLS----------QQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 98 RDVVLSGIFKSIGLYeQPTETQVALAR----EMLALLNMQAFEAQYFGLLSTGEQQRVLFA-------RALMNEPSLLIL 166
Cdd:PRK03695 79 TPPFAMPVFQYLTLH-QPDKTRTEAVAsalnEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 167 DEPANGLDfVGREqlmATLSQIRQHFPQT--AVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNHTLSQLFDIP 244
Cdd:PRK03695 158 DEPMNSLD-VAQQ---AALDRLLSELCQQgiAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVN 233
|
....*....
gi 505962082 245 VALYQHHGR 253
Cdd:PRK03695 234 FRRLDVEGH 242
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-226 |
6.63e-17 |
|
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: 77.37 E-value: 6.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRgySAHHVREhIGYVSGllrdrfSAGEIV 97
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKR--RKKFLRR-IGVVFG------QKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 98 RDV-VLSGIFKSIGLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFV 176
Cdd:cd03267 108 WDLpVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505962082 177 GREQLMATLSQI-RQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQG 226
Cdd:cd03267 188 AQENIRNFLKEYnRER--GTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-206 |
9.26e-17 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 78.30 E-value: 9.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 35 GLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRgysAHHVReHIGYV--SGLLRDRFSAGEIVrdvvlsgifkSIGLY 112
Cdd:TIGR01187 3 GPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV---PPHLR-HINMVfqSYALFPHMTVEENV----------AFGLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 113 EQ--PTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQ 190
Cdd:TIGR01187 69 MRkvPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQE 148
|
170
....*....|....*.
gi 505962082 191 HFPQTaVIYVSHFIEE 206
Cdd:TIGR01187 149 QLGIT-FVFVTHDQEE 163
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-190 |
1.15e-16 |
|
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: 75.67 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 12 KSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYdfLTAGEIQLFGMVPGQRGYsAHHVREHIGYVsglLRDrf 91
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGR--RTGLGVSGEVLINGRPLD-KRSFRKIIGYV---PQD-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 sageivrDVVLsgifksiglyeqPTETqvalAREMLallnmqAFEAQYFGlLSTGEQQRVLFARALMNEPSLLILDEPAN 171
Cdd:cd03213 91 -------DILH------------PTLT----VRETL------MFAAKLRG-LSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170
....*....|....*....
gi 505962082 172 GLDFVGREQLMATLSQIRQ 190
Cdd:cd03213 141 GLDSSSALQVMSLLRRLAD 159
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-234 |
1.35e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.95 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 21 INWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIqlfgMVPGQR--GYSAHHVREHigyvsGLLRDrFSAGEIVR 98
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI----LLRGQHieGLPGHQIARM-----GVVRT-FQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 99 DV-----------------VLSGIFKSIGlYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEP 161
Cdd:PRK11300 94 EMtvienllvaqhqqlktgLFSGLLKTPA-FRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505962082 162 SLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTN 234
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNEH-NVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 244
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-209 |
2.45e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.75 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGEcwlVYGL---NGAGKTTLLNMIN-AYDfLTAGEIQLFGMVpgQRGYSAHHVREH-IGYVS 84
Cdd:COG1129 12 KSFGGVKALDGVSLELRPGE---VHALlgeNGAGKSTLMKILSgVYQ-PDSGEILLDGEP--VRFRSPRDAQAAgIAIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 85 ---GLLRDrFSAGE---IVRDVVLSGIFKSIGLYEQptetqvalAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALM 158
Cdd:COG1129 86 qelNLVPN-LSVAEnifLGREPRRGGLIDWRAMRRR--------ARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505962082 159 NEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTE 209
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQ--GVAIIYISHRLDEVFE 205
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
9-234 |
3.43e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.51 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 9 AKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSAHHVREHIGYV--SGL 86
Cdd:PRK09493 8 SKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVfqQFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 87 LRDRFSAGEIVrdvvlsgIFKSIGLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLIL 166
Cdd:PRK09493 88 LFPHLTALENV-------MFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505962082 167 DEPANGLDFVGREQLMATLSQIRQHfPQTAVIyVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTN 234
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEE-GMTMVI-VTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
11-202 |
7.19e-16 |
|
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: 73.55 E-value: 7.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 11 RKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSAHHVREHIGYVSGlLRDR 90
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPG-LKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 91 FSAGEIVRdvvlsgIFKSIGLYEQPTetqvalAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPA 170
Cdd:TIGR01189 88 LSALENLH------FWAAIHGGAQRT------IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|...
gi 505962082 171 NGLDFVGREQLMAtlsQIRQHFPQT-AVIYVSH 202
Cdd:TIGR01189 156 TALDKAGVALLAG---LLRAHLARGgIVLLTTH 185
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-209 |
7.87e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 72.85 E-value: 7.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGEcwlVYGL---NGAGKTTLLNMINAYDFLTAGEIQLFGMVpgQRGYSAHHVREH-IGYVsg 85
Cdd:cd03216 8 KRFGGVKALDGVSLSVRRGE---VHALlgeNGAGKSTLMKILSGLYKPDSGEILVDGKE--VSFASPRDARRAgIAMV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 86 llrdrfsageivrdvvlsgifksiglyeqptetqvalaremlallnMQafeaqyfglLSTGEQQRVLFARALMNEPSLLI 165
Cdd:cd03216 81 ----------------------------------------------YQ---------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505962082 166 LDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTE 209
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQ--GVAVIFISHRLDEVFE 147
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-226 |
1.05e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.77 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMV--PGQRGYSAHHVREHIGYVSGLLRDRFSAGE 95
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsSTSKQKEIKPVRKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 96 IVRDVVLSGifKSIGLYEQPTETQVALAREMLALlNMQAFEAQYFGLlSTGEQQRVLFARALMNEPSLLILDEPANGLDF 175
Cdd:PRK13643 102 VLKDVAFGP--QNFGIPKEKAEKIAAEKLEMVGL-ADEFWEKSPFEL-SGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505962082 176 VGREQLMATLSQIRQhfPQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQG 226
Cdd:PRK13643 178 KARIEMMQLFESIHQ--SGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-207 |
1.17e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.83 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 13 SGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGmvpgqRGYSAHHVRE----HIGYVSGllr 88
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG-----KPVRIRSPRDairaGIAYVPE--- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 89 DRFSAGEI----VRD-VVLSGI--FKSIGLYEQPTETqvALAREMLALLNMQAF-EAQYFGLLSTGEQQRVLFARALMNE 160
Cdd:COG1129 335 DRKGEGLVldlsIREnITLASLdrLSRGGLLDRRRER--ALAEEYIKRLRIKTPsPEQPVGNLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505962082 161 PSLLILDEPANGLDfVG--RE--QLMATLSQirqhfpQ-TAVIYVSHFIEEV 207
Cdd:COG1129 413 PKVLILDEPTRGID-VGakAEiyRLIRELAA------EgKAVIVISSELPEL 457
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
18-174 |
1.32e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 73.87 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSAHHVREHIGYVsgllrdrfsageiv 97
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVGMV-------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 98 rdvvlsgiFKSIGLYE-----------------QPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNE 160
Cdd:COG1126 83 --------FQQFNLFPhltvlenvtlapikvkkMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170
....*....|....
gi 505962082 161 PSLLILDEPANGLD 174
Cdd:COG1126 155 PKVMLFDEPTSALD 168
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-174 |
1.33e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.98 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 2 LFSIQQGAKRKSGRtlLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG--MVPgQRGYSAhhVREH 79
Cdd:PRK09700 265 VFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdISP-RSPLDA--VKKG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 80 IGYVSGLLRD-----RFSAGE---IVRDVVLSGIFKSIGLYEQPTETQVALAREMLALLNMQAFEaQYFGLLSTGEQQRV 151
Cdd:PRK09700 340 MAYITESRRDngffpNFSIAQnmaISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSVN-QNITELSGGNQQKV 418
|
170 180
....*....|....*....|...
gi 505962082 152 LFARALMNEPSLLILDEPANGLD 174
Cdd:PRK09700 419 LISKWLCCCPEVIIFDEPTRGID 441
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-250 |
2.00e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.67 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 3 FSIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQrgYSAHHVREHIGY 82
Cdd:PRK10575 12 FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLES--WSSKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 83 VSGLLRDrfSAGEIVRDVVLSGIFK---SIGLYEQPTETQValaREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMN 159
Cdd:PRK10575 90 LPQQLPA--AEGMTVRELVAIGRYPwhgALGRFGAADREKV---EEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 160 EPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNHTLSQ 239
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLT-VIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQ 243
|
250
....*....|.
gi 505962082 240 LFDIPVALYQH 250
Cdd:PRK10575 244 IYGIPMGILPH 254
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
13-244 |
2.07e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.07 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 13 SGRTLLSDINWQVNEGECWLVYGLNGAGKTT---LLNMINAYDFLTAGEIQLFGMVPGQRgySAHHVREHIGYVSGLLRD 89
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAK--TVWDIREKVGIVFQNPDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 RFsAGEIVRDVVlsgifkSIGLYEQ--PTETQVALAREMLA---LLNMQAFEAQYfglLSTGEQQRVLFARALMNEPSLL 164
Cdd:PRK13640 96 QF-VGATVGDDV------AFGLENRavPRPEMIKIVRDVLAdvgMLDYIDSEPAN---LSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 165 ILDEPANGLDFVGREQLMATLSQIRQHfPQTAVIYVSHFIEEvTEDFTHALLLKQGTIQNQGRIEAVLTNHTLSQL--FD 242
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKK-NNLTVISITHDIDE-ANMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEigLD 243
|
..
gi 505962082 243 IP 244
Cdd:PRK13640 244 IP 245
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-234 |
2.10e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 74.10 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG--MVPGQRGYSAHHVREHIGYVSgllrdRFSAGE 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITPETGNKNLKKLRKKVSLVF-----QFPEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 96 IVRDVVLSGIF---KSIGLYEQPTETQ-------VALAREMLallNMQAFEaqyfglLSTGEQQRVLFARALMNEPSLLI 165
Cdd:PRK13641 98 LFENTVLKDVEfgpKNFGFSEDEAKEKalkwlkkVGLSEDLI---SKSPFE------LSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505962082 166 LDEPANGLDFVGREQLMatlsQIRQHFpQTA---VIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTN 234
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMM----QLFKDY-QKAghtVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSD 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
16-202 |
2.22e-15 |
|
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: 72.85 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 16 TLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-----MVPGQRgysAHHVREHIGYVsgllrdr 90
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlfaLDEDAR---ARLRARHVGFV------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 91 fsageivrdvvlsgiFKSIGLYeqPTET---QVAL-------------AREMLALLNMQAFEAQYFGLLSTGEQQRVLFA 154
Cdd:COG4181 96 ---------------FQSFQLL--PTLTaleNVMLplelagrrdararARALLERVGLGHRLDHYPAQLSGGEQQRVALA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505962082 155 RALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTAVIyVSH 202
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVL-VTH 205
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-231 |
2.83e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.63 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMV--PGQRGYSAHHVREHIGYVSGLLRDRFSAGE 95
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitSTSKNKDIKQIRKKVGLVFQFPESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 96 IVRDVVLSGifKSIGLYEQPTEtqvALAREMLALLNM--QAFEAQYFGLlSTGEQQRVLFARALMNEPSLLILDEPANGL 173
Cdd:PRK13649 103 VLKDVAFGP--QNFGVSQEEAE---ALAREKLALVGIseSLFEKNPFEL-SGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505962082 174 DFVGREQLMATLSQIrqHFPQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAV 231
Cdd:PRK13649 177 DPKGRKELMTLFKKL--HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-202 |
2.86e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 72.93 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 17 LLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSAH-HVREH-IGYV---SGLLRDrF 91
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaELRNQkLGFIyqfHHLLPD-F 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SAGEIVRDVVLSGIFKsiglyeqPTETQvALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPAN 171
Cdd:PRK11629 103 TALENVAMPLLIGKKK-------PAEIN-SRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190
....*....|....*....|....*....|.
gi 505962082 172 GLDFVGREQLMATLSQIRQHfPQTAVIYVSH 202
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRL-QGTAFLVVTH 204
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-202 |
3.05e-15 |
|
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: 72.24 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQrgYSAHHVREHIGYV-------SGLLRDR 90
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQ--LDPADLRRNIGYVpqdvtlfYGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 91 FSAG-------EIVRDVVLSGIfksiglyeqptetqVALAREMLALLNMQAFEAQYFglLSTGEQQRVLFARALMNEPSL 163
Cdd:cd03245 98 ITLGapladdeRILRAAELAGV--------------TDFVNKHPNGLDLQIGERGRG--LSGGQRQAVALARALLNDPPI 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 505962082 164 LILDEPANGLDFVGREQLMatlSQIRQHFPQTAVIYVSH 202
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLK---ERLRQLLGDKTLIIITH 197
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-241 |
3.36e-15 |
|
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: 72.71 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGmvpgQR--GYSAHH-VREHIGYVSgllRDRfsag 94
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG----EDitGLPPHRiARLGIGYVP---EGR---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 95 eivrdvvlsGIFKS--------IGLYEQPTETQVALARE-MLALL-NMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLL 164
Cdd:COG0410 88 ---------RIFPSltveenllLGAYARRDRAEVRADLErVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 165 ILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYV---SHFIEEVTEdftHALLLKQGTIQNQGRIEAVLTNHTLSQLF 241
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLNRE--GVTILLVeqnARFALEIAD---RAYVLERGRIVLEGTAAELLADPEVREAY 233
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
10-253 |
3.39e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.81 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGM----VPGQRgySAHHV---REHIGY 82
Cdd:COG4604 9 KRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvatTPSRE--LAKRLailRQENHI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 83 VSgllrdRFSageiVRDVVLSGIFKsiglYEQ--PTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNE 160
Cdd:COG4604 87 NS-----RLT----VRELVAFGRFP----YSKgrLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 161 PSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTAVIyVSHFIeevteDFT-----HALLLKQGTIQNQGRIEAVLTNH 235
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVI-VLHDI-----NFAscyadHIVAMKDGRVVAQGTPEEIITPE 227
|
250
....*....|....*...
gi 505962082 236 TLSQLFDIPVALYQHHGR 253
Cdd:COG4604 228 VLSDIYDTDIEVEEIDGK 245
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-222 |
3.98e-15 |
|
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: 71.90 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 12 KSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRgysahHVREHIGYVSGLLRDRF 91
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK-----ERRKSIGYVMQDVDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SaGEIVRDVVLSGIfKSIGLYEQPTETQvalaremLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPAN 171
Cdd:cd03226 85 F-TDSVREELLLGL-KELDAGNEQAETV-------LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505962082 172 GLDFVGREQLmATLsqIRQHFPQ-TAVIYVSHFIEEVTEDFTHALLLKQGTI 222
Cdd:cd03226 156 GLDYKNMERV-GEL--IRELAAQgKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
14-188 |
4.20e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 72.80 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSAHHVREHIGYVSGLLRDRFSA 93
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVGIVFQNPDDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 94 GEIVRDVVLSGIfkSIGLYEQPTETQValaREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGL 173
Cdd:PRK13639 94 PTVEEDVAFGPL--NLGLSKEEVEKRV---KEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170
....*....|....*
gi 505962082 174 DFVGREQLMATLSQI 188
Cdd:PRK13639 169 DPMGASQIMKLLYDL 183
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
18-230 |
5.02e-15 |
|
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: 73.19 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG--MVPGQRGysahhVREHIGYV--SGLLRDRFSA 93
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydVVREPRK-----VRRSIGIVpqYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 94 GEivrDVVLSGifksiGLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGL 173
Cdd:TIGR01188 84 RE---NLEMMG-----RLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505962082 174 DFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEdfthalLLKQGTIQNQGRIEA 230
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEE--GVTILLTTHYMEEADK------LCDRIAIIDHGRIIA 204
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-190 |
5.41e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.22 E-value: 5.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQrGYSAHHVREHIGYV-SGllRDRFSAGEI 96
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD-WQTAKIMREAVAIVpEG--RRVFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 97 VRDVVLSGIFKSIGLYEQPTETQVALaremlaLLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFV 176
Cdd:PRK11614 98 EENLAMGGFFAERDQFQERIKWVYEL------FPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170
....*....|....
