|
Name |
Accession |
Description |
Interval |
E-value |
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
14-370 |
0e+00 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 541.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQ 93
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMG 173
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 174 ALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSVNIFEA 253
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 254 NILEDNSDSLSLASELLDAPVFIDRGVTTpAETTETLIALRPEKIYLTTEKPEGDSNWSCGTVDNIAYLGDITSYYVKLA 333
Cdd:PRK11607 259 VLKERQEDGLVIDSPGLVHPLKVDADASV-VDNVPVHVALRPEKIMLCEEPPADGCNFAVGEVIHIAYLGDLSIYHVRLK 337
|
330 340 350
....*....|....*....|....*....|....*...
gi 2485516087 334 SGKRVQATMANVER-RGERPTWGDRVYVSWEASSPILL 370
Cdd:PRK11607 338 SGQMISAQLQNAHRyRKGLPTWGDEVRLCWEADSCVVL 375
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
11-370 |
0e+00 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 533.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 11 AEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNM 90
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 91 MFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDE 170
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 171 PMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSVNI 250
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 251 FEANILEDNSDSLSLASELLDAPVFIDRGVTTPAettetLIALRPEKIYLTtekPEGDSNWSCGTVDNIAYLGDITSYYV 330
Cdd:COG3842 242 LPGTVLGDEGGGVRTGGRTLEVPADAGLAAGGPV-----TVAIRPEDIRLS---PEGPENGLPGTVEDVVFLGSHVRYRV 313
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2485516087 331 KLASGKRVQATMANveRRGERPTWGDRVYVSWEASSPILL 370
Cdd:COG3842 314 RLGDGQELVVRVPN--RAALPLEPGDRVGLSWDPEDVVVL 351
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
45-370 |
1.08e-145 |
|
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: 415.35 E-value: 1.08e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 45 LLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDR 124
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 125 VAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHD 204
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 205 QEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSVNIFEANILEDNSDSLSLASeLLDAPVFIDRGVTTPA 284
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAG-VEGRRCDIYTDVPVEK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 285 EtTETLIALRPEKIYLTTEKPEGDSNWSCGTVDNIAYLGDITSYYVKLASGKR--VQATMANVERRGErPTWGDRVYVSW 362
Cdd:TIGR01187 240 D-QPLHVVLRPEKIVIEEEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQKvlVSEFFNEDDPHMS-PSIGDRVGLTW 317
|
....*...
gi 2485516087 363 EASSPILL 370
Cdd:TIGR01187 318 HPGSEVVL 325
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
15-365 |
2.98e-141 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 404.84 E-value: 2.98e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQS 94
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 YALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGA 174
Cdd:COG3839 84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 175 LDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGS--VNIFE 252
Cdd:COG3839 164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppMNLLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 253 ANILEDNsdsLSLASELLDAPvfidrGVTTPAETTETLIALRPEKIYLTtekPEGDSNWScGTVDNIAYLGDITSYYVKL 332
Cdd:COG3839 244 GTVEGGG---VRLGGVRLPLP-----AALAAAAGGEVTLGIRPEHLRLA---DEGDGGLE-ATVEVVEPLGSETLVHVRL 311
|
330 340 350
....*....|....*....|....*....|...
gi 2485516087 333 AsGKRVQATManveRRGERPTWGDRVYVSWEAS 365
Cdd:COG3839 312 G-GQELVARV----PGDTRLRPGDTVRLAFDPE 339
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
15-246 |
9.67e-138 |
|
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: 391.60 E-value: 9.67e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQS 94
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 YALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGA 174
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485516087 175 LDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIG 246
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
15-364 |
1.18e-137 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 395.67 E-value: 1.18e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDI-TALPPYLRPTNMMFQ 93
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMG 173
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 174 ALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSVNIFEA 253
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 254 NILEDnsdslSLASELLDAPvfidrgVTTPAETTETLIALRPEKIYLTTEkPEGDSNWSCgTVDNIAYLGDITSYYVKLA 333
Cdd:COG1118 243 RVIGG-----QLEADGLTLP------VAEPLPDGPAVAGVRPHDIEVSRE-PEGENTFPA-TVARVSELGPEVRVELKLE 309
|
330 340 350
....*....|....*....|....*....|...
gi 2485516087 334 --SGKRVQATMANVERRGERPTWGDRVYVSWEA 364
Cdd:COG1118 310 dgEGQPLEAEVTKEAWAELGLAPGDPVYLRPRP 342
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-340 |
8.24e-131 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 379.29 E-value: 8.24e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 1 MAVTNNTSAQAEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITA 80
Cdd:PRK09452 1 SKKLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 81 LPPYLRPTNMMFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLA 160
Cdd:PRK09452 81 VPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 161 KRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRM 240
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 241 TAEFIGSVNIFEANILEDNSDSLSLAS-ELLDAPVFIDRGVtTPAETTETLiaLRPEKIYLTTEKPEGDSNWSCGTVDNI 319
Cdd:PRK09452 241 VARFIGEINIFDATVIERLDEQRVRANvEGRECNIYVNFAV-EPGQKLHVL--LRPEDLRVEEINDDEHAEGLIGYVRER 317
|
330 340
....*....|....*....|.
gi 2485516087 320 AYLGDITSYYVKLASGKRVQA 340
Cdd:PRK09452 318 NYKGMTLDSVVELENGKMVMV 338
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
15-366 |
3.54e-120 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 351.65 E-value: 3.54e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQS 94
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 YALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGA 174
Cdd:TIGR03265 85 YALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 175 LDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSVNIFEAN 254
Cdd:TIGR03265 165 LDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPGT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 255 ILEDnsdslslaSELLDAPVFIDRGVTTPAETTETLIALRPEKIYLtteKPEGDS-NWSCGTVDNIAYLGDI--TSYYVK 331
Cdd:TIGR03265 245 RGGG--------SRARVGGLTLACAPGLAQPGASVRLAVRPEDIRV---SPAGNAaNLLLARVEDMEFLGAFyrLRLRLE 313
|
330 340 350
....*....|....*....|....*....|....*..
gi 2485516087 332 LASGKRVQA--TMANVERRGERPtwGDRVYVSWEASS 366
Cdd:TIGR03265 314 GLPGQALVAdvSASEVERLGIRA--GQPIWIELPAER 348
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
15-227 |
2.62e-118 |
|
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: 341.42 E-value: 2.62e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQS 94
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 YALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGA 174
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 175 LDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
17-247 |
4.36e-102 |
|
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: 301.18 E-value: 4.36e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 17 IKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQSYA 96
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 97 LFPHMTVEQNIAMGLK----QDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPM 172
Cdd:cd03296 85 LFRHMTVFDNVAFGLRvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485516087 173 GALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGS 247
Cdd:cd03296 165 GALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
9-232 |
1.31e-100 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 298.16 E-value: 1.31e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 9 AQAEVLLSIKGISKSFDS----TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPY 84
Cdd:COG1116 2 SAAAPALELRGVSKRFPTggggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 85 LRptnMMFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPK 164
Cdd:COG1116 82 RG---VVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 165 LLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSyGRIAQVGSPIDI 232
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLS-ARPGRIVEEIDV 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
15-227 |
1.11e-99 |
|
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: 294.16 E-value: 1.11e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQS 94
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 YALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGA 174
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 175 LDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
17-250 |
9.28e-98 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 290.16 E-value: 9.28e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 17 IKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQSYA 96
Cdd:TIGR00968 3 IANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 97 LFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALD 176
Cdd:TIGR00968 83 LFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 177 KKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSVNI 250
Cdd:TIGR00968 163 AKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNV 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
15-232 |
1.19e-96 |
|
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: 286.68 E-value: 1.19e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDS----TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPylrPTNM 90
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 91 MFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDE 170
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485516087 171 PMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSyGRIAQVGSPIDI 232
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLS-ARPGRIVAEVEV 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
15-360 |
3.16e-95 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 287.90 E-value: 3.16e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFD-STLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQ 93
Cdd:PRK11650 4 LKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMG 173
Cdd:PRK11650 84 NYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 174 ALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGS--VNIF 251
Cdd:PRK11650 164 NLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpaMNLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 252 EANILEDnsDSLSLASELLDAPVFIDRGVTTPAETTetlIALRPEKIYLTTEKPEGDSnwscgTVDNIAYLGDITSYYVK 331
Cdd:PRK11650 244 DGRVSAD--GAAFELAGGIALPLGGGYRQYAGRKLT---LGIRPEHIALSSAEGGVPL-----TVDTVELLGADNLAHGR 313
|
330 340 350
....*....|....*....|....*....|..
