|
Name |
Accession |
Description |
Interval |
E-value |
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-342 |
1.91e-142 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 407.18 E-value: 1.91e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGM 80
Cdd:COG3842 3 MPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDE 160
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 161 ALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFIVDATV 240
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 241 LNGIVRNGRvmCPDLDTSWDLDAVQAIDDIFDGDLVDIAIPPHSVDIGPAHHPDYIFAEITSVLFQVTSYSVTAKTQSGH 320
Cdd:COG3842 242 LPGTVLGDE--GGGVRTGGRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEGPENGLPGTVEDVVFLGSHVRYRVRLGDGQ 319
|
330 340
....*....|....*....|....*
gi 499323150 321 SFRMSIT---CSLPEIGETIGLSID 342
Cdd:COG3842 320 ELVVRVPnraALPLEPGDRVGLSWD 344
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-342 |
3.07e-124 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 360.93 E-value: 3.07e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGM 80
Cdd:COG3839 1 MASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDE 160
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 161 ALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFI----- 235
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIgsppm 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 236 --VDATVLNGIVRNGrvmcpdlDTSWDLDAVQAIDdifDGDLVDIAIPPHSVDIGPAHHPDyIFAEITSV---------L 304
Cdd:COG3839 240 nlLPGTVEGGGVRLG-------GVRLPLPAALAAA---AGGEVTLGIRPEHLRLADEGDGG-LEATVEVVeplgsetlvH 308
|
330 340 350
....*....|....*....|....*....|....*...
gi 499323150 305 FQVTSYSVTAKTQSGHSFRmsitcslpeIGETIGLSID 342
Cdd:COG3839 309 VRLGGQELVARVPGDTRLR---------PGDTVRLAFD 337
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-349 |
2.92e-109 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 322.48 E-value: 2.92e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFrdGTFG-LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGED-MTHVPPERRRMGM 80
Cdd:COG1118 2 SIEVRNISKRF--GSFTlLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlFTNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDE 160
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 161 ALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFIVDATV 240
Cdd:COG1118 160 PFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 241 LNGIVRNGRVMCPDldtsWDLDAVQAIDDifdgDLVDIAIPPHSVDIGPAHHPDYIF-AEITSVLFQVTSYSVTAKTQSG 319
Cdd:COG1118 240 LRGRVIGGQLEADG----LTLPVAEPLPD----GPAVAGVRPHDIEVSREPEGENTFpATVARVSELGPEVRVELKLEDG 311
|
330 340 350
....*....|....*....|....*....|....*..
gi 499323150 320 HSFRMSITCS-------LPEIGETIGLSIDNPMVYRA 349
Cdd:COG1118 312 EGQPLEAEVTkeawaelGLAPGDPVYLRPRPARVFLP 348
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-217 |
1.33e-102 |
|
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: 300.59 E-value: 1.33e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMVFQ 83
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALS 163
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499323150 164 ALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVA 217
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-235 |
4.74e-102 |
|
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: 299.92 E-value: 4.74e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMVFQ 83
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALS 163
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499323150 164 ALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFI 235
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-245 |
9.50e-94 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 284.15 E-value: 9.50e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMVFQ 83
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALS 163
Cdd:PRK09452 94 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 164 ALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFIVDATVLNG 243
Cdd:PRK09452 174 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDA 253
|
..
gi 499323150 244 IV 245
Cdd:PRK09452 254 TV 255
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-325 |
3.67e-92 |
|
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: 278.22 E-value: 3.67e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 35 LIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMVFQQHAVWPHMSVAKNVGYPLARSGQKGASISKR 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 115 VERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHD 194
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 195 RAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFIVDATVLNGIV----RNGRVMCPDLDTSWDLDAVQAIDdi 270
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVierkSEQVVLAGVEGRRCDIYTDVPVE-- 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 271 fDGDLVDIAIPPHSVDI---GPAHHPDYIFAEITSVLFQVTSYSVTAKTQSGHSFRMS 325
Cdd:TIGR01187 239 -KDQPLHVVLRPEKIVIeeeDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQKVLVS 295
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-217 |
1.03e-90 |
|
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: 270.67 E-value: 1.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMVFQ 83
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALS 163
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499323150 164 ALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVA 217
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-216 |
1.54e-87 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 264.26 E-value: 1.54e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFG---LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERrrmGM 80
Cdd:COG1116 8 LELRGVSKRFPTGGGGvtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR---GV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDE 160
Cdd:COG1116 85 VFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 161 ALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGN--GRIQQV 216
Cdd:COG1116 165 PFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-216 |
9.22e-86 |
|
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: 258.17 E-value: 9.22e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFG---LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERrrmGM 80
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR---GY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDE 160
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 161 ALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGN--GRIQQV 216
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-235 |
8.53e-85 |
|
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: 256.46 E-value: 8.53e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGMV 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVelRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLE--GFGSRRPASLSGGQRQRVALARAIIADPTVLLLD 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 160 EALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFI 235
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-235 |
1.77e-84 |
|
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: 255.73 E-value: 1.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFrdGTF-GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMV 81
Cdd:cd03296 2 SIEVRNVSKRF--GDFvALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQHAVWPHMSVAKNVGYPL----ARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLL 157
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 158 LDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFI 235
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-235 |
4.10e-80 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 248.60 E-value: 4.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGM 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDE 160
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 161 ALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFI 235
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFI 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-235 |
8.25e-80 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 248.02 E-value: 8.25e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGM 80
Cdd:PRK11000 1 MASVTLRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDE 160
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 161 ALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFI 235
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFI 234
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-235 |
3.20e-79 |
|
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: 241.86 E-value: 3.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDgtFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMVFQ 83
Cdd:cd03299 1 LKVENLSKDWKE--FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALS 163
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499323150 164 ALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFI 235
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-237 |
4.94e-78 |
|
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: 240.24 E-value: 4.94e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 17 TFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE------RRRMGMVFQQHAVWPH 90
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrRKKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 91 MSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLR 170
Cdd:cd03294 117 RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIR 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499323150 171 DALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFIVD 237
Cdd:cd03294 197 REMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG 263
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-250 |
5.83e-76 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 237.70 E-value: 5.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 6 LRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMVFQQH 85
Cdd:PRK11432 9 LKNITKRFGSNTV-IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 86 AVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSAL 165
Cdd:PRK11432 88 ALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 166 DEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFIVDATVLNGIV 245
Cdd:PRK11432 168 DANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPATL 247
|
....*
gi 499323150 246 RNGRV 250
Cdd:PRK11432 248 SGDYV 252
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
3-248 |
1.28e-75 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 237.20 E-value: 1.28e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFRDG---TFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTH-----VPPE 74
Cdd:NF040933 2 TVRVENVTKIFKKGkkeVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 75 RRRMGMVFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPT 154
Cdd:NF040933 82 DRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 155 VLLLDEALSALDEPLRDAlRRELV-SLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVAR 233
Cdd:NF040933 162 VLLLDEPFSNLDARIRDS-ARALVkKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250
....*....|....*
gi 499323150 234 FIVDATVLNGIVRNG 248
Cdd:NF040933 241 LIGDINLLEGKVEEE 255
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-226 |
6.60e-75 |
|
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: 231.02 E-value: 6.60e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-----RRRM 78
Cdd:COG1127 6 IEVRNLTKSFGDRVV-LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyelRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 79 GMVFQQHAVWPHMSVAKNVGYPL-ARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLL 157
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 158 LDEALSALDePLR-DALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:COG1127 165 YDEPTAGLD-PITsAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
4-248 |
1.03e-74 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 234.20 E-value: 1.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDgtFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMVFQ 83
Cdd:NF040840 2 IRIENLSKDWKE--FKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALS 163
Cdd:NF040840 80 NYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 164 ALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFIVDATVLNG 243
Cdd:NF040840 160 ALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEG 239
|
....*
gi 499323150 244 IVRNG 248
Cdd:NF040840 240 VAEKG 244
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-323 |
1.82e-74 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 234.73 E-value: 1.82e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMVFQ 83
Cdd:PRK11607 20 LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALS 163
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 164 ALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFIVDATVLNG 243
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 244 IVRNGRVMCPDLDTSWDLDAVQAIDD--IFDGDLVDIAIPPHSV---DIGPAHHPDYIFAEITSV--LFQVTSYSV---- 312
Cdd:PRK11607 259 VLKERQEDGLVIDSPGLVHPLKVDADasVVDNVPVHVALRPEKImlcEEPPADGCNFAVGEVIHIayLGDLSIYHVrlks 338
|
330
....*....|....*
gi 499323150 313 ----TAKTQSGHSFR 323
Cdd:PRK11607 339 gqmiSAQLQNAHRYR 353
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-226 |
2.46e-74 |
|
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: 229.14 E-value: 2.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGMV 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQhavwP-----HMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVL 156
Cdd:COG1122 81 FQN----PddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 157 LLDEALSALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-235 |
7.73e-74 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 228.10 E-value: 7.73e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFglqDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMVFQ 83
Cdd:COG3840 2 LRLDDLTYRYGDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALS 163
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 164 ALDePlrdALRRELVSL----TRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFI 235
Cdd:COG3840 159 ALD-P---ALRQEMLDLvdelCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-222 |
1.74e-72 |
|
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: 224.69 E-value: 1.74e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-----RRRM 78
Cdd:cd03261 1 IELRGLTKSFGGRTV-LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyrlRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 79 GMVFQQHAVWPHMSVAKNVGYPLARSGQKGAS-ISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLL 157
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPLREHTRLSEEeIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 158 LDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTEL 222
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-248 |
9.62e-72 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 226.89 E-value: 9.62e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMVF 82
Cdd:PRK10851 2 SIEIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QQHAVWPHMSVAKNVGYPLA----RSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLL 158
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTvlprRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 159 DEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFIVDA 238
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEV 240
|
250
....*....|
gi 499323150 239 TVLNGIVRNG 248
Cdd:PRK10851 241 NRLQGTIRGG 250
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-212 |
8.06e-69 |
|
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: 213.20 E-value: 8.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMT----HVPPERRRMG 79
Cdd:cd03229 1 LELKNVSKRYGQKTV-LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQHAVWPHMSVAKNVGYPlarsgqkgasiskrvertlalvglegfgsrrpasLSGGQRQRVALARAIIADPTVLLLD 159
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499323150 160 EALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGR 212
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-213 |
2.32e-68 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 213.75 E-value: 2.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSS-IKLRDLSVSFRDG---TFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-- 74
Cdd:COG1136 1 MSPlLELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 75 ----RRRMGMVFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAII 150
Cdd:COG1136 81 arlrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499323150 151 ADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDrAEAISIADRIVVLGNGRI 213
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-213 |
4.99e-67 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 210.04 E-value: 4.99e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDG---TFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE------ 74
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 75 RRRMGMVFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPT 154
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 155 VLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRaEAISIADRIVVLGNGRI 213
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-229 |
9.79e-67 |
|
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: 210.43 E-value: 9.79e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFG---LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRM 78
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKafRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 79 GMVFQQ--HAVWPHMSVAKNVGYPLARSGQKGasISKRVERTLALVGL-EGFGSRRPASLSGGQRQRVALARAIIADPTV 155
Cdd:COG1124 82 QMVFQDpyASLHPRHTVDRILAEPLRIHGLPD--REERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499323150 156 LLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATA 229
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
16-235 |
1.89e-66 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 213.56 E-value: 1.89e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 16 GTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPP------ERRRMGMVFQQHAVWP 89
Cdd:TIGR01186 5 GKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 90 HMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPL 169
Cdd:TIGR01186 85 HMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 170 RDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFI 235
Cdd:TIGR01186 165 RDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFI 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-226 |
3.65e-66 |
|
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: 217.08 E-value: 3.65e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFG----LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE----- 74
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 75 RRRMGMVFQ--QHAVWPHMSVAKNVGYPL-ARSGQKGASISKRVERTLALVGL-EGFGSRRPASLSGGQRQRVALARAII 150
Cdd:COG1123 341 RRRVQMVFQdpYSSLNPRMTVGDIIAEPLrLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 151 ADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-235 |
4.61e-66 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 208.31 E-value: 4.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrdGTFG-LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE----RRRM 78
Cdd:COG1126 2 IEIENLHKSF--GDLEvLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinklRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 79 GMVFQQHAVWPHMSVAKNVGYPLARS-GQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLL 157
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 158 LDEALSALDePlrdalrrELV--------SLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATA 229
Cdd:COG1126 160 FDEPTSALD-P-------ELVgevldvmrDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
....*.
gi 499323150 230 DVARFI 235
Cdd:COG1126 231 RTRAFL 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-235 |
7.59e-66 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 211.09 E-value: 7.59e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFR--DGTF-GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPP-----ER 75
Cdd:COG1135 2 IELENLSKTFPtkGGPVtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelraAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 76 RRMGMVFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTV 155
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 156 LLLDEALSALDeP---------LRDaLRRELvsltrreGLTTVHVTHDrAEAI-SIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:COG1135 162 LLCDEATSALD-PettrsildlLKD-INREL-------GLTIVLITHE-MDVVrRICDRVAVLENGRIVEQGPVLDVFAN 231
|
250
....*....|
gi 499323150 226 PATADVARFI 235
Cdd:COG1135 232 PQSELTRRFL 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-225 |
1.31e-65 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 207.22 E-value: 1.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDgTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-RRRMGMVF 82
Cdd:COG1131 1 IEVRGLTKRYGD-KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QQHAVWPHMSVAKNVGYpLAR-SGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEA 161
Cdd:COG1131 80 QEPALYPDLTVRENLRF-FARlYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499323150 162 LSALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:COG1131 159 TSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
8-245 |
5.84e-65 |
|
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: 209.57 E-value: 5.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 8 DLSVSFRDGTFGLqDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDM------THVPPERRRMGMV 81
Cdd:COG4148 4 EVDFRLRRGGFTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargIFLPPHRRRIGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQHAVWPHMSVAKNVGYPLARSGQKGASISkrVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEA 161
Cdd:COG4148 83 FQEARLFPHLSVRGNLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 162 LSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFIVDATVL 241
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVL 240
|
....
gi 499323150 242 NGIV 245
Cdd:COG4148 241 EATV 244
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-213 |
7.22e-65 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 206.25 E-value: 7.22e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSF---RDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERrr 77
Cdd:COG4525 1 MSMLTVRHVSVRYpggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 78 mGMVFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLL 157
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499323150 158 LDEALSALdeplrDALRRE-----LVSLTRREGLTTVHVTHDRAEAISIADRIVVL--GNGRI 213
Cdd:COG4525 158 MDEPFGAL-----DALTREqmqelLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRI 215
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-213 |
1.25e-64 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 204.91 E-value: 1.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 2 SSIKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-----RR 76
Cdd:COG3638 1 PMLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRalrrlRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 77 RMGMVFQQHAVWPHMSVAKNV-----GY-PLARSGqkgASISKRVERTLAL-----VGLEGFGSRRPASLSGGQRQRVAL 145
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVlagrlGRtSTWRSL---LGLFPPEDRERALealerVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499323150 146 ARAIIADPTVLLLDEALSALDePLR-----DALRRelvsLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:COG3638 158 ARALVQEPKLILADEPVASLD-PKTarqvmDLLRR----IAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-221 |
1.44e-64 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 204.13 E-value: 1.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-----RRRM 78
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipylRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 79 GMVFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLL 158
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 159 DEALSALDEplrdALRRELVSL---TRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTE 221
Cdd:COG2884 162 DEPTGNLDP----ETSWEIMELleeINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-215 |
5.01e-63 |
|
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: 199.83 E-value: 5.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIE---PEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGG------EDMTHVPPERRRMGMVFQQHAVWPH 90
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 91 MSVAKNVGYPLARSGQKgaSISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLR 170
Cdd:cd03297 90 LNVRENLAFGLKRKRNR--EDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499323150 171 DALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQ 215
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-226 |
8.28e-63 |
|
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: 199.73 E-value: 8.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFG---LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPP-----ER 75
Cdd:cd03258 2 IELKNVSKVFGDTGGKvtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelrkAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 76 RRMGMVFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTV 155
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499323150 156 LLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDrAEAI-SIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHE-MEVVkRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-212 |
2.85e-62 |
|
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: 197.69 E-value: 2.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 5 KLRDLSVSFRDG-TFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGMV 81
Cdd:cd03225 1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQhavwP-HM----SVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVL 156
Cdd:cd03225 81 FQN----PdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 157 LLDEALSALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGR 212
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-210 |
1.33e-61 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 196.16 E-value: 1.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSfRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEP---SSGSVLIGGEDMTHVPPERRRMG 79
Cdd:COG4136 1 MLSLENLTIT-LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQHAVWPHMSVAKNVGYPLARSGQKGASIsKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLD 159
Cdd:COG4136 80 ILFQDDLLFPHLSVGENLAFALPPTIGRAQRR-ARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499323150 160 EALSALDEPLRDALRRELVSLTRREGLTTVHVTHDrAEAISIADRIVVLGN 210
Cdd:COG4136 159 EPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD-EEDAPAAGRVLDLGN 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-253 |
4.09e-61 |
|
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: 196.42 E-value: 4.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSfRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPP-ER-RRMGMV 81
Cdd:COG1120 2 LEAENLSVG-YGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrELaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQHAVWPHMSVAKNVG---YP-LARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLL 157
Cdd:COG1120 81 PQEPPAPFGLTVRELVAlgrYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 158 LDEALSALDepLR------DALRRelvsLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADV 231
Cdd:COG1120 161 LDEPTSHLD--LAhqlevlELLRR----LARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEV 234
|
250 260
....*....|....*....|..
gi 499323150 232 arFIVDATVLNGIVRNGRVMCP 253
Cdd:COG1120 235 --YGVEARVIEDPVTGRPLVLP 254
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-213 |
1.07e-60 |
|
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: 193.90 E-value: 1.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrdGTFG-LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE----RRRM 78
Cdd:cd03262 1 IEIKNLHKSF--GDFHvLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 79 GMVFQQHAVWPHMSVAKNVGY-PLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLL 157
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 158 LDEALSALDEPLRDALRRELVSLTrREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-213 |
1.48e-60 |
|
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: 194.32 E-value: 1.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-----RRRM 78
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 79 GMVFQQHAVWPHMSVAKNVgyPLARSGQKGA--SISKRV---ERTLAL-----VGLEGFGSRRPASLSGGQRQRVALARA 148
Cdd:cd03256 81 GMIFQQFNLIERLSVLENV--LSGRLGRRSTwrSLFGLFpkeEKQRALaalerVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 149 IIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-213 |
2.53e-58 |
|
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: 187.70 E-value: 2.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDlsVSFRDGTFGLqDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMVFQ 83
Cdd:cd03298 1 VRLDK--IRFSYGEQPM-HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALS 163
Cdd:cd03298 78 ENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499323150 164 ALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-222 |
7.59e-58 |
|
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: 187.00 E-value: 7.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTfGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVE-----PSSGSVLIGGEDMTHVPPE---- 74
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 75 RRRMGMVFQQHAVWPhMSVAKNVGYPLARSGQKG-ASISKRVERTLALVGLEGFGSRR--PASLSGGQRQRVALARAIIA 151
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLkEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 152 DPTVLLLDEALSALD-------EPLRDALRRElvsltrregLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTEL 222
Cdd:cd03260 159 EPEVLLLDEPTSALDpistakiEELIAELKKE---------YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-213 |
1.22e-57 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 185.79 E-value: 1.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGMV 81
Cdd:COG4619 1 LELEGLSFRVGGKPI-LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPewRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQhAVWPHMSVAKNVGYPLARSGQKGASisKRVERTLALVGL-EGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDE 160
Cdd:COG4619 80 PQE-PALWGGTVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499323150 161 ALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-238 |
2.14e-57 |
|
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: 186.22 E-value: 2.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGtFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-RRRMGMVF 82
Cdd:COG4555 2 IEVENLSKKYGKV-PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEAL 162
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 163 SALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFIVDA 238
Cdd:COG4555 161 NGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVAL 235
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-213 |
1.20e-56 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 183.86 E-value: 1.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFG---LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-----R 75
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 76 RRMGMVFQ--QHAVWPHMSVAKNVGYPL--ARSGQKGASISKRVERTLALVGL-EGFGSRRPASLSGGQRQRVALARAII 150
Cdd:cd03257 82 KEIQMVFQdpMSSLNPRMTIGEQIAEPLriHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499323150 151 ADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-225 |
2.33e-56 |
|
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: 192.28 E-value: 2.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 2 SSIKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMG 79
Cdd:COG4988 335 PSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVfQQHAVWPHMSVAKNVgyplaRSGQKGASISkRVERTLALVGLEGFGSRRP-----------ASLSGGQRQRVALARA 148
Cdd:COG4988 415 WV-PQNPYLFAGTIRENL-----RLGRPDASDE-ELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499323150 149 IIADPTVLLLDEALSALDEPLRDALRRELVSLTRreGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITH-RLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-225 |
2.72e-55 |
|
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: 191.97 E-value: 2.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDlsVSFR---DGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRR 77
Cdd:COG2274 473 DIELEN--VSFRypgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAslRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 78 MGMVFQQHAVWpHMSVAKNVgyplaRSGQKGASIsKRVERTLALVGLEGFGSRRP-----------ASLSGGQRQRVALA 146
Cdd:COG2274 551 IGVVLQDVFLF-SGTIRENI-----TLGDPDATD-EEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 147 RAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRreGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAH-RLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-227 |
1.90e-54 |
|
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: 186.26 E-value: 1.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGT-FGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPS---SGSVLIGGEDMTHVPPERR--R 77
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 78 MGMVFQ--QHAVWPhMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTV 155
Cdd:COG1123 85 IGMVFQdpMTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499323150 156 LLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPA 227
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-225 |
3.00e-54 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 178.36 E-value: 3.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVppeRRRMGM 80
Cdd:COG1121 4 MPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA---RRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAV---WPhMSVAKNVGypLARSGQKG------ASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIA 151
Cdd:COG1121 80 VPQRAEVdwdFP-ITVRDVVL--MGRYGRRGlfrrpsRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 152 DPTVLLLDEALSALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRI-----QQVATPTELLSA 225
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLVahgppEEVLTPENLSRA 234
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-229 |
2.33e-53 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 175.54 E-value: 2.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 24 NLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMVFQQHAVWPHMSVAKNVGYPLAR 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 104 SGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDePlrdALRRELVSLT-- 181
Cdd:PRK10771 99 GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD-P---ALRQEMLTLVsq 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499323150 182 --RREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLS--APATA 229
Cdd:PRK10771 175 vcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSgkASASA 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-225 |
3.89e-53 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 184.21 E-value: 3.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGM 80
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLEslRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWpHMSVAKNVGYplarsGQKGASiSKRVERTLALVGLEGFGSRRP-----------ASLSGGQRQRVALARAI 149
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRY-----GRPDAT-DEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 150 IADPTVLLLDEALSALD----EPLRDALRRElvsltrREGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:COG1132 492 LKDPPILILDEATSALDteteALIQEALERL------MKGRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-235 |
9.10e-53 |
|
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: 174.41 E-value: 9.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-----RRRM 78
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrklRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 79 GMVFQQHAVWPHMSVAKNVGYP-LARSG--QKGASISKRVERTLAL-----VGLEGFGSRRPASLSGGQRQRVALARAII 150
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGrLGYKPtwRSLLGRFSEEDKERALsalerVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 151 ADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELlsapaTAD 230
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL-----DDE 236
|
....*
gi 499323150 231 VARFI 235
Cdd:TIGR02315 237 VLRHI 241
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-227 |
1.94e-52 |
|
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: 173.39 E-value: 1.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPP-ERRRMGMV- 81
Cdd:cd03219 1 LEVRGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPhEIARLGIGr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 -FQQHAVWPHMSVAKNV----------GYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAII 150
Cdd:cd03219 80 tFQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499323150 151 ADPTVLLLDEALSALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPA 227
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-235 |
3.92e-52 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 172.58 E-value: 3.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDM----THVPPERRRMG 79
Cdd:PRK09493 2 IEFKNVSKHFGPTQV-LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpkVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQHAVWPHMSVAKNVGY-PLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLL 158
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499323150 159 DEALSALDEPLRDALRRELVSLTrREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFI 235
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
9-233 |
4.08e-52 |
|
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: 176.07 E-value: 4.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 9 LSVSFRDGTFGLqDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDM------THVPPERRRMGMVF 82
Cdd:TIGR02142 3 ARFSKRLGDFSL-DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkgIFLPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QQHAVWPHMSVAKNVGYPLARSgqKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEAL 162
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMKRA--RPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499323150 163 SALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVAR 233
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAR 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-213 |
1.15e-51 |
|
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: 169.12 E-value: 1.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTfGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-RRRMGMVF 82
Cdd:cd03230 1 IEVRNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QQHAVWPHMSVAKNVgyplarsgqkgasiskrvertlalvglegfgsrrpaSLSGGQRQRVALARAIIADPTVLLLDEAL 162
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499323150 163 SALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:cd03230 124 SGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
15-215 |
1.45e-51 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 171.81 E-value: 1.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 15 DGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERrrmGMVFQQHAVWPHMSVA 94
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---GVVFQNEGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 95 KNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALR 174
Cdd:PRK11248 89 DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499323150 175 RELVSLTRREGLTTVHVTHDRAEAISIADRIVVL--GNGRIQQ 215
Cdd:PRK11248 169 TLLLKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVE 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-212 |
2.45e-51 |
|
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: 168.33 E-value: 2.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDG-TFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGM 80
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEslRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWpHMSVAKNVgyplarsgqkgasiskrvertlalvglegfgsrrpasLSGGQRQRVALARAIIADPTVLLLDE 160
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499323150 161 ALSALDEPLRDALRRELvsLTRREGLTTVHVTHdRAEAISIADRIVVLGNGR 212
Cdd:cd03228 123 ATSALDPETEALILEAL--RALAKGKTVIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-216 |
2.89e-51 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 169.66 E-value: 2.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 24 NLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMVFQQHAVWPHMSVAKNVGYPLAR 103
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 104 SGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRR 183
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|...