gi 505962082 177 GREQLMATLSQIRQ 190
Cdd:PRK11614 172 IIQQIFDTIEQLRE 185
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-202 |
6.09e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 73.99 E-value: 6.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQlfgmVPGQ------RGYSAHHVREHIGYV---SGLLR 88
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYR----VAGQdvatldADALAQLRREHFGFIfqrYHLLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 89 DRFSAGEIVRDVVLSGIfksiglyeqPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDE 168
Cdd:PRK10535 100 HLTAAQNVEVPAVYAGL---------ERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 505962082 169 PANGLDFVGREQLMATLSQIRQ--HfpqtAVIYVSH 202
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQLRDrgH----TVIIVTH 202
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-245 |
6.15e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.53 E-value: 6.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 12 KSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRgySAHHVREHIGYVSGLLRDRF 91
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKE--NIREVRKFVGLVFQNPDDQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SAGEIVRDVVLSGIfkSIGLYEQPTETQVALAREMLALLNMQAFEAQYfglLSTGEQQRVLFARALMNEPSLLILDEPAN 171
Cdd:PRK13652 92 FSPTVEQDIAFGPI--NLGLDEETVAHRVSSALHMLGLEELRDRVPHH---LSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505962082 172 GLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNHTL--SQLFDIPV 245
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLPETYGMT-VIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLlaRVHLDLPS 241
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-188 |
7.55e-15 |
|
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: 71.53 E-value: 7.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINA---YDFLTAGEIQLFGMVPgqrgySAHHVREHIGYVSGLlrDRF 91
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPR-----KPDQFQKCVAYVRQD--DIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SAGEIVRDVVL-SGIFKSIGLYEQPTETQVAlAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPA 170
Cdd:cd03234 93 LPGLTVRETLTyTAILRLPRKSSDAIRKKRV-EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170
....*....|....*...
gi 505962082 171 NGLDFVGREQLMATLSQI 188
Cdd:cd03234 172 SGLDSFTALNLVSTLSQL 189
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
14-232 |
8.98e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.19 E-value: 8.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIqLFGMVPGQrgYSAH---HVREHIGYVSGLLRDR 90
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPID--YSRKglmKLRESVGMVFQDPDNQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 91 FSAGEIVRDVVLSGIfkSIGLYEQPTETQV--ALAREMLALLNMQAFEAqyfglLSTGEQQRVLFARALMNEPSLLILDE 168
Cdd:PRK13636 95 LFSASVYQDVSFGAV--NLKLPEDEVRKRVdnALKRTGIEHLKDKPTHC-----LSFGQKKRVAIAGVLVMEPKVLVLDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505962082 169 PANGLDFVGREQLMATLSQIRQHFPQTAVIyVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVL 232
Cdd:PRK13636 168 PTAGLDPMGVSEIMKLLVEMQKELGLTIII-ATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
18-226 |
1.00e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 71.58 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQL------FGMVPGQRGYSAhhVREHIGYVsgllrdrF 91
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdFSKTPSDKAIRE--LRRNVGMV-------F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SAGEI-----VRDVVLSGIFKSIGLYEQPTETQvalAREMLALLNMQAFeAQYFGL-LSTGEQQRVLFARALMNEPSLLI 165
Cdd:PRK11124 89 QQYNLwphltVQQNLIEAPCRVLGLSKDQALAR---AEKLLERLRLKPY-ADRFPLhLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505962082 166 LDEPANGLDfvgrEQLMATLSQIRQHFPQTAV--IYVSHFIEEVTEDFTHALLLKQGTIQNQG 226
Cdd:PRK11124 165 FDEPTAALD----PEITAQIVSIIRELAETGItqVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-202 |
1.18e-14 |
|
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: 69.94 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSAHhvREHIGYVsgLLRDRFSAG 94
Cdd:cd03246 15 PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL--GDHVGYL--PQDDELFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 95 EIvRDVVLSGifksiglyeqptetqvalaremlallnmqafeaqyfgllstGEQQRVLFARALMNEPSLLILDEPANGLD 174
Cdd:cd03246 91 SI-AENILSG-----------------------------------------GQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180
....*....|....*....|....*...
gi 505962082 175 FVGREQLMATLSQIRQhfPQTAVIYVSH 202
Cdd:cd03246 129 VEGERALNQAIAALKA--AGATRIVIAH 154
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
12-239 |
1.31e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 71.69 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 12 KSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRgySAHHVREHIGYVSGLLRDRF 91
Cdd:PRK13647 15 KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAE--NEKWVRSKVGLVFQDPDDQV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SAGEIVRDVVLSGIfkSIGLYEQPTETQValaREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPAN 171
Cdd:PRK13647 93 FSSTVWDDVAFGPV--NMGLDKDEVERRV---EEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505962082 172 GLDFVGREQLMATLSqiRQHFPQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEaVLTNHTLSQ 239
Cdd:PRK13647 168 YLDPRGQETLMEILD--RLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS-LLTDEDIVE 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-232 |
2.01e-14 |
|
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: 72.47 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 13 SGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMV-----PGQRGysahhvrEHIGYV---- 83
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADlsqwdREELG-------RHIGYLpqdv 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 84 ---SGLLRD---RF---SAGEIVRDVVLSGIFKSIGLYEQPTETQVALARemlallnmqafeaqyfGLLSTGEQQRVLFA 154
Cdd:COG4618 416 elfDGTIAEniaRFgdaDPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGG----------------ARLSGGQRQRIGLA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 155 RALMNEPSLLILDEP-ANgLDFVGREQLMATLSQIRQHfpQTAVIYVSH---FIEEVtedfTHALLLKQGTIQNQGRIEA 230
Cdd:COG4618 480 RALYGDPRLVVLDEPnSN-LDDEGEAALAAAIRALKAR--GATVVVITHrpsLLAAV----DKLLVLRDGRVQAFGPRDE 552
|
..
gi 505962082 231 VL 232
Cdd:COG4618 553 VL 554
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
18-236 |
2.20e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 70.43 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQL------FGMVPGQRgySAHHVREHIGYVsgllrdrF 91
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaghqfdFSQKPSEK--AIRLLRQKVGMV-------F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SAGEI-----VRDVVLSGIFKSIGLyeqPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLIL 166
Cdd:COG4161 89 QQYNLwphltVMENLIEAPCKVLGL---SKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505962082 167 DEPANGLDfvgrEQLMATLSQIRQHFPQTAV--IYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNHT 236
Cdd:COG4161 166 DEPTAALD----PEITAQVVEIIRELSQTGItqVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQPQT 233
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-234 |
2.70e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 71.27 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGEcwLV-Y-GLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRgySAHHVReHIGYVSG----L----- 86
Cdd:COG4586 38 VDDISFTIEPGE--IVgFiGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKR--RKEFAR-RIGVVFGqrsqLwwdlp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 87 LRDRFSageivrdvvlsgIFKSIglYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLIL 166
Cdd:COG4586 113 AIDSFR------------LLKAI--YRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505962082 167 DEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTN 234
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEYNRER-GTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-236 |
2.99e-14 |
|
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: 71.76 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 21 INWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQL------FGMV---PGQRGYSAHHVrehigyvsGLLRDRF 91
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewVDMTkpgPDGRGRAKRYI--------GILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SAgeIVRDVVLSGIFKSIGLyEQPTETQValaREMLALLNMQAFEAQ--------YFGLLSTGEQQRVLFARALMNEPSL 163
Cdd:TIGR03269 375 DL--YPHRTVLDNLTEAIGL-ELPDELAR---MKAVITLKMVGFDEEkaeeildkYPDELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505962082 164 LILDEPANGLDFVGREQLMATLSQIRQHFPQTAVIyVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNHT 236
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREEMEQTFII-VSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEELT 520
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-209 |
3.01e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 70.50 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGySAHHVREHIGYVSGLLRDRFSAGEIV 97
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE-NLWDIRNKAGMVFQNPDNQIVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 98 RDVVlsgiFKSIGLYEQPTETQvALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFVG 177
Cdd:PRK13633 105 EDVA----FGPENLGIPPEEIR-ERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190
....*....|....*....|....*....|..
gi 505962082 178 REQLMATLSQIRQHFPQTaVIYVSHFIEEVTE 209
Cdd:PRK13633 180 RREVVNTIKELNKKYGIT-IILITHYMEEAVE 210
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-220 |
4.08e-14 |
|
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: 69.57 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 11 RKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMI-NAYDfLTAGEIQLFGMvpGQRGYSAHHVREHIGYVSgllrd 89
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIpRFYD-VDSGRILIDGH--DVRDYTLASLRRQIGLVS----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 rfsageivRDVVL-SG-IFKSIgLYEQPTETQ---VALAREMLALLNMQAFEAQYF-------GLLSTGEQQRVLFARAL 157
Cdd:cd03251 83 --------QDVFLfNDtVAENI-AYGRPGATReevEEAARAANAHEFIMELPEGYDtvigergVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505962082 158 MNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIyVSH---FIE-----------EVTEDFTHALLLKQG 220
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMKN--RTTFV-IAHrlsTIEnadrivvledgKIVERGTHEELLAQG 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-226 |
5.30e-14 |
|
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: 69.18 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 12 KSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMvPGqRGYSAHHVREHIGYVsglLRDRF 91
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI-DI-RDISRKSLRSMIGVV---LQDTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 sageivrdvVLSG-IFKSIGL-YEQPTETQVALAREMLAL----------LNMQAFEAQyfGLLSTGEQQRVLFARALMN 159
Cdd:cd03254 88 ---------LFSGtIMENIRLgRPNATDEEVIEAAKEAGAhdfimklpngYDTVLGENG--GNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505962082 160 EPSLLILDEPANGLDFVGREQLMATLSQIRQhfpQTAVIYVSHFIeEVTEDFTHALLLKQGTIQNQG 226
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMK---GRTSIIIAHRL-STIKNADKILVLDDGKIIEEG 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-251 |
8.46e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 8.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMInaydfltageiqlFGMVPGQRGYSAHHVREHIGYVSGLLR-DRFSA 93
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVV-------------LGLVAPDEGVIKRNGKLRIGYVPQKLYlDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 94 GEIVRDVVLSGIFKSiglyeqpTETQVALAREMLALLNMQAFEAqyfglLSTGEQQRVLFARALMNEPSLLILDEPANGL 173
Cdd:PRK09544 84 LTVNRFLRLRPGTKK-------EDILPALKRVQAGHLIDAPMQK-----LSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 174 DFVGREQLMATLSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQgTIQNQGRIEAVLTNHTLSQLFDI----PVALYQ 249
Cdd:PRK09544 152 DVNGQVALYDLIDQLRREL-DCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHPEFISMFGPrgaeQLGIYR 229
|
..
gi 505962082 250 HH 251
Cdd:PRK09544 230 HH 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-222 |
9.23e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.95 E-value: 9.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 7 QGAKRKSG-RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQ-RGYSAHHVREHIGYV- 83
Cdd:PRK10419 16 GGLSGKHQhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRAQRKAFRRDIQMVf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 84 ---SGLLRDRFSAGEIVRDVV--LSGIFKSiglyeqpteTQVALAREMLALLNMQAFEAQYF-GLLSTGEQQRVLFARAL 157
Cdd:PRK10419 96 qdsISAVNPRKTVREIIREPLrhLLSLDKA---------ERLARASEMLRAVDLDDSVLDKRpPQLSGGQLQRVCLARAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505962082 158 MNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIEEVtEDFTH-ALLLKQGTI 222
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQF-GTACLFITHDLRLV-ERFCQrVMVMDNGQI 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-226 |
1.21e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 69.75 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG--------------MVPGQRGYSAH- 74
Cdd:PRK11432 14 KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvthrsiqqrdicMVFQSYALFPHm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 75 HVREHIGYvsGLLRDRFSAGEIVRDVvlsgifksiglyeqptetqvalaREMLALLNMQAFEAQYFGLLSTGEQQRVLFA 154
Cdd:PRK11432 94 SLGENVGY--GLKMLGVPKEERKQRV-----------------------KEALELVDLAGFEDRYVDQISGGQQQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 155 RALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTAvIYVSHfieEVTEDFT---HALLLKQGTIQNQG 226
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITS-LYVTH---DQSEAFAvsdTVIVMNKGKIMQIG 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-222 |
1.24e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.55 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 9 AKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIqLFGMVPgqrgysAHHVREHIgyvsgllR 88
Cdd:PRK11247 19 SKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAP------LAEAREDT-------R 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 89 DRFSAGEI-----VRDVV---LSGIFKsiglyeqptetqvALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNE 160
Cdd:PRK11247 85 LMFQDARLlpwkkVIDNVglgLKGQWR-------------DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 161 PSLLILDEPANGLDFVGR---EQLMATLSQiRQHFpqtAVIYVSHFIEEVTEDFTHALLLKQGTI 222
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRiemQDLIESLWQ-QHGF---TVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-232 |
1.38e-13 |
|
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: 68.03 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMI-NAYDfLTAGEIQlfgmVPGQ--RGYSAHHVREHIGYVSgllrdr 90
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfRFYD-VSSGSIL----IDGQdiREVTLDSLRRAIGVVP------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 91 fsageivRDVVL--SGIFKSIGlYEQP--TETQVALAREMLALLN-MQAFEAQY------FGL-LSTGEQQRVLFARALM 158
Cdd:cd03253 82 -------QDTVLfnDTIGYNIR-YGRPdaTDEEVIEAAKAAQIHDkIMRFPDGYdtivgeRGLkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505962082 159 NEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpqTAVIYVSHFIEEVTeDFTHALLLKQGTIQNQGRIEAVL 232
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKG---RTTIVIAHRLSTIV-NADKIIVLKDGRIVERGTHEELL 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
10-234 |
2.08e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.07 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLfgmvpgqRGYSAHHVREHIGYVS----- 84
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVV-------NGQTINLVRDKDGQLKvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 85 --GLLRDRFS---------AGEIVRDVVLSGIFKSIGLYEQPTETQVALAREMLALlnMQAFEAQYFGLLSTGEQQRVLF 153
Cdd:PRK10619 86 qlRLLRTRLTmvfqhfnlwSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGI--DERAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 154 ARALMNEPSLLILDEPANGLDfvgrEQLMATLSQIRQHFPQ--TAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAV 231
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALD----PELVGEVLRIMQQLAEegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
...
gi 505962082 232 LTN 234
Cdd:PRK10619 240 FGN 242
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-229 |
3.02e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.10 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMinaydfltageiqLFGMVPGQ----------RGYSAHHVREHIGYV 83
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNA-------------LLGFLPYQgslkingielRELDPESWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 84 S-------GLLRDRFSAGEIvrdvvlsgifksiglyeQPTETQVALAremLALLNMQAF-EAQYFGL----------LST 145
Cdd:PRK11174 429 GqnpqlphGTLRDNVLLGNP-----------------DASDEQLQQA---LENAWVSEFlPLLPQGLdtpigdqaagLSV 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 146 GEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIyVSHFIEEvTEDFTHALLLKQGTIQNQ 225
Cdd:PRK11174 489 GQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRR--QTTLM-VTHQLED-LAQWDQIWVMQDGQIVQQ 564
|
....
gi 505962082 226 GRIE 229
Cdd:PRK11174 565 GDYA 568
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-187 |
4.48e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.98 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLfgmvpgqRGYSAHHVREH-------IGYVSGl 86
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLW-------QGEPIRRQRDEyhqdllyLGHQPG- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 87 LRDRFSAGEIVRdvvlsgIFKSIGLYEQPTETQVALARemlalLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLIL 166
Cdd:PRK13538 85 IKTELTALENLR------FYQRLHGPGDDEALWEALAQ-----VGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180
....*....|....*....|.