gi 2485516087 332 LASGK---RVQATManverrgeRPTWGDRVYV 360
Cdd:PRK11650 314 WGGQPlvvRLPHQE--------RPAAGSTLWL 337
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
14-366 |
1.19e-93 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 283.89 E-value: 1.19e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDStLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQ 93
Cdd:NF040840 1 MIRIENLSKDWKE-FKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMG 173
Cdd:NF040840 80 NYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 174 ALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSVNIFEA 253
Cdd:NF040840 160 ALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 254 NILEDNSDSlslaselldapvFIDRG---VTTPAETTETL-IALRPEKIYLTTEKPEGDS-NWSCGTVDNIAYLGDITSY 328
Cdd:NF040840 240 VAEKGGEGT------------ILDTGnikIELPEEKKGKVrIGIRPEDITISTEKVKTSArNEFKGKVEEIEDLGPLVKL 307
|
330 340 350
....*....|....*....|....*....|....*...
gi 2485516087 329 YVKLASGKRVQATMANVERRGERPtwGDRVYVSWEASS 366
Cdd:NF040840 308 TLDVGIILVAFITRSSFLDLEINE--GKEVYASFKASA 343
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
17-247 |
5.42e-91 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 275.43 E-value: 5.42e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 17 IKGISKSF-DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPY-LRpTNMMF-- 92
Cdd:COG1125 4 FENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVeLR-RRIGYvi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 93 QSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEP--YARRKPQQLSGGQQQRVALARSLAKRPKLLLLDE 170
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485516087 171 PMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGS 247
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
17-370 |
1.32e-90 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 276.49 E-value: 1.32e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 17 IKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPD--SGRIVLDGQDITALPPYLRPTNMMFQS 94
Cdd:TIGR03258 8 IDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAglTGRIAIADRDLTHAPPHKRGLALLFQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 YALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGA 174
Cdd:TIGR03258 88 YALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 175 LDKKLRTEMQLELVDILEKV-GVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSVNIFEA 253
Cdd:TIGR03258 168 LDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANILPA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 254 NILEDNSDSLSLASELLDAPVF-IDRGvttPAETTETLIALRPEKIYLtTEKPEGDSNWScGTVDNIAYLGDITSYYVKL 332
Cdd:TIGR03258 248 IALGITEAPGLVDVSCGGAVIFaFGDG---RHDGRDKLACIRPEHLAL-TPRPAGEGRFH-ATIASVEWHGAALHLLCDL 322
|
330 340 350
....*....|....*....|....*....|....*...
gi 2485516087 333 ASGKRVQATMANVERRGERPTWGDRVYVSWEASSPILL 370
Cdd:TIGR03258 323 DAACDEPMLVTMLRGRGPAPERGAKLALDCEADDAVLI 360
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
15-323 |
8.52e-90 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 273.90 E-value: 8.52e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQS 94
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 YALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGA 174
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 175 LDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSVNIFEAN 254
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPAT 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516087 255 IledNSDSLSLASELLDAPvfidRGVTTPAETTETLIALRPEKIYLTTekpEGDSNWSCgTVDNIAYLG 323
Cdd:PRK11432 247 L---SGDYVDIYGYRLPRP----AAFAFNLPDGECTVGVRPEAITLSE---QGEESQRC-TIKHVAYMG 304
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
17-255 |
1.11e-88 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 271.19 E-value: 1.11e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 17 IKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQSYA 96
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 97 LFPHMTVEQNIAMGLKQdkLPKNE------ITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDE 170
Cdd:PRK10851 85 LFRHMTVFDNIAFGLTV--LPRRErpnaaaIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 171 PMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSVNI 250
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNR 242
|
....*
gi 2485516087 251 FEANI 255
Cdd:PRK10851 243 LQGTI 247
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
15-250 |
2.73e-85 |
|
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: 258.42 E-value: 2.73e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFdSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQS 94
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 YALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGA 174
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 175 LDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSVNI 250
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
15-247 |
4.93e-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: 258.00 E-value: 4.93e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSF-DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP--YLRPTNMM 91
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPveLRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 FQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEP--YARRKPQQLSGGQQQRVALARSLAKRPKLLLLD 169
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 170 EPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGS 247
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-249 |
5.81e-84 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 260.42 E-value: 5.81e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 20 ISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP----YLRPTNM-M-FQ 93
Cdd:COG4175 33 ILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKkelrELRRKKMsMvFQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMG 173
Cdd:COG4175 113 HFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFS 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 174 ALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSVN 249
Cdd:COG4175 193 ALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDVD 268
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-249 |
2.79e-80 |
|
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: 246.79 E-value: 2.79e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 20 ISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP----YLRPTN--MMFQ 93
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelrELRRKKisMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMG 173
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 174 ALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSVN 249
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVD 265
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
14-248 |
2.01e-79 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 243.36 E-value: 2.01e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITA----LPPYLRPTN 89
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskkdINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 MMFQSYALFPHMTVEQNIAMGLKQ-DKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLL 168
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 169 DEPMGALDKklrtEMQLELVDILEKV---GVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFI 245
Cdd:COG1126 161 DEPTSALDP----ELVGEVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFL 236
|
...
gi 2485516087 246 GSV 248
Cdd:COG1126 237 SKV 239
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
16-247 |
5.58e-79 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 246.87 E-value: 5.58e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 16 SIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQSY 95
Cdd:PRK11000 5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 96 ALFPHMTVEQNIAMGLKQDKLPKNEITDRV---AAMLKLVKMepyARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPM 172
Cdd:PRK11000 85 ALYPHLSVAENMSFGLKLAGAKKEEINQRVnqvAEVLQLAHL---LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485516087 173 GALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGS 247
Cdd:PRK11000 162 SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGS 236
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
34-246 |
9.13e-79 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 241.58 E-value: 9.13e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 34 SLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQSYALFPHMTVEQNIAMGLKQ 113
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFPHLTVAQNIGLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 114 D-KLPKNEITdRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLA-KRPkLLLLDEPMGALDKKLRTEMqLELV-DI 190
Cdd:COG3840 99 GlKLTAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDEPFSALDPALRQEM-LDLVdEL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 191 LEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIG 246
Cdd:COG3840 176 CRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-239 |
5.61e-78 |
|
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: 239.88 E-value: 5.61e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 10 QAEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP-----PY 84
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekelyEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 85 LRPTNMMFQSYALFPHMTVEQNIAMGLKQ-DKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRP 163
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 164 KLLLLDEP--------MGALDkklrtEMQLELVDILekvGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYES 235
Cdd:COG1127 161 EILLYDEPtagldpitSAVID-----ELIRELRDEL---GLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAS 232
|
....
gi 2485516087 236 PNSR 239
Cdd:COG1127 233 DDPW 236
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
12-223 |
3.98e-77 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 237.25 E-value: 3.98e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 12 EVLLSIKGISKSFDS----TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPY--- 84
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 85 -LRPTN--MMFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAK 161
Cdd:COG1136 82 rLRRRHigFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 162 RPKLLLLDEPMGALDKKLRTE-MQLeLVDILEKVGVTCLMVTHDqEEAMTMASRIAIMSYGRI 223
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEvLEL-LRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
15-248 |
7.80e-77 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 240.36 E-value: 7.80e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDS----TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPY-LRPT- 88
Cdd:COG1135 2 IELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSEReLRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 89 ---NMMFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKL 165
Cdd:COG1135 82 rkiGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 166 LLLDEPMGALDKKlRTEMQLEL-VDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEF 244
Cdd:COG1135 162 LLCDEATSALDPE-TTRSILDLlKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
....