gi 499323150 184 EGLTTVHVTHDRAEAISIADRIVVLGNGRIQQV 216
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-224 |
3.38e-51 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 171.07 E-value: 3.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGT-FGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDM---THVPPERRRMG 79
Cdd:TIGR04520 1 IEVENVSFSYPESEkPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQhavwPH-----MSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPT 154
Cdd:TIGR04520 81 MVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 155 VLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISiADRIVVLGNGRIQQVATPTELLS 224
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFS 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-213 |
1.11e-50 |
|
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: 166.84 E-value: 1.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 5 KLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHvpperrrmgmvfqq 84
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 85 havWPHMSVAKNVGYplarsgqkgasiskrVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSA 164
Cdd:cd03214 66 ---LSPKELARKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499323150 165 LDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:cd03214 128 LDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-227 |
1.80e-50 |
|
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: 168.68 E-value: 1.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFrdGtfGLQ---DINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERR- 76
Cdd:COG0411 2 DPLLEVRGLTKRF--G--GLVavdDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 77 RMGMV--FQQHAVWPHMSVAKNV---------------GYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQ 139
Cdd:COG0411 78 RLGIArtFQNPRLFPELTVLENVlvaaharlgrgllaaLLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 140 RQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATP 219
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
....*...
gi 499323150 220 TELLSAPA 227
Cdd:COG0411 238 AEVRADPR 245
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-235 |
2.55e-50 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 171.14 E-value: 2.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFG---LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPP-----ER 75
Cdd:PRK11153 2 IELKNISKVFPQGGRTihaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrkAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 76 RRMGMVFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTV 155
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 156 LLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFI 235
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFI 241
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-234 |
2.40e-48 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 167.52 E-value: 2.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 17 TFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPP------ERRRMGMVFQQHAVWPH 90
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevRRKKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 91 MSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLR 170
Cdd:PRK10070 121 MTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499323150 171 DALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARF 234
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-212 |
5.70e-48 |
|
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: 158.95 E-value: 5.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 5 KLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGMVF 82
Cdd:cd00267 1 EIENLSFRYGGRTA-LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEelRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QqhavwphmsvaknvgyplarsgqkgasiskrvertlalvglegfgsrrpasLSGGQRQRVALARAIIADPTVLLLDEAL 162
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499323150 163 SALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGR 212
Cdd:cd00267 109 SGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-211 |
1.85e-47 |
|
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: 160.32 E-value: 1.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRrmgMVFQQHAVWPHMSVAKNVGY 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---VVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 100 PLARSGQKGASISKR--VERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRREL 177
Cdd:TIGR01184 78 AVDRVLPDLSKSERRaiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190
....*....|....*....|....*....|....
gi 499323150 178 VSLTRREGLTTVHVTHDRAEAISIADRIVVLGNG 211
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-221 |
4.89e-47 |
|
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: 159.14 E-value: 4.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTfG----LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE----- 74
Cdd:COG4181 9 IELRGLTKTVGTGA-GeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDararl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 75 -RRRMGMVFQQHAVWPHMSVAKNVGYPLARSGQKGAsiSKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADP 153
Cdd:COG4181 88 rARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDA--RARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 154 TVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAiSIADRIVVLGNGRIQQVATPTE 221
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAATA 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-227 |
1.10e-46 |
|
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: 166.48 E-value: 1.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFRDGTFG-LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMG 79
Cdd:COG4987 333 SLELEDVSFRYPGAGRPvLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDdlRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQHAVWpHMSVAKNVGypLARSgqkGASiSKRVERTLALVGLEGFGSRRP-----------ASLSGGQRQRVALARA 148
Cdd:COG4987 413 VVPQRPHLF-DTTLRENLR--LARP---DAT-DEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 149 IIADPTVLLLDEALSALDEPLRDALRRELvsLTRREGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLSAPA 227
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLADL--LEALAGRTVLLITH-RLAGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-163 |
1.21e-46 |
|
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: 155.50 E-value: 1.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTH--VPPERRRMGMVFQQHAVWPHMSVAKNV 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 98 GYPLARSGQKGASISKRVERTLALVGLEGFGSRR----PASLSGGQRQRVALARAIIADPTVLLLDEALS 163
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-213 |
1.44e-46 |
|
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: 157.31 E-value: 1.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 5 KLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEdmtHVPPERRRMGMVFQQ 84
Cdd:cd03235 1 EVEDLTVSYGGHPV-LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 85 HAV---WPhMSVAKNVGypLARSGQKGA--SISK----RVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTV 155
Cdd:cd03235 77 RSIdrdFP-ISVRDVVL--MGLYGHKGLfrRLSKadkaKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 156 LLLDEALSALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLgNGRI 213
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLL-NRTV 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-213 |
1.78e-46 |
|
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: 157.18 E-value: 1.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTH-----VPPERRRM 78
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 79 GMVFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLL 158
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 159 DEALSALDEPLRDALRRELVSLTRReGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-235 |
2.12e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 157.87 E-value: 2.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFrdGTF-GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGE--DMTHVPPE----- 74
Cdd:COG4161 2 SIQLKNINCFY--GSHqALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEkairl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 75 -RRRMGMVFQQHAVWPHMSVAKN-VGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIAD 152
Cdd:COG4161 80 lRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 153 PTVLLLDEALSALDePlrdALRRELVSLTR---REGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATpTELLSAPATA 229
Cdd:COG4161 160 PQVLLFDEPTAALD-P---EITAQVVEIIRelsQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTE 234
|
....*.
gi 499323150 230 DVARFI 235
Cdd:COG4161 235 AFAHYL 240
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-213 |
7.84e-46 |
|
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: 155.60 E-value: 7.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFGLQ---DINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-RRRMG 79
Cdd:cd03266 2 ITADALTKRFRDVKKTVQavdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEaRRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLD 159
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499323150 160 EALSALDEPLRDALrRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:cd03266 162 EPTTGLDVMATRAL-REFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-224 |
3.29e-45 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 154.13 E-value: 3.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERR-RMGMVF--QQHAVWPHMSVAKN 96
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaRAGIGYvpEGRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 97 VgyPLARSGQKGASISKRVERTLALV-GLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRR 175
Cdd:cd03224 96 L--LLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499323150 176 ELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:cd03224 174 AIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
3-221 |
6.42e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 155.59 E-value: 6.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFRDGT-F---GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMT----HVPPE 74
Cdd:PRK13637 2 SIKIENLTHIYMEGTpFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 75 RRRMGMVFQ--QHAVWPHmSVAKNVGYPLARSGQKGASISKRVERTLALVGL--EGFGSRRPASLSGGQRQRVALARAII 150
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499323150 151 ADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTE 221
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-227 |
1.10e-44 |
|
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: 153.21 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERR-RMG 79
Cdd:COG0410 1 MPMLEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVF--QQHAVWPHMSVAKN--VGyplARSGQKGASISKRVERTLAL--VgLEGFGSRRPASLSGGQRQRVALARAIIADP 153
Cdd:COG0410 80 IGYvpEGRRIFPSLTVEENllLG---AYARRDRAEVRADLERVYELfpR-LKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499323150 154 TVLLLDEA---LSALdepLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPA 227
Cdd:COG0410 156 KLLLLDEPslgLAPL---IVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-235 |
1.28e-44 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 153.25 E-value: 1.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGE--DMTHVPPE------RRRMGMVFQQHAVWPHM 91
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDkairelRRNVGMVFQQYNLWPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 92 SVAKN-VGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDePLR 170
Cdd:PRK11124 98 TVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD-PEI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 171 DAlrrELVSLTR---REGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTElLSAPATADVARFI 235
Cdd:PRK11124 177 TA---QIVSIIRelaETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFKNYL 240
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-231 |
1.54e-44 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 153.39 E-value: 1.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSfRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPER--RRMGM 80
Cdd:PRK13548 2 MLEARNLSVR-LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWPHMSVAKNVG---YPLARSGQKGASIskrVERTLALVGLEGFGSRRPASLSGGQRQRVALARAII------A 151
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAmgrAPHGLSRAEDDAL---VAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 152 DPTVLLLDEALSALD----EPLRDALRRelvsLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPA 227
Cdd:PRK13548 158 PPRWLLLDEPTSALDlahqHHVLRLARQ----LAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPET 233
|
....
gi 499323150 228 TADV 231
Cdd:PRK13548 234 LRRV 237
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-212 |
1.87e-44 |
|
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: 151.48 E-value: 1.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSfRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-RRRMGMVF 82
Cdd:COG4133 3 LEAENLSCR-RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QQHAVWPHMSVAKNVGYpLARsgQKGASISK-RVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEA 161
Cdd:COG4133 82 HADGLKPELTVRENLRF-WAA--LYGLRADReAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499323150 162 LSALDEPLRDALrRELVSLTRREGLTTVHVTHDRAEAisIADRIVVLGNGR 212
Cdd:COG4133 159 FTALDAAGVALL-AELIAAHLARGGAVLLTTHQPLEL--AAARVLDLGDFK 206
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-215 |
5.49e-44 |
|
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: 150.42 E-value: 5.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTfGLQDINLKIEPEEFVvLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-RRRMGMVF 82
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEAL 162
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499323150 163 SALDEPLRDALRRELVSLTrrEGLTTVHVTHDRAEAISIADRIVVLGNGRIQQ 215
Cdd:cd03264 159 AGLDPEERIRFRNLLSELG--EDRIVILSTHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-227 |
9.46e-44 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 153.29 E-value: 9.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSF--RDGTF-GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEP---SSGSVLIGGEDMTHVPPER-- 75
Cdd:COG0444 2 LEVRNLKVYFptRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 76 ----RRMGMVFQ--QHAVWPHMSVAKNVGYPLARSGQ-KGASISKRVERTLALVGL---EGFGSRRPASLSGGQRQRVAL 145
Cdd:COG0444 82 kirgREIQMIFQdpMTSLNPVMTVGDQIAEPLRIHGGlSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 146 ARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFEN 241
|
..
gi 499323150 226 PA 227
Cdd:COG0444 242 PR 243
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-213 |
2.58e-43 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 150.21 E-value: 2.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 6 LRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMgmvFQQH 85
Cdd:PRK11247 15 LNAVSKRYGERTV-LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLM---FQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 86 AVWPHMSVAKNVGYplarsGQKGaSISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSAL 165
Cdd:PRK11247 91 RLLPWKKVIDNVGL-----GLKG-QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499323150 166 DEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:PRK11247 165 DALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-224 |
4.99e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 150.27 E-value: 4.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFRDGT--FGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMT--HVPPERR 76
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 77 RMGMVFQQhavwPH-----MSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIA 151
Cdd:PRK13650 82 KIGMVFQN----PDnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499323150 152 DPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEaISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-227 |
7.56e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 151.04 E-value: 7.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSF--RDGTFG--------LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPP 73
Cdd:COG4608 8 LEVRDLKKHFpvRGGLFGrtvgvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 74 E-----RRRMGMVFQ--QHAVWPHMSVAKNVGYPLARSGQK-GASISKRVERTLALVGL-EGFGSRRPASLSGGQRQRVA 144
Cdd:COG4608 88 RelrplRRRMQMVFQdpYASLNPRMTVGDIIAEPLRIHGLAsKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 145 LARAIIADPTVLLLDEALSALDEP--------LRDaLRRELvsltrreGLTTVHVTHDRAEAISIADRIVVLGNGRIQQV 216
Cdd:COG4608 168 IARALALNPKLIVCDEPVSALDVSiqaqvlnlLED-LQDEL-------GLTYLFISHDLSVVRHISDRVAVMYLGKIVEI 239
|
250
....*....|.
gi 499323150 217 ATPTELLSAPA 227
Cdd:COG4608 240 APRDELYARPL 250
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-213 |
1.27e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 148.70 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGT----FGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERR--R 77
Cdd:COG1101 2 LELKNLSKTFNPGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 78 MGMVFQ--QHAVWPHMSVAKNVGYPLARSGQKGASIS---KRVER---TLALVGLeGFGSR---RPASLSGGQRQRVALA 146
Cdd:COG1101 82 IGRVFQdpMMGTAPSMTIEENLALAYRRGKRRGLRRGltkKRRELfreLLATLGL-GLENRldtKVGLLSGGQRQALSLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499323150 147 RAIIADPTVLLLDEALSALDePLRDA----LRRELVsltRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALD-PKTAAlvleLTEKIV---EENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
20-235 |
2.30e-42 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 148.02 E-value: 2.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGE---------------DMTHVPPERRRMGMVFQQ 84
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlkpdrdgelvpaDRRQLQRIRTRLGMVFQS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 85 HAVWPHMSVAKNV-GYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALS 163
Cdd:COG4598 104 FNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTS 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 164 ALD-EPLRDALR--RELVsltrREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFI 235
Cdd:COG4598 184 ALDpELVGEVLKvmRDLA----EEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFL 254
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-231 |
5.09e-42 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 146.80 E-value: 5.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSfRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERR-RMGMVF 82
Cdd:COG4559 2 LEAENLSVR-LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELaRRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QQHAvwpHMS----VAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAII-------A 151
Cdd:COG4559 81 PQHS---SLAfpftVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 152 DPTVLLLDEALSALDEPLRDALRRELVSLTRReGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADV 231
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERV 236
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-213 |
9.75e-42 |
|
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: 144.67 E-value: 9.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMVFQ 83
Cdd:cd03268 1 LKTNDLTKTYGKKRV-LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHAVWPHMSVAKNVGYplarsGQKGASIS-KRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEAL 162
Cdd:cd03268 80 APGFYPNLTARENLRL-----LARLLGIRkKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499323150 163 SALDePLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:cd03268 155 NGLD-PDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-230 |
1.20e-41 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 145.95 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 2 SSIKLRDLSVSFrdGTF-GLQDINLKIEPEEFVVLIGPSGSGKTTMLRT-------IAGF-VEpssGSVLIGGEDM--TH 70
Cdd:COG1117 10 PKIEVRNLNVYY--GDKqALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGArVE---GEILLDGEDIydPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 71 VPPE--RRRMGMVFQQHAVWPhMSVAKNVGYPLARSGQKGAS-ISKRVERTLALVG--------LegfgsRRPA-SLSGG 138
Cdd:COG1117 85 VDVVelRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSeLDEIVEESLRKAAlwdevkdrL-----KKSAlGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 139 QRQRVALARAIIADPTVLLLDEALSALD-------EPLRDALRRElvsltrregLTTVHVTHDRAEAISIADRIVVLGNG 211
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDpistakiEELILELKKD---------YTIVIVTHNMQQAARVSDYTAFFYLG 229
|
250 260
....*....|....*....|..