gi 505962082 167 DEPANGLDFVGREQLMATLSQ 187
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLAQ 174
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-209 |
4.75e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.13 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGEcwlVYGL---NGAGKTTLLNMINAYDFLTAGEIQLFGmVPgQRGYSAHHVREH-IGYVSG--LLRDRF 91
Cdd:COG3845 21 NDDVSLTVRPGE---IHALlgeNGAGKSTLMKILYGLYQPDSGEILIDG-KP-VRIRSPRDAIALgIGMVHQhfMLVPNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SAGEivrDVVLsGIFKSIGLYEQPTEtqvalAREMLallnmQAFEAQYfGL----------LSTGEQQRVLFARALMNEP 161
Cdd:COG3845 96 TVAE---NIVL-GLEPTKGGRLDRKA-----ARARI-----RELSERY-GLdvdpdakvedLSVGEQQRVEILKALYRGA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505962082 162 SLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTE 209
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAE--GKSIIFITHKLREVMA 206
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
10-222 |
5.55e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.04 E-value: 5.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYdfltAGEIQLFGMVPGQR--GYSAHHVREHIGYVSGLL 87
Cdd:PRK13642 15 EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGL----FEEFEGKVKIDGELltAENVWNLRRKIGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 88 RDRFSAGEIVRDVvlsgifkSIGLYEQ--PTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLI 165
Cdd:PRK13642 91 DNQFVGATVEDDV-------AFGMENQgiPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505962082 166 LDEPANGLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEVTEDfTHALLLKQGTI 222
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKYQLT-VLSITHDLDEAASS-DRILVMKAGEI 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-234 |
6.73e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.55 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 11 RKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVpgqrgYSAH---HVREHIGYVS--- 84
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGIT-----ISKEnlkEIRKKIGIIFqnp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 85 ---------------GLLRDRFSAGEIvRDVVLSgifksiglyeqptetqVALAREMLALLNmqaFEAQYfglLSTGEQQ 149
Cdd:PRK13632 93 dnqfigatveddiafGLENKKVPPKKM-KDIIDD----------------LAKKVGMEDYLD---KEPQN---LSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 150 RVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEVTE-DftHALLLKQGTIQNQGRI 228
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKT-LISITHDMDEAILaD--KVIVFSEGKLIAQGKP 226
|
....*.
gi 505962082 229 EAVLTN 234
Cdd:PRK13632 227 KEILNN 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-229 |
9.25e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 67.73 E-value: 9.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 25 VNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEiqlfGMVPGQRGY-SAHHVREHIGYVSgllrdRFSAgeivRDVVLS 103
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGD----ATVAGKSILtNISDVHQNMGYCP-----QFDA----IDDLLT 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 104 GiFKSIGLYEQ----PTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGRE 179
Cdd:TIGR01257 2029 G-REHLYLYARlrgvPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505962082 180 QLMATL-SQIRQhfpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIE 229
Cdd:TIGR01257 2108 MLWNTIvSIIRE---GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQ 2155
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-174 |
1.00e-12 |
|
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: 65.64 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 9 AKRKSGRTLLSDINWQVNEGEcwlVYGL---NGAGKTTLLNMINAYDFLTAGEIQLFG-----MVPGQRGysahhvREHI 80
Cdd:cd03218 7 SKRYGKRKVVNGVSLSVKQGE---IVGLlgpNGAGKTTTFYMIVGLVKPDSGKILLDGqditkLPMHKRA------RLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 81 GYV---SGLLRDRfsageIVRDVVLSgIFKSIGLyeqPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARAL 157
Cdd:cd03218 78 GYLpqeASIFRKL-----TVEENILA-VLEIRGL---SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARAL 148
|
170
....*....|....*..
gi 505962082 158 MNEPSLLILDEPANGLD 174
Cdd:cd03218 149 ATNPKFLLLDEPFAGVD 165
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
35-226 |
1.26e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.80 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 35 GLNGAGKTTLLNMINAYDFLTAGEIQLFG--MVPGQRGYSAhhVREHIGYVSGLLRDRFSAGEIVRDVVLSgiFKSIGLY 112
Cdd:PRK13638 34 GANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLA--LRQQVATVFQDPEQQIFYTDIDSDIAFS--LRNLGVP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 113 EQPTETQValaREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHf 192
Cdd:PRK13638 110 EAEITRRV---DEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ- 185
|
170 180 190
....*....|....*....|....*....|....
gi 505962082 193 pQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQG 226
Cdd:PRK13638 186 -GNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-241 |
1.55e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 65.30 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 9 AKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMInaydfltageiqlFGMVPGQRGySAHHVREHIGYVSGLLR 88
Cdd:PRK10895 10 AKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMV-------------VGIVPRDAG-NIIIDDEDISLLPLHAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 89 DRFSAGEIVRDvvlSGIFKSIGLYEQ-----------PTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARAL 157
Cdd:PRK10895 76 ARRGIGYLPQE---ASIFRRLSVYDNlmavlqirddlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 158 MNEPSLLILDEPANGLDFVGreqlMATLSQIRQHFPQT--AVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNH 235
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPIS----VIDIKRIIEHLRDSglGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
....*.
gi 505962082 236 TLSQLF 241
Cdd:PRK10895 229 HVKRVY 234
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
11-239 |
1.55e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 65.63 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 11 RKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMV--PGQRGYSAHHVREHIGYVSGLLR 88
Cdd:COG4167 22 RRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKleYGDYKYRCKHIRMIFQDPNTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 89 DRFSAGEIvrdvvLSGIFK-SIGLYEQPTETQVALAREMLALLNMQAFeaQYFGLLSTGEQQRVLFARALMNEPSLLILD 167
Cdd:COG4167 102 PRLNIGQI-----LEEPLRlNTDLTAEEREERIFATLRLVGLLPEHAN--FYPHMLSSGQKQRVALARALILQPKIIIAD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505962082 168 EPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTN--HTLSQ 239
Cdd:COG4167 175 EALAALDMSVRSQIINLMLELQEKL-GISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANpqHEVTK 247
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-246 |
1.65e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.39 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQrgYSAHHVREHIGYvsgLLRDRFSAG 94
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQH--YASKEVARRIGL---LAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 95 EI-VRDVVLSGIFKSIGLYEQ-PTETQVALAREMLALlNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANG 172
Cdd:PRK10253 95 DItVQELVARGRYPHQPLFTRwRKEDEEAVTKAMQAT-GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 173 LDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNHTLSQLF-------DIPV 245
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYT-LAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYglrcmiiDDPV 252
|
.
gi 505962082 246 A 246
Cdd:PRK10253 253 A 253
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
7-232 |
2.45e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 64.72 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 7 QGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSA--HH---VREHIg 81
Cdd:COG1134 31 RRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLELGAgfHPeltGRENI- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 82 YVSGLLRDrFSAGEI---VRDVV-LSGIFKSIglyEQPTETqvalaremlallnmqafeaqYfgllSTGEQQRVLFARAL 157
Cdd:COG1134 110 YLNGRLLG-LSRKEIdekFDEIVeFAELGDFI---DQPVKT--------------------Y----SSGMRARLAFAVAT 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505962082 158 MNEPSLLILDEpanGLdFVG----REQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVL 232
Cdd:COG1134 162 AVDPDILLVDE---VL-AVGdaafQKKCLARIRELRES--GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-202 |
3.46e-12 |
|
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: 65.84 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMI-NAYDFLTaGEIQLFGMVPGQrgYSAHHVREHIGYV-------SGLLRD 89
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLaGLLDPLQ-GEVTLDGVPVSS--LDQDEVRRRVSVCaqdahlfDTTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 --RFSAGEiVRDVVLSGIFKSIGLYEQPTETQVALAREMLAllnMQAFeaqyfglLSTGEQQRVLFARALMNEPSLLILD 167
Cdd:TIGR02868 428 nlRLARPD-ATDEELWAALERVGLADWLRALPDGLDTVLGE---GGAR-------LSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|....*
gi 505962082 168 EPANGLDFVGREQLMATLsqiRQHFPQTAVIYVSH 202
Cdd:TIGR02868 497 EPTEHLDAETADELLEDL---LAALSGRTVVLITH 528
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-233 |
4.62e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.50 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 3 FSIQQGAKRK--SGRTLLSDINWQVNEGECWLVYGLNGAGKTT----LLNMINAydfltAGEIQLFGMVPGQRGYSAH-H 75
Cdd:PRK15134 285 FPIRKGILKRtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQLlP 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 76 VREHIGYV----SGLLRDRFSAGEIVRDvvlsgifksiGL-YEQPTETqvALAREMLALLNMQ------AFEAQYFGLLS 144
Cdd:PRK15134 360 VRHRIQVVfqdpNSSLNPRLNVLQIIEE----------GLrVHQPTLS--AAQREQQVIAVMEevgldpETRHRYPAEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 145 TGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQN 224
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKH-QLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
....*....
gi 505962082 225 QGRIEAVLT 233
Cdd:PRK15134 507 QGDCERVFA 515
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
14-202 |
5.09e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.05 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLS-DINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-----MVPGQRG----------YSAHHVR 77
Cdd:PRK11000 14 GDVVISkDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndVPPAERGvgmvfqsyalYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 78 EHIGYvsGLLRDRFSAGEIVRDVvlsgifksiglyeqpteTQVALAREMLALLNMQAFEaqyfglLSTGEQQRVLFARAL 157
Cdd:PRK11000 94 ENMSF--GLKLAGAKKEEINQRV-----------------NQVAEVLQLAHLLDRKPKA------LSGGQRQRVAIGRTL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505962082 158 MNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTaVIYVSH 202
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRT-MIYVTH 192
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-236 |
5.38e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.45 E-value: 5.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 24 QVNEGECWLVYGLNGAGKTTLLNMINAydFLTA--GEIQLFG-----MVPGQRGysahhvrehigyVSGLLRDR--FSAG 94
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAG--FLTPasGSLTLNGqdhttTPPSRRP------------VSMLFQENnlFSHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 95 EIVRDVVLsGIFKSIGLYEQPTETQVALAREMLALLNMQAFEAQyfglLSTGEQQRVLFARALMNEPSLLILDEPANGLD 174
Cdd:PRK10771 87 TVAQNIGL-GLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQ----LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505962082 175 FVGREQLMATLSQI-RQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNHT 236
Cdd:PRK10771 162 PALRQEMLTLVSQVcQER--QLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-174 |
8.57e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.97 E-value: 8.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGM-VPGQRGYSAHHVREHIGYV---SGLLRD 89
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdITRLKNREVPFLRRQIGMIfqdHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 RFSAGEIVRDVVLSGIfksiglYEQPTETQVALAREMLALLNmqafEAQYFGL-LSTGEQQRVLFARALMNEPSLLILDE 168
Cdd:PRK10908 94 RTVYDNVAIPLIIAGA------SGDDIRRRVSAALDKVGLLD----KAKNFPIqLSGGEQQRVGIARAVVNKPAVLLADE 163
|
....*.
gi 505962082 169 PANGLD 174
Cdd:PRK10908 164 PTGNLD 169
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
18-222 |
9.64e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.49 E-value: 9.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAY---DFLTAGEIQLFGMVPGQRGYSAHHVRE---HIGYVSGL--LRD 89
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIRKsraNTGYIFQQfnLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 RFSageiVRDVVLSGIFKSIGLYE------QPTETQVALarEMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSL 163
Cdd:PRK09984 100 RLS----VLENVLIGALGSTPFWRtcfswfTREQKQRAL--QALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505962082 164 LILDEPANGLDFVGREQLMATLSQIRQHFPQTAVIYVsHFIEEVTEDFTHALLLKQGTI 222
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGITVVVTL-HQVDYALRYCERIVALRQGHV 231
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-202 |
1.03e-11 |
|
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: 63.53 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGEcwlVYGL---NGAGKTTLLNMI------NAYdflTAGEIqLFGmvpGQ--RGYSAHHVRE----HIGY 82
Cdd:COG0444 21 VDGVSFDVRRGE---TLGLvgeSGSGKSTLARAIlgllppPGI---TSGEI-LFD---GEdlLKLSEKELRKirgrEIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 83 V------SglLRDRFSAGEIVRDVVLsgIFKSIglyeqpTETQV-ALAREMLALLNMQAFEA---QYFGLLSTGEQQRVL 152
Cdd:COG0444 91 IfqdpmtS--LNPVMTVGDQIAEPLR--IHGGL------SKAEArERAIELLERVGLPDPERrldRYPHELSGGMRQRVM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505962082 153 FARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSH 202
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQREL-GLAILFITH 209
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-243 |
1.05e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.72 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 16 TLLSDINWQVNEGECWLVYGLNGAGKTTLLN-----MINAYDFLTAGEIqlfgmvpgqrgYSAHHVREHIGYVSGLLRDR 90
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDI-----------YIGDKKNNHELITNPYSKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 91 FSAGEIVRDVVLSGIFKSIGLYEQPTETQ-----VAL------AREMLAL-LNMQAFEAQY-----FGLlSTGEQQRVLF 153
Cdd:PRK13631 109 KNFKELRRRVSMVFQFPEYQLFKDTIEKDimfgpVALgvkkseAKKLAKFyLNKMGLDDSYlerspFGL-SGGQKRRVAI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 154 ARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLT 233
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN--NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFT 265
|
250
....*....|
gi 505962082 234 NHTLSQLFDI 243
Cdd:PRK13631 266 DQHIINSTSI 275
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
11-222 |
1.05e-11 |
|
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: 62.87 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 11 RKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQrgYSAHHVREHIGYVSGllRDR 90
Cdd:cd03248 23 TRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ--YEHKYLHSKVSLVGQ--EPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 91 FSAGEIVRDVvlsgifkSIGLYEQPTETQVALAREMLALLNMQAFEAQYF-------GLLSTGEQQRVLFARALMNEPSL 163
Cdd:cd03248 99 LFARSLQDNI-------AYGLQSCSFECVKEAAQKAHAHSFISELASGYDtevgekgSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505962082 164 LILDEPANGLDFVGREQLMATLSQIRQhfpQTAVIYVSHFIEEVtEDFTHALLLKQGTI 222
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPE---RRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-215 |
1.15e-11 |
|
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: 64.19 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 9 AKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVpgqrgysahhvreHIGYVsGLLR 88
Cdd:TIGR03719 329 TKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV-------------KLAYV-DQSR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 89 DRFSAGEIVRDVVLSG--IFKsIGLYEQPTetqvalaREMLALLNMQAFEAQ-YFGLLSTGEQQRVLFARALMNEPSLLI 165
Cdd:TIGR03719 395 DALDPNKTVWEEISGGldIIK-LGKREIPS-------RAYVGRFNFKGSDQQkKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505962082 166 LDEPANGLDFvgrEQLMAtLSQIRQHFPQTAVIyVSH---FIEEVTedfTHAL 215
Cdd:TIGR03719 467 LDEPTNDLDV---ETLRA-LEEALLNFAGCAVV-ISHdrwFLDRIA---THIL 511
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
13-202 |
1.45e-11 |
|
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: 61.02 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 13 SGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINaydfltageiqlfGMVPGQRGYSAHHVREHIGYVSgllrdrfs 92
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALA-------------GLWPWGSGRIGMPEGEDLLFLP-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 93 ageivrdvvlsgifksiglyEQPTETQVALaREMLALLNMQAfeaqyfglLSTGEQQRVLFARALMNEPSLLILDEPANG 172
Cdd:cd03223 71 --------------------QRPYLPLGTL-REQLIYPWDDV--------LSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180 190
....*....|....*....|....*....|
gi 505962082 173 LDFvgrEQLMATLSQIRQHFpqTAVIYVSH 202
Cdd:cd03223 122 LDE---ESEDRLYQLLKELG--ITVISVGH 146
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-226 |
1.48e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.85 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIqLFGMVPgqrgYSAHH---VREHIGYVSGLLRDRFsAG 94
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQA----ITDDNfekLRKHIGIVFQNPDNQF-VG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 95 EIVR-DVvlsgifkSIGLYEQ--PTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPAN 171
Cdd:PRK13648 99 SIVKyDV-------AFGLENHavPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 172 GLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEVTEDfTHALLLKQGTIQNQG 226
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNIT-IISITHDLSEAMEA-DHVIVMNKGTVYKEG 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
18-241 |
1.58e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 63.17 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGEcwlVY---GLNGAGKTTLLNMINAYDFLTAGEIQLFGM-VPGQRGYSAHHVREHIGYV---SGLLRDR 90
Cdd:COG1135 21 LDDVSLTIEKGE---IFgiiGYSGAGKSTLIRCINLLERPTSGSVLVDGVdLTALSERELRAARRKIGMIfqhFNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 91 FSAGEIVRDVVLSGIfksiglyeqPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPA 170
Cdd:COG1135 98 TVAENVALPLEIAGV---------PKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505962082 171 NGLDFVGREQLMATLSQIRQHFPQTAVIyVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTN--HTLSQLF 241
Cdd:COG1135 169 SALDPETTRSILDLLKDINRELGLTIVL-ITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANpqSELTRRF 240
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
9-174 |
1.65e-11 |
|
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: 62.29 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 9 AKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLfgmvpgqRGYSAHHVREHIgyvsgllR 88
Cdd:TIGR04406 8 IKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILI-------DGQDITHLPMHE-------R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 89 DRFSAGEIVRDvvlSGIFKSIGLYEQ-----------PTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARAL 157
Cdd:TIGR04406 74 ARLGIGYLPQE---ASIFRKLTVEENimavleirkdlDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARAL 150
|
170
....*....|....*..