gi 2485516087 245 IGSV 248
Cdd:COG1135 241 LPTV 244
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-248 |
2.96e-76 |
|
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: 244.04 E-value: 2.96e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 7 TSAQAEVLLSIKGISKSFDS-----TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITAL 81
Cdd:COG1123 253 AAAAAEPLLEVRNLSKRYPVrgkggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 82 P-----PYLRPTNMMFQ--SYALFPHMTVEQNIAMGLK-QDKLPKNEITDRVAAMLKLVKMEP-YARRKPQQLSGGQQQR 152
Cdd:COG1123 333 SrrslrELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRlHGLLSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 153 VALARSLAKRPKLLLLDEPMGALDKKLRTE-MQLeLVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPID 231
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQiLNL-LRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
250
....*....|....*..
gi 2485516087 232 IYESPNSRMTAEFIGSV 248
Cdd:COG1123 492 VFANPQHPYTRALLAAV 508
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
15-222 |
4.63e-75 |
|
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: 230.15 E-value: 4.63e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITAL----PPYLRPTNM 90
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedelPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 91 MFQSYALFPHMTVEQNIAMGlkqdklpkneitdrvaamlklvkmepyarrkpqqLSGGQQQRVALARSLAKRPKLLLLDE 170
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2485516087 171 PMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGR 222
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
15-223 |
1.54e-74 |
|
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: 230.07 E-value: 1.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDS----TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP----YLR 86
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 87 PTNM--MFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPK 164
Cdd:cd03255 81 RRHIgfVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 165 LLLLDEPMGALDKKLRTE-MQLeLVDILEKVGVTCLMVTHDQEEAMtMASRIAIMSYGRI 223
Cdd:cd03255 161 IILADEPTGNLDSETGKEvMEL-LRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
22-258 |
6.74e-74 |
|
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: 233.59 E-value: 6.74e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 22 KSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP------YLRPTNMMFQSY 95
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 96 ALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGAL 175
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 176 DKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSVNIFEANI 255
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240
|
...
gi 2485516087 256 LED 258
Cdd:TIGR01186 241 AER 243
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
15-229 |
1.01e-71 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 223.40 E-value: 1.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRP-TNMMFQ 93
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SYALFPHMTVEQNIAM--GLKqdKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEP 171
Cdd:COG1131 81 EPALYPDLTVRENLRFfaRLY--GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 172 MGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSP 229
Cdd:COG1131 159 TSGLDPEARREL-WELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-227 |
1.35e-71 |
|
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: 222.56 E-value: 1.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 19 GISKSFDS-TLavdDVSLDIhKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDG-------QDITaLPPYLRPTNM 90
Cdd:cd03297 5 DIEKRLPDfTL---KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKIN-LPPQQRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 91 MFQSYALFPHMTVEQNIAMGLKqdKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDE 170
Cdd:cd03297 80 VFQQYALFPHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2485516087 171 PMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-226 |
5.00e-71 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 222.82 E-value: 5.00e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFD----STLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITAlPPYLRptNM 90
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADR--GV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 91 MFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDE 170
Cdd:COG4525 81 VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 171 PMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSY--GRIAQV 226
Cdd:COG4525 161 PFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVER 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-254 |
1.14e-70 |
|
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: 221.22 E-value: 1.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTL----AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDIT--ALPPYLRP 87
Cdd:COG1124 1 MLEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTrrRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 88 TNMMFQSY--ALFPHMTVEQNIAMGLKQDKLPknEITDRVAAMLKLVKMEP-YARRKPQQLSGGQQQRVALARSLAKRPK 164
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 165 LLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEF 244
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTREL 238
|
250
....*....|
gi 2485516087 245 IGSVNIFEAN 254
Cdd:COG1124 239 LAASLAFERA 248
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
15-240 |
1.94e-70 |
|
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: 220.45 E-value: 1.94e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITAL-PPYLRPT----N 89
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLsEAELYRLrrrmG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 MMFQSYALFPHMTVEQNIAMGLKQD-KLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLL 168
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485516087 169 DEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRM 240
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPLV 232
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
15-234 |
7.56e-69 |
|
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: 216.04 E-value: 7.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSF-DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPY-LRPT-NMM 91
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLReLRRKvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 FQS--YALFpHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLD 169
Cdd:COG1122 81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485516087 170 EPMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYE 234
Cdd:COG1122 160 EPTAGLDPRGRREL-LELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
15-223 |
2.76e-67 |
|
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: 211.23 E-value: 2.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDIT----ALPPYLRPTNM 90
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 91 MFQSYALFPHMTVEQNIAMGLKQ-DKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLD 169
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 170 EPMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:cd03262 161 EPTSALDPELVGEV-LDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
14-236 |
3.57e-67 |
|
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: 211.67 E-value: 3.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDST----LAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPY-LRP- 87
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKeLRKa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 88 ---TNMMFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPK 164
Cdd:cd03258 81 rrrIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 165 LLLLDEPMGALDKKlRTEMQLELV-DILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESP 236
Cdd:cd03258 161 VLLCDEATSALDPE-TTQSILALLrDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
15-227 |
1.25e-66 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 209.91 E-value: 1.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSF-DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP----PYLRPT- 88
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreiPYLRRRi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 89 NMMFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLL 168
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485516087 169 DEPMGALDKklrtEMQLELVDILE---KVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:COG2884 162 DEPTGNLDP----ETSWEIMELLEeinRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
11-236 |
2.02e-66 |
|
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: 210.67 E-value: 2.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 11 AEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRpTNM 90
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI-ARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 91 ----MFQSYALFPHMTVEQNIAMGLKQ----------DKLPKN-----EITDRVAAMLKLVKMEPYARRKPQQLSGGQQQ 151
Cdd:COG0411 80 giarTFQNPRLFPELTVLENVLVAAHArlgrgllaalLRLPRArreerEARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 152 RVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGR-IAQvGSPI 230
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRvIAE-GTPA 238
|
....*.
gi 2485516087 231 DIYESP 236
Cdd:COG0411 239 EVRADP 244
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
32-309 |
3.73e-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: 210.73 E-value: 3.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 32 DVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDG---QDITA---LPPYLRPTNMMFQSYALFPHMTVEQ 105
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgifLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 106 NIAMGLKQDKLPKNEIT-DRVAAMLKLvkmEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQ 184
Cdd:COG4148 97 NLLYGRKRAPRAERRISfDEVVELLGI---GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 185 LELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSVNIFEANILE-DNSDSL 263
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVAAhDPDYGL 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2485516087 264 SLASeLLDAPVFIDRGVTTPAETteTLIALRPEKIYLTTEKPEGDS 309
Cdd:COG4148 254 TRLA-LGGGRLWVPRLDLPPGTR--VRVRIRARDVSLALEPPEGSS 296
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
14-223 |
1.23e-64 |
|
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: 205.05 E-value: 1.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFD----STLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTN 89
Cdd:cd03257 1 LLEVKNLSVSFPtgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 -----MMFQSY--ALFPHMTVEQNIAMGLK--QDKLPKNEITDRVAAMLKLVKMEP-YARRKPQQLSGGQQQRVALARSL 159
Cdd:cd03257 81 rkeiqMVFQDPmsSLNPRMTIGEQIAEPLRihGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 160 AKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
8-236 |
2.31e-64 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 207.66 E-value: 2.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 8 SAQAEVLLSIKGISKSFDSTL-----------AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQ 76
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPVRGglfgrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 77 DITALPP-YLRPTN----MMFQ-SYA-LFPHMTVEQNIAMGLK-QDKLPKNEITDRVAAMLKLVKMEP-YARRKPQQLSG 147
Cdd:COG4608 81 DITGLSGrELRPLRrrmqMVFQdPYAsLNPRMTVGDIIAEPLRiHGLASKAERRERVAELLELVGLRPeHADRYPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 148 GQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTE-MQLeLVDILEKVGVTCLMVTHDQeeAMT--MASRIAIMSYGRIA 224
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQvLNL-LEDLQDELGLTYLFISHDL--SVVrhISDRVAVMYLGKIV 237
|
250
....*....|..