gi 499323150 212 RIQQVATPTELLSAPA---TAD 230
Cdd:COG1117 230 ELVEFGPTEQIFTNPKdkrTED 251
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-224 |
2.98e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 145.54 E-value: 2.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFR---DGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTH--VPPER 75
Cdd:PRK13635 1 MKEEIIRVEHISFRypdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 76 RRMGMVFQQhavwPH-----MSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAII 150
Cdd:PRK13635 81 RQVGMVFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 151 ADPTVLLLDEALSALDEplrdALRRELVSLTRR----EGLTTVHVTHDRAEAISiADRIVVLGNGRIQQVATPTELLS 224
Cdd:PRK13635 157 LQPDIIILDEATSMLDP----RGRREVLETVRQlkeqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-225 |
3.13e-41 |
|
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: 144.30 E-value: 3.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 11 VSFRDGTFG--------LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHV--PPERRRMGM 80
Cdd:cd03251 1 VEFKNVTFRypgdgppvLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYtlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VfQQHAVWPHMSVAKNVGYplarsGQKGASiSKRVERTLALVGL--------EGFGSR---RPASLSGGQRQRVALARAI 149
Cdd:cd03251 81 V-SQDVFLFNDTVAENIAY-----GRPGAT-REEVEEAARAANAhefimelpEGYDTVigeRGVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 150 IADPTVLLLDEALSALDEPLRDALRRELVSLTrrEGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLM--KNRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-226 |
3.75e-41 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 144.51 E-value: 3.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIG----------GEDMTH 70
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTV-LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtarslSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 71 VPPERRRMGMVFQQHAVWPHMSVAKNV--GyPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARA 148
Cdd:PRK11264 80 IRQLRQHVGFVFQNFNLFPHRTVLENIieG-PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 149 IIADPTVLLLDEALSALDEPLRDALRRELVSLTrREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLA-QEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-224 |
1.67e-40 |
|
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: 142.37 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGMV 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDslRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQHAVWpHMSVAKNVGY--PLARSGQ-----KGASISKRVERTlalvgLEGFGSR---RPASLSGGQRQRVALARAIIA 151
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYgrPDATDEEvieaaKAAQIHDKIMRF-----PDGYDTIvgeRGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499323150 152 DPTVLLLDEALSALDEPLRDALRRELVSLTRreGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAH-RLSTIVNADKIIVLKDGRIVERGTHEELLA 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-222 |
2.66e-40 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 141.10 E-value: 2.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTF-GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDM-THVPPERRRMGMV 81
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQHAVWPHMSVAKNVgYPLAR-SGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDE 160
Cdd:cd03263 81 PQFDALFDELTVREHL-RFYARlKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499323150 161 ALSALDEplrdALRRELVSLTR--REGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTEL 222
Cdd:cd03263 160 PTSGLDP----ASRRAIWDLILevRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-224 |
3.63e-40 |
|
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: 141.52 E-value: 3.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGMVFQQHAVWPhMSVAKNV 97
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwlRSQIGLVSQEPVLFD-GTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 98 GYplarsGQKGASiSKRVERTLALVGLEGFGSRRP-----------ASLSGGQRQRVALARAIIADPTVLLLDEALSALD 166
Cdd:cd03249 98 RY-----GKPDAT-DEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499323150 167 ----EPLRDALRRelvsltRREGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:cd03249 172 aeseKLVQEALDR------AMKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMA 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-213 |
7.17e-40 |
|
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: 140.03 E-value: 7.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGMVfQQHAVWPHMSVAKNV 97
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYV-PQDVTLFYGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 98 --GYPLARsgqkgasiSKRVERTLALVGLEGFGSRRP-----------ASLSGGQRQRVALARAIIADPTVLLLDEALSA 164
Cdd:cd03245 99 tlGAPLAD--------DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499323150 165 LD----EPLRDALRRELvsltrrEGLTTVHVTHdRAEAISIADRIVVLGNGRI 213
Cdd:cd03245 171 MDmnseERLKERLRQLL------GDKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-213 |
9.59e-40 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 140.01 E-value: 9.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMT-----HVPPERRRM 78
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 79 GMVFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLL 158
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 159 DEALSALDEPLRDALRReLVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:PRK10908 162 DEPTGNLDDALSEGILR-LFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-223 |
1.09e-39 |
|
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: 140.05 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGMV 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKslRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQHAVWPHmSVAKNV--GYPLARsgqkgasiSKRVERTLALVGLEGFGSRRP-----------ASLSGGQRQRVALARA 148
Cdd:cd03254 83 LQDTFLFSG-TIMENIrlGRPNAT--------DEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 149 IIADPTVLLLDEALSALD----EPLRDALRRelvsltRREGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELL 223
Cdd:cd03254 154 MLRDPKILILDEATSNIDteteKLIQEALEK------LMKGRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-225 |
2.79e-39 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 139.45 E-value: 2.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSfRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLI------GGEDMTHVppeRRR 77
Cdd:COG1119 4 LELRNVTVR-RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerrGGEDVWEL---RKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 78 MGMV--FQQHAVWPHMSVAKNVgyplaRSGqKGASI----------SKRVERTLALVGLEGFGSRRPASLSGGQRQRVAL 145
Cdd:COG1119 80 IGLVspALQLRFPRDETVLDVV-----LSG-FFDSIglyreptdeqRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 146 ARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTS 233
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
15-222 |
2.82e-39 |
|
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: 138.66 E-value: 2.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 15 DGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-RRRMGMVFQQHAVWPHMSV 93
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 94 AKNVgYPLAR-SGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDA 172
Cdd:cd03265 91 WENL-YIHARlYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499323150 173 LRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTEL 222
Cdd:cd03265 170 VWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
11-226 |
6.30e-39 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 138.81 E-value: 6.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 11 VSFRDGT--FG----LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE---------- 74
Cdd:TIGR03005 1 VRFSDVTkrFGiltvLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRngplvpadek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 75 -----RRRMGMVFQQHAVWPHMSVAKNVGY-PLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARA 148
Cdd:TIGR03005 81 hlrqmRNKIGMVFQSFNLFPHKTVLDNVTEaPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 149 IIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQP 238
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-227 |
1.44e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 139.00 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGT-F---GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIG------GEDMTHVPP 73
Cdd:PRK13634 3 ITFQKVEHRYQYKTpFerrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 74 ERRRMGMVFQ--QHAVWPHmSVAKNVGYPLARSGQKGASISKRVERTLALVGL-EGFGSRRPASLSGGQRQRVALARAII 150
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499323150 151 ADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPA 227
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-231 |
1.55e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 138.20 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGG---EDMTHVPPERRRMGM 80
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQhavwPHMS-VAKNVGYPLARSGQK----GASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTV 155
Cdd:PRK13644 82 VFQN----PETQfVGRTVEEDLAFGPENlclpPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 156 LLLDEALSALDEPLRDALRRELVSLtRREGLTTVHVTHDrAEAISIADRIVVLGNGRIQQVATPTELLSAPATADV 231
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-225 |
2.28e-38 |
|
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: 136.85 E-value: 2.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 11 VSFR---DGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGMVFQQH 85
Cdd:cd03252 6 VRFRykpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 86 AVWpHMSVAKNVGyplarSGQKGASIsKRVERTLALVGLEGFGSRRP-----------ASLSGGQRQRVALARAIIADPT 154
Cdd:cd03252 86 VLF-NRSIRDNIA-----LADPGMSM-ERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499323150 155 VLLLDEALSALDEPLRDALRRELVSLTrrEGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-224 |
3.07e-38 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 137.24 E-value: 3.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 2 SSIKLRDLSVSFRDGTFG--------LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPP 73
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGGLFgakqrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 74 E-----RRRMGMVFQQ--HAVWPHMSVAKNVGYPLARsgQKGASISKRVERTLALVGLEGFGS----RRPASLSGGQRQR 142
Cdd:TIGR02769 81 KqrrafRRDVQLVFQDspSAVNPRMTVRQIIGEPLRH--LTSLDESEQKARIAELLDMVGLRSedadKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 143 VALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTEL 222
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQL 238
|
..
gi 499323150 223 LS 224
Cdd:TIGR02769 239 LS 240
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-229 |
3.27e-38 |
|
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: 142.90 E-value: 3.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSF--RDGTFG--------LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVePSSGSVLIGGEDMTHVP- 72
Cdd:COG4172 276 LEARDLKVWFpiKRGLFRrtvghvkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 73 ----PERRRMGMVFQQ--HAVWPHMSVAKNVGYPLA--RSGQKGASISKRVERTLALVGL-EGFGSRRPASLSGGQRQRV 143
Cdd:COG4172 355 ralrPLRRRMQVVFQDpfGSLSPRMTVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 144 ALARAIIADPTVLLLDEALSALD--------EPLRDalrrelvsLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQ 215
Cdd:COG4172 435 AIARALILEPKLLVLDEPTSALDvsvqaqilDLLRD--------LQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
250
....*....|....
gi 499323150 216 VATPTELLSAPATA 229
Cdd:COG4172 507 QGPTEQVFDAPQHP 520
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-225 |
1.43e-37 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 141.78 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFR-DGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGM 80
Cdd:TIGR02203 331 VEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAslRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VfQQHAVWPHMSVAKNVGYplarsGQKGASISKRVERTLALVGLEGFGSRRP-----------ASLSGGQRQRVALARAI 149
Cdd:TIGR02203 411 V-SQDVVLFNDTIANNIAY-----GRTEQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 150 IADPTVLLLDEALSALD-EPLR---DALRRELvsltrrEGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:TIGR02203 485 LKDAPILILDEATSALDnESERlvqAALERLM------QGRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-208 |
1.53e-37 |
|
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: 140.88 E-value: 1.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 2 SSIKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMG 79
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQhavwPHM---SVAKNVGypLARSGQKGASIskrvERTLALVGLEGFGSRRP-----------ASLSGGQRQRVAL 145
Cdd:TIGR02857 400 WVPQH----PFLfagTIAENIR--LARPDASDAEI----REALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499323150 146 ARAIIADPTVLLLDEALSALDEPLRDALRRELVSLtrREGLTTVHVTHDRAEAISiADRIVVL 208
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-232 |
1.78e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 135.59 E-value: 1.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGE----DMTHVPPERRRMG 79
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikyDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQ---HAVWPhmSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVL 156
Cdd:PRK13639 82 IVFQNpddQLFAP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 157 LLDEALSALDEPLRDALRRELVSLTrREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVA 232
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKA 234
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-213 |
2.33e-37 |
|
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: 133.15 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 8 DLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDmTHVPPERRRMGMVFQqhav 87
Cdd:cd03226 4 NISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP-IKAKERRKSIGYVMQ---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 88 wphmsvakNVGYPLARS--------GQKGASISK-RVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLL 158
Cdd:cd03226 79 --------DVDYQLFTDsvreelllGLKELDAGNeQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499323150 159 DEALSALDeplRDALRR--ELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:cd03226 151 DEPTSGLD---YKNMERvgELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-213 |
4.48e-37 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 136.54 E-value: 4.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 22 DINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGG------EDMTHVPPERRRMGMVFQQHAVWPHMSVAK 95
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaEKGICLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 96 NVGYPLARSGQkgASISKRVErtlaLVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPlRdalRR 175
Cdd:PRK11144 96 NLRYGMAKSMV--AQFDKIVA----LLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP-R---KR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499323150 176 ELVS----LTRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:PRK11144 166 ELLPylerLAREINIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-252 |
8.49e-37 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 133.22 E-value: 8.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 2 SSIKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPER--RRMG 79
Cdd:PRK11231 1 MTLRTENLTVGYGTKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQHAVWPHMSVAKNVGYplARS------GQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADP 153
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAY--GRSpwlslwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 154 TVLLLDEALSALDeplrdaLRR--ELVSLTRR---EGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPAT 228
Cdd:PRK11231 158 PVVLLDEPTTYLD------INHqvELMRLMRElntQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLL 231
|
250 260
....*....|....*....|....
gi 499323150 229 ADVarFIVDATVLNGIVrNGRVMC 252
Cdd:PRK11231 232 RTV--FDVEAEIHPEPV-SGTPMC 252
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
20-235 |
1.28e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 132.79 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE---------------RRRMGMVFQQ 84
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrllRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 85 HAVWPHMSVAKNV-GYPLARSGQKGASISKRVERTLALVGLEGFGSRR-PASLSGGQRQRVALARAIIADPTVLLLDEAL 162
Cdd:PRK10619 101 FNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499323150 163 SALDEPLRDALRRELVSLTrREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFI 235
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-218 |
3.26e-36 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 131.09 E-value: 3.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 7 RDLSVSFRDG---TFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPP------ERRR 77
Cdd:PRK11629 9 DNLCKRYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 78 MGMVFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLL 157
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499323150 158 LDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDraeaISIADRI---VVLGNGRIQQVAT 218
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHD----LQLAKRMsrqLEMRDGRLTAELS 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-225 |
1.39e-35 |
|
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: 136.03 E-value: 1.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRmgmvfqqhavwPHM-------- 91
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG-----------RHIgylpqdve 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 92 ----SVAKNVgyplARSGQkgaSISKRVERTLALVGL--------EGFGSR---RPASLSGGQRQRVALARAIIADPTVL 156
Cdd:COG4618 417 lfdgTIAENI----ARFGD---ADPEKVVAAAKLAGVhemilrlpDGYDTRigeGGARLSGGQRQRIGLARALYGDPRLV 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 157 LLDEALSALDEPLRDALRRELVSLtRREGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:COG4618 490 VLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITH-RPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
20-227 |
1.96e-35 |
|
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: 128.81 E-value: 1.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPP-ERRRMGMVF--QQHAVWPHMSVAKN 96
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYlpQEASIFRKLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 97 VGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDePLRDALRRE 176
Cdd:cd03218 96 ILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD-PIAVQDIQK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499323150 177 LVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPA 227
Cdd:cd03218 175 IIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-213 |
5.30e-35 |
|
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: 125.79 E-value: 5.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGT-FGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRmgmvf 82
Cdd:cd03246 1 LEVENVSFRYPGAEpPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 qqhavwphmsvaKNVGYplarsgqkgasISKRVErtlaLVGlegfGSRRPASLSGGQRQRVALARAIIADPTVLLLDEAL 162
Cdd:cd03246 76 ------------DHVGY-----------LPQDDE----LFS----GSIAENILSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499323150 163 SALDEPLRDALRRELVSLtRREGLTTVHVTHdRAEAISIADRIVVLGNGRI 213
Cdd:cd03246 125 SHLDVEGERALNQAIAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-244 |
9.25e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 125.49 E-value: 9.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGT-FGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMT--HVPPERRRMGM 80
Cdd:PRK13632 8 IKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkeNLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQhavwPH-----MSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTV 155
Cdd:PRK13632 88 IFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 156 LLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAIsIADRIVVLGNGRIQQVATPTELLSAPATADVAR-- 233
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEILEKAKid 242
|
250
....*....|....
gi 499323150 234 --FIVD-ATVLNGI 244
Cdd:PRK13632 243 spFIYKlSKKLKGI 256
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
1.01e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 125.69 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMT--HVPPERRRM 78
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 79 GMVFQQ---HAVWPhmSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTV 155
Cdd:PRK13652 81 GLVFQNpddQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499323150 156 LLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-222 |
1.34e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 125.26 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSfRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDM-----THVPPERRRM 78
Cdd:PRK11831 8 VDMRGVSFT-RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 79 GMVFQQHAVWPHMSVAKNVGYPLARSGQKGASISKR-VERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLL 157
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHStVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 158 LDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTEL 222
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-213 |
1.41e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 124.46 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 6 LRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVP-PERRRMGMV--F 82
Cdd:COG4674 13 VEDLTVSF-DGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDeHEIARLGIGrkF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QQHAVWPHMSVAKNVGypLARSGQKG----------ASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIAD 152
Cdd:COG4674 92 QKPTVFEELTVFENLE--LALKGDRGvfaslfarltAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 153 PTVLLldealsaLDEP---LRDALRRELVSLTRR--EGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:COG4674 170 PKLLL-------LDEPvagMTDAETERTAELLKSlaGKHSVVVVEHDMEFVRQIARKVTVLHQGSV 228
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
10-226 |
1.80e-33 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 130.85 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 10 SVSFR---DGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGMVFQQ 84
Cdd:TIGR03797 456 RVTFRyrpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQavRRQLGVVLQN 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 85 HAVWPHmSVAKNVGyplarsgqKGASIS-KRVERTLALVGLEGFGSRRP-----------ASLSGGQRQRVALARAIIAD 152
Cdd:TIGR03797 536 GRLMSG-SIFENIA--------GGAPLTlDEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRK 606
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 153 PTVLLLDEALSALDEplrdaLRRELVSltrrEGLTTVHVT-----HdRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:TIGR03797 607 PRILLFDEATSALDN-----RTQAIVS----ESLERLKVTriviaH-RLSTIRNADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
7-224 |
2.57e-33 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 130.25 E-value: 2.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 7 RDLSVSFRDGTFG--------LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RR 76
Cdd:TIGR01846 452 LRGAITFENIRFRyapdspevLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRR 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 77 RMGMVFQQHAVWPHmSVAKNVgyplaRSGQKGASIsKRVERTLALVGLEGFGSRRP-----------ASLSGGQRQRVAL 145
Cdd:TIGR01846 532 QMGVVLQENVLFSR-SIRDNI-----ALCNPGAPF-EHVIHAAKLAGAHDFISELPqgyntevgekgANLSGGQRQRIAI 604
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 146 ARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRreGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:TIGR01846 605 ARALVGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEELLA 680
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-213 |
4.04e-33 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 122.00 E-value: 4.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTfGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMThvPPERRRMGMVFQ 83
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD--IAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHAVWPHMSVAKNVGYpLAR-SGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEAL 162
Cdd:cd03269 78 ERGLYPKMKVIDQLVY-LAQlKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499323150 163 SALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:cd03269 157 SGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-226 |
4.64e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 123.41 E-value: 4.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFRDGT--------FGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVP 72
Cdd:COG4167 2 SALLEVRNLSKTFKYRTglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 73 PERR--RMGMVFQ--QHAVWPHMSVAKNVGYPLARSGQKGASI-SKRVERTLALVGL-EGFGSRRPASLSGGQRQRVALA 146
Cdd:COG4167 82 YKYRckHIRMIFQdpNTSLNPRLNIGQILEEPLRLNTDLTAEErEERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 147 RAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-224 |
6.44e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 123.66 E-value: 6.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDG-----TFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGG---EDMTHVPPER 75
Cdd:PRK13633 5 IKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 76 RRMGMVFQQhavwPHMS-----VAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAII 150
Cdd:PRK13633 85 NKAGMVFQN----PDNQivatiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 151 ADPTVLLLDEALSALDEplrdALRRELVS----LTRREGLTTVHVTHDRAEAISiADRIVVLGNGRIQQVATPTELLS 224
Cdd:PRK13633 161 MRPECIIFDEPTAMLDP----SGRREVVNtikeLNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFK 233
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-226 |
7.20e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 122.71 E-value: 7.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVE--PS---SGSVLIGGEDMTHVPPE- 74
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEV-LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 75 -RRRMGMVFQQHAVWPHMSVAKNV--GYPLARSGQKGASISKRVERTLALVGL-EGFGSR--RPA-SLSGGQRQRVALAR 147
Cdd:PRK14247 80 lRRRVQMVFQIPNPIPNLSIFENValGLKLNRLVKSKKELQERVRWALEKAQLwDEVKDRldAPAgKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 148 AIIADPTVLLLDEALSALDePLRDALRRELVsLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLD-PENTAKIESLF-LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-227 |
8.59e-33 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 122.87 E-value: 8.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-----RRRMGMVFQQH--AVWPHMS 92
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkafRRDIQMVFQDSisAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 93 VAKNVGYPLAR-SGQKGASISKRVERTLALVGL-EGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLR 170
Cdd:PRK10419 108 VREIIREPLRHlLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 171 DALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELL--SAPA 227
Cdd:PRK10419 188 AGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLtfSSPA 246
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-226 |
1.05e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 121.67 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFRdGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERR-RMG 79
Cdd:COG1137 1 MMTLEAENLVKSYG-KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRaRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVF--QQHAVWPHMSVAKNV-----GYPLARSGQKgasisKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIAD 152
Cdd:COG1137 80 IGYlpQEASIFRKLTVEDNIlavleLRKLSKKERE-----ERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499323150 153 PTVLLLDEALSALDePL--RDAlrRELVSLTRREGLtTVHVT-HDRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:COG1137 155 PKFILLDEPFAGVD-PIavADI--QKIIRHLKERGI-GVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-255 |
1.05e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 122.89 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMT--HVPPERRRMGMVFQQ-HAVWPHMSVAKN 96
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 97 VGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRE 176
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 177 LVSLTRREGLTTVHVTHDRAEAISiADRIVVLGNGRIQQVATPTELLSapATADVARFIVDATVLNGIVRNGRVMCPDL 255
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA--TSEDMVEIGLDVPFSSNLMKDLRKNGFDL 258
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
10-225 |
1.93e-32 |
|
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: 127.24 E-value: 1.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 10 SVSFRDGTFG-------LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGM 80
Cdd:COG5265 357 EVRFENVSFGydperpiLKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VfQQHAVWPHMSVAKNVGYplarsGQKGASISKrVERTLALVGLEGFGSRRPAS-----------LSGGQRQRVALARAI 149
Cdd:COG5265 437 V-PQDTVLFNDTIAYNIAY-----GRPDASEEE-VEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTL 509
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 150 IADPTVLLLDEALSALDEPLRDALRRELVSLTRreGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAH-RLSTIVDADEILVLEAGRIVERGTHAELLAQ 582
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-270 |
3.32e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 121.38 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGMV 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQhavwPH-----MSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVL 156
Cdd:PRK13647 85 FQD----PDdqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 157 LLDEALSALDEPLRDALRRELVSLTrREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPtELLSAPATADVA--RF 234
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDIVEQAglRL 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 499323150 235 IVDATVLNGIVRNGRVMCP-DLDtswdlDAVQAIDDI 270
Cdd:PRK13647 239 PLVAQIFEDLPELGQSKLPlTVK-----EAVQIIRKL 270
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-213 |
3.82e-32 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 119.94 E-value: 3.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 5 KLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERR-RMGM--V 81
Cdd:TIGR03410 2 EVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIayV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQHAVWPHMSVAKNVGYPLARSGQKGASIskrVERTLALVG-LEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDE 160
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRSRKI---PDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 161 AL-----SALDEpLRDALRRelvsLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:TIGR03410 158 PTegiqpSIIKD-IGRVIRR----LRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-236 |
4.02e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 120.92 E-value: 4.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVE------PSSGSVLIGGEDMTHVPP--ERRRMGMVFQQHAVWPHM 91
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAikLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 92 SVAKNVGYPLARSGQKGA-SISKRVERTLALVGLEGFGSRR---PAS-LSGGQRQRVALARAIIADPTVLLLDEALSALD 166
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWKEVYDRlnsPASqLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 167 EPLRDALRRELVSLTRRegLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVARFIV 236
Cdd:PRK14246 186 IVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYVI 253
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-208 |
7.21e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 118.11 E-value: 7.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGedmthvppeRRRMGMVFQQHAVWPHM--SVAKNV 97
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVPDSLplTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 98 GY----PLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDAL 173
Cdd:NF040873 79 AMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180 190
....*....|....*....|....*....|....*
gi 499323150 174 rRELVSLTRREGLTTVHVTHDrAEAISIADRIVVL 208
Cdd:NF040873 159 -IALLAEEHARGATVVVVTHD-LELVRRADPCVLL 191
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-225 |
9.66e-32 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 125.15 E-value: 9.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPER--RRMGMVFQQHAVWPHmSVAKNV 97
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 98 gyplARSGQKgASISKRVER-TLALV---------GLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDE 167
Cdd:TIGR01842 413 ----ARFGEN-ADPEKIIEAaKLAGVhelilrlpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 168 PLRDALRRELVSLTRReGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:TIGR01842 488 EGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-218 |
1.94e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 123.59 E-value: 1.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPP---ERRRMGM 80
Cdd:COG1129 5 LEMRGISKSF-GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWPHMSVAKNV--GYPLARSGQ-KGASISKRVERTLALVGLEgFGSRRPAS-LSGGQRQRVALARAIIADPTVL 156
Cdd:COG1129 84 IHQELNLVPNLSVAENIflGREPRRGGLiDWRAMRRRARELLARLGLD-IDPDTPVGdLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499323150 157 LLDEALSALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRIqqVAT 218
Cdd:COG1129 163 ILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRL--VGT 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-227 |
3.84e-31 |
|
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: 123.26 E-value: 3.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFGLQ---DINLKIEPEEFVVLIGPSGSGKT----TMLRTIAGFVEPSSGSVLIGGEDMTHVPPER- 75
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEavkGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 76 -----RRMGMVFQQ--HAVWPHMSVAKNVGYPLAR-SGQKGASISKRVERTLALVGLegfgsRRPAS--------LSGGQ 139
Cdd:COG4172 87 rrirgNRIAMIFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGI-----PDPERrldayphqLSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 140 RQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATP 219
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPT 241
|
....*...