gi 505962082 158 MNEPSLLILDEPANGLD 174
Cdd:TIGR04406 151 ATNPKFILLDEPFAGVD 167
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-220 |
1.69e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.75 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMInaydfltAGEIQ---LFGMVPGQRGYSAHHVREHIGYVS--GLLRD 89
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQgnnFTGTILANNRKPTKQILKRTGFVTqdDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 RFSAGEIVRDVVLSGIFKSIGlyeqpTETQVALAREMLALLNMQAFEAQYFGL-----LSTGEQQRVLFARALMNEPSLL 164
Cdd:PLN03211 154 HLTVRETLVFCSLLRLPKSLT-----KQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLL 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505962082 165 ILDEPANGLDFVGREQLMATLSQIRQHfPQTAVIYVSHFIEEVTEDFTHALLLKQG 220
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPSSRVYQMFDSVLVLSEG 283
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-220 |
2.27e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 63.26 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGE-CWLVyGLNGAGKTTLLNMIN-AYDfLTAGEIQLFGmVPgQRGYSAHHVREHIGYV-------S 84
Cdd:COG1132 352 DRPVLKDISLTIPPGEtVALV-GPSGSGKSTLVNLLLrFYD-PTSGRILIDG-VD-IRDLTLESLRRQIGVVpqdtflfS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 85 GLLRD--RFSAGEIVRDVVLSGIfksiglyeqptetQVALAREMLallnmQAFEAQYF-------GLLSTGEQQRVLFAR 155
Cdd:COG1132 428 GTIREniRYGRPDATDEEVEEAA-------------KAAQAHEFI-----EALPDGYDtvvgergVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505962082 156 ALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpqTAVIYVSH------------FIE--EVTEDFTHALLLKQG 220
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMKG---RTTIVIAHrlstirnadrilVLDdgRIVEQGTHEELLARG 565
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-249 |
2.57e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 62.31 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGySAHHVREHIGYVSGLLRDRFSA 93
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS-KLQGIRKLVGIVFQNPETQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 94 GEIVRDVVlsgiFKSIGLYEQPTETQVALAREmLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGL 173
Cdd:PRK13644 93 RTVEEDLA----FGPENLCLPPIEIRKRVDRA-LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505962082 174 DfvgREQLMATLSQIRQ-HFPQTAVIYVSHFIEEVtEDFTHALLLKQGTIQNQGRIEAVLTNHTLSQLFDIPVALYQ 249
Cdd:PRK13644 168 D---PDSGIAVLERIKKlHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPSLIE 240
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-209 |
2.70e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINA-YDFLT-AGEIqLFGMVPGQrgysAHHVR--EHIG---- 81
Cdd:PRK13549 13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYPHGTyEGEI-IFEGEELQ----ASNIRdtERAGiaii 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 82 -----YVSGL--LRDRFSAGEIVRdvvlSGIFKSIGLYEQptetqvalAREMLALLNMQAFEAQYFGLLSTGEQQRVLFA 154
Cdd:PRK13549 88 hqelaLVKELsvLENIFLGNEITP----GGIMDYDAMYLR--------AQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 155 RALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTE 209
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH--GIACIYISHKLNEVKA 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-235 |
5.20e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 62.15 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMIN-AYDfLTAGEIQLFGmVPGQRgYSAHHVREHIGYV-------SGLLRD 89
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWD-PQQGEILLNG-QPIAD-YSEAALRQAISVVsqrvhlfSATLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 RFS-AGEIVRDVVLSGIFKSIGLyEQPTETQVALAremlallnmqafeaQYFG----LLSTGEQQRVLFARALMNEPSLL 164
Cdd:PRK11160 433 NLLlAAPNASDEALIEVLQQVGL-EKLLEDDKGLN--------------AWLGeggrQLSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505962082 165 ILDEPANGLDFVgREQLMatLSQIRQHFPQTAVIYVSHFIEEVtEDFTHALLLKQGTIQNQGRIEAVLTNH 235
Cdd:PRK11160 498 LLDEPTEGLDAE-TERQI--LELLAEHAQNKTVLMITHRLTGL-EQFDRICVMDNGQIIEQGTHQELLAQQ 564
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-202 |
5.53e-11 |
|
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: 62.30 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGmVPgQRGYSAHHVREHIGYVS---------- 84
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG-VP-LADADADSWRDQIAWVPqhpflfagti 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 85 ----GLLRDRFSAGEIVRDVVLSGIFKSIGLYEQPTETQVALAREMLallnmqafeaqyfgllSTGEQQRVLFARALMNE 160
Cdd:TIGR02857 413 aeniRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGL----------------SGGQAQRLALARAFLRD 476
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505962082 161 PSLLILDEPANGLDfVGREQLMatLSQIRQHFPQTAVIYVSH 202
Cdd:TIGR02857 477 APLLLLDEPTAHLD-AETEAEV--LEALRALAQGRTVLLVTH 515
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
12-234 |
7.21e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.59 E-value: 7.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 12 KSGRTL-LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQrgYSAHHVREHIGYVSGLLRDR 90
Cdd:PRK10070 37 KTGLSLgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAK--ISDAELREVRRKKIAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 91 FSAgeIVRDVVLSGIFKSIGLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPA 170
Cdd:PRK10070 115 FAL--MPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505962082 171 NGLDFVGREQLMATLSQIrQHFPQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTN 234
Cdd:PRK10070 193 SALDPLIRTEMQDELVKL-QAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-234 |
8.61e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.87 E-value: 8.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFgmvpgqrgYSAHHVREHIGYVSGLLRDRFSAGEIV 97
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWI--------FKDEKNKKKTKEKEKVLEKLVIQKTRF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 98 RDV-VLSGIFKSIG---------LYEQPTETQVA---------------LAREMLAL--LNMQAFEAQYFGLlSTGEQQR 150
Cdd:PRK13651 95 KKIkKIKEIRRRVGvvfqfaeyqLFEQTIEKDIIfgpvsmgvskeeakkRAAKYIELvgLDESYLQRSPFEL-SGGQKRR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 151 VLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIrqHFPQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEA 230
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL--NKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYD 251
|
....
gi 505962082 231 VLTN 234
Cdd:PRK13651 252 ILSD 255
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-209 |
9.44e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.85 E-value: 9.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 12 KSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMinaydFL----TAGEIQLFGmvpgqrgysahhvrehIGYVSGLL 87
Cdd:TIGR01271 1229 EAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSA-----LLrllsTEGEIQIDG----------------VSWNSVTL 1287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 88 RD-RFSAGEIVRDV-VLSGIF-KSIGLYEQPTETQVALAREMLAL----------LNMQAFEAQYfgLLSTGEQQRVLFA 154
Cdd:TIGR01271 1288 QTwRKAFGVIPQKVfIFSGTFrKNLDPYEQWSDEEIWKVAEEVGLksvieqfpdkLDFVLVDGGY--VLSNGHKQLMCLA 1365
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 155 RALMNEPSLLILDEPANGLDFVGREQLMATLsqiRQHFPQTAVIYVSHFIEEVTE 209
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKTL---KQSFSNCTVILSEHRVEALLE 1417
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-231 |
1.03e-10 |
|
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: 61.36 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFL--TAGEIqLFGM----------VPGQRGYS--------- 72
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRI-IYHValcekcgyveRPSKVGEPcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 73 ---------AHHVREHIGYVSGLLRDRFSA--GEivrDVVLSGIFKSIGLYEQPTETQVALAREMLALLNMQAFEAQYFG 141
Cdd:TIGR03269 91 peevdfwnlSDKLRRRIRKRIAIMLQRTFAlyGD---DTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 142 LLSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTAVIyVSHFIEEVTEDFTHALLLKQGT 221
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVL-TSHWPEVIEDLSDKAIWLENGE 246
|
250
....*....|
gi 505962082 222 IQNQGRIEAV 231
Cdd:TIGR03269 247 IKEEGTPDEV 256
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-239 |
1.84e-10 |
|
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: 60.61 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMI-NAYDFLTAGEIQLFGMVPGQRGySAHHVREHIGYVSgllRDRFSA 93
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRN-PAQAIRAGIAMVP---EDRKRH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 94 GeIV------RDVVLSGIFKSIGLYEQPTETQVALAREMLALLNMQAFEAQY-FGLLSTGEQQRVLFARALMNEPSLLIL 166
Cdd:TIGR02633 349 G-IVpilgvgKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLpIGRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505962082 167 DEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLkqgtiqNQGRIEAVLTNHTLSQ 239
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQE--GVAIIVVSSELAEVLGLSDRVLVI------GEGKLKGDFVNHALTQ 492
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-226 |
2.13e-10 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 59.04 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNminaydfltageiQLFGMVPGQRGysahhvreHIgYVSGL---------LR 88
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLL-------------ALFRLVELSSG--------SI-LIDGVdiskiglhdLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 89 DRFSAgeIVRDVVL-SG-IFKSIGLYEQPTETQVALAREMLALLnmQAFEAQYFGL----------LSTGEQQRVLFARA 156
Cdd:cd03244 78 SRISI--IPQDPVLfSGtIRSNLDPFGEYSDEELWQALERVGLK--EFVESLPGGLdtvveeggenLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 157 LMNEPSLLILDEPANGLDFVGREQLMATlsqIRQHFPQTAVIYVSHFIEEVTeDFTHALLLKQGTIQNQG 226
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKT---IREAFKDCTVLTIAHRLDTII-DSDRILVLDKGRVVEFD 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-226 |
2.26e-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: 58.09 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 13 SGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMI-NAYDFLTaGEIQLFGmvpgqrgysahhvrEHIGYVSGLLRDRF 91
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLtGDLKPQQ-GEITLDG--------------VPVSDLEKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SageivrdvVLSgifKSIGLYEqpTETQVALAREmlallnmqafeaqyfglLSTGEQQRVLFARALMNEPSLLILDEPAN 171
Cdd:cd03247 78 S--------VLN---QRPYLFD--TTLRNNLGRR-----------------FSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 172 GLDFVGREQLmatLSQIRQHFPQTAVIYVSHFIEEVtEDFTHALLLKQGTIQNQG 226
Cdd:cd03247 128 GLDPITERQL---LSLIFEVLKDKTLIWITHHLTGI-EHMDKILFLENGKIIMQG 178
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
12-247 |
3.04e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.07 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 12 KSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMInAYDFLTA---------GEIQLFG----MVPGQRGYSAHHVRE 78
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKAL-AGDLTGGgaprgarvtGDVTLNGeplaAIDAPRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 79 HIGyvsgllRDRFSAGeiVRDVVLSGIFKSIGLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARAL- 157
Cdd:PRK13547 90 QAA------QPAFAFS--AREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 158 --------MNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIE 229
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDW-NLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250
....*....|....*...
gi 505962082 230 AVLTNHTLSQLFDIPVAL 247
Cdd:PRK13547 241 DVLTPAHIARCYGFAVRL 258
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-177 |
3.35e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMInaYDFL--TAGEIQLFGmvpgqRGYSAHHVREH----IGYVSgllRDRF 91
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVL--YGALprTSGYVTLDG-----HEVVTRSPQDGlangIVYIS---EDRK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SAGeivrdVVLSGIFK---SIGLYEQPTETQVAL--AREMLALLN-MQAFEA------QYFGLLSTGEQQRVLFARALMN 159
Cdd:PRK10762 338 RDG-----LVLGMSVKenmSLTALRYFSRAGGSLkhADEQQAVSDfIRLFNIktpsmeQAIGLLSGGNQQKVAIARGLMT 412
|
170
....*....|....*...
gi 505962082 160 EPSLLILDEPANGLDfVG 177
Cdd:PRK10762 413 RPKVLILDEPTRGVD-VG 429
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-240 |
3.71e-10 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 58.69 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 2 LFSIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINA----------YDFLTAGEIQLFGMVPGQRGY 71
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGrlapdhgtatYIMRSGAELELYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 72 SAhhvREHIGYVSGLLRD----RFSAGEIVRDVVLSgifksIGL--YEQPTETQVALAREMLALLNMQAFEAQYFgllST 145
Cdd:TIGR02323 83 LM---RTEWGFVHQNPRDglrmRVSAGANIGERLMA-----IGArhYGNIRATAQDWLEEVEIDPTRIDDLPRAF---SG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 146 GEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQ 225
Cdd:TIGR02323 152 GMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDL-GLAVIIVTHDLGVARLLAQRLLVMQQGRVVES 230
|
250
....*....|....*..
gi 505962082 226 GRIEAVLTN--HTLSQL 240
Cdd:TIGR02323 231 GLTDQVLDDpqHPYTQL 247
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
12-232 |
3.85e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 59.73 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 12 KSGRTLLSDINWQV-NEGECWLVyGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSAhhVREHIGYVSgllrdr 90
Cdd:PRK10790 351 RDDNLVLQNINLSVpSRGFVALV-GHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV--LRQGVAMVQ------ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 91 fsageivRD-VVLSG-IFKSIGLYEQPTETQV--ALAREMLALLNMQAFEAQYFGL------LSTGEQQRVLFARALMNE 160
Cdd:PRK10790 422 -------QDpVVLADtFLANVTLGRDISEEQVwqALETVQLAELARSLPDGLYTPLgeqgnnLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505962082 161 PSLLILDEPANGLDfVGREQLMA-TLSQIRQHfpqTAVIYVSHFIEEVTEDFThALLLKQGTIQNQGRIEAVL 232
Cdd:PRK10790 495 PQILILDEATANID-SGTEQAIQqALAAVREH---TTLVVIAHRLSTIVEADT-ILVLHRGQAVEQGTHQQLL 562
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
9-227 |
3.88e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.68 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 9 AKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMI---NAYDFLTAGEIQLFGMVPGQR------GYSAHH---- 75
Cdd:TIGR00955 32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrSPKGVKGSGSVLLNGMPIDAKemraisAYVQQDdlfi 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 76 ----VREHIgYVSGLLR--DRFSAGE---IVRDVVlsgifksiglyeqptetqvalarEMLALLNMQAFEAQYFGL---L 143
Cdd:TIGR00955 112 ptltVREHL-MFQAHLRmpRRVTKKEkreRVDEVL-----------------------QALGLRKCANTRIGVPGRvkgL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 144 STGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfPQTAVIYVSHFIEEVTEDFTHALLLKQGTIQ 223
Cdd:TIGR00955 168 SGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQPSSELFELFDKIILMAEGRVA 246
|
....