gi 2485516087 225 QVGSPIDIYESP 236
Cdd:COG4608 238 EIAPRDELYARP 249
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
15-232 |
4.54e-63 |
|
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: 201.51 E-value: 4.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRptNMM--- 91
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEI--ARLgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 --FQSYALFPHMTVEQNIAMGLKQDKLP----------KNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSL 159
Cdd:cd03219 79 rtFQIPRLFPELTVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 160 AKRPKLLLLDEPMGALDKKLRTEMqlelVDILEKV---GVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDI 232
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEEL----AELIRELrerGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
32-227 |
6.67e-63 |
|
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: 200.03 E-value: 6.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 32 DVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQSYALFPHMTVEQNIAMGL 111
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 112 KQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDIL 191
Cdd:cd03298 96 SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 2485516087 192 EKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
17-248 |
1.37e-62 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 203.88 E-value: 1.37e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 17 IKGISKSFD----STLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP-PYLRPTN-- 89
Cdd:PRK11153 4 LKNISKVFPqggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSeKELRKARrq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 --MMFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLL 167
Cdd:PRK11153 84 igMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 168 LDEPMGALDKKlRTEMQLELV-DILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIG 246
Cdd:PRK11153 164 CDEATSALDPA-TTRSILELLkDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQ 242
|
..
gi 2485516087 247 SV 248
Cdd:PRK11153 243 ST 244
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
30-240 |
1.60e-62 |
|
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: 200.00 E-value: 1.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 30 VDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPylrPTNMMFQSYALFPHMTVEQNIAM 109
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 110 GLKQ--DKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLEL 187
Cdd:TIGR01184 78 AVDRvlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 188 VDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDI-YESPNSRM 240
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRDRL 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
34-229 |
7.48e-62 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 198.27 E-value: 7.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 34 SLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQSYALFPHMTVEQNIAMGLKQ 113
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 114 DKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMqLELVD-ILE 192
Cdd:PRK10771 99 GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM-LTLVSqVCQ 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 2485516087 193 KVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSP 229
Cdd:PRK10771 178 ERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPT 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-222 |
4.64e-61 |
|
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: 195.38 E-value: 4.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 16 SIKGISKSFDS--TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP--YLRPTNMM 91
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkeLRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 FQsyalFP-HM----TVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLL 166
Cdd:cd03225 81 FQ----NPdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 167 LLDEPMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGR 222
Cdd:cd03225 157 LLDEPTAGLDPAGRREL-LELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
14-245 |
1.12e-60 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 195.66 E-value: 1.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDS-TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP-----YLRP 87
Cdd:COG3638 2 MLELRNLSKRYPGgTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralrrLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 88 TNMMFQSYALFPHMTVEQNIAMGL---------------KQDKlpkneitDRVAAMLKLVKMEPYARRKPQQLSGGQQQR 152
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGRlgrtstwrsllglfpPEDR-------ERALEALERVGLADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 153 VALARSLAKRPKLLLLDEPMGALDKKL-RTEMQLeLVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIaqvgspid 231
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV-------- 225
|
250
....*....|....
gi 2485516087 232 IYESPNSRMTAEFI 245
Cdd:COG3638 226 VFDGPPAELTDAVL 239
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
15-208 |
1.65e-60 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 193.85 E-value: 1.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPD---SGRIVLDGQDITALPPYLRPTNMM 91
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 FQSYALFPHMTVEQNIAMGLKqDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEP 171
Cdd:COG4136 82 FQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 2485516087 172 MGALDKKLRTEMqLELV-DILEKVGVTCLMVTHDQEEA 208
Cdd:COG4136 161 FSKLDAALRAQF-REFVfEQIRQRGIPALLVTHDEEDA 197
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
18-248 |
2.29e-60 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 194.54 E-value: 2.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 18 KGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLR----PTNMMFQ 93
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlirqEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SYALFPHMTVEQNIAMG-LKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPM 172
Cdd:PRK09493 85 QFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 173 GALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSV 248
Cdd:PRK09493 165 SALDPELRHEV-LKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
15-234 |
6.98e-59 |
|
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: 190.86 E-value: 6.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSF-DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP-----YLRPT 88
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 89 NMMFQSYALFPHMTVEQNIAMGLKQDK---------LPKNEItDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSL 159
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRstwrslfglFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 160 AKRPKLLLLDEPMGALDKKLRTE-MQLeLVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYE 234
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQvMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTD 234
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
34-227 |
1.19e-58 |
|
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: 189.30 E-value: 1.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 34 SLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQSYALFPHMTVEQNIAMGLKQ 113
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 114 DKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMqLELVDIL-E 192
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEM-LALVKQLcS 176
|
170 180 190
....*....|....*....|....*....|....*
gi 2485516087 193 KVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:TIGR01277 177 ERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
14-248 |
2.17e-58 |
|
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: 189.87 E-value: 2.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNM--M 91
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIayV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 FQSYALFPHMTVEQNIAMGL-----------KQDKlpkneitDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLA 160
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRyphlglfgrpsAEDR-------EAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 161 KRPKLLLLDEPMGALDkkLRteMQLELVDIL----EKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIyesp 236
Cdd:COG1120 154 QEPPLLLLDEPTSHLD--LA--HQLEVLELLrrlaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV---- 225
|
250
....*....|..
gi 2485516087 237 nsrMTAEFIGSV 248
Cdd:COG1120 226 ---LTPELLEEV 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-236 |
5.95e-58 |
|
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: 196.28 E-value: 5.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 12 EVLLSIKGISKSF--DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPD---SGRIVLDGQDITALPPYLR 86
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 87 PTN--MMFQS--YALFPhMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKR 162
Cdd:COG1123 82 GRRigMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 163 PKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESP 236
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
14-234 |
1.29e-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: 187.76 E-value: 1.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRpTNM--M 91
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIgvL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 FQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEP 171
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 172 MGALDKKLRTEMQLELVDiLEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYE 234
Cdd:COG4555 160 TNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-236 |
1.32e-57 |
|
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: 189.88 E-value: 1.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDS---TL-AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETP---DSGRIVLDGQDITALPPY-- 84
Cdd:COG0444 1 LLEVRNLKVYFPTrrgVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 85 --LRPTN--MMFQ-SY-ALFPHMTVEQNIAMGLK-QDKLPKNEITDRVAAMLKLVKMEP---YARRKPQQLSGGQQQRVA 154
Cdd:COG0444 81 rkIRGREiqMIFQdPMtSLNPVMTVGDQIAEPLRiHGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 155 LARSLAKRPKLLLLDEPMGALDKKLRTE-MQLeLVDILEKVGVTCLMVTHDQEEAMTMASRIAIMsY-GRIAQVGSPIDI 232
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQiLNL-LKDLQRELGLAILFITHDLGVVAEIADRVAVM-YaGRIVEEGPVEEL 238
|
....