gi 499323150 220 TELLSAPA 227
Cdd:COG4172 242 AELFAAPQ 249
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-208 |
4.64e-31 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 117.12 E-value: 4.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 11 VSFR-DGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGMVFQQHAV 87
Cdd:PRK10247 13 VGYLaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 88 WPHmSVAKNVGYPLARSGQkgasiskRVERTLALVGLEGFG------SRRPASLSGGQRQRVALARAIIADPTVLLLDEA 161
Cdd:PRK10247 93 FGD-TVYDNLIFPWQIRNQ-------QPDPAIFLDDLERFAlpdtilTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499323150 162 LSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEaISIADRIVVL 208
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-213 |
4.97e-31 |
|
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: 115.22 E-value: 4.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPP---ERRRMGM 80
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPrdaRRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQqhavwphmsvaknvgyplarsgqkgasiskrvertlalvglegfgsrrpasLSGGQRQRVALARAIIADPTVLLLDE 160
Cdd:cd03216 80 VYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499323150 161 ALSALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-252 |
5.51e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 117.49 E-value: 5.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPER--RRMGMV 81
Cdd:COG4604 2 IEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQHAVWPHMSVAKNVG---YPLARsGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLL 158
Cdd:COG4604 81 RQENHINSRLTVRELVAfgrFPYSK-GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 159 DEALSALDepLRDA------LRRelvsLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVa 232
Cdd:COG4604 160 DEPLNNLD--MKHSvqmmklLRR----LADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDI- 232
|
250 260
....*....|....*....|
gi 499323150 233 rFIVDATVLNGivrNGRVMC 252
Cdd:COG4604 233 -YDTDIEVEEI---DGKRIC 248
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-212 |
5.98e-31 |
|
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: 116.76 E-value: 5.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSF----RDGTF--GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLI----GGEDMTHVPP 73
Cdd:COG4778 5 LEVENLSKTFtlhlQGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 74 E------RRRMGMVFQQHAVWPHMS----VAKnvgyPLARSGQKGASISKRVERTLALVGL-EGFGSRRPASLSGGQRQR 142
Cdd:COG4778 85 ReilalrRRTIGYVSQFLRVIPRVSaldvVAE----PLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 143 VALARAIIADPTVLLLDEALSALDEPLRDALrRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGR 212
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVV-VELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-230 |
7.15e-31 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 120.72 E-value: 7.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPER--RRM 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTV-LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 79 GMVFQQHAVWPHMSVAKNVG---YP-LARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPT 154
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEmgrTPhRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499323150 155 VLLLDEALSALDepLRDALRR-ELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATAD 230
Cdd:PRK09536 160 VLLLDEPTASLD--INHQVRTlELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRA 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-213 |
1.50e-30 |
|
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: 114.96 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVS-----FRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPS--SGSVLIGGEDMTHVPP 73
Cdd:cd03213 1 GVTLSFRNLTVTvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 74 eRRRMGMVFQQHAVWPHMSVAKNVGYPLARSGqkgasiskrvertlalvglegfgsrrpasLSGGQRQRVALARAIIADP 153
Cdd:cd03213 81 -RKIIGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499323150 154 TVLLLDEALSALDePLRDALRRELVSLTRREGLTTVHVTHD-RAEAISIADRIVVLGNGRI 213
Cdd:cd03213 131 SLLFLDEPTSGLD-SSSALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-212 |
2.52e-30 |
|
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: 114.49 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSF----RDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGedmthvpperrRMG 79
Cdd:cd03250 1 ISVEDASFTWdsgeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQhaVW-PHMSVAKNV--GYPLarsgqkgasISKRVERTLALVGLE------GFGSR-----RPASLSGGQRQRVAL 145
Cdd:cd03250 70 YVSQE--PWiQNGTIRENIlfGKPF---------DEERYEKVIKACALEpdleilPDGDLteigeKGINLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499323150 146 ARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHdRAEAISIADRIVVLGNGR 212
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-217 |
3.05e-30 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 114.88 E-value: 3.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERR------RMGMVFQQHAVWPHMSV 93
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 94 AKNVGYP-LARsgqkGASISKRVERTLALVGLEGFGSR---RPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPL 169
Cdd:PRK10584 106 LENVELPaLLR----GESSRQSRNGAKALLEQLGLGKRldhLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499323150 170 RDALRRELVSLTRREGLTTVHVTHDRAEAiSIADRIVVLGNGRIQQVA 217
Cdd:PRK10584 182 GDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQEEA 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-235 |
4.13e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 115.26 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTfGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTI--AGFVEPS---SGSVLIGGEDM----THVPPE 74
Cdd:PRK14239 6 LQVSDLSVYYNKKK-ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIysprTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 75 RRRMGMVFQQHAVWPhMSVAKNVGYPLARSGQKGASI-SKRVERTLALVGL-EGFGSRRPAS---LSGGQRQRVALARAI 149
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIwDEVKDRLHDSalgLSGGQQQRVCIARVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 150 IADPTVLLLDEALSALDePLrDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATA 229
Cdd:PRK14239 164 ATSPKIILLDEPTSALD-PI-SAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHK 241
|
....*.
gi 499323150 230 DVARFI 235
Cdd:PRK14239 242 ETEDYI 247
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-224 |
9.08e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 115.33 E-value: 9.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTH----VPPERRRMG 79
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrkgLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQ--HAVWPhMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLL 157
Cdd:PRK13636 86 MVFQDpdNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499323150 158 LDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-214 |
9.26e-30 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 113.97 E-value: 9.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEdmthVPPERR-----RMGMVF-QQHAVWPHMSV 93
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRkkflrRIGVVFgQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 94 AKnvGYPLARS--GQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRD 171
Cdd:cd03267 113 ID--SFYLLAAiyDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499323150 172 ALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQ 214
Cdd:cd03267 191 NIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-194 |
1.57e-29 |
|
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: 118.62 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPP-ERRRMGMV 81
Cdd:TIGR02868 334 TLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQHAVWPHMSVAKNVgyplaRSGQKGASiSKRVERTLALVGLEGFGSRRP-----------ASLSGGQRQRVALARAII 150
Cdd:TIGR02868 414 CAQDAHLFDTTVRENL-----RLARPDAT-DEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499323150 151 ADPTVLLLDEALSALDEPLRDALRRELVSLTrrEGLTTVHVTHD 194
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLLAAL--SGRTVVLITHH 529
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-219 |
2.27e-29 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 118.37 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 2 SSIKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIggedmthvpPERRRMgMV 81
Cdd:COG4178 361 GALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARV-LF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQHAVWPHMSVAKNVGYPLARSgqkgaSIS-KRVERTLALVGLEGFGSR------RPASLSGGQRQRVALARAIIADPT 154
Cdd:COG4178 431 LPQRPYLPLGTLREALLYPATAE-----AFSdAELREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPD 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 155 VLLLDEALSALDEPLRDALRRELvsLTRREGLTTVHVTHdRAEAISIADRIVVL---GNGRIQQVATP 219
Cdd:COG4178 506 WLFLDEATSALDEENEAALYQLL--REELPGTTVISVGH-RSTLAAFHDRVLELtgdGSWQLLPAEAP 570
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-249 |
2.59e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 114.04 E-value: 2.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 8 DLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRT-------IAGFvePSSGSVLIGGEDMTH---VPPERRR 77
Cdd:PRK14271 26 NLTLGFAGKTV-LDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGY--RYSGDVLLGGRSIFNyrdVLEFRRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 78 MGMVFQQHAVWPhMSVAKNVgyplaRSGQKGASISKRVE-RTLALVGLEGFG---------SRRPASLSGGQRQRVALAR 147
Cdd:PRK14271 103 VGMLFQRPNPFP-MSIMDNV-----LAGVRAHKLVPRKEfRGVAQARLTEVGlwdavkdrlSDSPFRLSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 148 AIIADPTVLLLDEALSALDEPLRDALRRELVSLTRRegLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPA 227
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPK 254
|
250 260
....*....|....*....|..
gi 499323150 228 TADVARFIVDatvLNGIVRNGR 249
Cdd:PRK14271 255 HAETARYVAG---LSGDVKDAK 273
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-223 |
3.91e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 117.75 E-value: 3.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 11 VSFRDGTF-------GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGMV 81
Cdd:PRK13657 335 VEFDDVSFsydnsrqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQhAVWPHMSVAKN--VGYPLA-----RSGQKGASISKRVERTLAlvGLEGFGSRRPASLSGGQRQRVALARAIIADPT 154
Cdd:PRK13657 415 FQD-AGLFNRSIEDNirVGRPDAtdeemRAAAERAQAHDFIERKPD--GYDTVVGERGRQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 155 VLLLDEALSALDEPLRDALRRELVSLtrREGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELL 223
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAH-RLSTVRNADRILVFDNGRVVESGSFDELV 557
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
11-226 |
4.49e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 118.29 E-value: 4.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 11 VSFRDGTFG---------LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMG 79
Cdd:TIGR00958 479 IEFQDVSFSypnrpdvpvLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQHAVWPHmSVAKNVGYPL---------ARSGQKGAS--ISKRVERTLALVGLEGfgsrrpASLSGGQRQRVALARA 148
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYGLtdtpdeeimAAAKAANAHdfIMEFPNGYDTEVGEKG------SQLSGGQKQRIAIARA 631
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 149 IIADPTVLLLDEALSALDEplrdALRRELVSLTRREGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-226 |
8.89e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 111.86 E-value: 8.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPS-----SGSVLIGGEDMTHV---P 72
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHV-IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPdvdP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 73 PE-RRRMGMVFQQHAVWPHMSVAKNV--GYPLARSGQKGASISKRVERTLALVGL-EGFGSR---RPASLSGGQRQRVAL 145
Cdd:PRK14267 81 IEvRREVGMVFQYPNPFPHLTIYDNVaiGVKLNGLVKSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 146 ARAIIADPTVLLLDEALSALDePLRDALRRELVsLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANID-PVGTAKIEELL-FELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
.
gi 499323150 226 P 226
Cdd:PRK14267 239 P 239
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-213 |
1.40e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 112.12 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFRDGTfGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVP-------PER 75
Cdd:COG4152 1 MLELKGLTKRFGDKT-AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 76 RRMgmvfqqhavWPHMSVAKNVGYpLAR-SGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPT 154
Cdd:COG4152 80 RGL---------YPKMKVGEQLVY-LARlKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 155 VLLLDEALSALDePL-RDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:COG4152 150 LLILDEPFSGLD-PVnVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-226 |
1.48e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.82 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 2 SSIKLRDLSVSFRDGTF-GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEP---SSGSVLIGGEDMTH--VPPER 75
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAktVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 76 RRMGMVFQQhavwPH-----MSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAII 150
Cdd:PRK13640 84 EKVGIVFQN----PDnqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 151 ADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAiSIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-229 |
3.63e-28 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 115.21 E-value: 3.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDG---TFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE------ 74
Cdd:PRK10535 5 LELKDIRRSYPSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADalaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 75 RRRMGMVFQQHAVWPHMSVAKNVGYPLARSGqkgASISKRVERTLALVGLEGFGSR---RPASLSGGQRQRVALARAIIA 151
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVPAVYAG---LERKQRLLRAQELLQRLGLEDRveyQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 152 DPTVLLLDEALSALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISiADRIVVLGNGRI---------QQVATPTEL 222
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIvrnppaqekVNVAGGTEP 239
|
....*..
gi 499323150 223 LSAPATA 229
Cdd:PRK10535 240 VVNTASG 246
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-226 |
4.87e-28 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 110.26 E-value: 4.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFR--DGTF------GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPER 75
Cdd:PRK15112 5 LEVRNLSKTFRyrTGWFrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 76 R--RMGMVFQ--QHAVWPHMSVAKNVGYPLA-RSGQKGASISKRVERTLALVGL-EGFGSRRPASLSGGQRQRVALARAI 149
Cdd:PRK15112 85 RsqRIRMIFQdpSTSLNPRQRISQILDFPLRlNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499323150 150 IADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:PRK15112 165 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
3-222 |
5.71e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.22 E-value: 5.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFRDGT-F---GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTH------VP 72
Cdd:PRK13649 2 GINLQNVSYTYQAGTpFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 73 PERRRMGMVFQqhavWPHM-----SVAKNVGYPLARSGQKGASISKRVERTLALVGL-EGFGSRRPASLSGGQRQRVALA 146
Cdd:PRK13649 82 QIRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 147 RAIIADPTVLLLDEALSALDEplrdALRRELVSLTR---REGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTEL 222
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDP----KGRKELMTLFKklhQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-224 |
1.24e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.07 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFR-DGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVL-----IGGEDMTHVppeRRR 77
Cdd:PRK13648 8 IVFKNVSFQYQsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFynnqaITDDNFEKL---RKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 78 MGMVFQQhavwPH-----MSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIAD 152
Cdd:PRK13648 85 IGIVFQN----PDnqfvgSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 153 PTVLLLDEALSALDEplrdALRRELVSLTRR----EGLTTVHVTHDRAEAISiADRIVVLGNGRIQQVATPTELLS 224
Cdd:PRK13648 161 PSVIILDEATSMLDP----DARQNLLDLVRKvkseHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3-233 |
1.24e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.53 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFRDGT----FGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEdmtHVPPE---- 74
Cdd:PRK13641 2 SIKFENVDYIYSPGTpmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGY---HITPEtgnk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 75 -----RRRMGMVFQqhavWPHMSVAKNVGYPLARSGQKGASISKRVERTLAL-----VGL-EGFGSRRPASLSGGQRQRV 143
Cdd:PRK13641 79 nlkklRKKVSLVFQ----FPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALkwlkkVGLsEDLISKSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 144 ALARAIIADPTVLLLDEALSALDEPLRDALrRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTEL- 222
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIf 233
|
250 260
....*....|....*....|.
gi 499323150 223 ----------LSAPATADVAR 233
Cdd:PRK13641 234 sdkewlkkhyLDEPATSRFAS 254
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-231 |
1.80e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 109.51 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDM-THVPPERRRMGMVF 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLV-VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEAL 162
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 163 SALDEPLRDALRRELVSLTRReGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADV 231
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCDV 234
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
11-226 |
5.32e-27 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 111.96 E-value: 5.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 11 VSFRDGTFG--------LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRR--MGM 80
Cdd:TIGR03796 478 VELRNITFGysplepplIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLAnsVAM 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VfQQHAVWPHMSVAKNVGYplarsgqKGASIS-KRVERTLALVGLEGFGSRRP-----------ASLSGGQRQRVALARA 148
Cdd:TIGR03796 558 V-DQDIFLFEGTVRDNLTL-------WDPTIPdADLVRACKDAAIHDVITSRPggydaelaeggANLSGGQRQRLEIARA 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 149 IIADPTVLLLDEALSALDEPLRDALRRELvsltRREGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:TIGR03796 630 LVRNPSILILDEATSALDPETEKIIDDNL----RRRGCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
5.83e-27 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 111.05 E-value: 5.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLS---VSFRDGTFGLQD-INLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGS--VLIGGE--DMTHVPPE- 74
Cdd:TIGR03269 280 IKVRNVSkryISVDRGVVKAVDnVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEwvDMTKPGPDg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 75 ----RRRMGMVFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVeRTLALVGL-----EGFGSRRPASLSGGQRQRVAL 145
Cdd:TIGR03269 360 rgraKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAV-ITLKMVGFdeekaEEILDKYPDELSEGERHRVAL 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 146 ARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-219 |
6.45e-27 |
|
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: 106.04 E-value: 6.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFRDGT-FGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMG 79
Cdd:cd03244 2 DIEFKNVSLRYRPNLpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHdlRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQhavwPHM---SVAKNVGyPLarsgqkGASISKRVERTLALVGLEGFGSRRP-----------ASLSGGQRQRVAL 145
Cdd:cd03244 82 IIPQD----PVLfsgTIRSNLD-PF------GEYSDEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499323150 146 ARAIIADPTVLLLDEALSALDePLRDALRRELVSlTRREGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATP 219
Cdd:cd03244 151 ARALLRKSKILVLDEATASVD-PETDALIQKTIR-EAFKDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-225 |
6.89e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 106.32 E-value: 6.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSS-IKLRDLSVSFRDGTFG---------------------LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSS 58
Cdd:COG1134 1 MSSmIEVENVSKSYRLYHEPsrslkelllrrrrtrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 59 GSVLIGGEdmthVPP--ErrrMGMVFQqhavwPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLS 136
Cdd:COG1134 81 GRVEVNGR----VSAllE---LGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 137 GGQRQRVALARAIIADPTVLLLDEALSALDEPLRD-ALRR--ELvsltRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKkCLARirEL----RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
250
....*....|..
gi 499323150 214 QQVATPTELLSA 225
Cdd:COG1134 225 VMDGDPEEVIAA 236
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
3-224 |
7.38e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 107.56 E-value: 7.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFRDGT----FGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTH------VP 72
Cdd:PRK13646 2 TIRFDNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 73 PERRRMGMVFQqhavWPHM-----SVAKNVGYplarsGQK--GASISKRVERTLALVGLEGFG----SRRPASLSGGQRQ 141
Cdd:PRK13646 82 PVRKRIGMVFQ----FPESqlfedTVEREIIF-----GPKnfKMNLDEVKNYAHRLLMDLGFSrdvmSQSPFQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 142 RVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTE 221
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
...
gi 499323150 222 LLS 224
Cdd:PRK13646 233 LFK 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-213 |
1.10e-26 |
|
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: 104.53 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGF--VEPSSGSVLIGGEDMTHVPP-ERRRMG- 79
Cdd:cd03217 1 LEIKDLHVSVGGKEI-LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPeERARLGi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 -MVFQqhavwphmsvaknvgYPLARSGQKGASISKRVErtlalvglEGFgsrrpaslSGGQRQRVALARAIIADPTVLLL 158
Cdd:cd03217 80 fLAFQ---------------YPPEIPGVKNADFLRYVN--------EGF--------SGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 159 DEALSALDeplRDALR--RELVSLTRREGLTTVHVTHDR--AEAIsIADRIVVLGNGRI 213
Cdd:cd03217 129 DEPDSGLD---IDALRlvAEVINKLREEGKSVLIITHYQrlLDYI-KPDRVHVLYDGRI 183
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-223 |
1.28e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 105.53 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 5 KLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGF--VEPSSGSVLIGGEDMTHVPP-ERRRMG-- 79
Cdd:COG0396 2 EIKNLHVSVEGKEI-LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPdERARAGif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQHAVWPHMSV------AKNvgyplARSGQKGASIS--KRVERTLALVGL-EGFgSRRP--ASLSGGQRQRVALARA 148
Cdd:COG0396 81 LAFQYPVEIPGVSVsnflrtALN-----ARRGEELSAREflKLLKEKMKELGLdEDF-LDRYvnEGFSGGEKKRNEILQM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 149 IIADPTVLLLDEALSALDeplRDALR--RELVSLTRREGLTTVHVTH-DRAEAISIADRIVVLGNGRIQQVATPtELL 223
Cdd:COG0396 155 LLLEPKLAILDETDSGLD---IDALRivAEGVNKLRSPDRGILIITHyQRILDYIKPDFVHVLVDGRIVKSGGK-ELA 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-213 |
2.15e-26 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 104.86 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSF--RDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMG 79
Cdd:cd03248 12 VKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQHAVWPHmSVAKNVGYPL-----------ARSGQKGASISKRVERTLALVGLEGfgsrrpASLSGGQRQRVALARA 148
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNIAYGLqscsfecvkeaAQKAHAHSFISELASGYDTEVGEKG------SQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 149 IIADPTVLLLDEALSALDEPLRDALRRELVSLTRReglTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPER---RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-226 |
2.18e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 105.46 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPER-RRMGMV- 81
Cdd:PRK11300 6 LSVSGLMMRF-GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiARMGVVr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 -FQQHAVWPHMSVAKNVGYPLARSGQKG--ASISK-----RVERT--------LALVGLEGFGSRRPASLSGGQRQRVAL 145
Cdd:PRK11300 85 tFQHVRLFREMTVIENLLVAQHQQLKTGlfSGLLKtpafrRAESEaldraatwLERVGLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 146 ARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 244
|
.
gi 499323150 226 P 226
Cdd:PRK11300 245 P 245
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-226 |
2.55e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 107.10 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 22 DINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRR-----MGMVFQQ--HAVWPHMSVA 94
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavrsdIQMIFQDplASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 95 KNVGYPLA--RSGQKGASISKRVERTLALVGL-EGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRD 171
Cdd:PRK15079 119 EIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 172 ALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:PRK15079 199 QVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-203 |
3.54e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 105.25 E-value: 3.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrdGTF-GLQDINLKIEPEEFVVLIGPSGSGKTTMLRT-------IAGF-VEpssGSVLIGGEDM--THVP 72
Cdd:PRK14243 11 LRTENLNVYY--GSFlAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGFrVE---GKVTFHGKNLyaPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 73 PE--RRRMGMVFQQHAVWPHmSVAKNVGYPLARSGQKGaSISKRVERTLALVGL--EGFGSRRPA--SLSGGQRQRVALA 146
Cdd:PRK14243 86 PVevRRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKG-DMDELVERSLRQAALwdEVKDKLKQSglSLSGGQQQRLCIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499323150 147 RAIIADPTVLLLDEALSALDePLrDALRRELVSLTRREGLTTVHVTHDRAEAISIAD 203
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALD-PI-STLRIEELMHELKEQYTIIIVTHNMQQAARVSD 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-166 |
6.47e-26 |
|
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: 102.44 E-value: 6.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 6 LRDLSVSfRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRmGMVFQQH 85
Cdd:TIGR01189 3 ARNLACS-RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE-NILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 86 --AVWPHMSVAKNVGYpLARSGQkgaSISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALS 163
Cdd:TIGR01189 81 lpGLKPELSALENLHF-WAAIHG---GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
...