gi 505962082 224 NQGR 227
Cdd:TIGR00955 247 YLGS 250
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-232 |
3.98e-10 |
|
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: 57.92 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMI--NAYDFLTAGEIQLFG-----MVPGQRgysahhvrehigyvsgl 86
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGeditdLPPEER----------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 87 lrdrfsageivrdvVLSGIFKSiglYEQPTETQ-VALArEMLALLNMQafeaqyfglLSTGEQQRVLFARALMNEPSLLI 165
Cdd:cd03217 75 --------------ARLGIFLA---FQYPPEIPgVKNA-DFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 166 LDEPANGLDFVGREQLMATLSQIRQhfPQTAVIYVSHF---IEEVTEDFTHalLLKQGTIQNQGRIEAVL 232
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLRE--EGKSVLIITHYqrlLDYIKPDRVH--VLYDGRIVKSGDKELAL 193
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-226 |
4.45e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 58.64 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSAH--HVREHIGYVSgllrdRFSAGE 95
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYirPVRKRIGMVF-----QFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 96 IVRDVVLSGIFKSIGLYEQPTETQVALAREMLALLN-----MQAFEAQyfglLSTGEQQRVLFARALMNEPSLLILDEPA 170
Cdd:PRK13646 98 LFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGfsrdvMSQSPFQ----MSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505962082 171 NGLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEVTEDFTHALLLKQGTIQNQG 226
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKT-IILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
18-202 |
4.89e-10 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 58.08 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMIN-AYD----FLTAGEIQLFGMVPGQRGYSAHHVREHIGYV--------- 83
Cdd:TIGR00972 17 LKNINLDIPKNQVTALIGPSGCGKSTLLRSLNrMNDlvpgVRIEGKVLFDGQDIYDKKIDVVELRRRVGMVfqkpnpfpm 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 84 -------SGL----LRDRFSAGEIVRdvvlsgifKSIglyeqpteTQVALAREMLALLNMQAFEaqyfglLSTGEQQRVL 152
Cdd:TIGR00972 97 siydniaYGPrlhgIKDKKELDEIVE--------ESL--------KKAALWDEVKDRLHDSALG------LSGGQQQRLC 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505962082 153 FARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFpqTAVIyVSH 202
Cdd:TIGR00972 155 IARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVI-VTH 201
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-239 |
5.07e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.17 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMI-NAYDFLTAGEIQLFGMVPGQRGySAHHVREHIGYVSgllRDRFS 92
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRN-PQQAIAQGIAMVP---EDRKR 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 93 AGeIV------RDVVLSGI--FKSIGLYEQPTETQVALaREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLL 164
Cdd:PRK13549 350 DG-IVpvmgvgKNITLAALdrFTGGSRIDDAAELKTIL-ESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505962082 165 ILDEPANGLDfVGRE----QLMATLSQirqhfPQTAVIYVSHFIEEVTEDFTHALLLkqgtiqNQGRIEAVLTNHTLSQ 239
Cdd:PRK13549 428 ILDEPTRGID-VGAKyeiyKLINQLVQ-----QGVAIIVISSELPEVLGLSDRVLVM------HEGKLKGDLINHNLTQ 494
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-209 |
5.45e-10 |
|
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: 59.18 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLfgmvpgQRGYSahhvrehIGYvsgLLRD-RFS 92
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP------QPGIK-------VGY---LPQEpQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 93 AGEIVRDVVLSGI---------FKSI-GLYEQPTETQVALAREMLALLNM--------------QAFEA-------QYFG 141
Cdd:TIGR03719 81 PTKTVRENVEEGVaeikdaldrFNEIsAKYAEPDADFDKLAAEQAELQEIidaadawdldsqleIAMDAlrcppwdADVT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505962082 142 LLSTGEQQRVLFARALMNEPSLLILDEPANGLDfvgrEQLMATLSQIRQHFPQTaVIYVSH---FIEEVTE 209
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGT-VVAVTHdryFLDNVAG 226
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-202 |
7.69e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMInaydfltAGEIQL-FGMVpgQRGYSAHhvrehIGYVSgllRDrfS 92
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL-------VGELEPdSGTV--KWSENAN-----IGYYA---QD--H 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 93 AGEIVRDVVLsgiFKSIGLYEQPTETQVALaREMLA-LLnmqaFEAQYFG----LLSTGEQQRVLFARALMNEPSLLILD 167
Cdd:PRK15064 392 AYDFENDLTL---FDWMSQWRQEGDDEQAV-RGTLGrLL----FSQDDIKksvkVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
170 180 190
....*....|....*....|....*....|....*
gi 505962082 168 EPANGLDFVGREQLMATLsqirQHFPQTaVIYVSH 202
Cdd:PRK15064 464 EPTNHMDMESIESLNMAL----EKYEGT-LIFVSH 493
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
9-174 |
7.98e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 57.35 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 9 AKRKSGRTLLSDINWQVNEGEcwlVYGL---NGAGKTTLLNMINAYDFLTAGEIQLFG-------MvpgqrgysahHVRE 78
Cdd:COG1137 10 VKSYGKRTVVKDVSLEVNQGE---IVGLlgpNGAGKTTTFYMIVGLVKPDSGRIFLDGedithlpM----------HKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 79 H--IGYV---SGLLRdRFSageiVRDVVLSgIFKSIGLyeqPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLF 153
Cdd:COG1137 77 RlgIGYLpqeASIFR-KLT----VEDNILA-VLELRKL---SKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180
....*....|....*....|.
gi 505962082 154 ARALMNEPSLLILDEPANGLD 174
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVD 168
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-202 |
8.21e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.48 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 16 TLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-----MVPGQRgysAHHVREHIGYV--SGLLR 88
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqMDEEAR---AKLRAKHVGFVfqSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 89 DRFSAGEivrDVVLSGIFKsiGLYEQPTETQvalAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDE 168
Cdd:PRK10584 101 PTLNALE---NVELPALLR--GESSRQSRNG---AKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190
....*....|....*....|....*....|....
gi 505962082 169 PANGLDFVGREQLMATLSQIRQHFpQTAVIYVSH 202
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNREH-GTTLILVTH 205
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
143-245 |
1.09e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 57.33 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 143 LSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTI 222
Cdd:PRK11231 139 LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ--GKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
90 100
....*....|....*....|...
gi 505962082 223 QNQGRIEAVLTNHTLSQLFDIPV 245
Cdd:PRK11231 217 MAQGTPEEVMTPGLLRTVFDVEA 239
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-220 |
1.65e-09 |
|
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: 55.71 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 12 KSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAydfltageiqlfgmvpgqrgysahhvREHIGYVSGllrdrf 91
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--------------------------RKTAGVITG------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 sageivrDVVLSG------IFKSIGLYEQ-PTETQVALAREmlALLnmqaFEAQYFGLlSTGEQQRVLFARALMNEPSLL 164
Cdd:cd03232 65 -------EILINGrpldknFQRSTGYVEQqDVHSPNLTVRE--ALR----FSALLRGL-SVEQRKRLTIGVELAAKPSIL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505962082 165 ILDEPANGLDFVGREQLMATLSQIRQHfPQTAVIYVSHFIEEVTEDFTHALLLKQG 220
Cdd:cd03232 131 FLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQPSASIFEKFDRLLLLKRG 185
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-245 |
1.84e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.58 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTA-----GEIQLFGMVPGQRGYSAHHVREHIGYVsgllrd 89
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLNRLRRQVSMV------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 rFSAGEI----VRDVVLSGIfKSIGLY-----EQPTETQVALAR---EMLALLNMQAFEaqyfglLSTGEQQRVLFARAL 157
Cdd:PRK14258 94 -HPKPNLfpmsVYDNVAYGV-KIVGWRpkleiDDIVESALKDADlwdEIKHKIHKSALD------LSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 158 MNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTAVIyVSHFIEEVTE--DFTHALLlkqgtiQNQGRIEAVLTNH 235
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVI-VSHNLHQVSRlsDFTAFFK------GNENRIGQLVEFG 238
|
250
....*....|
gi 505962082 236 TLSQLFDIPV 245
Cdd:PRK14258 239 LTKKIFNSPH 248
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-231 |
1.98e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.49 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 9 AKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGmvpgqRGYSA--HHVREHIGYvsGL 86
Cdd:PRK09700 12 GKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN-----INYNKldHKLAAQLGI--GI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 87 LRDRFSAgeIVRDVVLSGIFksIGlyEQPTETQVAL-----------AREMLALLNMQAFEAQYFGLLSTGEQQRVLFAR 155
Cdd:PRK09700 85 IYQELSV--IDELTVLENLY--IG--RHLTKKVCGVniidwremrvrAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505962082 156 ALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAV 231
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE--GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-207 |
2.08e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.23 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGEcwlVYGL---NGAGKTTLLNMINAYDFLTAGEIQLFGMVpgQRGYSAhhvrehigyvsgllRDRFSAG 94
Cdd:PRK11288 20 LDDISFDCRAGQ---VHALmgeNGAGKSTLLKILSGNYQPDAGSILIDGQE--MRFAST--------------TAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 95 EIV--------------RDVVLSGIFKSIGLYEQptETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNE 160
Cdd:PRK11288 81 VAIiyqelhlvpemtvaENLYLGQLPHKGGIVNR--RLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505962082 161 PSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEV 207
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAE--GRVILYVSHRMEEI 203
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-239 |
2.24e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.39 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 17 LLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAY-----DFLTAGEIQLFGMVPGQRGYSAHHVREHIGYVSGLlRDRF 91
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEVRREVGMVFQY-PNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SAGEIVRDVV----LSGIFKSIGLYEQPTE---TQVALAREMLALLNmqafeaQYFGLLSTGEQQRVLFARALMNEPSLL 164
Cdd:PRK14267 98 PHLTIYDNVAigvkLNGLVKSKKELDERVEwalKKAALWDEVKDRLN------DYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505962082 165 ILDEPANGLDFVGREQLMATLSQIRQHFpqtAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTN--HTLSQ 239
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEY---TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENpeHELTE 245
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-231 |
2.64e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 55.89 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQ-----LFGMVPGQ---RG----------YSAHHVREH 79
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLfggtdLTGLDEHEiarLGigrkfqkptvFEELTVFEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 80 IgyVSGLLRDRfsageivrdvvlsGIFKSigLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMN 159
Cdd:COG4674 106 L--ELALKGDR-------------GVFAS--LFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 160 EPSLLILDEPANGLDFVGREQLMATLSQIRQHfpqTAVIYVSH---FIEEVTEDFThalLLKQGTIQNQGRIEAV 231
Cdd:COG4674 169 DPKLLLLDEPVAGMTDAETERTAELLKSLAGK---HSVVVVEHdmeFVRQIARKVT---VLHQGSVLAEGSLDEV 237
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
14-232 |
3.92e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 55.46 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMI---NAYDfLTAGEIQLFG-----MVPGQRgysahhVREHIGY--- 82
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPKYE-VTSGSILLDGedileLSPDER------ARAGIFLafq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 83 ---------VSGLLRdrfSAGEIVRDvvlsgifksiglYEQPTETQVALAREMLALLNM-QAFEAQYFGL-LSTGEQQRV 151
Cdd:COG0396 85 ypveipgvsVSNFLR---TALNARRG------------EELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 152 LFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQhfPQTAVIYVSH---FIEEVTEDFTHalLLKQGTIQNQGRI 228
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRS--PDRGILIITHyqrILDYIKPDFVH--VLVDGRIVKSGGK 225
|
....
gi 505962082 229 EAVL 232
Cdd:COG0396 226 ELAL 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-222 |
4.18e-09 |
|
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: 55.23 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 1 MLFSIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQ-------LF----GMVPGQR 69
Cdd:cd03220 21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTvrgrvssLLglggGFNPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 70 GysahhvREHIgYVSGLL--RDRFSAGEIVRDVV-LSGIFKSIglyEQPTETqvalaremlallnmqafeaqyfglLSTG 146
Cdd:cd03220 101 G------RENI-YLNGRLlgLSRKEIDEKIDEIIeFSELGDFI---DLPVKT------------------------YSSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505962082 147 EQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTI 222
Cdd:cd03220 147 MKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ--GKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
144-202 |
4.41e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.89 E-value: 4.41e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 505962082 144 STGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSH 202
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREF-NTAIIMITH 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-249 |
4.76e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 56.65 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGmVPgQRGYSAHHVREHIGYVSGllrdrfsageiv 97
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG-VP-LVQYDHHYLHRQVALVGQ------------ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 98 RDVVLSGIFK---SIGLYEQPTETQVALAREMLALLNMQAFEAQYF-------GLLSTGEQQRVLFARALMNEPSLLILD 167
Cdd:TIGR00958 563 EPVLFSGSVReniAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDtevgekgSQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 168 EPANGLDfvgrEQLMATLSQIRQHFPQTaVIYVSHFIEEVtEDFTHALLLKQGTIQNQGrieavltnhTLSQLFDIPVAL 247
Cdd:TIGR00958 643 EATSALD----AECEQLLQESRSRASRT-VLLIAHRLSTV-ERADQILVLKKGSVVEMG---------THKQLMEDQGCY 707
|
..
gi 505962082 248 YQ 249
Cdd:TIGR00958 708 KH 709
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-234 |
5.43e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.44 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMIN----AYD--FLTAGEIQLFGMVPGQrgYSAHHVREHIGYVSGLlR 88
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieIYDskIKVDGKVLYFGKDIFQ--IDAIKLRKEVGMVFQQ-P 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 89 DRFSAGEIVRDVVLSgiFKSIGLYE--------QPTETQVALAREMLALLNMQAFEaqyfglLSTGEQQRVLFARALMNE 160
Cdd:PRK14246 100 NPFPHLSIYDNIAYP--LKSHGIKEkreikkivEECLRKVGLWKEVYDRLNSPASQ------LSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505962082 161 PSLLILDEPANGLDFVGREQLMATLSQIRQhfpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTN 234
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKN---EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-226 |
6.07e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.49 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 17 LLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMvpgqrgysahhvreHIGYVsGLLRDRFSAGEI 96
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGL--------------NIAKI-GLHDLRFKITII 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 97 VRDVVL-SGIFK-SIGLYEQPTETQVALAREMLAL----------LNMQAFEAQYFglLSTGEQQRVLFARALMNEPSLL 164
Cdd:TIGR00957 1366 PQDPVLfSGSLRmNLDPFSQYSDEEVWWALELAHLktfvsalpdkLDHECAEGGEN--LSVGQRQLVCLARALLRKTKIL 1443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505962082 165 ILDEPANGLDFVGREQLMATlsqIRQHFPQTAVIYVSHFIEEVTeDFTHALLLKQGTIQNQG 226
Cdd:TIGR00957 1444 VLDEATAAVDLETDNLIQST---IRTQFEDCTVLTIAHRLNTIM-DYTRVIVLDKGEVAEFG 1501
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
18-234 |
7.40e-09 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 54.81 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINaydFL---TAGEIQLFG----MVPGQRGY----SAHHVREhigyvsgl 86
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCIN---LLetpDSGEIRVGGeeirLKPDRDGElvpaDRRQLQR-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 87 LRDRfsageivrdvvLSGIFKSIGLY----------EQPTETQ-------VALAREMLALLNMQAFEAQYFGLLSTGEQQ 149
Cdd:COG4598 93 IRTR-----------LGMVFQSFNLWshmtvlenviEAPVHVLgrpkaeaIERAEALLAKVGLADKRDAYPAHLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 150 RVLFARALMNEPSLLILDEPANGLD--FVGrEQL--MATLSQI-RqhfpqTAVIyVSH---FIEEVTedfTHALLLKQGT 221
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDpeLVG-EVLkvMRDLAEEgR-----TMLV-VTHemgFARDVS---SHVVFLHQGR 231
|
250
....*....|...
gi 505962082 222 IQNQGRIEAVLTN 234
Cdd:COG4598 232 IEEQGPPAEVFGN 244
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
10-207 |
7.50e-09 |
|
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: 55.60 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINA------YDfltaGEIqLFGMVPGQrgysAHHVR--EHIG 81
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtWD----GEI-YWSGSPLK----ASNIRdtERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 82 YVsgLLRDRFSageIVRDV-VLSGIFKSIGLYEQPTETQVAL----AREMLALLNMQAF-EAQYFGLLSTGEQQRVLFAR 155
Cdd:TIGR02633 80 IV--IIHQELT---LVPELsVAENIFLGNEITLPGGRMAYNAmylrAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505962082 156 ALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEV 207
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH--GVACVYISHKLNEV 204
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-189 |
8.70e-09 |
|
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: 54.47 E-value: 8.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMvpGQRGYSAHHVREHIGYVS-------GLLRDR 90
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGV--DIRDLNLRWLRSQIGLVSqepvlfdGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 91 FSAG-------EIVRDVVLSGIFKSIGLYEQPTETQVAlaremlallnmqafeaQYFGLLSTGEQQRVLFARALMNEPSL 163
Cdd:cd03249 97 IRYGkpdatdeEVEEAAKKANIHDFIMSLPDGYDTLVG----------------ERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180
....*....|....*....|....*.
gi 505962082 164 LILDEPANGLDFVGREQLMATLSQIR 189
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAM 186
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-174 |
9.32e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.11 E-value: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 1 MLFSIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGmvpgqRGYSAHHVREHI 80
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG-----GDIDDPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 81 GYVSGL--LRDRFSAGEIVRdvvlsgiFKSiGLYEQPtETQVALAremLALLNMQAFEAQYFGLLSTGEQQRVLFARALM 158
Cdd:PRK13539 76 HYLGHRnaMKPALTVAENLE-------FWA-AFLGGE-ELDIAAA---LEAVGLAPLAHLPFGYLSAGQKRRVALARLLV 143
|
170
....*....|....*.