gi 2485516087 233 YESP 236
Cdd:COG0444 239 FENP 242
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
15-223 |
1.95e-57 |
|
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: 184.52 E-value: 1.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRP-TNMMFQ 93
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SYALFPHMTVEQNIamglkqdklpkneitdrvaamlklvkmepyarrkpqQLSGGQQQRVALARSLAKRPKLLLLDEPMG 173
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2485516087 174 ALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:cd03230 125 GLDPESRREF-WELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-237 |
4.72e-57 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 186.06 E-value: 4.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 11 AEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP---YLrP 87
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRrigYV-P 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 88 tnmmfQSYAL---FPhMTVEQNIAMGLKQD----KLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLA 160
Cdd:COG1121 82 -----QRAEVdwdFP-ITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485516087 161 KRPKLLLLDEPMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQvGSPIDIYESPN 237
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEAL-YELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPEN 230
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
20-222 |
1.26e-56 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 183.99 E-value: 1.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 20 ISKSFD-STLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP----PYLR-PTNMMFQ 93
Cdd:TIGR02673 7 VSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRgrqlPLLRrRIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMG 173
Cdd:TIGR02673 87 DFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2485516087 174 ALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGR 222
Cdd:TIGR02673 167 NLDPDLSERI-LDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
15-223 |
1.76e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 183.48 E-value: 1.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP--------YLR 86
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpewrrqvaYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 87 PTNMMFqsyalfpHMTVEQNIAMGLKQDKLPKNEitDRVAAMLKLVKMEPYARRKP-QQLSGGQQQRVALARSLAKRPKL 165
Cdd:COG4619 81 QEPALW-------GGTVRDNLPFPFQLRERKFDR--ERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 166 LLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
15-245 |
2.44e-54 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 179.05 E-value: 2.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQ--------DITALPPYLR 86
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqkpSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 87 PTNMMFQSYALFPHMTVEQN-IAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKL 165
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 166 LLLDEPMGALDKklrtEMQLELVDI---LEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSpIDIYESPNSRMTA 242
Cdd:COG4161 163 LLFDEPTAALDP----EITAQVVEIireLSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFA 237
|
...
gi 2485516087 243 EFI 245
Cdd:COG4161 238 HYL 240
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-233 |
3.99e-54 |
|
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: 179.55 E-value: 3.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFD--STLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDiTALPPYL----RPT 88
Cdd:TIGR04520 1 IEVENVSFSYPesEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD-TLDEENLweirKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 89 NMMFQSyalfPH-----MTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRP 163
Cdd:TIGR04520 80 GMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485516087 164 KLLLLDEPMGALDKKLRTEMqLELVDIL-EKVGVTCLMVTHDQEEAmTMASRIAIMSYGRIAQVGSPIDIY 233
Cdd:TIGR04520 156 DIIILDEATSMLDPKGRKEV-LETIRKLnKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
14-225 |
4.04e-54 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 179.13 E-value: 4.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITAlPPYLRptNMMFQ 93
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER--GVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMG 173
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 174 ALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMS--YGRIAQ 225
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
29-233 |
2.90e-53 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 177.26 E-value: 2.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP-YLRPTN----MMFQ--SYALFpHM 101
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKkKLKDLRkkvgLVFQfpEHQLF-EE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 102 TVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKM-EPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLR 180
Cdd:TIGR04521 99 TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 181 TEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIY 233
Cdd:TIGR04521 179 KEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
17-215 |
3.04e-53 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 175.11 E-value: 3.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 17 IKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP-----YLRPT-NM 90
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSkkaskFRREKlGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 91 MFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDE 170
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2485516087 171 PMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAmTMASRI 215
Cdd:TIGR03608 161 PTGSLDPKNRDEV-LDLLLELNDEGKTIIIVTHDPEVA-KQADRV 203
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
15-229 |
3.97e-53 |
|
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: 175.39 E-value: 3.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSF--DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRP-TNMM 91
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQsLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 FQSYALFPHMTVEQNIAM--GLKqdKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLD 169
Cdd:cd03263 81 PQFDALFDELTVREHLRFyaRLK--GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485516087 170 EPMGALDKKLRTEMQlelvDILEKV--GVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSP 229
Cdd:cd03263 159 EPTSGLDPASRRAIW----DLILEVrkGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
15-245 |
5.44e-53 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 175.59 E-value: 5.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQ--------DITALPPYLR 86
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 87 PTNMMFQSYALFPHMTVEQN-IAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKL 165
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 166 LLLDEPMGALDKklrtEMQLELVDI---LEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSpIDIYESPNSRMTA 242
Cdd:PRK11124 163 LLFDEPTAALDP----EITAQIVSIireLAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFK 237
|
...
gi 2485516087 243 EFI 245
Cdd:PRK11124 238 NYL 240
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
8-247 |
7.20e-53 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 175.76 E-value: 7.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 8 SAQAEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP---Y 84
Cdd:COG4598 2 TDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 85 LRPTN------------MMFQSYALFPHMTVEQNIAMG-LKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQ 151
Cdd:COG4598 82 LVPADrrqlqrirtrlgMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 152 RVALARSLAKRPKLLLLDEPMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPID 231
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPELVGEV-LKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAE 240
|
250
....*....|....*.
gi 2485516087 232 IYESPNSRMTAEFIGS 247
Cdd:COG4598 241 VFGNPKSERLRQFLSS 256
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
15-229 |
1.51e-52 |
|
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: 173.91 E-value: 1.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGF-----ETPDSGRIVLDGQDITALPPYL---- 85
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 86 RPTNMMFQSYALFPhMTVEQNIAMGLK-QDKLPKNEITDRVAAMLKLVKMEPYARRK--PQQLSGGQQQRVALARSLAKR 162
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRlHGIKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516087 163 PKLLLLDEPMGALD--KKLRTEmqlELVDILEKVgVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSP 229
Cdd:cd03260 160 PEVLLLDEPTSALDpiSTAKIE---ELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
8-225 |
3.45e-52 |
|
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: 173.39 E-value: 3.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 8 SAQAEVLLSIKGISKSFDS---TLAV-DDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP- 82
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTgagELTIlKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 83 ---PYLRPTNM--MFQSYALFPHMTVEQNIAM-----GLKQDKlpkneitDRVAAMLKLVKMEPYARRKPQQLSGGQQQR 152
Cdd:COG4181 82 darARLRARHVgfVFQSFQLLPTLTALENVMLplelaGRRDAR-------ARARALLERVGLGHRLDHYPAQLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 153 VALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAmTMASRIAIMSYGRIAQ 225
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
15-239 |
9.16e-52 |
|
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: 171.96 E-value: 9.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLR-------- 86
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlgigyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 87 PtnmmfQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLL 166
Cdd:cd03218 81 P-----QEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 167 LLDEPMGALDKKLRTEMQlELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSR 239
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQ-KIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-250 |
2.58e-51 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 175.99 E-value: 2.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 18 KGISKS--FDST---LAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP-PYLRPTN-- 89
Cdd:PRK10070 27 QGLSKEqiLEKTglsLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdAELREVRrk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 ---MMFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLL 166
Cdd:PRK10070 107 kiaMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 167 LLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIG 246
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
|
....