gi 499323150 164 ALD 166
Cdd:TIGR01189 157 ALD 159
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-224 |
7.51e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 104.70 E-value: 7.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 19 GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGG-------EDMTHVPPERRRMGMVFQ--QHAVWP 89
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRLRKEIGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 90 HmSVAKNVGYPLARSGQKGASISKRVERTLALVGL-EGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEP 168
Cdd:PRK13645 106 E-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 169 LRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-213 |
7.73e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 104.32 E-value: 7.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTfGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVE----PSSGSVLIG------GEDMTHVPP 73
Cdd:PRK09984 5 IRVEKLAKTFNQHQ-ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLGrtvqreGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 74 ERRRMGMVFQQHAVWPHMSVAKNV------GYPLARSGQKGAS--ISKRVERTLALVGLEGFGSRRPASLSGGQRQRVAL 145
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVligalgSTPFWRTCFSWFTreQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 146 ARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-226 |
8.14e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 105.43 E-value: 8.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-----RRRMGMVFQQhavwPHMSV- 93
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkllRQKIQIVFQN----PYGSLn 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 94 -AKNVGYPLARSGQKGASISK--RVERTLAL---VGLEG-FGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALD 166
Cdd:PRK11308 107 pRKKVGQILEEPLLINTSLSAaeRREKALAMmakVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 167 EPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:PRK11308 187 VSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-226 |
8.51e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.01 E-value: 8.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVePSSGSVLIGGEDMTHVPPERRRmgmvf 82
Cdd:PRK11174 349 TIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWR----- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 qQHAVW-------PHMSVAKNV--GYPLARSGQ-----KGASISKRVERtLALvGLEGFGSRRPASLSGGQRQRVALARA 148
Cdd:PRK11174 423 -KHLSWvgqnpqlPHGTLRDNVllGNPDASDEQlqqalENAWVSEFLPL-LPQ-GLDTPIGDQAAGLSVGQAQRLALARA 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 149 IIADPTVLLLDEALSALDeplRDALRRELVSLTR-REGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLD---AHSEQLVMQALNAaSRRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-223 |
1.22e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.05 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 19 GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMT------HVPPERRRMGMVFQ-QHAVWPHM 91
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQfPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 92 SVAKNVGYPLARSGQKGASISKRVERTLALVGL-EGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLR 170
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499323150 171 DALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELL 223
Cdd:PRK13643 181 IEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-213 |
1.97e-25 |
|
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: 100.58 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 5 KLRDLSVSFRdgtfgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPP-ERRRMGMVF- 82
Cdd:cd03215 6 EVRGLSVKGA-----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 ----QQHAVWPHMSVAKNvgyplarsgqkgasiskrvertLALvglegfgsrrPASLSGGQRQRVALARAIIADPTVLLL 158
Cdd:cd03215 81 pedrKREGLVLDLSVAEN----------------------IAL----------SSLLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 159 DEALSALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
7-193 |
2.12e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 101.49 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 7 RDLSVSfRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDmTHVPPERRRMGMVFQQHA 86
Cdd:PRK13539 6 EDLACV-RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-IDDPDVAEACHYLGHRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 87 VWPHMSVAKNVGYPLARSGQKGASIskrvERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALD 166
Cdd:PRK13539 84 MKPALTVAENLEFWAAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....*..
gi 499323150 167 ePLRDALRRELVSLTRREGLTTVHVTH 193
Cdd:PRK13539 160 -AAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
11-223 |
2.31e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 107.03 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 11 VSFRDGTF--------GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTH--VPPERRRMGM 80
Cdd:PRK11176 342 IEFRNVTFtypgkevpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQhavwPHM---SVAKNVGYplARSGQKG-ASISKRVERTLAL-------VGLEGFGSRRPASLSGGQRQRVALARAI 149
Cdd:PRK11176 422 VSQN----VHLfndTIANNIAY--ARTEQYSrEQIEEAARMAYAMdfinkmdNGLDTVIGENGVLLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499323150 150 IADPTVLLLDEALSALDEPLRDALRRELVSLTRREgltTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELL 223
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQKNR---TSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-213 |
3.76e-25 |
|
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: 101.07 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFG---------------------LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVL 62
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgefwaLKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 63 IGGEDmthVPPerRRMGMVFQqhavwPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQR 142
Cdd:cd03220 81 VRGRV---SSL--LGLGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499323150 143 VALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-213 |
9.40e-25 |
|
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: 98.92 E-value: 9.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRD-GTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMVF 82
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QQHavwPHM---SVAKNVGyplarsgqkgasiskrvertlalvglegfgsRRpasLSGGQRQRVALARAIIADPTVLLLD 159
Cdd:cd03247 81 NQR---PYLfdtTLRNNLG-------------------------------RR---FSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499323150 160 EALSALDEPLRDALRRELVSLTrrEGLTTVHVTHdRAEAISIADRIVVLGNGRI 213
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVL--KDKTLIWITH-HLTGIEHMDKILFLENGKI 174
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-213 |
2.10e-24 |
|
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: 99.27 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPS---SGSVLIGGEDMThvpPE--RRRMGMVFQQHAVWPHMSVA 94
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRK---PDqfQKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 95 KNVGY-PLARSG--QKGASISKRVERT-LALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLR 170
Cdd:cd03234 100 ETLTYtAILRLPrkSSDAIRKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499323150 171 DALRRELVSLTRREG--LTTVHvtHDRAEAISIADRIVVLGNGRI 213
Cdd:cd03234 180 LNLVSTLSQLARRNRivILTIH--QPRSDLFRLFDRILLLSSGEI 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-226 |
2.32e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 100.25 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 2 SSIKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMT--HVPPERRRMG 79
Cdd:PRK10575 10 TTFALRNVSFRVPGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQHAVWPHMSVAKNVG---YPLARS-GQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTV 155
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVAigrYPWHGAlGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499323150 156 LLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-214 |
3.35e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.22 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGgedmTHVpperrRMGMVFQ 83
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----ETV-----KIGYFDQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHAVW-PHMSVAKNVgyplaRSGQKGASISKRveRTLalvgLEGFG-----SRRPAS-LSGGQRQRVALARAIIADPTVL 156
Cdd:COG0488 386 HQEELdPDKTVLDEL-----RDGAPGGTEQEV--RGY----LGRFLfsgddAFKPVGvLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 157 LLDEALSALDEPLRDALrreLVSLTRREGlTTVHVTHDRaEAI-SIADRIVVLGNGRIQ 214
Cdd:COG0488 455 LLDEPTNHLDIETLEAL---EEALDDFPG-TVLLVSHDR-YFLdRVATRILEFEDGGVR 508
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-214 |
3.41e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.22 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 6 LRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIggedmthvpPERRRMGMVFQQH 85
Cdd:COG0488 1 LENLSKSFGGRPL-LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 86 AVWPHMSVAKNV--GYP--------LARSGQKGASISK----------------------RVERTLALVGL-EGFGSRRP 132
Cdd:COG0488 71 PLDDDLTVLDTVldGDAelraleaeLEELEAKLAEPDEdlerlaelqeefealggweaeaRAEEILSGLGFpEEDLDRPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 133 ASLSGGQRQRVALARAIIADPTVLLLDEALSALDEP----LRDALRrelvsltRREGlTTVHVTHDRA--EAisIADRIV 206
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLEsiewLEEFLK-------NYPG-TVLVVSHDRYflDR--VATRIL 220
|
....*...
gi 499323150 207 VLGNGRIQ 214
Cdd:COG0488 221 ELDRGKLT 228
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-225 |
5.83e-24 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 102.90 E-value: 5.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 2 SSIKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMG 79
Cdd:TIGR01193 472 GDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHtlRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQhavwPHM---SVAKNvgypLARSGQKGASISKrVERTLALVGLE--------GFG---SRRPASLSGGQRQRVAL 145
Cdd:TIGR01193 552 YLPQE----PYIfsgSILEN----LLLGAKENVSQDE-IWAACEIAEIKddienmplGYQtelSEEGSSISGGQKQRIAL 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 146 ARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRReglTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-219 |
7.75e-24 |
|
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: 103.17 E-value: 7.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 23 INLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDM-THVPPERRRMGMVFQQHAVWPHMSVAKNVGYPL 101
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 102 ARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELvsLT 181
Cdd:TIGR01257 1029 QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LK 1106
|
170 180 190
....*....|....*....|....*....|....*...
gi 499323150 182 RREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATP 219
Cdd:TIGR01257 1107 YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
4-225 |
2.10e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 97.22 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRdgtfgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVePSSGSVLIGGEDMTHVPPER--RRMGMV 81
Cdd:COG4138 1 LQLNDVAVAGR-----LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAElaRHRAYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQHAVWPHMSVAKnvgYpLARSGQKGASISKrVERTLALV----GLEGFGSRRPASLSGGQRQRVALARAII-ADPTV- 155
Cdd:COG4138 75 SQQQSPPFAMPVFQ---Y-LALHQPAGASSEA-VEQLLAQLaealGLEDKLSRPLTQLSGGEWQRVRLAAVLLqVWPTIn 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 156 -----LLLDEALSALD---EPLRDALRRELVSLtrreGLTTVHVTHDRAEAISIADRIVVLGNGRI------QQVATPtE 221
Cdd:COG4138 150 pegqlLLLDEPMNSLDvaqQAALDRLLRELCQQ----GITVVMSSHDLNHTLRHADRVWLLKQGKLvasgetAEVMTP-E 224
|
....
gi 499323150 222 LLSA 225
Cdd:COG4138 225 NLSE 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-218 |
2.11e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.87 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMT-HVPPERRRMG--M 80
Cdd:COG3845 6 LELRGITKRF-GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDAIALGigM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWPHMSVAKNVgyPLARSGQKGASISKRVERTLALVGLEGFG-----SRRPASLSGGQRQRVALARAIIADPTV 155
Cdd:COG3845 85 VHQHFMLVPNLTVAENI--VLGLEPTKGGRLDRKAARARIRELSERYGldvdpDAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499323150 156 LLLDEALSALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRIqqVAT 218
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKV--VGT 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-208 |
2.33e-23 |
|
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: 94.91 E-value: 2.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLI-GGEDMTHVPperrrmgmvf 82
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLP---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 qQHAVWPHMSVAKNVGYPLARSgqkgasiskrvertlalvglegfgsrrpasLSGGQRQRVALARAIIADPTVLLLDEAL 162
Cdd:cd03223 71 -QRPYLPLGTLREQLIYPWDDV------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499323150 163 SALDEPLRDALRRELvsltRREGLTTVHVTHdRAEAISIADRIVVL 208
Cdd:cd03223 120 SALDEESEDRLYQLL----KELGITVISVGH-RPSLWKFHDRVLDL 160
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-225 |
2.34e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 100.95 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGM 80
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VfQQHAVWPHMSVAKNVGYplarsgqkGASISK-RVERTLALVGL--------EGFGSR---RPASLSGGQRQRVALARA 148
Cdd:PRK10790 420 V-QQDPVVLADTFLANVTL--------GRDISEeQVWQALETVQLaelarslpDGLYTPlgeQGNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499323150 149 IIADPTVLLLDEALSALDEPLRDALRRELVSLtrREGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAH-RLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-213 |
2.97e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.49 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 5 KLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPP-ERRRMGMVF- 82
Cdd:COG3845 259 EVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPrERRRLGVAYi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 ----QQHAVWPHMSVAKNV--GYPLARSGQKGASISKRVERTLA--LVglEGFGSRRP------ASLSGGQRQRVALARA 148
Cdd:COG3845 339 pedrLGRGLVPDMSVAENLilGRYRRPPFSRGGFLDRKAIRAFAeeLI--EEFDVRTPgpdtpaRSLSGGNQQKVILARE 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 149 IIADPTVLLLDEALSALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-224 |
3.79e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.46 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGT----FGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSV--LIGGEDMTHVPPE--- 74
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEkek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 75 ---------------------RRRMGMVFQ--QHAVWpHMSVAKNVGYPLARSGQKGASISKRVERTLALVGL-EGFGSR 130
Cdd:PRK13651 83 vleklviqktrfkkikkikeiRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 131 RPASLSGGQRQRVALARAIIADPTVLLLDEALSALD-EPLRDALrrELVSLTRREGLTTVHVTHDRAEAISIADRIVVLG 209
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEIL--EIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
250
....*....|....*
gi 499323150 210 NGRIQQVATPTELLS 224
Cdd:PRK13651 240 DGKIIKDGDTYDILS 254
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-213 |
4.21e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 96.53 E-value: 4.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 7 RDLSVSFRDGTfGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVP------PERRRM-- 78
Cdd:PRK11701 10 RGLTKLYGPRK-GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalseAERRRLlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 79 ---GMVfQQHA---VWPHMSVAKNVGYPLARSGQKG-ASISKRVERTLALVGLEgfGSR---RPASLSGGQRQRVALARA 148
Cdd:PRK11701 89 tewGFV-HQHPrdgLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEID--AARiddLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 149 IIADPTVLLLDEALSALD----EPLRDALRRelvsLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDvsvqARLLDLLRG----LVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-225 |
1.31e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 95.44 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 2 SSIKLRDLSVSFRDGTFGL-QDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPER--RRM 78
Cdd:PRK10253 4 SVARLRGEQLTLGYGKYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 79 GMVFQQHAVWPHMSVAKNVG------YPLARSGQKgaSISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIAD 152
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVArgryphQPLFTRWRK--EDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499323150 153 PTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-213 |
1.63e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 96.31 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGedmtHVPPERR-----RMGMVF---QQhaVWPHM 91
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG----YVPFKRRkefarRIGVVFgqrSQ--LWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 92 SVA------KNVgYPLARSGQKgasisKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSAL 165
Cdd:COG4586 112 PAIdsfrllKAI-YRIPDAEYK-----KRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499323150 166 DEPLRDALRRELVSLTRREGlTTVHVT-HDRAEAISIADRIVVLGNGRI 213
Cdd:COG4586 186 DVVSKEAIREFLKEYNRERG-TTILLTsHDMDDIEALCDRVIVIDHGRI 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-216 |
1.79e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.39 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSF--RDGTF--------GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVP- 72
Cdd:PRK10261 314 LQVRNLVTRFplRSGLLnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 73 ----PERRRMGMVFQQ--HAVWPHMSVAKNVGYPLARSG-QKGASISKRVERTLALVGLE-GFGSRRPASLSGGQRQRVA 144
Cdd:PRK10261 394 gklqALRRDIQFIFQDpyASLDPRQTVGDSIMEPLRVHGlLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRIC 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499323150 145 LARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQV 216
Cdd:PRK10261 474 IARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEI 545
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-212 |
2.09e-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: 91.36 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGgedmthvppERRRMGmVFQ 83
Cdd:cd03221 1 IELENLSKTYGGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------STVKIG-YFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QhavwphmsvaknvgyplarsgqkgasiskrvertlalvglegfgsrrpasLSGGQRQRVALARAIIADPTVLLLDEALS 163
Cdd:cd03221 70 Q--------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499323150 164 ALDEPLRDALRRELVSLTRreglTTVHVTHDRAEAISIADRIVVLGNGR 212
Cdd:cd03221 100 HLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-229 |
2.81e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.47 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSF--RDGTF--------GLQDINLKIEPEEFVVLIGPSGSGKTT----MLRTIAgfvepSSGSVLIGGE--- 66
Cdd:PRK15134 276 LDVEQLQVAFpiRKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQplh 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 67 --DMTHVPPERRRMGMVFQ--QHAVWPHMSVAKNVGYPLaRSGQKGASISKRVERTLAL---VGLEGFGSRR-PASLSGG 138
Cdd:PRK15134 351 nlNRRQLLPVRHRIQVVFQdpNSSLNPRLNVLQIIEEGL-RVHQPTLSAAQREQQVIAVmeeVGLDPETRHRyPAEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 139 QRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVAT 218
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
250
....*....|.
gi 499323150 219 PTELLSAPATA 229
Cdd:PRK15134 510 CERVFAAPQQE 520
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-224 |
2.95e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 93.80 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFRdGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVP---PERRR 77
Cdd:PRK10895 1 MATLTAKNLAKAYK-GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhaRARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 78 MGMVFQQHAVWPHMSVAKNVGYPLA-RSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVL 156
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 157 LLDEALSALDePLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:PRK10895 160 LLDEPFAGVD-PISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-227 |
3.17e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 93.79 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE---RRRMGMVFQQHAVWPHMSVAKN 96
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkimREAVAIVPEGRRVFSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 97 vgypLARSG--QKGASISKRVERTLALVG-LEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALdEPLRDAL 173
Cdd:PRK11614 101 ----LAMGGffAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL-APIIIQQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499323150 174 RRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPA 227
Cdd:PRK11614 176 IFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
7-166 |
5.09e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 92.17 E-value: 5.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 7 RDLSVSfRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMgMVFQQHA 86
Cdd:PRK13538 5 RNLACE-RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD-LLYLGHQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 87 --VWPHMSVAKNVGYPLARSGQKGAsisKRVERTLALVGLEGFgSRRPAS-LSGGQRQRVALARAIIADPTVLLLDEALS 163
Cdd:PRK13538 83 pgIKTELTALENLRFYQRLHGPGDD---EALWEALAQVGLAGF-EDVPVRqLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
...
gi 499323150 164 ALD 166
Cdd:PRK13538 159 AID 161
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-212 |
8.26e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 94.51 E-value: 8.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDmthVPPE----RR 76
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAV-VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP---VPARarlaRA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 77 RMGMVFQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVL 156
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 157 LLDEALSALDEPLRDALRRELVSLTRReGLTTVHVTHDRAEAISIADRIVVLGNGR 212
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-213 |
8.95e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.86 E-value: 8.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 5 KLRDLSvsfRDGTFglQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMT-HVPPERRRMGMVF- 82
Cdd:COG1129 258 EVEGLS---VGGVV--RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAIRAGIAYv 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 ----QQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLAlvglEGFGSR---RPAS-------LSGGQRQRVALARA 148
Cdd:COG1129 333 pedrKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALA----EEYIKRlriKTPSpeqpvgnLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 149 IIADPTVLLldealsaLDEPLR--D--------ALRRELVsltrREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:COG1129 409 LATDPKVLI-------LDEPTRgiDvgakaeiyRLIRELA----AEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-166 |
1.33e-21 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 91.02 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 14 RDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRmGMVFQQHA--VWPHM 91
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR-GLLYLGHApgIKTTL 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 92 SVAKNVGYPLARSGQKGasiskrVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALD 166
Cdd:cd03231 89 SVLENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-219 |
1.39e-21 |
|
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: 90.93 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFR-DGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMG 79
Cdd:cd03369 6 EIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEdlRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQhavwphmsvaknvgyPLARSGqkgaSISKRVERTLALVGLEGFGSRRPAS----LSGGQRQRVALARAIIADPTV 155
Cdd:cd03369 86 IIPQD---------------PTLFSG----TIRSNLDPFDEYSDEEIYGALRVSEgglnLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 156 LLLDEALSALDEPlRDALRRELVsltRRE--GLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATP 219
Cdd:cd03369 147 LVLDEATASIDYA-TDALIQKTI---REEftNSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-232 |
1.78e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 92.38 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 8 DLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTH----VPPERRRMGMVFQ 83
Cdd:PRK13638 6 DLWFRYQDEPV-LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYskrgLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 --QHAVWpHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEA 161
Cdd:PRK13638 85 dpEQQIF-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499323150 162 LSALDEplrdALRRELVSLTRR---EGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATADVA 232
Cdd:PRK13638 164 TAGLDP----AGRTQMIAIIRRivaQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQA 233
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-226 |
7.11e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 91.73 E-value: 7.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFRDGT--FGLQD-INLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVE-P---SSGSVLIGGEDMTHVPP 73
Cdd:PRK11022 1 MALLNVDKLSVHFGDESapFRAVDrISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 74 ERRR------MGMVFQQhavwPHMSV--AKNVGYPL--ARSGQKGASISKRVERT---LALVGLEGFGSR---RPASLSG 137
Cdd:PRK11022 81 KERRnlvgaeVAMIFQD----PMTSLnpCYTVGFQImeAIKVHQGGNKKTRRQRAidlLNQVGIPDPASRldvYPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 138 GQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVA 217
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
....*....
gi 499323150 218 TPTELLSAP 226
Cdd:PRK11022 237 KAHDIFRAP 245
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-227 |
1.85e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 90.29 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIG---------GEDMTHVPPE---------RRRMGMV 81
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknNHELITNPYSkkiknfkelRRRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQqhavWPHM-----SVAKNVGY-PLARsGQKGASISKRVERTLALVGL-EGFGSRRPASLSGGQRQRVALARAIIADPT 154
Cdd:PRK13631 122 FQ----FPEYqlfkdTIEKDIMFgPVAL-GVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499323150 155 VLLLDEALSALDePLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPA 227
Cdd:PRK13631 197 ILIFDEPTAGLD-PKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-227 |
2.32e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.08 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 6 LRDLSVSFRDGTFGLQ---DINLKIEPEEFVVLIGPSGSGKT----TMLRTI-AGFVEPSSGSVLIGGEDMTHVPPERRR 77
Cdd:PRK15134 8 IENLSVAFRQQQTVRTvvnDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLLHASEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 78 ------MGMVFQQHAVW--PHMSVAKNVGYPLarSGQKGasISKRVERTLALVGLEGFGSRRPAS--------LSGGQRQ 141
Cdd:PRK15134 88 gvrgnkIAMIFQEPMVSlnPLHTLEKQLYEVL--SLHRG--MRREAARGEILNCLDRVGIRQAAKrltdyphqLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 142 RVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTE 221
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAAT 243
|
....*.