gi 505962082 159 NEPSLLILDEPANGLD 174
Cdd:PRK13539 144 SNRPIWILDEPTAALD 159
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-222 |
1.15e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.06 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 19 SDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSAhhvREHIGYVSgLLRDRFSAG---- 94
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ---RLARGLVY-LPEDRQSSGlyld 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 95 EIVRDVVLSGIFKSIGLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLD 174
Cdd:PRK15439 356 APLAWNVCALTHNRRGFWIKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505962082 175 FVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTI 222
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQ--NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-190 |
1.20e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 55.35 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMIN-AYDfLTAGEIQLFGMvpGQRGYSAHHVREHIGYV--SGLLRDRf 91
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQrVFD-PQSGRILIDGT--DIRTVTRASLRRNIAVVfqDAGLFNR- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SAGEIVRdvvlsgifksIGlYEQPTETQVALAREMLALLNMQAFEAQYFG--------LLSTGEQQRVLFARALMNEPSL 163
Cdd:PRK13657 424 SIEDNIR----------VG-RPDATDEEMRAAAERAQAHDFIERKPDGYDtvvgergrQLSGGERQRLAIARALLKDPPI 492
|
170 180
....*....|....*....|....*..
gi 505962082 164 LILDEPANGLDFVGREQLMATLSQIRQ 190
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDELMK 519
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-249 |
1.20e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.63 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 19 SDINWQVNEGECwlVYGLNGAGKTTLLNMINAYDFLTAGEiQLFG--MVPG--QRGYSAHHVREHIGYVSgllrdRFSAG 94
Cdd:PRK13645 30 TSLTFKKNKVTC--VIGTTGSGKSTMIQLTNGLIISETGQ-TIVGdyAIPAnlKKIKEVKRLRKEIGLVF-----QFPEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 95 EIVRDVVLSGI-FKSIGLYEQPTETQVALArEMLALLNM-------QAFEaqyfglLSTGEQQRVLFARALMNEPSLLIL 166
Cdd:PRK13645 102 QLFQETIEKDIaFGPVNLGENKQEAYKKVP-ELLKLVQLpedyvkrSPFE------LSGGQKRRVALAGIIAMDGNTLVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 167 DEPANGLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNHTLSQLFDI-PV 245
Cdd:PRK13645 175 DEPTGGLDPKGEEDFINLFERLNKEYKKR-IIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIEIdPP 253
|
....
gi 505962082 246 ALYQ 249
Cdd:PRK13645 254 KLYQ 257
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
11-234 |
1.32e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.39 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 11 RKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-MVPGQRGYSAHHVREHIGYVsgllrd 89
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGeNIPAMSRSRLYTVRKRMSML------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 rFSAGEIVRDVvlsGIFKSIGLyeqPTETQVALAREMLALLNMQAFEAqyFGL----------LSTGEQQRVLFARALMN 159
Cdd:PRK11831 90 -FQSGALFTDM---NVFDNVAY---PLREHTQLPAPLLHSTVMMKLEA--VGLrgaaklmpseLSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 160 EPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTAVIyVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTN 234
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVV-VSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAN 234
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-202 |
1.64e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 17 LLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQRGYSAHHVREHIGYVSGLlrdrfSAGEI 96
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGI-----NPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 97 VRDVVLSGIFKSIGLYEqptetqvalAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDfv 176
Cdd:PRK13540 91 LRENCLYDIHFSPGAVG---------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD-- 159
|
170 180
....*....|....*....|....*..
gi 505962082 177 gREQLMATLSQIRQHFPQ-TAVIYVSH 202
Cdd:PRK13540 160 -ELSLLTIITKIQEHRAKgGAVLLTSH 185
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
141-239 |
1.73e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.76 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 141 GLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQhfpQTAVIYVSHFIEEVTEDFTHALLLKQG 220
Cdd:PRK14247 145 GKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK---DMTIVLVTHFPQQAARISDYVAFLYKG 221
|
90 100
....*....|....*....|.
gi 505962082 221 TIQNQGRIEAVLTN--HTLSQ 239
Cdd:PRK14247 222 QIVEWGPTREVFTNprHELTE 242
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-177 |
3.29e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.54 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 17 LLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMvPGQRGYSAHHVrEHIGYVSGLLRDrFSAGEI 96
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK-TATRGDRSRFM-AYLGHLPGLKAD-LSTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 97 VRdvVLSGIFksiGLYEQPTETQValaremLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFV 176
Cdd:PRK13543 103 LH--FLCGLH---GRRAKQMPGSA------LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
.
gi 505962082 177 G 177
Cdd:PRK13543 172 G 172
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-208 |
3.98e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 52.41 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 1 MLFSIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIqLFgmvPGQ--RGYSAHHVRE 78
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL-LF---EGEdiSTLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 79 HIGYVS---GLLrdrfsaGEIVRDVVlsgIFKSIGLYEQPTETQVA--LAREMLALLNMQafeaQYFGLLSTGEQQRVLF 153
Cdd:PRK10247 82 QVSYCAqtpTLF------GDTVYDNL---IFPWQIRNQQPDPAIFLddLERFALPDTILT----KNIAELSGGEKQRISL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505962082 154 ARALMNEPSLLILDEPANGLDFVGREQLMATLSQ-IRQHfpQTAVIYVSHFIEEVT 208
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRyVREQ--NIAVLWVTHDKDEIN 202
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-229 |
4.13e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.52 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 2 LFSIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-----MVPGQrgysAHHV 76
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpcarLTPAK----AHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 77 REHIGYVSGLLRDRFSageiVRDVVLSGIFKSIGLYEQPTEtqvalareMLALLNMQAFEAQYFGLLSTGEQQRVLFARA 156
Cdd:PRK15439 87 GIYLVPQEPLLFPNLS----VKENILFGLPKRQASMQKMKQ--------LLAALGCQLDLDSSAGSLEVADRQIVEILRG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505962082 157 LMNEPSLLILDEPANGLDFVGREQLmatLSQIRQHFPQ-TAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIE 229
Cdd:PRK15439 155 LMRDSRILILDEPTASLTPAETERL---FSRIRELLAQgVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTA 225
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
33-202 |
6.23e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 33 VYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVpgqrgysahhvreHIGYV--SgllRDRFSAGEIVRDVVLSG--IFKs 108
Cdd:PRK11819 355 IIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV-------------KLAYVdqS---RDALDPNKTVWEEISGGldIIK- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 109 IGLYEQPtetqvalAREMLALLNMQAFEAQYF-GLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFvgrEQLMAtLSQ 187
Cdd:PRK11819 418 VGNREIP-------SRAYVGRFNFKGGDQQKKvGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV---ETLRA-LEE 486
|
170
....*....|....*
gi 505962082 188 IRQHFPQTAVIyVSH 202
Cdd:PRK11819 487 ALLEFPGCAVV-ISH 500
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
12-233 |
6.97e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.79 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 12 KSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGM-VPGQRgysAHHVREHIGYVS------ 84
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIpLTKLQ---LDSWRSRLAVVSqtpflf 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 85 --------GLLRDRFSAGEIVRDVVLSGIFKSIGLYEQPTETQVALAREMLallnmqafeaqyfgllSTGEQQRVLFARA 156
Cdd:PRK10789 402 sdtvanniALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVML----------------SGGQKQRISIARA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505962082 157 LMNEPSLLILDEPANGLDFVGREQLMATLSQIRQhfpQTAVIYVSHFIEEVTEDfTHALLLKQGTIQNQGRIEAVLT 233
Cdd:PRK10789 466 LLLNAEILILDDALSAVDGRTEHQILHNLRQWGE---GRTVIISAHRLSALTEA-SEILVMQHGHIAQRGNHDQLAQ 538
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-250 |
8.95e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.15 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 4 SIQQGAKRKSGRTL-LSDINWQVNEGE-CWLVyGLNGAGKTTLLNMINAYDFLTAGEIQLFGMV-----PGQRG------ 70
Cdd:PRK11650 5 KLQAVRKSYDGKTQvIKGIDLDVADGEfIVLV-GPSGCGKSTLLRMVAGLERITSGEIWIGGRVvnelePADRDiamvfq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 71 ----YSAHHVREHIGYvsGLLRDRFSAGEIVRDVvlsgifksiglyeqpteTQVALAREMLALLNMQAFEaqyfglLSTG 146
Cdd:PRK11650 84 nyalYPHMSVRENMAY--GLKIRGMPKAEIEERV-----------------AEAARILELEPLLDRKPRE------LSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 147 EQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTAvIYVSHfieevteDFTHALLLKQGTI-QNQ 225
Cdd:PRK11650 139 QRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTS-LYVTH-------DQVEAMTLADRVVvMNG 210
|
250 260
....*....|....*....|....*
gi 505962082 226 GRIEAVLTnhtlsqlfdiPVALYQH 250
Cdd:PRK11650 211 GVAEQIGT----------PVEVYEK 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-232 |
9.55e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 51.71 E-value: 9.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 3 FSIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG--MVPGQRGYSAHHVREHI 80
Cdd:PRK15112 14 FRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 81 GYVSGLLRDRFSAGEIVrDVVLSgifKSIGLYEQPTETQVALAREMLALLNMQAfeAQYFGLLSTGEQQRVLFARALMNE 160
Cdd:PRK15112 94 QDPSTSLNPRQRISQIL-DFPLR---LNTDLEPEQREKQIIETLRQVGLLPDHA--SYYPHMLAPGQKQRLGLARALILR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505962082 161 PSLLILDEPANGLDFVGREQLMATLSQIrQHFPQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVL 232
Cdd:PRK15112 168 PKVIIADEALASLDMSMRSQLINLMLEL-QEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-175 |
9.77e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.11 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMinaydfltageiqLFGMVPGQRGYSAHHVREHIGYVSGLLRDRFSAG 94
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRL-------------LAGALKGTPVAGCVDVPDNQFGREASLIDAIGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 95 EIVRDVVlsGIFKSIGLYEQPTetqvALARemlallnmqafeaqyFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLD 174
Cdd:COG2401 110 GDFKDAV--ELLNAVGLSDAVL----WLRR---------------FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
.
gi 505962082 175 F 175
Cdd:COG2401 169 R 169
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-177 |
9.94e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.10 E-value: 9.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 13 SGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMI--NAYDFLTAGEIQLFGmvpgqRGYSAHHVREHIG----YVSgl 86
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDG-----KEVDVSTVSDAIDaglaYVT-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 87 lRDRFSAG-----EIVRDVVLSGIFK--SIGLYEQPTETQVAlaREMLALLNMQAFE-AQYFGLLSTGEQQRVLFARALM 158
Cdd:NF040905 344 -EDRKGYGlnlidDIKRNITLANLGKvsRRGVIDENEEIKVA--EEYRKKMNIKTPSvFQKVGNLSGGNQQKVVLSKWLF 420
|
170
....*....|....*....
gi 505962082 159 NEPSLLILDEPANGLDfVG 177
Cdd:NF040905 421 TDPDVLILDEPTRGID-VG 438
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
143-209 |
1.23e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 51.83 E-value: 1.23e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 143 LSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQ---LMATLSQIRqhfpQTAVIYVSHFIEEVTE 209
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQifrLLARLNQLQ----GTSILLISHDLESISQ 224
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
33-209 |
1.33e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 33 VYGLNGAGKTTLLNMINAYDFLTAGEIQLfgmvpgQRGYSahhvrehIGYvsgLLRD-RFSAGEIVRDVVLSGI------ 105
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARP------APGIK-------VGY---LPQEpQLDPEKTVRENVEEGVaevkaa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 106 ---FKSIG-LYEQPTETQVALAREMLALLNM--------------QAFEA-------QYFGLLSTGEQQRVLFARALMNE 160
Cdd:PRK11819 102 ldrFNEIYaAYAEPDADFDALAAEQGELQEIidaadawdldsqleIAMDAlrcppwdAKVTKLSGGERRRVALCRLLLEK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505962082 161 PSLLILDEPANGLDfvgrEQLMATLSQIRQHFPQTaVIYVSH---FIEEVTE 209
Cdd:PRK11819 182 PDMLLLDEPTNHLD----AESVAWLEQFLHDYPGT-VVAVTHdryFLDNVAG 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
35-206 |
1.52e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 35 GLNGAGKTTLLNMinaydfLT------AGEIQLFGMVPGQRGYSahhVREHIGYVSgllrDRFSA-GEI-VR-DVVLSGi 105
Cdd:NF033858 299 GSNGCGKSTTMKM------LTgllpasEGEAWLFGQPVDAGDIA---TRRRVGYMS----QAFSLyGELtVRqNLELHA- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 106 fksiGLYEQPTETQVALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGRE---QLM 182
Cdd:NF033858 365 ----RLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDmfwRLL 440
|
170 180
....*....|....*....|....*
gi 505962082 183 ATLSqiRQhfpQTAVIYVS-HFIEE 206
Cdd:NF033858 441 IELS--RE---DGVTIFIStHFMNE 460
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-243 |
1.61e-07 |
|
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: 50.95 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 11 RKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVPGQrgYSAHHVREHIGYVsglLRDR 90
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAL--ADPAWLRRQVGVV---LQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 91 FSAGEIVRDVVlsgifkSIGLYEQPTETQVALAREMLA---LLNMQAFEAQYFGL----LSTGEQQRVLFARALMNEPSL 163
Cdd:cd03252 86 VLFNRSIRDNI------ALADPGMSMERVIEAAKLAGAhdfISELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 164 LILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIyVSHFIEEVtEDFTHALLLKQGTIQNQGRIEAVLTNHTL-SQLFD 242
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAG--RTVII-IAHRLSTV-KNADRIIVMEKGRIVEQGSHDELLAENGLyAYLYQ 235
|
.
gi 505962082 243 I 243
Cdd:cd03252 236 L 236
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
123-202 |
2.00e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.12 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 123 AREMLALLNMQAFEAQ-YFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVS 201
Cdd:PRK11308 134 ALAMMAKVGLRPEHYDrYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQEL-GLSYVFIS 212
|
.
gi 505962082 202 H 202
Cdd:PRK11308 213 H 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
18-174 |
2.37e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 50.95 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIqlfgMVPGQR--GYSA---HHVREHIGYVS---GLLRD 89
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV----LVDGQDltALSEkelRKARRQIGMIFqhfNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 RFSAGEIVRDVVLSGIFKS-IglyeqptETQVAlarEMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDE 168
Cdd:PRK11153 97 RTVFDNVALPLELAGTPKAeI-------KARVT---ELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDE 166
|
....*.
gi 505962082 169 PANGLD 174
Cdd:PRK11153 167 ATSALD 172
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
143-234 |
2.52e-07 |
|
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: 51.22 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 143 LSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSH-------FIEEVtedfthaL 215
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQREL-GMALLLITHdlgvvrrFADRV-------A 228
|
90
....*....|....*....