gi 2485516087 247 SVNI 250
Cdd:PRK10070 267 GVDI 270
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
15-223 |
2.71e-51 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 171.78 E-value: 2.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIvLDGQdiTALPPYLRPTNMMFQS 94
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT--APLAEAREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 YALFPHMTVEQNIAMGLKQDKlpkneitdRVAAM--LKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPM 172
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGLKGQW--------RDAALqaLAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2485516087 173 GALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
15-239 |
5.49e-51 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 170.21 E-value: 5.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLR-------- 86
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlgigyl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 87 PtnmmfQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLL 166
Cdd:COG1137 84 P-----QEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 167 LLDEPMGALDKKLRTEMQlELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSR 239
Cdd:COG1137 159 LLDEPFAGVDPIAVADIQ-KIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVR 230
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
14-223 |
9.91e-51 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 169.13 E-value: 9.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDS----TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPpY----- 84
Cdd:NF038007 1 MLNMQNAEKCYITktikTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLS-Ysqkii 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 85 LRPT--NMMFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKR 162
Cdd:NF038007 80 LRREliGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485516087 163 PKLLLLDEPMGALDKKLRTEMQLELVDILEKvGVTCLMVTHDQeEAMTMASRIAIMSYGRI 223
Cdd:NF038007 160 PALLLADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTHSD-EASTYGNRIINMKDGKL 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
27-223 |
1.57e-50 |
|
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: 168.36 E-value: 1.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 27 TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP----PYLRPT-NMMFQSYALFPHM 101
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraiPYLRRKiGVVFQDFRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 102 TVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDkklrT 181
Cdd:cd03292 94 NVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD----P 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2485516087 182 EMQLELVDILEKV---GVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:cd03292 170 DTTWEIMNLLKKInkaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
14-234 |
1.75e-50 |
|
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: 169.02 E-value: 1.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSF-DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITA-----LPPYLRP 87
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrgkkLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 88 TNMMFQSYALFPHMTVEQNIAMGLKQDK---------LPKNEiTDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARS 158
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKptwrsllgrFSEED-KERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 159 LAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYE 234
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
15-229 |
5.23e-50 |
|
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: 167.23 E-value: 5.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTN---MM 91
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgigYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 FQSYALFPHMTVEQNIAMGLKqdKLPKNEITDRVAAMLKLV-KMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDE 170
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAY--ARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516087 171 PMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSP 229
Cdd:cd03224 159 PSEGLAPKIVEEI-FEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTA 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-235 |
5.43e-50 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 169.04 E-value: 5.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 11 AEVLLSIKGISKSFD--STLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQ--------DITa 80
Cdd:PRK13635 2 KEEIIRVEHISFRYPdaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwDVR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 81 lppylRPTNMMFQSY-ALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSL 159
Cdd:PRK13635 81 -----RQVGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485516087 160 AKRPKLLLLDEPMGALDKKLRTEMqLELVDIL-EKVGVTCLMVTHDQEEAMTmASRIAIMSYGRIAQVGSPIDIYES 235
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREV-LETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
30-171 |
5.51e-50 |
|
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: 164.74 E-value: 5.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 30 VDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTN--MMFQSYALFPHMTVEQNI 107
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEigYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 108 AMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRK----PQQLSGGQQQRVALARSLAKRPKLLLLDEP 171
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
32-309 |
1.28e-49 |
|
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: 170.29 E-value: 1.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 32 DVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDG---QDITA---LPPYLRPTNMMFQSYALFPHMTVEQ 105
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgifLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 106 NIAMGLKQDKLPKNEITDrvAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQL 185
Cdd:TIGR02142 95 NLRYGMKRARPSERRISF--ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 186 ELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPN-SRMTAEFIGSvnIFEANILE-DNSDSL 263
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDlPWLAREDQGS--LIEGVVAEhDQHYGL 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2485516087 264 SlASELLDAPVFIDRGVTTPAEttETLIALRPEKIYLTTEKPEGDS 309
Cdd:TIGR02142 251 T-ALRLGGGHLWVPENLGPTGA--RLRLRVPARDVSLALQKPEATS 293
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-235 |
3.02e-49 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 167.59 E-value: 3.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP----YL---Rp 87
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRrrigYLpeeR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 88 tnmmfqsyALFPHMTV-EQNIAMG-LKQdkLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKL 165
Cdd:COG4152 81 --------GLYPKMKVgEQLVYLArLKG--LSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 166 LLLDEPMGALD----KKLRTEMqLELVDilekVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYES 235
Cdd:COG4152 151 LILDEPFSGLDpvnvELLKDVI-RELAA----KGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-236 |
3.22e-49 |
|
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: 173.33 E-value: 3.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 9 AQAEVLLSIKGISKSF-----------DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFEtPDSGRIVLDGQD 77
Cdd:COG4172 270 PDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 78 ITALPPY-LRPT----NMMFQS-YA-LFPHMTVEQNIAMGLK--QDKLPKNEITDRVAAMLKLVKMEPYAR-RKPQQLSG 147
Cdd:COG4172 349 LDGLSRRaLRPLrrrmQVVFQDpFGsLSPRMTVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDPAARhRYPHEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 148 GQQQRVALARSLAKRPKLLLLDEPMGALDkklRTeMQLELVDIL----EKVGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALD---VS-VQAQILDLLrdlqREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
250
....*....|...
gi 2485516087 224 AQVGSPIDIYESP 236
Cdd:COG4172 505 VEQGPTEQVFDAP 517
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
14-208 |
4.91e-49 |
|
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: 164.19 E-value: 4.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP-YLRPTNMMF 92
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 93 QSYALFPHMTVEQNIAMGLKQDKLPKNEitDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPM 172
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 2485516087 173 GALDKklrtEMQLELVDILEKV---GVTCLMVTHDQEEA 208
Cdd:COG4133 160 TALDA----AGVALLAELIAAHlarGGAVLLTTHQPLEL 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-218 |
1.29e-48 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 170.97 E-value: 1.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 11 AEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDItalppylRPTN- 89
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-------RFRSp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 ---------MMFQSYALFPHMTVEQNIAMGLKQDKLP---KNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALAR 157
Cdd:COG1129 74 rdaqaagiaIIHQELNLVPNLSVAENIFLGREPRRGGlidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485516087 158 SLAKRPKLLLLDEPMGALDKKlRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIM 218
Cdd:COG1129 154 ALSRDARVLILDEPTASLTER-EVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
13-229 |
2.07e-48 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 164.17 E-value: 2.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 13 VLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTN--M 90
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRraV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 91 MFQSYAL-FPhMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLA------KRP 163
Cdd:PRK13548 81 LPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485516087 164 KLLLLDEPMGALDkkLRteMQLELVDIL------EKVGVTCLMvtHDQEEAMTMASRIAIMSYGRIAQVGSP 229
Cdd:PRK13548 160 RWLLLDEPTSALD--LA--HQHHVLRLArqlaheRGLAVIVVL--HDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
17-229 |
1.39e-47 |
|
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: 161.00 E-value: 1.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 17 IKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPT-NMMFQSY 95
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRiGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 96 ALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGAL 175
Cdd:cd03265 83 SVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 176 DKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSP 229
Cdd:cd03265 163 DPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
16-227 |
1.64e-47 |
|
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: 159.14 E-value: 1.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 16 SIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMmfqSY 95
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI---AY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 96 alfphmtVEQniamglkqdklpkneitdrvaaMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGAL 175
Cdd:cd03214 78 -------VPQ----------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 176 DKKlrteMQLELVDIL----EKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:cd03214 129 DIA----HQIELLELLrrlaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-240 |
5.50e-47 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 161.01 E-value: 5.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSF---------DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP-- 82
Cdd:PRK10419 3 LLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 83 ---PYLRPTNMMFQSY--ALFPHMTVEQNIAMGLKQ-DKLPKNEITDRVAAMLKLVKMEP-YARRKPQQLSGGQQQRVAL 155
Cdd:PRK10419 83 qrkAFRRDIQMVFQDSisAVNPRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 156 ARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIA--QVGSPIDIY 233
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVetQPVGDKLTF 242
|
....*..
gi 2485516087 234 ESPNSRM 240
Cdd:PRK10419 243 SSPAGRV 249
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-248 |
7.19e-47 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 160.28 E-value: 7.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTN--MM 91
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRraVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 FQSYAL-FPhMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLA-------KRP 163
Cdd:COG4559 81 PQHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 164 KLLLLDEPMGALDKKLrtemQLELVDIL-----EKVGVtcLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIyespns 238
Cdd:COG4559 160 RWLFLDEPTSALDLAH----QHAVLRLArqlarRGGGV--VAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEV------ 227
|
250
....*....|
gi 2485516087 239 rMTAEFIGSV 248
Cdd:COG4559 228 -LTDELLERV 236
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
12-236 |
9.12e-47 |
|
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: 159.38 E-value: 9.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 12 EVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLR----- 86
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 87 ---PtnmmfQSYALFPHMTVEQNIAMGLKQDKlPKNEITDRVAAMLKLV-KMEPYARRKPQQLSGGQQQRVALARSLAKR 162
Cdd:COG0410 81 gyvP-----EGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 163 PKLLLLDEP-MGaLDKKLRTEMqlelVDILEKV---GVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESP 236
Cdd:COG0410 155 PKLLLLDEPsLG-LAPLIVEEI----FEIIRRLnreGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
32-224 |
1.24e-46 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 158.26 E-value: 1.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 32 DVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDI-----TALPPYLRPTNMMFQSYALFPHMTVEQN 106
Cdd:TIGR02982 23 DINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELhgaskKQLVQLRRRIGYIFQAHNLLGFLTARQN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 107 IAMGLK-QDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKlrteMQL 185
Cdd:TIGR02982 103 VQMALElQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSK----SGR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2485516087 186 ELVDILEKV----GVTCLMVTHDQeEAMTMASRIAIMSYGRIA 224
Cdd:TIGR02982 179 DVVELMQKLakeqGCTILMVTHDN-RILDVADRILQMEDGKLL 220
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
14-239 |
1.45e-46 |
|
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: 159.59 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAV---------DDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP- 83
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFgakqrapvlTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 84 ----YLRPTNMMFQ-SYALF-PHMTVEQNIAMGLKQ-DKLPKNEITDRVAAMLKLVKMEP-YARRKPQQLSGGQQQRVAL 155
Cdd:TIGR02769 82 qrraFRRDVQLVFQdSPSAVnPRMTVRQIIGEPLRHlTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 156 ARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIA--QVGSPIDIY 233
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVeeCDVAQLLSF 241
|
....*.