gi 499323150 222 LLSAPA 227
Cdd:PRK15134 244 LFSAPT 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
1.03e-19 |
|
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: 89.86 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTT---MLRTIAGFvEPSSGSVL-----------------I 63
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVlmhVLRGMDQY-EPTSGRIIyhvalcekcgyverpskV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 64 G------GEDMTHVPPE------------RRRMGMVFQQ-HAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGL 124
Cdd:TIGR03269 79 GepcpvcGGTLEPEEVDfwnlsdklrrriRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 125 EGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVhVTHDRAEAIS-IAD 203
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMV-LTSHWPEVIEdLSD 237
|
250 260
....*....|....*....|.
gi 499323150 204 RIVVLGNGRIQQVATPTELLS 224
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVA 258
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
13-224 |
1.60e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 86.80 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 13 FRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAG-FVEPS-------SGSVLIGGEDMTHVPPER--RRMGMVF 82
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGaprgarvTGDVTLNGEPLAAIDAPRlaRLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QQHAVWPHMSVAKNV---GYPLAR-SGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAI--------- 149
Cdd:PRK13547 90 QAAQPAFAFSAREIVllgRYPHARrAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 150 IADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
5-212 |
3.91e-19 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 88.40 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 5 KLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSS--GSVLIGGEDMTHvpPERRRMGMVF 82
Cdd:PLN03211 70 KISDETRQIQERTI-LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK--QILKRTGFVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QQHAVWPHMSVAKNVGY------PLARSGQKGASISKRVERTLALVGLEG--FGSRRPASLSGGQRQRVALARAIIADPT 154
Cdd:PLN03211 147 QDDILYPHLTVRETLVFcsllrlPKSLTKQEKILVAESVISELGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 155 VLLLDEALSALDEPLRDALRRELVSLTRReGLTTVHVTHDRAEAI-SIADRIVVLGNGR 212
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPSSRVyQMFDSVLVLSEGR 284
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-215 |
4.10e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 88.11 E-value: 4.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGMV 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQHAVWPHMsvaknvgyplaRSGQKGASISKRVERTLALVG------LEGfGSRRPASLSGGQRQRVALARAIIADPTV 155
Cdd:PRK10522 403 FTDFHLFDQL-----------LGPEGKPANPALVEKWLERLKmahkleLED-GRISNLKLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 156 LLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISiADRIVVLGNGRIQQ 215
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-203 |
1.46e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 83.93 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSS-----GSVLIGGEDM----THV 71
Cdd:PRK14258 5 IPAIKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 72 PPERRRMGMVFQQHAVWPhMSVAKNVGY--------------PLARSGQKGASISKRVERTLALVGLEgfgsrrpasLSG 137
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFP-MSVYDNVAYgvkivgwrpkleidDIVESALKDADLWDEIKHKIHKSALD---------LSG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 138 GQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIAD 203
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-224 |
2.14e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.03 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFRDGTFG-LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMG 79
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAalRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFQQhavwPHM---SVAKNVgyplaRSGQKGASISKRVErTLALVGLE-------------GFGSRRpasLSGGQRQRV 143
Cdd:PRK11160 418 VVSQR----VHLfsaTLRDNL-----LLAAPNASDEALIE-VLQQVGLEklleddkglnawlGEGGRQ---LSGGEQRRL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 144 ALARAIIADPTVLLLDEALSALDEplrdALRRELVSLTRR--EGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTE 221
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDA----ETERQILELLAEhaQNKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQE 559
|
...
gi 499323150 222 LLS 224
Cdd:PRK11160 560 LLA 562
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-211 |
2.14e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.99 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE---RRRMGM 80
Cdd:PRK09700 6 ISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWPHMSVAKNV-----------GYPLArsgqKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAI 149
Cdd:PRK09700 85 IYQELSVIDELTVLENLyigrhltkkvcGVNII----DWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499323150 150 IADPTVLLLDEALSALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNG 211
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-211 |
2.58e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 82.31 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVE--PSSGSVliggedmthvpperrrmgmVFQQHAVWPHMSVAKNV 97
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCV-------------------DVPDNQFGREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 98 GyplaRSGQKGASIskrveRTLALVGLegfGS-----RRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDA 172
Cdd:COG2401 107 G----RKGDFKDAV-----ELLNAVGL---SDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499323150 173 LRRELVSLTRREGLTTVHVTHdRAEAIS--IADRIVVLGNG 211
Cdd:COG2401 175 VARNLQKLARRAGITLVVATH-HYDVIDdlQPDLLIFVGYG 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-213 |
5.82e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.72 E-value: 5.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPER-RRMG--M 80
Cdd:PRK15439 12 LCARSISKQY-SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKaHQLGiyL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWPHMSVAKNVGYPLARSgqkgASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDE 160
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPKR----QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499323150 161 ALSALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:PRK15439 167 PTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-208 |
1.11e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.85 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 2 SSIKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDmTHVPPERRRMGMV 81
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-TRQALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQHAV-WPHMSVAKNVgYPLARSGQKG------ASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPT 154
Cdd:PRK15056 84 PQSEEVdWSFPVLVEDV-VMMGRYGHMGwlrrakKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499323150 155 VLLLDEALSALD---EPLRDALRRELvsltRREGLTTVHVTHDRAEAISIADRIVVL 208
Cdd:PRK15056 163 VILLDEPFTGVDvktEARIISLLREL----RDEGKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
6-237 |
3.19e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.98 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 6 LRDLSVSFRDGTFGLQdinlkIEPEEFVVLIGPSGSGKTTMLRTIAGFVePSSGSVLIGGEDMTHVPPER--RRMGMVFQ 83
Cdd:PRK03695 3 LNDVAVSTRLGPLSAE-----VRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAElaRHRAYLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHAVWPHMSVAKnvgYpLARSGQKGASIS---KRVERTLALVGLEGFGSRRPASLSGGQRQRVALA-------RAIIADP 153
Cdd:PRK03695 77 QQTPPFAMPVFQ---Y-LTLHQPDKTRTEavaSALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 154 TVLLLDEALSALDEPLRDALRReLVSLTRREGLTTVHVTHDRAEAISIADRI------VVLGNGRIQQVATPtELLSAPA 227
Cdd:PRK03695 153 QLLLLDEPMNSLDVAQQAALDR-LLSELCQQGIAVVMSSHDLNHTLRHADRVwllkqgKLLASGRRDEVLTP-ENLAQVF 230
|
250
....*....|
gi 499323150 228 TADVARFIVD 237
Cdd:PRK03695 231 GVNFRRLDVE 240
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-222 |
4.41e-17 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 82.15 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 2 SSIKLRDLSVSFR----DGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGE--DMTHVPPER 75
Cdd:COG4615 326 QTLELRGVTYRYPgedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQpvTADNREAYR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 76 RRMGMVFQQHAVWPHMsvaknvgYplarsGQKGASISKRVERTLALVGLEG--------FGSRRpasLSGGQRQRVALAR 147
Cdd:COG4615 406 QLFSAVFSDFHLFDRL-------L-----GLDGEADPARARELLERLELDHkvsvedgrFSTTD---LSQGQRKRLALLV 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 148 AIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAeAISIADRIVVLGNGRIQQVATPTEL 222
Cdd:COG4615 471 ALLEDRPILVFDEWAADQDPEFRRVFYTELLPELKARGKTVIAISHDDR-YFDLADRVLKMDYGKLVELTGPAAL 544
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-214 |
4.50e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 82.52 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLiGGEDMTHVPperrrmgmvfqQHAVWPHMSVAKNVgy 99
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-AERSIAYVP-----------QQAWIMNATVRGNI-- 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 100 pLARSGQKGASISKRV-----ERTLALV--GLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDA 172
Cdd:PTZ00243 742 -LFFDEEDAARLADAVrvsqlEADLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER 820
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499323150 173 LRRELVsLTRREGLTTVHVTHdRAEAISIADRIVVLGNGRIQ 214
Cdd:PTZ00243 821 VVEECF-LGALAGKTRVLATH-QVHVVPRADYVVALGDGRVE 860
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-226 |
6.85e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 81.68 E-value: 6.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGMVFQQhavwPHM---SVA 94
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSRLAVVSQT----PFLfsdTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 95 KNV--GYPLARSGQ--KGASISKRVERTLAL-VGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEpl 169
Cdd:PRK10789 407 NNIalGRPDATQQEieHVARLASVHDDILRLpQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG-- 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499323150 170 rdalRRE---LVSLTR-REGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLSAP 226
Cdd:PRK10789 485 ----RTEhqiLHNLRQwGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-218 |
1.43e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMtHVPPERRRMG- 79
Cdd:PRK11288 2 SPYLSFDGIGKTF-PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-RFASTTAALAa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 ---MVFQQ-HAVwPHMSVAKNVgyPLARSGQKGASISKRVERTLALVGLEGFG-----SRRPASLSGGQRQRVALARAII 150
Cdd:PRK11288 80 gvaIIYQElHLV-PEMTVAENL--YLGQLPHKGGIVNRRLLNYEAREQLEHLGvdidpDTPLKYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 151 ADPTVLLLDEALSALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRiqQVAT 218
Cdd:PRK11288 157 RNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGR--YVAT 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-213 |
2.10e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 19 GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPP-ERRRMGMVF-----QQHAVWPHMS 92
Cdd:PRK15439 278 GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaQRLARGLVYlpedrQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 93 VAKNV-GYPLARSG--QKGASISKRVERTLALVGLEGFGSRRPA-SLSGGQRQRVALARAIIADPTVLLLDEALSALDEP 168
Cdd:PRK15439 358 LAWNVcALTHNRRGfwIKPARENAVLERYRRALNIKFNHAEQAArTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499323150 169 LRDALRRELVSLTrREGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:PRK15439 438 ARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-225 |
3.26e-16 |
|
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: 79.99 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDG-TFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGM-V 81
Cdd:TIGR00957 1285 VEFRNYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKItI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQHAVWPHMSVAKNVGyPLARSGQKgasiskRVERTLALVGLEGFGSRRPA-----------SLSGGQRQRVALARAII 150
Cdd:TIGR00957 1365 IPQDPVLFSGSLRMNLD-PFSQYSDE------EVWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALL 1437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 151 ADPTVLLLDEALSALDEPLRDALRRELvsLTRREGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLSA 225
Cdd:TIGR00957 1438 RKTKILVLDEATAAVDLETDNLIQSTI--RTQFEDCTVLTIAH-RLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-229 |
4.30e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 79.63 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFRDGTFG-LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVP-PERRRMGM 80
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPvLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGlTDLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWPHMSVAKNVGyPLARSGQKG-------ASISKRVERTLalVGLEGFGSRRPASLSGGQRQRVALARAIIADP 153
Cdd:PLN03232 1314 IIPQSPVLFSGTVRFNID-PFSEHNDADlwealerAHIKDVIDRNP--FGLDAEVSEGGENFSVGQRQLLSLARALLRRS 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 154 TVLLLDEALSAL----DEPLRDALRRELVSLTRregLTTVHvthdRAEAISIADRIVVLGNGRIQQVATPTELLSAPATA 229
Cdd:PLN03232 1391 KILVLDEATASVdvrtDSLIQRTIREEFKSCTM---LVIAH----RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSA 1463
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-224 |
5.48e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 79.40 E-value: 5.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFR-DGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMthvpperRRMGMv 81
Cdd:PLN03130 1237 SIKFEDVVLRYRpELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI-------SKFGL- 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 fqqhavwphMSVAKNVGY----PLARSG-----------QKGASISKRVERT-LALV------GLEGFGSRRPASLSGGQ 139
Cdd:PLN03130 1309 ---------MDLRKVLGIipqaPVLFSGtvrfnldpfneHNDADLWESLERAhLKDVirrnslGLDAEVSEAGENFSVGQ 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 140 RQRVALARAIIADPTVLLLDEALSALDepLR-DAL-----RRELVSLTRregLTTVHvthdRAEAISIADRIVVLGNGRI 213
Cdd:PLN03130 1380 RQLLSLARALLRRSKILVLDEATAAVD--VRtDALiqktiREEFKSCTM---LIIAH----RLNTIIDCDRILVLDAGRV 1450
|
250
....*....|.
gi 499323150 214 QQVATPTELLS 224
Cdd:PLN03130 1451 VEFDTPENLLS 1461
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-224 |
7.19e-16 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 76.82 E-value: 7.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGE-----DMTHVPPERRRMGMVFQ-QHAVWPHMSV 93
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRisfssQFSWIMPGTIKENIIFGvSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 94 AKnvgyplarSGQKGASISKRVERTLALVGLEGFgsrrpaSLSGGQRQRVALARAIIADPTVLLLDEALSALD-----EP 168
Cdd:cd03291 133 VK--------ACQLEEDITKFPEKDNTVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDvftekEI 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 169 LRDALRRELVSLTRreglttVHVThDRAEAISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:cd03291 199 FESCVCKLMANKTR------ILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQS 247
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-212 |
1.11e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.66 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 17 TFG----LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGfVEPS---SGSVLIGGEDMT--HV-PPERRRMGMVFQQHA 86
Cdd:PRK13549 14 TFGgvkaLDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQasNIrDTERAGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 87 VWPHMSVAKNV--GYPLARSGQKG-ASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALS 163
Cdd:PRK13549 93 LVKELSVLENIflGNEITPGGIMDyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499323150 164 ALDEPLRDALrRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGR 212
Cdd:PRK13549 173 SLTESETAVL-LDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-226 |
1.84e-15 |
|
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: 77.17 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 15 DGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGfVEPS---SGSVLIGGEDM--THV-PPERRRMGMVFQQHAVW 88
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLkaSNIrDTERAGIVIIHQELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 89 PHMSVAKNV--GYPLARSGQKG--ASISKRVERTLALVGLEGFGSRRPAS-LSGGQRQRVALARAIIADPTVLLLDEALS 163
Cdd:TIGR02633 91 PELSVAENIflGNEITLPGGRMayNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499323150 164 ALDEPLRDALrRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGriQQVAT-PTELLSAP 226
Cdd:TIGR02633 171 SLTEKETEIL-LDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG--QHVATkDMSTMSED 231
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-224 |
2.30e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.01 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPS---SGSVLIGGEDMThVPPERRRMGMVFQQHAVWPHMSVAKN 96
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID-AKEMRAISAYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 97 VGYPLARSGQKGASISKRVERTLAL-------------VGLEGfgsrRPASLSGGQRQRVALARAIIADPTVLLLDEALS 163
Cdd:TIGR00955 120 LMFQAHLRMPRRVTKKEKRERVDEVlqalglrkcantrIGVPG----RVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499323150 164 ALDEPLRDALRRELVSLTRReGLTTVHVTHD-RAEAISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
10-224 |
3.26e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.09 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 10 SVSFRDGTFG---------LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEP-SSGSVLIGGEdMTHVPperrRMG 79
Cdd:PLN03130 614 AISIKNGYFSwdskaerptLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGT-VAYVP----QVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFqqhavwpHMSVAKNV--GYPLARSGQKGASISKRVERTLALV---GLEGFGsRRPASLSGGQRQRVALARAIIADPT 154
Cdd:PLN03130 689 WIF-------NATVRDNIlfGSPFDPERYERAIDVTALQHDLDLLpggDLTEIG-ERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 155 VLLLDEALSALD-----EPLRDALRRELVSLTRreglttVHVThDRAEAISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:PLN03130 761 VYIFDDPLSALDahvgrQVFDKCIKDELRGKTR------VLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-211 |
3.35e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 73.52 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVL----IGGEDMTHVPPERRRMGMVFQQHAVWP-HMSVA 94
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLlNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 95 KNV--GYPLARSGQKGASISKRVERTLALVGlegFGSR-----RPASLSGGQRQRVALARAIIADPTVLLLDEALSALDE 167
Cdd:cd03290 97 ENItfGSPFNKQRYKAVTDACSLQPDIDLLP---FGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499323150 168 PLRDALRRE-LVSLTRREGLTTVHVTHdRAEAISIADRIVVLGNG 211
Cdd:cd03290 174 HLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-222 |
4.47e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 76.32 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrdGTF-GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGE-----DMThvppERRR 77
Cdd:NF033858 267 IEARGLTMRF--GDFtAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvdagDIA----TRRR 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 78 MGMVFQQHAVWPHMSVAKNvgypL---AR-SGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADP 153
Cdd:NF033858 341 VGYMSQAFSLYGELTVRQN----LelhARlFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKP 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 154 TVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAiSIADRIVVLGNGRIQQVATPTEL 222
Cdd:NF033858 417 ELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAAL 484
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-225 |
5.27e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.61 E-value: 5.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 57 SSGSVLIGGEDMT-HVPPERRRMGMVFQQHAVWPHMSVAKNVGYplarsGQKGASIsKRVERTLALVGLEGFGSRRP--- 132
Cdd:PTZ00265 1275 NSGKILLDGVDICdYNLKDLRNLFSIVSQEPMLFNMSIYENIKF-----GKEDATR-EDVKRACKFAAIDEFIESLPnky 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 133 --------ASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHdRAEAISIADR 204
Cdd:PTZ00265 1349 dtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427
|
170 180
....*....|....*....|....*.
gi 499323150 205 IVVLGN-----GRIQQVATPTELLSA 225
Cdd:PTZ00265 1428 IVVFNNpdrtgSFVQAHGTHEELLSV 1453
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-219 |
5.36e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 5.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVliggedmthVPPERRRMGMVFQ 83
Cdd:PRK09544 5 VSLENVSVSFGQRRV-LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHAVWPHM--SVAKnvgYPLARSGQKGASISKRVERTLALVGLEgfgsrRP-ASLSGGQRQRVALARAIIADPTVLLLDE 160
Cdd:PRK09544 75 KLYLDTTLplTVNR---FLRLRPGTKKEDILPALKRVQAGHLID-----APmQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 161 ALSALD-------EPLRDALRRELvsltrreGLTTVHVTHDRAEAISIADRIVVLgNGRIQQVATP 219
Cdd:PRK09544 147 PTQGVDvngqvalYDLIDQLRREL-------DCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTP 204
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-207 |
8.74e-15 |
|
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: 72.83 E-value: 8.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 19 GLQDINLKIEPEEF-----VVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPperrrmgmvfQQHAVWPHMSV 93
Cdd:cd03237 9 TLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP----------QYIKADYEGTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 94 aknvgYPLARSGQKGASISKRVERTLAL-VGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDA 172
Cdd:cd03237 79 -----RDLLSSITKDFYTHPYFKTEIAKpLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180 190
....*....|....*....|....*....|....*
gi 499323150 173 LRRELVSLTRREGLTTVHVTHDRAEAISIADRIVV 207
Cdd:cd03237 154 ASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-213 |
1.26e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.99 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGE----DMTHVPPeRR 76
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPL-LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivaRLQQDPP-RN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 77 RMGMVF---------------QQHAVWPHMSV---AKNVGyPLAR-----SGQKGASISKRVERTLALVGLEGfgSRRPA 133
Cdd:PRK11147 79 VEGTVYdfvaegieeqaeylkRYHDISHLVETdpsEKNLN-ELAKlqeqlDHHNLWQLENRINEVLAQLGLDP--DAALS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 134 SLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLtrrEGlTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF---QG-SIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-195 |
3.84e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.43 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGgedmthvppERRRMGMVFQ 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLL-IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG---------ETVKLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHAvwpHMSVAKNVgYPLARSGQKGASISKRVERTLALVGLEGF-GS---RRPASLSGGQRQRVALARAIIADPTVLLLD 159
Cdd:TIGR03719 393 SRD---ALDPNKTV-WEEISGGLDIIKLGKREIPSRAYVGRFNFkGSdqqKKVGQLSGGERNRVHLAKTLKSGGNVLLLD 468
|
170 180 190
....*....|....*....|....*....|....*..
gi 499323150 160 EALSALD-EPLRdALRRELVSLTrreGLTTVhVTHDR 195
Cdd:TIGR03719 469 EPTNDLDvETLR-ALEEALLNFA---GCAVV-ISHDR 500
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
8-209 |
4.80e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 70.26 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 8 DLSVSfRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVppERRRMgMVFQQH-- 85
Cdd:PRK13543 16 ALAFS-RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG--DRSRF-MAYLGHlp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 86 AVWPHMSVAKNVGYPLARSGqkgasisKRVERT----LALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEA 161
Cdd:PRK13543 92 GLKADLSTLENLHFLCGLHG-------RRAKQMpgsaLAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499323150 162 LSALDEPLRDALRRELVSLTRREGLTTVhVTHDRAEAISIADRIVVLG 209
Cdd:PRK13543 165 YANLDLEGITLVNRMISAHLRGGGAALV-TTHGAYAAPPVRTRMLTLE 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-224 |
8.29e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 72.74 E-value: 8.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 27 IEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGED-MTHVPPERRRMGMVFQQHAVWPHMSVAKNVgYPLAR-S 104
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISDVHQNMGYCPQFDAIDDLLTGREHL-YLYARlR 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 105 GQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTrRE 184
Cdd:TIGR01257 2041 GVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII-RE 2119
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499323150 185 GLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:TIGR01257 2120 GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKS 2159
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-224 |
1.30e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.74 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 21 QDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMT-HVPPERRRMGMVF-----QQHAVWPHMSVA 94
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYitesrRDNGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 95 KNVGYP--LARSGQKGAS--ISKRVERTLA-----LVGLEGFG-SRRPASLSGGQRQRVALARAIIADPTVLLLDEALSA 164
Cdd:PRK09700 360 QNMAISrsLKDGGYKGAMglFHEVDEQRTAenqreLLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499323150 165 LDEplrdALRRELVSLTRR---EGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:PRK09700 440 IDV----GAKAEIYKVMRQladDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMS 498
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-235 |
2.95e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.92 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDgTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMThvppERRRMGMVFQ 83
Cdd:NF033858 2 ARLEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA----DARHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHA---------VWPHMSVAKNVGYpLAR-SGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADP 153
Cdd:NF033858 77 RIAympqglgknLYPTLSVFENLDF-FGRlFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 154 TVLLLDEALSALDePL-R-------DALRRElvsltrREGLTTVHVTH--DRAEAIsiaDRIVVLGNGRIQQVATPTELL 223
Cdd:NF033858 156 DLLILDEPTTGVD-PLsRrqfweliDRIRAE------RPGMSVLVATAymEEAERF---DWLVAMDAGRVLATGTPAELL 225
|
250
....*....|...