gi 505962082 216 LLKQGTIQNQGRIEAVLTN 234
Cdd:COG4172 229 VMRQGEIVEQGPTAELFAA 247
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
105-231 |
2.68e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.01 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 105 IFKSIGLYEQPT-ETQVALAREMLALLNM---QAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQ 180
Cdd:PRK10261 127 IAESIRLHQGASrEEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQ 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 505962082 181 LMATLSQIRQHFpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAV 231
Cdd:PRK10261 207 ILQLIKVLQKEM-SMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-204 |
2.75e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 17 LLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVpgqrgysahhvrehigYVSGLLRD--RFSAG 94
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDL----------------IVARLQQDppRNVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 95 EiVRDVVLSGIfKSIGLY------------EQPTET---QVALAREMLALLNMQAFEA------QYFGL--------LST 145
Cdd:PRK11147 82 T-VYDFVAEGI-EEQAEYlkryhdishlveTDPSEKnlnELAKLQEQLDHHNLWQLENrinevlAQLGLdpdaalssLSG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505962082 146 GEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIrqhfpQTAVIYVSH---FI 204
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF-----QGSIIFISHdrsFI 216
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-227 |
3.19e-07 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 49.72 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMInaYDFLTA--GEIQLFGMvpgqrgysahhvreHIGYVsGLLRDRFSAGE 95
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILAL--FRFLEAeeGKIEIDGI--------------DISTI-PLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 96 IVRD-VVLSGIFKS-IGLYEQPTETQValaremlallnMQAFEAQYFGL-LSTGEQQRVLFARALMNEPSLLILDEPANG 172
Cdd:cd03369 87 IPQDpTLFSGTIRSnLDPFDEYSDEEI-----------YGALRVSEGGLnLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 173 LDFVGREQLMATlsqIRQHFPQTAVIYVSHFIEEVTeDFTHALLLKQGTIQNQGR 227
Cdd:cd03369 156 IDYATDALIQKT---IREEFTNSTILTIAHRLRTII-DYDKILVMDAGEVKEYDH 206
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-174 |
4.27e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 49.70 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGM-VPGQrgySAHHVREHIGYVsgllrdrF-- 91
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKL---PEYKRAKYIGRV-------Fqd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 -SAG-----EIVRDVVLS---GifKSIGLYEQPTETQVALAREMLALLNMqAFEAQYF---GLLSTGEQQRVLFARALMN 159
Cdd:COG1101 89 pMMGtapsmTIEENLALAyrrG--KRRGLRRGLTKKRRELFRELLATLGL-GLENRLDtkvGLLSGGQRQALSLLMATLT 165
|
170
....*....|....*
gi 505962082 160 EPSLLILDEPANGLD 174
Cdd:COG1101 166 KPKLLLLDEHTAALD 180
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-177 |
5.00e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.29 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 9 AKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFG-----------------MVPGQR-- 69
Cdd:PRK11288 260 LDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpidirsprdairagimLCPEDRka 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 70 -GYSAHH-VREHIGYVSgllRDRFSAGEIVRDvvlsgifksiglyeQPTETQvaLAREMLALLNMQAFEA-QYFGLLSTG 146
Cdd:PRK11288 340 eGIIPVHsVADNINISA---RRHHLRAGCLIN--------------NRWEAE--NADRFIRSLNIKTPSReQLIMNLSGG 400
|
170 180 190
....*....|....*....|....*....|.
gi 505962082 147 EQQRVLFARALMNEPSLLILDEPANGLDfVG 177
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGID-VG 430
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-174 |
5.40e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 49.73 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 3 FSIQQGAKRKSGRTL--LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGM-VPGQRGYSAHHVREH 79
Cdd:COG4608 17 FPVRGGLFGRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQdITGLSGRELRPLRRR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 80 IGYV----SGLLRDRFSAGEIVRDV-VLSGIfksiglyeQPTETQVALAREMLAL--LNmQAFEAQYFGLLSTGEQQRVL 152
Cdd:COG4608 97 MQMVfqdpYASLNPRMTVGDIIAEPlRIHGL--------ASKAERRERVAELLELvgLR-PEHADRYPHEFSGGQRQRIG 167
|
170 180
....*....|....*....|..
gi 505962082 153 FARALMNEPSLLILDEPANGLD 174
Cdd:COG4608 168 IARALALNPKLIVCDEPVSALD 189
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
143-190 |
5.42e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.09 E-value: 5.42e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 505962082 143 LSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQ 190
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQ 204
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
143-202 |
8.15e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.42 E-value: 8.15e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 143 LSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfPQTAVIYVSH 202
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQN-NNTTILLISH 217
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-253 |
8.16e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 49.08 E-value: 8.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLN----MINaydflTAGEIQLFGM----VPGQRGYSAHHV-REHIGYVS 84
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSaflrLLN-----TEGDIQIDGVswnsVPLQKWRKAFGViPQKVFIFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 85 GLLRDRFSAGEIVRDVVLSGIFKSIGLYeqptetqvALAREMLALLNMQAFEAQYfgLLSTGEQQRVLFARALMNEPSLL 164
Cdd:cd03289 91 GTFRKNLDPYGKWSDEEIWKVAEEVGLK--------SVIEQFPGQLDFVLVDGGC--VLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 165 ILDEPANGLDFVGREQLMATLsqiRQHFPQTAVIYVSHFIEEVTEdFTHALLLKQGTIQNQGRIEAVLTNHTLSQLFDIP 244
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTL---KQAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISP 236
|
250
....*....|..
gi 505962082 245 ---VALYQHHGR 253
Cdd:cd03289 237 sdrLKLFPRRNS 248
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-202 |
9.18e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 48.49 E-value: 9.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGEcwlVYGL---NGAGKTTLLNMIN-AYDFL----TAGEIQLFGMVPGQRGYSAHHVREHIGYV------ 83
Cdd:COG1117 27 LKDINLDIPENK---VTALigpSGCGKSTLLRCLNrMNDLIpgarVEGEILLDGEDIYDPDVDVVELRRRVGMVfqkpnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 84 ---S-------GL----LRDRFSAGEIVRdvvlsgifKSIglyeqpteTQVALAREMLALLNMQAFEaqyfglLSTGEQQ 149
Cdd:COG1117 104 fpkSiydnvayGLrlhgIKSKSELDEIVE--------ESL--------RKAALWDEVKDRLKKSALG------LSGGQQQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505962082 150 RVLFARALMNEPSLLILDEPANGLDFV--GR-EQLMATLsqiRQHFpqTAVIyVSH 202
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPIstAKiEELILEL---KKDY--TIVI-VTH 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-192 |
1.30e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 48.23 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAgEIQLFGMVP--GQRGYSAH----HVREHIGYVsgllrdrF 91
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNP-EVTITGSIVynGHNIYSPRtdtvDLRKEIGMV-------F 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SAGE-----IVRDVV----LSGIfKSIGLYEQPTET---QVALAREMLALLNMQAFEaqyfglLSTGEQQRVLFARALMN 159
Cdd:PRK14239 93 QQPNpfpmsIYENVVyglrLKGI-KDKQVLDEAVEKslkGASIWDEVKDRLHDSALG------LSGGQQQRVCIARVLAT 165
|
170 180 190
....*....|....*....|....*....|...
gi 505962082 160 EPSLLILDEPANGLDFVGREQLMATLSQIRQHF 192
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDDY 198
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-220 |
1.45e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 47.64 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 10 KRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMInaydfltAGEIQLFGMVPGQRGYSAHHVREHigyvsgllrD 89
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL-------ANRTEGNVSVEGDIHYNGIPYKEF---------A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 RFSAGEIvrdvvlsgIFKSIGLYEQPTETqvalAREML-ALLNMQAfeAQYFGLLSTGEQQRVLFARALMNEPSLLILDE 168
Cdd:cd03233 79 EKYPGEI--------IYVSEEDVHFPTLT----VRETLdFALRCKG--NEFVRGISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505962082 169 PANGLD------FVGREQLMATLSQIrqhfpqTAVIYVSHFIEEVTEDFTHALLLKQG 220
Cdd:cd03233 145 STRGLDsstaleILKCIRTMADVLKT------TTFVSLYQASDEIYDLFDKVLVLYEG 196
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-239 |
2.22e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 12 KSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLN-MINAYDFLTAGEIQLFGMVPgqrgysahhvreHIGYVSGLlrdr 90
Cdd:PLN03130 627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTVA------------YVPQVSWI---- 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 91 FSAgeIVRDVVLSGIFKSIGLYEQPTETqVALAREMLALLNMQAFEAQYFGL-LSTGEQQRVLFARALMNEPSLLILDEP 169
Cdd:PLN03130 691 FNA--TVRDNILFGSPFDPERYERAIDV-TALQHDLDLLPGGDLTEIGERGVnISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505962082 170 ANGLD-FVGREQLMATLSQIRQHFPQTAVIYVSHFIEEVTEdfthALLLKQGTIQNQGRIEAVLTNHTLSQ 239
Cdd:PLN03130 768 LSALDaHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDR----IILVHEGMIKEEGTYEELSNNGPLFQ 834
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-228 |
2.57e-06 |
|
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: 48.47 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 13 SGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEI---------------QLFGMVPgQRGYSAHH-- 75
Cdd:TIGR01257 941 SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvggkdietnldavrQSLGMCP-QHNILFHHlt 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 76 VREHIGYVSGLLRDRFSAGEIVRDVVLsgifKSIGLYEQPTEtqvalaremlallnmqafEAQYfglLSTGEQQRVLFAR 155
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAML----EDTGLHHKRNE------------------EAQD---LSGGMQRKLSVAI 1074
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505962082 156 ALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQhfpQTAVIYVSHFIEEVTedfthaLLLKQGTIQNQGRI 228
Cdd:TIGR01257 1075 AFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS---GRTIIMSTHHMDEAD------LLGDRIAIISQGRL 1138
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-232 |
2.90e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 47.89 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMI-NAYDfLTAGEIqlfgMVPGQ--RGYSAHHVREHIGyvsgllrdrf 91
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfRFYD-VTSGRI----LIDGQdiRDVTQASLRAAIG---------- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 sageIV-RDVVL--SGIFKSIGlYEQP--TETQVALAREMLALLNM-----QAFEAQY--FGL-LSTGEQQRVLFARALM 158
Cdd:COG5265 436 ----IVpQDTVLfnDTIAYNIA-YGRPdaSEEEVEAAARAAQIHDFieslpDGYDTRVgeRGLkLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505962082 159 NEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIyVSHFIEEVTeDFTHALLLKQGTIQNQGRIEAVL 232
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVARG--RTTLV-IAHRLSTIV-DADEILVLEAGRIVERGTHAELL 580
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2-240 |
3.93e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.84 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 2 LFSIQQGAKRKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQ----------LFGMVPGQRgy 71
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdgqlrdLYALSEAER-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 72 sAHHVREHIGYV-----SGLlRDRFSAGEIVRDVVLSgifksIGL--YEQPTETQVA-LAREMLALLNMQAFEAQYfgll 143
Cdd:PRK11701 84 -RRLLRTEWGFVhqhprDGL-RMQVSAGGNIGERLMA-----VGArhYGDIRATAGDwLERVEIDAARIDDLPTTF---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 144 STGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIeEVTEDFTHALL-LKQGTI 222
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVREL-GLAVVIVTHDL-AVARLLAHRLLvMKQGRV 230
|
250 260
....*....|....*....|
gi 505962082 223 QNQGRIEAVLTN--HTLSQL 240
Cdd:PRK11701 231 VESGLTDQVLDDpqHPYTQL 250
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-235 |
4.05e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.58 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGmvpgqrgySAHHVRehigyVSGLLRDRFSAGEiv 97
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--------SAALIA-----ISSGLNGQLTGIE-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 98 rDVVLSGIFksIGLyeqpTETQVA-LAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFV 176
Cdd:PRK13545 105 -NIELKGLM--MGL----TKEKIKeIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505962082 177 GREQLMATLSQIRQHfpQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTNH 235
Cdd:PRK13545 178 FTKKCLDKMNEFKEQ--GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHY 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
143-207 |
4.52e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 4.52e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 143 LSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTaVIYVSHFIEEV 207
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKT-IITIAHRIASI 1422
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
18-174 |
4.63e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 47.32 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMvpGQRGYSAHHVREHIGYVSGLL---------- 87
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH--DLRDYTLASLRNQVALVSQNVhlfndtiann 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 88 -----RDRFSAGEIVRDVVLSGIFKSIGLYEQPTETQVAlarEMLALLnmqafeaqyfgllSTGEQQRVLFARALMNEPS 162
Cdd:PRK11176 437 iayarTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIG---ENGVLL-------------SGGQRQRIAIARALLRDSP 500
|
170
....*....|..
gi 505962082 163 LLILDEPANGLD 174
Cdd:PRK11176 501 ILILDEATSALD 512
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-209 |
4.72e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.33 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 9 AKRKSGRTLLSDINWQVNEGEcwlVYGL---NGAGKTTLLNMINAYDFLTAGEIQLFGMVPGqrGYSAHHVREH-IGYVS 84
Cdd:COG3845 265 VRDDRGVPALKDVSLEVRAGE---ILGIagvAGNGQSELAEALAGLRPPASGSIRLDGEDIT--GLSPRERRRLgVAYIP 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 85 ------GLLRD----------RFSAGEIVRDVVLSgiFKSIglyeqptetqVALAREMlallnMQAF------EAQYFGL 142
Cdd:COG3845 340 edrlgrGLVPDmsvaenlilgRYRRPPFSRGGFLD--RKAI----------RAFAEEL-----IEEFdvrtpgPDTPARS 402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505962082 143 LSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSHFIEEVTE 209
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA--GAAVLLISEDLDEILA 467
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
143-231 |
5.16e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 46.66 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 143 LSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfPQTAVIYVSHFIEEVTEDFTHALLLKQGTI 222
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQK-ENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
....*....
gi 505962082 223 QNQGRIEAV 231
Cdd:PRK11022 233 VETGKAHDI 241
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-234 |
5.69e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.63 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 13 SGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYD-----FLTAGEIqlfgMVPGQRGYSAHHVREHIGYVSGLL 87
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDV----LLGGRSIFNYRDVLEFRRRVGMLF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 88 RDRFSAGEIVRDVVLSGI----------FKSIGlyeQPTETQVALAREMLALLNMQAFEaqyfglLSTGEQQRVLFARAL 157
Cdd:PRK14271 108 QRPNPFPMSIMDNVLAGVrahklvprkeFRGVA---QARLTEVGLWDAVKDRLSDSPFR------LSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505962082 158 MNEPSLLILDEPANGLDFVGREQLMATlsqIRQHFPQTAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTN 234
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEF---IRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-184 |
6.74e-06 |
|
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: 45.86 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 25 VNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFgmvpgqrgysahhvREHIGYVSGLLRDRFSAgeIVRDVvLSG 104
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE--------------LDTVSYKPQYIKADYEG--TVRDL-LSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 105 IFKsiGLYEQPT-ETQVALAREMLALLNMQAFEaqyfglLSTGEQQRVLFARALMNEPSLLILDEPANGLDFvgrEQ-LM 182
Cdd:cd03237 85 ITK--DFYTHPYfKTEIAKPLQIEQILDREVPE------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV---EQrLM 153
|
..
gi 505962082 183 AT 184
Cdd:cd03237 154 AS 155
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
123-209 |
7.72e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.54 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 123 AREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHfpQTAVIYVSH 202
Cdd:PRK10762 122 ADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ--GRGIVYISH 199
|
....*..
gi 505962082 203 FIEEVTE 209
Cdd:PRK10762 200 RLKEIFE 206
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-202 |
8.13e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMInaydfltAGEIQ-LFGMV---PGQRG--YSAHHVrehigyvSGLl 87
Cdd:PLN03073 521 GPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLI-------SGELQpSSGTVfrsAKVRMavFSQHHV-------DGL- 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 88 rdrfsageivrDVVLSGIFKSIGLYEQPTETQVALAREMLALLNMQAFEAQYfgLLSTGEQQRVLFARALMNEPSLLILD 167
Cdd:PLN03073 586 -----------DLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMY--TLSGGQKSRVAFAKITFKKPHILLLD 652
|
170 180 190
....*....|....*....|....*....|....*
gi 505962082 168 EPANGLDFVGREQLMATLSQIrqhfpQTAVIYVSH 202
Cdd:PLN03073 653 EPSNHLDLDAVEALIQGLVLF-----QGGVLMVSH 682
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
143-209 |
1.16e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 1.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505962082 143 LSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIrqhfpQTAVIYVSH---FIEE-VTE 209
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSY-----QGTVLLVSHdrqFVDNtVTE 506
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
121-213 |
1.18e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 121 ALAREMLALLN----MQAFEAQYFgllSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQirqhFPQTa 196
Cdd:PLN03073 322 ARAASILAGLSftpeMQVKATKTF---SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK----WPKT- 393
|
90 100
....*....|....*....|
gi 505962082 197 VIYVSH---FIEEVTEDFTH 213
Cdd:PLN03073 394 FIVVSHareFLNTVVTDILH 413
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
143-212 |
1.19e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.54 E-value: 1.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 143 LSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGR---EQLMATLSQirqhfpQTAVIYVSHFIEEV--TEDFT 212
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTlriEELMHELKE------QYTIIIVTHNMQQAarVSDMT 220
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-202 |
1.22e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.62 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMInaydFLTAGEIQLFGMVPgqrgysahhvrehigyvsgllrdRFSAGEIV 97
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG----LYASGKARLISFLP-----------------------KFSRNKLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 98 RDVVLSGIFKsIGLyeqpteTQVALAREMlallnmqafeaqyfGLLSTGEQQRVLFARALMNEP--SLLILDEPANGLDF 175
Cdd:cd03238 64 FIDQLQFLID-VGL------GYLTLGQKL--------------STLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQ 122
|
170 180
....*....|....*....|....*..