gi 2485516087 234 ESPNSR 239
Cdd:TIGR02769 242 KHPAGR 247
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
16-222 |
1.08e-45 |
|
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: 153.94 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 16 SIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLrptnmmfqsy 95
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 96 alfphmtVEQNIAMglkqdkLPkneitdrvaamlklvkmepyarrkpqQLSGGQQQRVALARSLAKRPKLLLLDEPMGAL 175
Cdd:cd00267 71 -------LRRRIGY------VP--------------------------QLSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2485516087 176 DKKLRTEMQLELVDILEKvGVTCLMVTHDQEEAMTMASRIAIMSYGR 222
Cdd:cd00267 112 DPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-229 |
2.10e-45 |
|
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: 165.39 E-value: 2.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSF--DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPY-LRptNMM 91
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAsLR--RQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 ---FQSYALFpHMTVEQNIAMGlkqdklpKNEITD-RVAAMLKLVKMEPYARRKPQ-----------QLSGGQQQRVALA 156
Cdd:COG2274 552 gvvLQDVFLF-SGTIRENITLG-------DPDATDeEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485516087 157 RSLAKRPKLLLLDEPMGALDKklRTEMQleLVDILEKV--GVTCLMVTHDqEEAMTMASRIAIMSYGRIAQVGSP 229
Cdd:COG2274 624 RALLRNPRILILDEATSALDA--ETEAI--ILENLRRLlkGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTH 693
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-224 |
2.44e-45 |
|
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: 152.97 E-value: 2.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITalppylrptnmmFQS 94
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS------------FAS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 yalfPHMTVEQNIAMglkqdklpkneitdrVaamlklvkmepyarrkpQQLSGGQQQRVALARSLAKRPKLLLLDEPMGA 174
Cdd:cd03216 69 ----PRDARRAGIAM---------------V-----------------YQLSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2485516087 175 LDKKlRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIA 224
Cdd:cd03216 113 LTPA-EVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
14-245 |
4.09e-45 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 155.15 E-value: 4.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRML-------AGFETpdSGRIVLDGQDITA----LP 82
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrmndlvPGVRI--EGKVLFDGQDIYDkkidVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 83 PYLRPTNMMFQSYALFPhMTVEQNIAMGLKQDKL-PKNEITDRV------AAMLKLVKMEpyARRKPQQLSGGQQQRVAL 155
Cdd:TIGR00972 79 ELRRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVeeslkkAALWDEVKDR--LHDSALGLSGGQQQRLCI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 156 ARSLAKRPKLLLLDEPMGALDKKLrTEMQLELVDILEKvGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYES 235
Cdd:TIGR00972 156 ARALAVEPEVLLLDEPTSALDPIA-TGKIEELIQELKK-KYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTN 233
|
250
....*....|
gi 2485516087 236 PNSRMTAEFI 245
Cdd:TIGR00972 234 PKEKRTEDYI 243
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
15-227 |
4.13e-45 |
|
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: 154.27 E-value: 4.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGeIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPT-NMMFQ 93
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRiGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SYALFPHMTVEQNIA-MG-LKqdKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEP 171
Cdd:cd03264 80 EFGVYPNFTVREFLDyIAwLK--GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 172 MGALDKKLRTEMQLELVDILEkvGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-223 |
5.15e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 155.63 E-value: 5.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSF-----DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRpTN 89
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKR-AK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 MM---FQSYAL--FPHMTVEQNIAMGLKQDK-------LPKNEItDRVAAMLKLVKM--EPYARRKPQQLSGGQQQRVAL 155
Cdd:COG1101 81 YIgrvFQDPMMgtAPSMTIEENLALAYRRGKrrglrrgLTKKRR-ELFRELLATLGLglENRLDTKVGLLSGGQRQALSL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516087 156 ARSLAKRPKLLLLDEPMGALDKKlRTEMQLELVD-ILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPK-TAALVLELTEkIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
15-223 |
5.70e-45 |
|
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: 153.53 E-value: 5.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQS 94
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 YALFPHMTVEQNIAMGLKQDKLPKNEItDRVaamLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGA 174
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRI-DEV---LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2485516087 175 LDKKLRTEMQlELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:cd03268 157 LDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
27-233 |
6.51e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 155.98 E-value: 6.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 27 TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDIT----ALPPYLRPTNMMFQ--SYALFPH 100
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSDIRKKVGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 101 mTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKM--EPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKK 178
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2485516087 179 LRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIY 233
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
16-218 |
1.13e-44 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 153.07 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 16 SIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP---YLrPtnmmf 92
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKrigYV-P----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 93 QSYAL---FPhMTVEQNIAMGL-----------KQDKlpkneitDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARS 158
Cdd:cd03235 75 QRRSIdrdFP-ISVRDVVLMGLyghkglfrrlsKADK-------AKVDEALERVGLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 159 LAKRPKLLLLDEPMGALDKKlrteMQLELVDILEKV---GVTCLMVTHDQEEAMTMASRIAIM 218
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPK----TQEDIYELLRELrreGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
12-250 |
1.93e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 154.38 E-value: 1.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 12 EVLLSIKGISKSF--DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP-PYLR-- 86
Cdd:PRK13632 5 SVMIKVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIRkk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 87 -------PTNMmfqsyalFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSL 159
Cdd:PRK13632 85 igiifqnPDNQ-------FIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 160 AKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAmTMASRIAIMSYGRIAQVGSPIDIYESpnsr 239
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNN---- 232
|
250
....*....|.
gi 2485516087 240 mtAEFIGSVNI 250
Cdd:PRK13632 233 --KEILEKAKI 241
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
15-227 |
1.87e-43 |
|
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: 149.74 E-value: 1.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP----YLrPtnm 90
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARnrigYL-P--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 91 mfQSYALFPHMTVeQNIAMGLKQDK-LPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLD 169
Cdd:cd03269 77 --EERGLYPKMKV-IDQLVYLAQLKgLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 170 EPMGALDkKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:cd03269 154 EPFSGLD-PVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-236 |
2.04e-43 |
|
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: 157.54 E-value: 2.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDS----TLAVDDVSLDIHKGEIFALLGGSGSGKS----TLLRMLAGFETPDSGRIVLDGQDITALPPY- 84
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 85 ---LRPTN--MMFQ--SYALFPHMTVEQNIAMGLK-QDKLPKNEITDRVAAMLKLVKM-EPYARRK--PQQLSGGQQQRV 153
Cdd:COG4172 86 lrrIRGNRiaMIFQepMTSLNPLHTIGKQIAEVLRlHRGLSGAAARARALELLERVGIpDPERRLDayPHQLSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 154 ALARSLAKRPKLLLLDEPMGALDKKLRTEMqLEL-VDILEKVGVTCLMVTHDqeeaMT----MASRIAIMSYGRIAQVGS 228
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQI-LDLlKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQGP 240
|
....*...