gi 499323150 224 SAPATADV-ARFI 235
Cdd:NF033858 226 ARTGADTLeAAFI 238
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-223 |
5.13e-13 |
|
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: 70.36 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 10 SVSFRDGTFG--------LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEdMTHVPperrrmgmv 81
Cdd:TIGR00957 636 SITVHNATFTwardlpptLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVP--------- 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 fqQHAVWPHMSVAKNV--GYPLARSGQKGAsiskrVERTLALVGLEGFGS-------RRPASLSGGQRQRVALARAIIAD 152
Cdd:TIGR00957 706 --QQAWIQNDSLRENIlfGKALNEKYYQQV-----LEACALLPDLEILPSgdrteigEKGVNLSGGQKQRVSLARAVYSN 778
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 153 PTVLLLDEALSALDEPLRDALRRELVSltrREGL----TTVHVTHdraeAISI---ADRIVVLGNGRIQQVATPTELL 223
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHIFEHVIG---PEGVlknkTRILVTH----GISYlpqVDVIIVMSGGKISEMGSYQELL 849
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-222 |
5.53e-13 |
|
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: 70.32 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 16 GTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGE-----DMTHVPPERRRMGMVFQ-QHAVWP 89
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRisfspQTSWIMPGTIKDNIIFGlSYDEYR 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 90 HMSVAKnvgyplarSGQKGASISKRVERTLALVGLEGFgsrrpaSLSGGQRQRVALARAIIADPTVLLLDEALSALD--- 166
Cdd:TIGR01271 518 YTSVIK--------ACQLEEDIALFPEKDKTVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDvvt 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 167 --EPLRDALRRELVSLTRreglttVHVThDRAEAISIADRIVVLGNGRIQQVATPTEL 222
Cdd:TIGR01271 584 ekEIFESCLCKLMSNKTR------ILVT-SKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
11-213 |
1.31e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 68.73 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 11 VSFRDGTFG-------LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGedmthvppeRRRMGmVFQ 83
Cdd:PLN03073 509 ISFSDASFGypggpllFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA---------KVRMA-VFS 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHAVwPHMSVAKNVGYPLARSgQKGASiSKRVERTLALVGLEGFGSRRPA-SLSGGQRQRVALARAIIADPTVLLLDEAL 162
Cdd:PLN03073 579 QHHV-DGLDLSSNPLLYMMRC-FPGVP-EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499323150 163 SALDEPLRDALRRELVSLtrrEGlTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:PLN03073 656 NHLDLDAVEALIQGLVLF---QG-GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-232 |
1.58e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 21 QDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMT-HVPPERRRMGMVF-----QQHAVWPHMSVA 94
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 95 KNVGYPLARSGQK-GASISKRVERTLALVGLEGFGSRRPA------SLSGGQRQRVALARAIIADPTVLLLDEALSALDE 167
Cdd:PRK11288 350 DNINISARRHHLRaGCLINNRWEAENADRFIRSLNIKTPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499323150 168 PLRDALRRELVSLTRReGLTTVHVTHDRAEAISIADRIVVLGNGRI-----QQVATPTELLSA--PATADVA 232
Cdd:PRK11288 430 GAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIagelaREQATERQALSLalPRTSAAV 500
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-214 |
1.97e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.93 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 22 DINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPS-SGSVLIGGEDM-------------THVPPERRRMGMVfqqhav 87
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVdirnpaqairagiAMVPEDRKRHGIV------ 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 88 wPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRP------ASLSGGQRQRVALARAIIADPTVLLLDEA 161
Cdd:TIGR02633 352 -PILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTAspflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499323150 162 LSALDEPLRDALRReLVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQ 214
Cdd:TIGR02633 431 TRGVDVGAKYEIYK-LINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-173 |
1.97e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.84 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGgedmthvppERRRMGMVFQ 83
Cdd:PRK11819 325 IEAENLSKSFGDRLL-IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG---------ETVKLAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 84 QHAvwpHMSVAKNV------GYPLARSGQKgaSISKRvertlALVGLEGF-GS---RRPASLSGGQRQRVALARAIIADP 153
Cdd:PRK11819 395 SRD---ALDPNKTVweeisgGLDIIKVGNR--EIPSR-----AYVGRFNFkGGdqqKKVGVLSGGERNRLHLAKTLKQGG 464
|
170 180
....*....|....*....|....
gi 499323150 154 TVLLLDEALSALD-EPLR---DAL 173
Cdd:PRK11819 465 NVLLLDEPTNDLDvETLRaleEAL 488
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-227 |
2.30e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.06 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFR--DGTF-GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPS---SGSVLIGGEDMTHVPpE 74
Cdd:PRK09473 10 DALLDVKDLRVTFStpDGDVtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLP-E 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 75 RR-------RMGMVFQQ--HAVWPHMSVAKNVGYPLARsgQKGASISKRVE---RTLALVGLEGFGSRR---PASLSGGQ 139
Cdd:PRK09473 89 KElnklraeQISMIFQDpmTSLNPYMRVGEQLMEVLML--HKGMSKAEAFEesvRMLDAVKMPEARKRMkmyPHEFSGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 140 RQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATP 219
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNA 246
|
....*...
gi 499323150 220 TELLSAPA 227
Cdd:PRK09473 247 RDVFYQPS 254
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-222 |
3.86e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.50 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 3 SIKLRDLSVSFRDG-TFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDM-THVPPERRRMGM 80
Cdd:PTZ00243 1308 SLVFEGVQMRYREGlPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIgAYGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWPHMSVAKNVGYPLARSgqkgasiSKRVERTLALVGL--------EGFGSR---RPASLSGGQRQRVALARAI 149
Cdd:PTZ00243 1388 MIPQDPVLFDGTVRQNVDPFLEAS-------SAEVWAALELVGLrervasesEGIDSRvleGGSNYSVGQRQLMCMARAL 1460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 150 IA-DPTVLLLDEALSALDEplrdALRRELVSLTRR--EGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTEL 222
Cdd:PTZ00243 1461 LKkGSGFILMDEATANIDP----ALDRQIQATVMSafSAYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-227 |
5.57e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.80 E-value: 5.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 6 LRDLSVSFRDG---TFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSV-------------LIGGEDMT 69
Cdd:PRK10261 15 VENLNIAFMQEqqkIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 70 HVPPERRR---MGMVFQQhavwPHMSVAK--NVGYPLARS-----GQKGASISKRVERTLALVGL---EGFGSRRPASLS 136
Cdd:PRK10261 95 AAQMRHVRgadMAMIFQE----PMTSLNPvfTVGEQIAESirlhqGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 137 GGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQV 216
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
|
250
....*....|.
gi 499323150 217 ATPTELLSAPA 227
Cdd:PRK10261 251 GSVEQIFHAPQ 261
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
10-222 |
7.42e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.92 E-value: 7.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 10 SVSFRDGTFG---------LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPS-SGSVLIGGEdMTHVPperrRMG 79
Cdd:PLN03232 614 AISIKNGYFSwdsktskptLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGS-VAYVP----QVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 80 MVFqqhavwpHMSVAKNVgypLARSGQKGASISKRVERTLALVGLEGFGSR-------RPASLSGGQRQRVALARAIIAD 152
Cdd:PLN03232 689 WIF-------NATVRENI---LFGSDFESERYWRAIDVTALQHDLDLLPGRdlteigeRGVNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499323150 153 PTVLLLDEALSALD-----EPLRDALRRELvsltrrEGLTTVHVThDRAEAISIADRIVVLGNGRIQQVATPTEL 222
Cdd:PLN03232 759 SDIYIFDDPLSALDahvahQVFDSCMKDEL------KGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-213 |
1.03e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.28 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGfvEPS----SGSVLIGGEDMTHVPPERR-RM 78
Cdd:CHL00131 8 LEIKNLHASVNENEI-LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERaHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 79 G--MVFQqhavwphmsvaknvgYPLARSGQKGASI------SKRVERT----------------LALVGL---------- 124
Cdd:CHL00131 85 GifLAFQ---------------YPIEIPGVSNADFlrlaynSKRKFQGlpeldplefleiinekLKLVGMdpsflsrnvn 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 125 EGFgsrrpaslSGGQRQRVALARAIIADPTVLLLDEALSALDeplRDALR--RELVSLTRREGLTTVHVTH-DRAEAISI 201
Cdd:CHL00131 150 EGF--------SGGEKKRNEILQMALLDSELAILDETDSGLD---IDALKiiAEGINKLMTSENSIILITHyQRLLDYIK 218
|
250
....*....|..
gi 499323150 202 ADRIVVLGNGRI 213
Cdd:CHL00131 219 PDYVHVMQNGKI 230
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-210 |
1.18e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 21 QDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIG-GEDMTHVPPE--RRRMGMVFQQHAVWPHmSVAKNV 97
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKwwRSKIGVVSQDPLLFSN-SIKNNI 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 98 GYPL----------------ARSGQKGA------------------------------------------SISKRV---- 115
Cdd:PTZ00265 481 KYSLyslkdlealsnyynedGNDSQENKnkrnscrakcagdlndmsnttdsneliemrknyqtikdsevvDVSKKVlihd 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 116 ------ERTLALVGlegfgsRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTV 189
Cdd:PTZ00265 561 fvsalpDKYETLVG------SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
250 260
....*....|....*....|.
gi 499323150 190 HVTHdRAEAISIADRIVVLGN 210
Cdd:PTZ00265 635 IIAH-RLSTIRYANTIFVLSN 654
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-213 |
1.37e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 19 GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE-------------RRRMGMVFQqh 85
Cdd:PRK10762 267 GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglangivyisedRKRDGLVLG-- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 86 avwphMSVAKNVGYP-LARSGQKGASISKRVERTLALVGLEGFGSRRPA------SLSGGQRQRVALARAIIADPTVLLL 158
Cdd:PRK10762 345 -----MSVKENMSLTaLRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSmeqaigLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 159 DEALSALDEplrdALRRELVSLTRR---EGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:PRK10762 420 DEPTRGVDV----GAKKEIYQLINQfkaEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-212 |
1.73e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 61.62 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 31 EFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVL-IGGEDMTHVPPERRRMGMVFqqhavwphmsvaknvgyplarsgqkga 109
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLIIVG--------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 110 siskrvertlalvglegfgsRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSL----TRREG 185
Cdd:smart00382 56 --------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRllllLKSEK 115
|
170 180 190
....*....|....*....|....*....|...
gi 499323150 186 LTTVHVTH------DRAEAISIADRIVVLGNGR 212
Cdd:smart00382 116 NLTVILTTndekdlGPALLRRRFDRRIVLLLIL 148
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-167 |
2.15e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.27 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTH-VPPERRRMGMVFQQHAVWPHMSVAKNVG 98
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 99 YPLARSgqkgaSISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDE 167
Cdd:PRK13540 97 YDIHFS-----PGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-213 |
2.59e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 62.28 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFRDGTFG---LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPS---SGSVLIGGEDM--THVP 72
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKipiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYkeFAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 73 PeRRRMGMVFQQHAVWPHMSvaknvgyplarsgqkgasiskrVERTLALVgLEGFGSRRPASLSGGQRQRVALARAIIAD 152
Cdd:cd03233 81 Y-PGEIIYVSEEDVHFPTLT----------------------VRETLDFA-LRCKGNEFVRGISGGERKRVSIAEALVSR 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 153 PTVLLLDEALSALDEplrdALRRELVS----LTRREGLTT-VHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:cd03233 137 ASVLCWDNSTRGLDS----STALEILKcirtMADVLKTTTfVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
40-214 |
2.76e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 40 GSGKTTMLRTIAGfVEP--SSGSVLIGGEDMT-------------HVPPERRRMGMVfqqhavwPHMSVAKNVGYPLARS 104
Cdd:PRK13549 298 GAGRTELVQCLFG-AYPgrWEGEIFIDGKPVKirnpqqaiaqgiaMVPEDRKRDGIV-------PVMGVGKNITLAALDR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 105 GQKGASISKRVERTLALVGLEGFGSRRP------ASLSGGQRQRVALARAIIADPTVLLLDEALSALD-----EPLRdaL 173
Cdd:PRK13549 370 FTGGSRIDDAAELKTILESIQRLKVKTAspelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgakyEIYK--L 447
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499323150 174 RRELVsltrREGLTTVHVTHDRAEAISIADRIVVLGNGRIQ 214
Cdd:PRK13549 448 INQLV----QQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-226 |
3.57e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.28 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDLSVSFR--DGTFGLQD-INLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEP----SSGSVLIGGEDMTHV-P 72
Cdd:PRK15093 1 MPLLDIRNLTIEFKtsDGWVKAVDrVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLsP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 73 PERRR-----MGMVFQ--QHAVWPHMSVAKNVGYPLARSGQKG---ASISKRVERTLALVGLEGFGSRR------PASLS 136
Cdd:PRK15093 81 RERRKlvghnVSMIFQepQSCLDPSERVGRQLMQNIPGWTYKGrwwQRFGWRKRRAIELLHRVGIKDHKdamrsfPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 137 GGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQV 216
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250
....*....|
gi 499323150 217 ATPTELLSAP 226
Cdd:PRK15093 241 APSKELVTTP 250
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-238 |
6.23e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.02 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 22 DINLKIEPEEFVVLIGPSGSGKT----TMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRRMGMVFQ--QHAVWPHMSVAK 95
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQnpRSAFNPLHTMHT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 96 NVGYPLARSGQKGASisKRVERTLALVGLEGFG---SRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDA 172
Cdd:PRK10418 101 HARETCLALGKPADD--ATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQAR 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 173 LRRELVSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLSAPATAdVARFIVDA 238
Cdd:PRK10418 179 ILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA-VTRSLVSA 243
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-206 |
6.45e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.37 E-value: 6.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 6 LRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGgedmthvppERRRMGMVFQQH 85
Cdd:PRK15064 322 VENLTKGFDNGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS---------ENANIGYYAQDH 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 86 AV----------WphMSVAKNVGYP-------LARSGQKGASISKRVErtlalvglegfgsrrpaSLSGGQRQRVALARA 148
Cdd:PRK15064 392 AYdfendltlfdW--MSQWRQEGDDeqavrgtLGRLLFSQDDIKKSVK-----------------VLSGGEKGRMLFGKL 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499323150 149 IIADPTVLLLDEALSALD----EPLRDALRrelvsltRREGlTTVHVTHDRAEAISIADRIV 206
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDmesiESLNMALE-------KYEG-TLIFVSHDREFVSSLATRII 506
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-218 |
1.02e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.82 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 6 LRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMT-HVPPERRRMG--MVF 82
Cdd:PRK10982 1 MSNISKSF-PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGisMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QQHAVWPHMSVAKNVGypLARSGQKGASI--SKRVERTLAL---VGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLL 157
Cdd:PRK10982 80 QELNLVLQRSVMDNMW--LGRYPTKGMFVdqDKMYRDTKAIfdeLDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499323150 158 LDEALSALDEPLRDALRRELVSLTRReGLTTVHVTHDRAEAISIADRIVVLGNGriQQVAT 218
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG--QWIAT 215
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-212 |
1.14e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.50 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGfVEPS---SGSVLIGGEdmthvppERR--------RMGMVF--QQHA 86
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGE-------VCRfkdirdseALGIVIihQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 87 VWPHMSVAKNV--GYPLARSGqkgaSIS-----KRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLD 159
Cdd:NF040905 89 LIPYLSIAENIflGNERAKRG----VIDwnetnRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499323150 160 EALSALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGR 212
Cdd:NF040905 165 EPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-224 |
1.62e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.95 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKLRDlsvsfrdGTFGLQDIN------LKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE 74
Cdd:PRK10938 1 MSSLQISQ-------GTFRLSDTKtlqlpsLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 75 RrrmgmvfQQHAV---WPH-----MSVAK-NVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVAL 145
Cdd:PRK10938 74 Q-------LQKLVsdeWQRnntdmLSPGEdDTGRTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 146 ARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTrREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:PRK10938 147 CQALMSEPDLLILDEPFDGLDVASRQQLAELLASLH-QSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-224 |
3.72e-10 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 59.54 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFG-LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPE--RRRMGM 80
Cdd:cd03288 20 IKIHDLCVRYENNLKPvLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHtlRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVW---------PHMSVAKNVGYPLARSGQKgasisKRVERTLAlVGLEGFGSRRPASLSGGQRQRVALARAIIA 151
Cdd:cd03288 100 ILQDPILFsgsirfnldPECKCTDDRLWEALEIAQL-----KNMVKSLP-GGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499323150 152 DPTVLLLDEALSALDEPLRDALRRelVSLTRREGLTTVHVTHdRAEAISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQK--VVMTAFADRTVVTIAH-RVSTILDADLVLVLSRGILVECDTPENLLA 243
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
2-193 |
5.47e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 60.53 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 2 SSIKLRDLSVSFRDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGfVEPSSGSVLiggedmthVPPERRRMGMV 81
Cdd:TIGR00954 450 NGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGE-LWPVYGGRL--------TKPAKGKLFYV 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 FQQhavwPHMSVA---KNVGYPLARSGQKGASIS-KRVERTLALVGLE-------GFGSRRPAS--LSGGQRQRVALARA 148
Cdd:TIGR00954 521 PQR----PYMTLGtlrDQIIYPDSSEDMKRRGLSdKDLEQILDNVQLThileregGWSAVQDWMdvLSGGEKQRIAMARL 596
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499323150 149 IIADPTVLLLDEALSALDEPLRDALRRelvsLTRREGLTTVHVTH 193
Cdd:TIGR00954 597 FYHKPQFAILDECTSAVSVDVEGYMYR----LCREFGITLFSVSH 637
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-213 |
5.60e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 5.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVL-------IGGEDMthvppERRRMGMVF---QQHAVWP 89
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEgvitydgITPEEI-----KKHYRGDVVynaETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 90 HMSVAKNVGYPLA-RSGQ---KGAS----ISKRVERTLALVGLE-----GFGSRRPASLSGGQRQRVALARAIIADPTVL 156
Cdd:TIGR00956 152 HLTVGETLDFAARcKTPQnrpDGVSreeyAKHIADVYMATYGLShtrntKVGNDFVRGVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 157 LLDEALSALDEplrdALRRELVSLTRreglTTVHVTHDRA---------EAISIADRIVVLGNGRI 213
Cdd:TIGR00956 232 CWDNATRGLDS----ATALEFIRALK----TSANILDTTPlvaiyqcsqDAYELFDKVIVLYEGYQ 289
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-195 |
9.13e-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: 59.95 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVliggedmthVPPERRRMGMVFQQHAVWPHMSVAKNV-- 97
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA---------RPQPGIKVGYLPQEPQLDPTKTVRENVee 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 98 -------------------GYP-------LARSG--------QKGASISKRVERTL-ALvglegfgsRRP------ASLS 136
Cdd:TIGR03719 92 gvaeikdaldrfneisakyAEPdadfdklAAEQAelqeiidaADAWDLDSQLEIAMdAL--------RCPpwdadvTKLS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 137 GGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRElvsLTRREGlTTVHVTHDR 195
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH---LQEYPG-TVVAVTHDR 218
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
20-173 |
1.87e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.80 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPpeRRRMGMVFQQHAVWPHMSVAKNVGY 99
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--KPYCTYIGHNLGLKLEMTVFENLKF 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499323150 100 plarsgqkGASISKRVERTLALV---GLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDAL 173
Cdd:PRK13541 94 --------WSEIYNSAETLYAAIhyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
22-208 |
1.98e-09 |
|
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: 56.43 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 22 DINLKIEPEEF-----VVLIGPSGSGKTTMLRTIAGFVEPSSGSVliggedmthvpperrrmgmvfqqhaVWPHMSVAKN 96
Cdd:cd03222 12 VFFLLVELGVVkegevIGIVGPNGTGKTTAVKILAGQLIPNGDND-------------------------EWDGITPVYK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 97 VGYplarsgqkgasiskrvertlalvglegfgsrrpASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRE 176
Cdd:cd03222 67 PQY---------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA 113
|
170 180 190
....*....|....*....|....*....|..
gi 499323150 177 LVSLTRREGLTTVHVTHDRAEAISIADRIVVL 208
Cdd:cd03222 114 IRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-213 |
2.65e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 1 MSSIKlrDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGF--VEPSSGSVLIGGEDMTHVPPERRR- 77
Cdd:PRK09580 1 MLSIK--DLHVSVEDKAI-LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 78 --MGMVFQQHAVWPHMS-----------VAKNVGY-PLARsgqkgASISKRVERTLALVGLegfgsrrPASL-------- 135
Cdd:PRK09580 78 egIFMAFQYPVEIPGVSnqfflqtalnaVRSYRGQePLDR-----FDFQDLMEEKIALLKM-------PEDLltrsvnvg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 136 -SGGQRQRVALARAIIADPTVLLLDEALSALDeplRDALR--RELVSLTRREGLTTVHVTH-DRAEAISIADRIVVLGNG 211
Cdd:PRK09580 146 fSGGEKKRNDILQMAVLEPELCILDESDSGLD---IDALKivADGVNSLRDGKRSFIIVTHyQRILDYIKPDYVHVLYQG 222
|
..