gi 505962082 176 VGREQLMATLSQIRQHfpQTAVIYVSH 202
Cdd:cd03238 123 QDINQLLEVIKGLIDL--GNTVILIEH 147
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-234 |
1.40e-05 |
|
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: 45.83 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 3 FSIQQGAKRKSGRTL--LSDINWQVNEGECWLVYGLNGAGKTTL----LNMINaydflTAGEIQLFGM-VPGQRGYSAHH 75
Cdd:COG4172 285 FPIKRGLFRRTVGHVkaVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFDGQdLDGLSRRALRP 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 76 VREHIGYV----SGLLRDRFSAGEIVRDvvlsgifksiGLY----EQPTETQVALAREMLALLNMQAFEAQ-YFGLLSTG 146
Cdd:COG4172 360 LRRRMQVVfqdpFGSLSPRMTVGQIIAE----------GLRvhgpGLSAAERRARVAEALEEVGLDPAARHrYPHEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 147 EQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIeEVTEDFTHALL-LKQGTIQNQ 225
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREH-GLAYLFISHDL-AVVRALAHRVMvMKDGKVVEQ 507
|
....*....
gi 505962082 226 GRIEAVLTN 234
Cdd:COG4172 508 GPTEQVFDA 516
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
143-213 |
2.11e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.50 E-value: 2.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 143 LSTGEQQRV----LFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQtaVIYVSHFiEEVTEDFTH 213
Cdd:cd03227 78 LSGGEKELSalalILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQ--VIVITHL-PELAELADK 149
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-202 |
2.87e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 44.70 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 20 DINWQVNEGECWLVYGLNGAGKTTL----LNMINAydflTAGEI-----QLFGMVPGQRgysaHHVREHIGYVS----GL 86
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFaraiIGLVKA----TDGEVawlgkDLLGMKDDEW----RAVRSDIQMIFqdplAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 87 LRDRFSAGEIVRDVVLsgIFKSiGLYEQPTETQValaREMLA-------LLNMQAFEaqyfglLSTGEQQRVLFARALMN 159
Cdd:PRK15079 111 LNPRMTIGEIIAEPLR--TYHP-KLSRQEVKDRV---KAMMLkvgllpnLINRYPHE------FSGGQCQRIGIARALIL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505962082 160 EPSLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSH 202
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREM-GLSLIFIAH 220
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
15-211 |
3.55e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMInaydfltAGEIQLF----GMVPGQR-GYSAHHVREHigyvsgLLRD 89
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL-------AGELAPVsgeiGLAKGIKlGYFAQHQLEF------LRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 90 RFSAGEIVRdvvlsgifksigLYEQPTETQValaREMLALLNMQAFE-AQYFGLLSTGEQQRVLFARALMNEPSLLILDE 168
Cdd:PRK10636 392 ESPLQHLAR------------LAPQELEQKL---RDYLGGFGFQGDKvTEETRRFSGGEKARLVLALIVWQRPNLLLLDE 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505962082 169 PANGLDFVGREQLMATLSQIrqhfpQTAVIYVS---HFIEEVTEDF 211
Cdd:PRK10636 457 PTNHLDLDMRQALTEALIDF-----EGALVVVShdrHLLRSTTDDL 497
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
141-187 |
3.65e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 3.65e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 505962082 141 GLLSTGEQQRVLFARALMNEPSLLILDEPANGLDfVGRE----QLMATLSQ 187
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID-VGAKfeiyQLIAELAK 439
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
136-174 |
4.49e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 4.49e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 505962082 136 EAQYFGLLST---GEQQRVLFARALMNEPSLLILDEPANGLD 174
Cdd:PRK15064 146 EEQHYGLMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
32-189 |
8.83e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.30 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 32 LVYGLNGAGKTTLLnminayDFLTAGeiqLFGMVPGQRGYSAHHVR------------EHIG--YVS----GLLRDRFSA 93
Cdd:COG0419 27 LIVGPNGAGKSTIL------EAIRYA---LYGKARSRSKLRSDLINvgseeasvelefEHGGkrYRIerrqGEFAEFLEA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 94 GEIVRDVVLSGIFKsIGLYEQ----PTETQVALAREMLALLNMQAFEAQYF---------GLLSTGEQQRVLFARALMne 160
Cdd:COG0419 98 KPSERKEALKRLLG-LEIYEElkerLKELEEALESALEELAELQKLKQEILaqlsgldpiETLSGGERLRLALADLLS-- 174
|
170 180
....*....|....*....|....*....
gi 505962082 161 pslLILDEPAngLDFVGREQLMATLSQIR 189
Cdd:COG0419 175 ---LILDFGS--LDEERLERLLDALEELA 198
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-174 |
1.11e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 6 QQGAKrKSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINayDFLTAGEIQLFGMVPGQRGYSAHHVREhIGYVSG 85
Cdd:TIGR00956 768 EVKIK-KEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGRPLDSSFQRS-IGYVQQ 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 86 llRDRFSAGEIVRDvvlSGIF-------KSIGLYEqptetQVALAREMLALLNMQAFEAQYFGL----LSTGEQQRVLFA 154
Cdd:TIGR00956 844 --QDLHLPTSTVRE---SLRFsaylrqpKSVSKSE-----KMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIG 913
|
170 180
....*....|....*....|.
gi 505962082 155 RALMNEPSLLI-LDEPANGLD 174
Cdd:TIGR00956 914 VELVAKPKLLLfLDEPTSGLD 934
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-232 |
1.55e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.11 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYDFLTAGEIQLFGMVpgqrgysahhvrEHIGYVSGLlrdrfsageiv 97
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV------------SVIAISAGL----------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 98 rDVVLSGI----FKSIGLYEQPTETQvALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANgl 173
Cdd:PRK13546 97 -SGQLTGIenieFKMLCMGFKRKEIK-AMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALS-- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505962082 174 dfVGrEQLMA--TLSQIRQHFPQTAVI-YVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVL 232
Cdd:PRK13546 173 --VG-DQTFAqkCLDKIYEFKEQNKTIfFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-221 |
1.80e-04 |
|
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: 41.30 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 17 LLSDINWQVNEGECWLVYGLNGAGKTTLLNMInaydfltAGEIQ-LFGMVpgqrgysahHVREHIGYVSG---LLRDRfs 92
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-------LGELEkLSGSV---------SVPGSIAYVSQepwIQNGT-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 93 ageiVRDVVLSGIFKSIGLYEQptetqvalAREMLALLN-MQAFEAqyfGL----------LSTGEQQRVLFARALMNEP 161
Cdd:cd03250 82 ----IRENILFGKPFDEERYEK--------VIKACALEPdLEILPD---GDlteigekginLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505962082 162 SLLILDEPANGLD-FVGR---EQ-LMATLSQIRqhfpqtAVIYVSHFIeEVTEDFTHALLLKQGT 221
Cdd:cd03250 147 DIYLLDDPLSAVDaHVGRhifENcILGLLLNNK------TRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
32-202 |
1.94e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.44 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 32 LVYGLNGAGKTTLLNMINAydfltageiQLFGMVPgQRGYSAHHVREHI--GYVSGLLRDRFSAG-----EIVR--DVVL 102
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKY---------ALTGELP-PNSKGGAHDPKLIreGEVRAQVKLAFENAngkkyTITRslAILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 103 SGIFKSIGlyeqptetqvalarEMLALLnmqafeAQYFGLLSTGeqQRVLF--------ARALMNEPSLLILDEPANGLD 174
Cdd:cd03240 96 NVIFCHQG--------------ESNWPL------LDMRGRCSGG--EKVLAsliirlalAETFGSNCGILALDEPTTNLD 153
|
170 180 190
....*....|....*....|....*....|...
gi 505962082 175 fvgREQLMATLSQI-----RQHFPQtaVIYVSH 202
Cdd:cd03240 154 ---EENIEESLAEIieerkSQKNFQ--LIVITH 181
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
15-248 |
2.47e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.22 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTtlLNMINAYDFLTAGEIQLFGMV--PGQRgYSAHHVREHigYVSGLLRDRFS 92
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVllDGKP-VAPCALRGR--KIATIMQNPRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 93 AGEIVRDVVLSGIFKSIGLYEQPTETQVALAREMLAL------LNMQAFEaqyfglLSTGEQQRVLFARALMNEPSLLIL 166
Cdd:PRK10418 91 AFNPLHTMHTHARETCLALGKPADDATLTAALEAVGLenaarvLKLYPFE------MSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 167 DEPANGLDFVGREQLMATLSQI-RQHFPqtAVIYVSHFIEEVTEDFTHALLLKQGTIQNQGRIEAVLTN--HTLSQ-LFD 242
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIvQKRAL--GMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNApkHAVTRsLVS 242
|
....*.
gi 505962082 243 IPVALY 248
Cdd:PRK10418 243 AHLALY 248
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
15-229 |
2.53e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.17 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 15 RTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMIN---AYDfLTAGEIQLFG-----MVPGQRG----YSAHHVREHIGY 82
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghpAYK-ILEGDILFKGesildLEPEERAhlgiFLAFQYPIEIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 83 VSG--LLRDRFSAGEivrdvvlsgifKSIGLYEQPTETQVALAREMLALLNMQA-FEAQY----FgllSTGEQQRVLFAR 155
Cdd:CHL00131 99 VSNadFLRLAYNSKR-----------KFQGLPELDPLEFLEIINEKLKLVGMDPsFLSRNvnegF---SGGEKKRNEILQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505962082 156 ALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQhfPQTAVIYVSHF---IEEVTEDFTHalLLKQGTIQNQGRIE 229
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIAEGINKLMT--SENSIILITHYqrlLDYIKPDYVH--VMQNGKIIKTGDAE 237
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
156-206 |
3.49e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 3.49e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 505962082 156 ALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFPQTAVIYVSHFIEE 206
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVATAYMEE 200
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
144-251 |
4.27e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.38 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 144 STGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLSQIRQHFpQTAVIYVSHFIeEVTEDFTHAL-LLKQGTI 222
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDF-GIAYLFISHDM-AVVERISHRVaVMYLGQI 542
|
90 100 110
....*....|....*....|....*....|...
gi 505962082 223 QNQGRIEAVLTN----HTLSQLFDIPVALYQHH 251
Cdd:PRK10261 543 VEIGPRRAVFENpqhpYTRKLMAAVPVADPSRQ 575
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
143-174 |
4.50e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.55 E-value: 4.50e-04
10 20 30
....*....|....*....|....*....|..
gi 505962082 143 LSTGEQQRVLFARALMNEPSLLILDEPANGLD 174
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
121-233 |
1.09e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 39.72 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 121 ALAREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATL-SQIRQhfpQTAVIY 199
Cdd:NF000106 123 ARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVrSMVRD---GATVLL 199
|
90 100 110
....*....|....*....|....*....|....*
gi 505962082 200 VSHFIEEvTEDFTHAL-LLKQGTIQNQGRIEAVLT 233
Cdd:NF000106 200 TTQYMEE-AEQLAHELtVIDRGRVIADGKVDELKT 233
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-202 |
1.17e-03 |
|
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: 38.51 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 28 GECWLVYGLNGAGKTTLLNMInaydfltAGEIQlfgmvpgqrgysahhvREHIGYVsgllrdRFSAGEIvrdvvlsgifk 107
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARAL-------ARELG----------------PPGGGVI------YIDGEDI----------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 108 siglyeqptetqvalaREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFVGREQLMATLS- 186
Cdd:smart00382 42 ----------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEEl 105
|
170
....*....|....*....
gi 505962082 187 ---QIRQHFPQTAVIYVSH 202
Cdd:smart00382 106 rllLLLKSEKNLTVILTTN 124
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
91-202 |
1.37e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 38.71 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 91 FSAGEIVRDVVLSGIFKSIGL-----YEQPTETQVALAREMLAllnmqaFEAQYFGLlSTGEQQRVLFARALMNEPSLLI 165
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVkilagQLIPNGDNDEWDGITPV------YKPQYIDL-SGGELQRVAIAAALLRNATFYL 94
|
90 100 110
....*....|....*....|....*....|....*..
gi 505962082 166 LDEPANGLDFVGREQLMATLSQIRQHFPQTAVIyVSH 202
Cdd:cd03222 95 FDEPSAYLDIEQRLNAARAIRRLSEEGKKTALV-VEH 130
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
12-239 |
1.68e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.57 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 12 KSGRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNminaydfltageiQLFGMVPGQRGYSAHhVREHIGYVSGLlrdRF 91
Cdd:PLN03232 627 KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLIS-------------AMLGELSHAETSSVV-IRGSVAYVPQV---SW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 92 SAGEIVRDVVLSGIFKSIGLYEQPTETqVALAREMLALLNMQAFEAQYFGL-LSTGEQQRVLFARALMNEPSLLILDEPA 170
Cdd:PLN03232 690 IFNATVRENILFGSDFESERYWRAIDV-TALQHDLDLLPGRDLTEIGERGVnISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 171 NGLD-FVGREQLMATLSQIRQHFPQTAVIYVSHFIEEVTEdfthALLLKQGTIQNQGRIEAVLTNHTLSQ 239
Cdd:PLN03232 769 SALDaHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDR----IILVSEGMIKEEGTFAELSKSGSLFK 834
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
124-202 |
2.38e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.02 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 124 REMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLDFvgREQL-MATLsqIRQHFPQTAVIYVSH 202
Cdd:PRK13409 194 DEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI--RQRLnVARL--IRELAEGKYVLVVEH 269
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-169 |
3.17e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.62 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 18 LSDINWQVNEGECWLVYGLNGAGKTTLLNMIN------AYDfltaGEIQLFGMVPGQRGYSAhhvREHIGYV-------- 83
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvyphgSYE----GEILFDGEVCRFKDIRD---SEALGIViihqelal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 84 SGLL---------RDRFSAGEIVRDVVLS---GIFKSIGLYEQPtETQValaremlallnmqafeaqyfGLLSTGEQQRV 151
Cdd:NF040905 90 IPYLsiaeniflgNERAKRGVIDWNETNRrarELLAKVGLDESP-DTLV--------------------TDIGVGKQQLV 148
|
170
....*....|....*...
gi 505962082 152 LFARALMNEPSLLILDEP 169
Cdd:NF040905 149 EIAKALSKDVKLLILDEP 166
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
143-189 |
3.71e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 3.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 505962082 143 LSTGEQQRVLFARALM---NEPSLLILDEPANGLDFVGREQLMATLSQIR 189
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLV 879
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
123-174 |
4.99e-03 |
|
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: 37.84 E-value: 4.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 505962082 123 AREMLALLNMQAFEAQYFGLLSTGEQQRVLFARALMNEPSLLILDEPANGLD 174
Cdd:COG1245 193 LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
14-226 |
5.92e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 37.08 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 14 GRTLLSDINWQVNEGECWLVYGLNGAGKTTLLNMINAYD--FLTAGEIQ-----LFGMVPGQRG----YSAHHVREHIGY 82
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEfkgkdLLELSPEDRAgegiFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 83 VSgllrDRFsageivrdvVLSGIFKSIGLYEQptetQVALAR--------EMLALLNMQAfeaqyfGLL--------STG 146
Cdd:PRK09580 93 VS----NQF---------FLQTALNAVRSYRG----QEPLDRfdfqdlmeEKIALLKMPE------DLLtrsvnvgfSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962082 147 EQQR--VLFARALmnEPSLLILDEPANGLDFVGREQLMATLSQIRQhfPQTAVIYVSHF---IEEVTEDFTHalLLKQGT 221
Cdd:PRK09580 150 EKKRndILQMAVL--EPELCILDESDSGLDIDALKIVADGVNSLRD--GKRSFIIVTHYqriLDYIKPDYVH--VLYQGR 223
|
....*
gi 505962082 222 IQNQG 226
Cdd:PRK09580 224 IVKSG 228
|
|
| |