gi 499323150 212 RI 213
Cdd:PRK09580 223 RI 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-224 |
6.44e-09 |
|
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: 56.02 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRD-GTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEpSSGSVLIGGEDMTHVPPE--RRRMGM 80
Cdd:cd03289 3 MTVKDLTAKYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQkwRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWPHmSVAKNvgypLARSGQ-KGASISKRVERtlalVGLEGFGSRRPASL-----------SGGQRQRVALARA 148
Cdd:cd03289 82 IPQKVFIFSG-TFRKN----LDPYGKwSDEEIWKVAEE----VGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 149 IIADPTVLLLDEALSALDEPLRDALRRelvSLTRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELLS 224
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPITYQVIRK---TLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-211 |
8.85e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.55 E-value: 8.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFrDGTFGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTHVPPERRR---MGM 80
Cdd:PRK10762 5 LQLKGIDKAF-PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 81 VFQQHAVWPHMSVAKNVGypLAR--SGQKGASISKRV----ERTLALVGLEgFGSRRPAS-LSGGQRQRVALARAIIADP 153
Cdd:PRK10762 84 IHQELNLIPQLTIAENIF--LGRefVNRFGRIDWKKMyaeaDKLLARLNLR-FSSDKLVGeLSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499323150 154 TVLLLDEALSALDEPLRDALR---RELvsltRREGLTTVHVTHDRAEAISIADRIVVLGNG 211
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFrviREL----KSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-198 |
1.05e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGfVEPSSGS---VLIG-----GEDMTHVppeR 75
Cdd:PRK10938 261 IVLNNGVVSYNDRPI-LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGYSndlTLFGrrrgsGETIWDI---K 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 76 RRMGMVFQQ-HAVWPHMSVAKNV---------GYPLARSGQKgasiSKRVERTLALVGLEGFGSRRP-ASLSGGQrQRVA 144
Cdd:PRK10938 336 KHIGYVSSSlHLDYRVSTSVRNVilsgffdsiGIYQAVSDRQ----QKLAQQWLDILGIDKRTADAPfHSLSWGQ-QRLA 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 145 L-ARAIIADPTVLLLDEALSALDePLRDALRRELVSLTRREGLTT-VHVTHDRAEA 198
Cdd:PRK10938 411 LiVRALVKHPTLLILDEPLQGLD-PLNRQLVRRFVDVLISEGETQlLFVSHHAEDA 465
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
114-213 |
1.73e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.51 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 114 RVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRRELVSLTrREGLTTVHVTH 193
Cdd:NF000106 124 RADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQ 202
|
90 100
....*....|....*....|
gi 499323150 194 DRAEAISIADRIVVLGNGRI 213
Cdd:NF000106 203 YMEEAEQLAHELTVIDRGRV 222
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-214 |
3.27e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 4 IKLRDLSVSFRDGTFgLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSV-LIGGEDMTHvpperrrmgmvF 82
Cdd:PRK10636 313 LKMEKVSAGYGDRII-LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGY-----------F 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QQHavwpHMSVAKNVGYPLarsgQKGASISKRVERTLALVGLEGFG------SRRPASLSGGQRQRVALARAIIADPTVL 156
Cdd:PRK10636 381 AQH----QLEFLRADESPL----QHLARLAPQELEQKLRDYLGGFGfqgdkvTEETRRFSGGEKARLVLALIVWQRPNLL 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 157 LLDEALSALDEPLRDALRRELVSLtrrEGLTTVhVTHDRAEAISIADRIVVLGNGRIQ 214
Cdd:PRK10636 453 LLDEPTNHLDLDMRQALTEALIDF---EGALVV-VSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-211 |
3.75e-08 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 53.42 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTM-LRTIAG-----FVEPSSgsvliggedmthvPPERRRMGM-----VFQQHAVW 88
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLaFDTIYAegqrrYVESLS-------------AYARQFLGQmdkpdVDSIEGLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 89 PHMSVAKNVGYPLARS--GQKG------------ASISKRVeRTLALVGLEGFG-SRRPASLSGGQRQRVALARAIIADP 153
Cdd:cd03270 78 PAIAIDQKTTSRNPRStvGTVTeiydylrllfarVGIRERL-GFLVDVGLGYLTlSRSAPTLSGGEAQRIRLATQIGSGL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 154 TVLL--LDEALSALDEPLRDALRRELVSLtRREGLTTVHVTHDRaEAISIADRIVVLGNG 211
Cdd:cd03270 157 TGVLyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE-DTIRAADHVIDIGPG 214
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
35-196 |
5.77e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 35 LIGPSGSGKTTMLRTIAGFVEPSSGSVLIGgedmTHVPperrrmgmV--FQQH--AVWPHMSVAKNVGyplarSGQKGAS 110
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLE--------VayFDQHraELDPEKTVMDNLA-----EGKQEVM 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 111 ISKRVERTLALvgLEGF-----GSRRPA-SLSGGQRQRVALARAIIADPTVLLLDEALSALD-EPLRdaLRRELvsLTRR 183
Cdd:PRK11147 413 VNGRPRHVLGY--LQDFlfhpkRAMTPVkALSGGERNRLLLARLFLKPSNLLILDEPTNDLDvETLE--LLEEL--LDSY 486
|
170
....*....|...
gi 499323150 184 EGlTTVHVTHDRA 196
Cdd:PRK11147 487 QG-TVLLVSHDRQ 498
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-208 |
1.10e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.37 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 35 LIGPSGSGKTTMLRTIAGFVEPSSGSvlIGGE-DMTHVPPERRrmGMVFQQH---AVWPHMSVAKNVGY----PLARSGQ 106
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGK--FDDPpDWDEILDEFR--GSELQNYftkLLEGDVKVIVKPQYvdliPKAVKGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 107 KGASISKRVER-TLALV----GLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALDEPLR---DALRRELV 178
Cdd:cd03236 107 VGELLKKKDERgKLDELvdqlELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaARLIRELA 186
|
170 180 190
....*....|....*....|....*....|
gi 499323150 179 sltrREGLTTVHVTHDRAEAISIADRIVVL 208
Cdd:cd03236 187 ----EDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-166 |
1.84e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 50.70 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTML-----RTIAGFVEpssGSVLIGGEDMThvPPERRRMGMVFQQHAVWPHMSVA 94
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLdvlagRKTAGVIT---GEILINGRPLD--KNFQRSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499323150 95 KnvgyPLARSGqkgasiskrvertlALVGlegfgsrrpasLSGGQRQRVALARAIIADPTVLLLDEALSALD 166
Cdd:cd03232 98 E----ALRFSA--------------LLRG-----------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-166 |
4.93e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 29 PEEFVVLIGPSGSGKTTMLRTIAGFVepsSGSVLIGGEDMTHVPPE----RRRMGMVFQQHAVWPHMSVAKNVGYPLARS 104
Cdd:TIGR00956 788 PGTLTALMGASGAGKTTLLNVLAERV---TTGVITGGDRLVNGRPLdssfQRSIGYVQQQDLHLPTSTVRESLRFSAYLR 864
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 105 GQKGASISKR---VERTL----------ALVGLEGFGsrrpasLSGGQRQRVALARAIIADPTVLL-LDEALSALD 166
Cdd:TIGR00956 865 QPKSVSKSEKmeyVEEVIkllemesyadAVVGVPGEG------LNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
11-207 |
5.22e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 11 VSFRDGTFGLQDINLKIEP-----EEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGgEDMTHVPperrrmgmvfQQH 85
Cdd:PRK13409 341 VEYPDLTKKLGDFSLEVEGgeiyeGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKP----------QYI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 86 AVWPHMSVAKNvgypLARSGQKGAS------ISKRVertlalvGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLD 159
Cdd:PRK13409 410 KPDYDGTVEDL----LRSITDDLGSsyykseIIKPL-------QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLD 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499323150 160 EALSALDEPLR----DALRRelvsLTRREGLTTVHVTHDRAEAISIADRIVV 207
Cdd:PRK13409 479 EPSAHLDVEQRlavaKAIRR----IAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-213 |
9.05e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPS---SGSVLIGGEDMTHVPPeRRRMGMVFQQHAVWPHMSV--- 93
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVP-RKTSAYISQNDVHVGVMTVket 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 94 ------AKNVGY------PLAR-------------------SGQKGASISKRVERTLALVGLE-----GFGSRRPASLSG 137
Cdd:PLN03140 260 ldfsarCQGVGTrydllsELARrekdagifpeaevdlfmkaTAMEGVKSSLITDYTLKILGLDickdtIVGDEMIRGISG 339
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 138 GQRQRVALARAIIADPTVLLLDEALSALDEPLRDALRR---ELVSLTrrEGLTTVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:PLN03140 340 GQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKclqQIVHLT--EATVLMSLLQPAPETFDLFDDIILLSEGQI 416
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-213 |
9.27e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 9.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEDMTH-------------VPPERRRMGmvfqqha 86
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneainhgfalVTEERRSTG------- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 87 VWPHMSVAKNVGYPLARS--GQKGASISKRVERTLALVgLEGFGSRRPA------SLSGGQRQRVALARAIIADPTVLLL 158
Cdd:PRK10982 337 IYAYLDIGFNSLISNIRNykNKVGLLDNSRMKSDTQWV-IDSMRVKTPGhrtqigSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499323150 159 DEALSALDEPLRDALRRELVSLTRRE-GLttVHVTHDRAEAISIADRIVVLGNGRI 213
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAKKDkGI--IIISSEMPELLGITDRILVMSNGLV 469
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
5-167 |
2.00e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.50 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 5 KLRDLSVSFRDGTF--GLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEdmthvpperrrMGMVF 82
Cdd:PRK13545 23 KLKDLFFRSKDGEYhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEAL 162
Cdd:PRK13545 92 ISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAL 171
|
....*
gi 499323150 163 SALDE 167
Cdd:PRK13545 172 SVGDQ 176
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
133-195 |
2.45e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 2.45e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499323150 133 ASLSGGQRQRVALARAIIADPTVLLLDEALSALDEplrdalrrELVS-----LTRREGlTTVHVTHDR 195
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--------ESVAwleqfLHDYPG-TVVAVTHDR 220
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-207 |
2.45e-06 |
|
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: 49.01 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 26 KIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVliggedmthvpperrrmgmvfqqhavwphmSVAKNVGY-Plars 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------------------------------DEDLKISYkP---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 105 gQK-GASISKRVERTLALVGLEGFGS------------------RRPASLSGGQRQRVALARAIIADPTVLLLDEALSAL 165
Cdd:COG1245 408 -QYiSPDYDGTVEEFLRSANTDDFGSsyykteiikplgleklldKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499323150 166 DEPLR----DALRRelvsLTRREGLTTVHVTHDraeaIS----IADRIVV 207
Cdd:COG1245 487 DVEQRlavaKAIRR----FAENRGKTAMVVDHD----IYlidyISDRLMV 528
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-211 |
2.47e-06 |
|
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: 47.32 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTMLRTIagfVEPSSGSVLIGGedmthvPPERRRMGMVFqqhavwphmsvaknvgy 99
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG---LYASGKARLISF------LPKFSRNKLIF----------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 100 plarsgqkgasISKRveRTLALVGLEGFGSRRPAS-LSGGQRQRVALARAIIADP--TVLLLDEALSALDEPLRDALRRE 176
Cdd:cd03238 65 -----------IDQL--QFLIDVGLGYLTLGQKLStLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEV 131
|
170 180 190
....*....|....*....|....*....|....*
gi 499323150 177 LVSLtRREGLTTVHVTHDRaEAISIADRIVVLGNG 211
Cdd:cd03238 132 IKGL-IDLGNTVILIEHNL-DVLSSADWIIDFGPG 164
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
5-223 |
3.53e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.89 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 5 KLRDLSVSFRDGT--FGLQDINLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGEdmthvpperrrMGMVF 82
Cdd:PRK13546 23 RMKDALIPKHKNKtfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 83 QQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEAL 162
Cdd:PRK13546 92 ISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499323150 163 SALDEPLRDALRRELVSLtRREGLTTVHVTHDRAEAISIADRIVVLGNGRIQQVATPTELL 223
Cdd:PRK13546 172 SVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
122-226 |
5.14e-06 |
|
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: 48.47 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 122 VGLEGFG-SRRPASLSGGQRQRVALARAIIADptvllLDEALSALDEP-----LRDALR--RELVSLtRREGLTTVHVTH 193
Cdd:TIGR00630 475 VGLDYLSlSRAAGTLSGGEAQRIRLATQIGSG-----LTGVLYVLDEPsiglhQRDNRRliNTLKRL-RDLGNTLIVVEH 548
|
90 100 110
....*....|....*....|....*....|....*....
gi 499323150 194 DRaEAISIADRIVVLG------NGRIQQVATPTELLSAP 226
Cdd:TIGR00630 549 DE-DTIRAADYVIDIGpgagehGGEVVASGTPEEILANP 586
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
10-206 |
1.53e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 10 SVSFRDGTFGLQD-INLKIEPEEFVVLIGPSGSGKTTMLRTIAGFVEPSSGSVLIGGE-DMTHVPPERRRMGMV------ 81
Cdd:PRK10636 6 SLQIRRGVRVLLDnATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPALPQPaleyvi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 82 -----FQQHAVWPHMSVAKNVGYPLARSGQKGASISKRVERTLALVGLEGFGS-----RRPAS-LSGGQRQRVALARAII 150
Cdd:PRK10636 86 dgdreYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFsneqlERPVSdFSGGWRMRLNLAQALI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499323150 151 ADPTVLLLDEALSALDeplRDA---LRRELVSLTRreglTTVHVTHDRAEAISIADRIV 206
Cdd:PRK10636 166 CRSDLLLLDEPTNHLD---LDAviwLEKWLKSYQG----TLILISHDRDFLDPIVDKII 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-208 |
4.56e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 35 LIGPSGSGKTTMLRTIAGFVEPSSGSVliggedmtHVPPE-----RRRMGMVFQQH-----------AVWPHM------S 92
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGELIPNLGDY--------EEEPSwdevlKRFRGTELQNYfkklyngeikvVHKPQYvdlipkV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 93 VAKNVGYPLARSGQKGAsISKRVERtlalVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALD--EPLR 170
Cdd:PRK13409 176 FKGKVRELLKKVDERGK-LDEVVER----LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirQRLN 250
|
170 180 190
....*....|....*....|....*....|....*....
gi 499323150 171 DA-LRRELVsltrrEGLTTVHVTHDRAEAISIADRIVVL 208
Cdd:PRK13409 251 VArLIRELA-----EGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
29-206 |
5.32e-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: 43.12 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 29 PEEFVVLIGPSGSGKTTMLRTIAgfvepssgsvLIGGEDMTHvppERRRMGmvfqqhavwphmsvaknvgyplARSGQKG 108
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG----------LALGGAQSA---TRRRSG----------------------VKAGCIV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 109 ASISkrVERTLALVGlegfgsrrpasLSGGQRQRVALA-----RAIIADPTVlLLDEALSALDepLRDALR-RELVSLTR 182
Cdd:cd03227 65 AAVS--AELIFTRLQ-----------LSGGEKELSALAlilalASLKPRPLY-ILDEIDRGLD--PRDGQAlAEAILEHL 128
|
170 180
....*....|....*....|....
gi 499323150 183 REGLTTVHVTHDrAEAISIADRIV 206
Cdd:cd03227 129 VKGAQVIVITHL-PELAELADKLI 151
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-166 |
6.45e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 35 LIGPSGSGKTTMLRTIA-----GFvePSSGSVL-----IGGEDMT------HVPPERRRM----GMVFQQHAVWPHMSVA 94
Cdd:PLN03073 208 LVGRNGTGKTTFLRYMAmhaidGI--PKNCQILhveqeVVGDDTTalqcvlNTDIERTQLleeeAQLVAQQRELEFETET 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 95 KNVGYPLARS------GQKGASISKRVERTLA----------LVGLEgFGS----RRPASLSGGQRQRVALARAIIADPT 154
Cdd:PLN03073 286 GKGKGANKDGvdkdavSQRLEEIYKRLELIDAytaearaasiLAGLS-FTPemqvKATKTFSGGWRMRIALARALFIEPD 364
|
170
....*....|..
gi 499323150 155 VLLLDEALSALD 166
Cdd:PLN03073 365 LLLLDEPTNHLD 376
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-208 |
7.59e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.39 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 35 LIGPSGSGKTTMLRTIAGFVEPSSGSVliggedmtHVPPE-----RRRMGMVFQQH-----------AVWPHM------S 92
Cdd:COG1245 104 ILGPNGIGKSTALKILSGELKPNLGDY--------DEEPSwdevlKRFRGTELQDYfkklangeikvAHKPQYvdlipkV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 93 VAKNVGYPLARSGQKGAsISKRVERtlalVGLEGFGSRRPASLSGGQRQRVALARAIIADPTVLLLDEALSALD--EPLR 170
Cdd:COG1245 176 FKGTVRELLEKVDERGK-LDELAEK----LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyQRLN 250
|
170 180 190
....*....|....*....|....*....|....*....
gi 499323150 171 DA-LRRELVsltrREGLTTVHVTHDRAEAISIADRIVVL 208
Cdd:COG1245 251 VArLIRELA----EEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
110-224 |
2.88e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 110 SISKRVErTLALVGLEGFGSRRP-ASLSGGQRQRVALARAIIA---DPTVLLLDEALSALDEPLRDALRRELVSLTrREG 185
Cdd:PRK00635 785 SIHEKIH-ALCSLGLDYLPLGRPlSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLT-HQG 862
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 499323150 186 LTTVHVTHDrAEAISIADRIVVLG------NGRIQQVATPTELLS 224
Cdd:PRK00635 863 HTVVIIEHN-MHVVKVADYVLELGpeggnlGGYLLASCSPEELIH 906
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-166 |
3.68e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTML-----RTIAGFVEpssGSVLIGGEdmthvpPER-----RRMGMVFQQHAVWP 89
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMdvlagRKTGGYIE---GDIRISGF------PKKqetfaRISGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 90 HMSVAKNVGY------PLARSGQKGASISKRVERTL-------ALVGLEGFgsrrpASLSGGQRQRVALARAIIADPTVL 156
Cdd:PLN03140 967 QVTVRESLIYsaflrlPKEVSKEEKMMFVDEVMELVeldnlkdAIVGLPGV-----TGLSTEQRKRLTIAVELVANPSII 1041
|
170
....*....|
gi 499323150 157 LLDEALSALD 166
Cdd:PLN03140 1042 FMDEPTSGLD 1051
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-211 |
1.03e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 130 RRPASLSGGQRQRVALARAIIADptvllLDEALSALDEPL-----RDALRR-ELVSLTRREGLTTVHVTHDRaEAISIAD 203
Cdd:PRK00635 472 RALATLSGGEQERTALAKHLGAE-----LIGITYILDEPSiglhpQDTHKLiNVIKKLRDQGNTVLLVEHDE-QMISLAD 545
|
....*...
gi 499323150 204 RIVVLGNG 211
Cdd:PRK00635 546 RIIDIGPG 553
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
129-228 |
1.47e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 129 SRRPASLSGGQRQRVALARAIIAdptvllldeALSA----LDEP-----------LRDALRReLVSLtrreGLTTVHVTH 193
Cdd:COG0178 480 DRSAGTLSGGEAQRIRLATQIGS---------GLVGvlyvLDEPsiglhqrdndrLIETLKR-LRDL----GNTVIVVEH 545
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 499323150 194 DRaEAISIADRIV-------VLGnGRIqqVA--TPTELLSAPAT 228
Cdd:COG0178 546 DE-DTIRAADYIIdigpgagEHG-GEV--VAqgTPEEILKNPDS 585
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
134-213 |
1.56e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 134 SLSGGQRQRVALARAIIADPTVLLldealsaLDEPLR--D--------ALRRELVSltrrEGLTTVHVTHDRAEAISIAD 203
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLI-------LDEPTRgiDvgakyeiyTIINELAA----EGKGVIVISSELPELLGMCD 472
|
90
....*....|
gi 499323150 204 RIVVLGNGRI 213
Cdd:NF040905 473 RIYVMNEGRI 482
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
33-63 |
4.41e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 37.13 E-value: 4.41e-03
10 20 30
....*....|....*....|....*....|.
gi 499323150 33 VVLIGPSGSGKTTMLRTIAGFVEPSSGSVLI 63
Cdd:cd00009 22 LLLYGPPGTGKTTLARAIANELFRPGAPFLY 52
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
2-51 |
4.46e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.44 E-value: 4.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 499323150 2 SSIKLRDLsvsfrdgtFGLQDINLKIE-PEEFVVLIGPSGSGKTTMLRTIA 51
Cdd:COG3950 4 KSLTIENF--------RGFEDLEIDFDnPPRLTVLVGENGSGKTTLLEAIA 46
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
14-51 |
7.58e-03 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 37.23 E-value: 7.58e-03
10 20 30
....*....|....*....|....*....|....*...
gi 499323150 14 RDGTFGLQDINLkiEPEEFVVLIGPSGSGKTTMLRTIA 51
Cdd:cd03243 15 KGETFVPNDINL--GSGRLLLITGPNMGGKSTYLRSIG 50
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
110-222 |
7.94e-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: 38.07 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499323150 110 SISKRVErTLALVGLEGFGSRRPA-SLSGGQRQRVALARAIIAD---PTVLLLDEALSALD----EPLRDALRReLVSLt 181
Cdd:TIGR00630 805 SISRKLQ-TLCDVGLGYIRLGQPAtTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHfddiKKLLEVLQR-LVDK- 881
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 499323150 182 rreGLTTVHVTHDrAEAISIADRIVVLG------NGRIQQVATPTEL 222
Cdd:TIGR00630 882 ---GNTVVVIEHN-LDVIKTADYIIDLGpeggdgGGTVVASGTPEEV 924
|
|
| BREX_3_BrxF |
NF033453 |
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ... |
33-51 |
8.11e-03 |
|
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins.
Pssm-ID: 468038 Cd Length: 149 Bit Score: 36.32 E-value: 8.11e-03
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
130-195 |
8.35e-03 |
|
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: 37.20 E-value: 8.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499323150 130 RRPASLSGGQRQ------RVALARAIIADPTVLLLDEALSALDEP-LRDALRRELVSLTRREGLTTVHVTHDR 195
Cdd:cd03240 111 DMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLAEIIEERKSQKNFQLIVITHDE 183
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-46 |
8.89e-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: 38.07 E-value: 8.89e-03
10 20
....*....|....*....|....*..
gi 499323150 20 LQDINLKIEPEEFVVLIGPSGSGKTTM 46
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| |