gi 2485516087 229 PIDIYESP 236
Cdd:COG4172 241 TAELFAAP 248
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-222 |
2.34e-43 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 148.30 E-value: 2.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTL--AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP-YLRPT-NM 90
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLeSLRKNiAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 91 MFQSYALFpHMTVEQNIamglkqdklpkneitdrvaamlklvkmepyarrkpqqLSGGQQQRVALARSLAKRPKLLLLDE 170
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 171 PMGALDkklrTEMQLELVDILEKV--GVTCLMVTHDqEEAMTMASRIAIMSYGR 222
Cdd:cd03228 123 ATSALD----PETEALILEALRALakGKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
11-222 |
6.88e-43 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 155.96 E-value: 6.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 11 AEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDitalppyLRPTN- 89
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP-------VRIRSp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 ---------MMFQSYALFPHMTVEQNIAMGLKQDK---LPKNEITDRVAAMLKL--VKMEPYArrKPQQLSGGQQQRVAL 155
Cdd:COG3845 75 rdaialgigMVHQHFMLVPNLTVAENIVLGLEPTKggrLDRKAARARIRELSERygLDVDPDA--KVEDLSVGEQQRVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485516087 156 ARSLAKRPKLLLLDEPMGALdkklrT--EMQlELVDILEKV---GVTCLMVTHDQEEAMTMASRIAIMSYGR 222
Cdd:COG3845 153 LKALYRGARILILDEPTAVL-----TpqEAD-ELFEILRRLaaeGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-229 |
1.89e-42 |
|
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: 155.69 E-value: 1.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 7 TSAQAEVLLSIKGISKSFD--STLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP- 83
Cdd:COG4987 326 APAPGGPSLELEDVSFRYPgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEd 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 84 -YLRPTNMMFQSYALFpHMTVEQNIAMGlkqdklpKNEITD-RVAAMLKLVKMEPYARRKPQ-----------QLSGGQQ 150
Cdd:COG4987 406 dLRRRIAVVPQRPHLF-DTTLRENLRLA-------RPDATDeELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 151 QRVALARSLAKRPKLLLLDEPMGALDKKlrTEMQLeLVDILEKV-GVTCLMVTHDqEEAMTMASRIAIMSYGRIAQVGSP 229
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAA--TEQAL-LADLLEALaGRTVLLITHR-LAGLERMDRILVLEDGRIVEQGTH 553
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-245 |
3.72e-42 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 147.88 E-value: 3.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 5 NNTSAQAEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRML-------AGFETpdSGRIVLDGQD 77
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGARV--EGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 78 ITAlpPYLRPTN------MMFQSYALFPhMTVEQNIAMGLK-QDKLPKNEITDRV-----AAML------KLvkmepyaR 139
Cdd:COG1117 80 IYD--PDVDVVElrrrvgMVFQKPNPFP-KSIYDNVAYGLRlHGIKSKSELDEIVeeslrKAALwdevkdRL-------K 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 140 RKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKK--LRTEmqlELVDILEKVgVTCLMVTHDQEEAMTMASRIAI 217
Cdd:COG1117 150 KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIstAKIE---ELILELKKD-YTIVIVTHNMQQAARVSDYTAF 225
|
250 260
....*....|....*....|....*...
gi 2485516087 218 MSYGRIAQVGSPIDIYESPNSRMTAEFI 245
Cdd:COG1117 226 FYLGELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
17-245 |
6.05e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 147.20 E-value: 6.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 17 IKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPY---------LRP 87
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqqkglirqLRQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 88 -TNMMFQSYALFPHMTVEQNIAMG-LKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKL 165
Cdd:PRK11264 86 hVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 166 LLLDEPMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFI 245
Cdd:PRK11264 166 ILFDEPTSALDPELVGEV-LNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFL 244
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
15-228 |
8.05e-42 |
|
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: 146.13 E-value: 8.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMF-- 92
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 93 -QSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLK-LVKMepyARRKPQQLSGGQQQRVALARSLAKRPKLLLLDE 170
Cdd:TIGR03410 81 pQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPvLKEM---LGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 171 PMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGS 228
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-229 |
9.53e-42 |
|
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: 153.76 E-value: 9.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 8 SAQAEVLLSIKGISKSF-DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLR 86
Cdd:COG4988 330 PAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 87 PTNMMF--QSYALFpHMTVEQNIAMGlkqdklpKNEITD-RVAAMLKLVKMEPYARRKPQ-----------QLSGGQQQR 152
Cdd:COG4988 410 RRQIAWvpQNPYLF-AGTIRENLRLG-------RPDASDeELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516087 153 VALARSLAKRPKLLLLDEPMGALDkkLRTEmqLELVDILEKV--GVTCLMVTHDqEEAMTMASRIAIMSYGRIAQVGSP 229
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLD--AETE--AEILQALRRLakGRTVILITHR-LALLAQADRILVLDDGRIVEQGTH 555
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
14-227 |
1.85e-41 |
|
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: 144.82 E-value: 1.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFD----STLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP-PYLRPT 88
Cdd:cd03266 1 MITADALTKRFRdvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 89 NMMFQSYALFPHMTVEQNIAM-----GLKQDklpknEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRP 163
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYfaglyGLKGD-----ELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 164 KLLLLDEPMGALDkKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:cd03266 156 PVLLLDEPTTGLD-VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
14-236 |
6.59e-41 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 144.36 E-value: 6.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMM-- 91
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 -FQSYALFPHMTVEQNIAMGLKQD----------KLP-----KNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVAL 155
Cdd:PRK11300 85 tFQHVRLFREMTVIENLLVAQHQQlktglfsgllKTPafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 156 ARSLAKRPKLLLLDEPMGALDKKLRTEMQlELVDIL-EKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYE 234
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELD-ELIAELrNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 243
|
..
gi 2485516087 235 SP 236
Cdd:PRK11300 244 NP 245
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
8-240 |
1.08e-40 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 144.52 E-value: 1.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 8 SAQAEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP----- 82
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrly 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 83 PYLRPTNMMFQSYALFPHMTVEQNIAMGLKQ-DKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAK 161
Cdd:PRK11831 81 TVRKRMSMLFQSGALFTDMNVFDNVAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 162 RPKLLLLDEP--------MGALDKklrtemqleLVDILEK-VGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDI 232
Cdd:PRK11831 161 EPDLIMFDEPfvgqdpitMGVLVK---------LISELNSaLGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
....*...
gi 2485516087 233 YESPNSRM 240
Cdd:PRK11831 232 QANPDPRV 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-223 |
4.44e-40 |
|
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: 139.87 E-value: 4.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 11 AEVLLSIKGISKSfdstLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNM 90
Cdd:cd03215 1 GEPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 91 MF------QSYALFPHMTVEQNIAMglkqdklpkneitdrvaamlklvkmepyarrkPQQLSGGQQQRVALARSLAKRPK 164
Cdd:cd03215 77 IAyvpedrKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516087 165 LLLLDEPMGALDKKLRTEMQLELVDILEKvGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:cd03215 125 VLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-223 |
1.28e-39 |
|
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: 139.70 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 16 SIKGISKSF-DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDItALPPYLRPTNMMFQS 94
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-KAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 --YALFPHmTVEQNIAMGLKQDKLPKNeitdRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPM 172
Cdd:cd03226 80 vdYQLFTD-SVREELLLGLKELDAGNE----QAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 173 GALDKKlrtEMQL--ELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:cd03226 155 SGLDYK---NMERvgELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
26-233 |
2.01e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 141.38 E-value: 2.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 26 STLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDiTALPPYL----RPTNMMFQSyalfPH- 100
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENLwdirNKAGMVFQN----PDn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 101 ----MTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALD 176
Cdd:PRK13633 97 qivaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2485516087 177 KKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTmASRIAIMSYGRIAQVGSPIDIY 233
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
30-229 |
2.34e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 141.02 E-value: 2.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 30 VDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPY--LRPTNMMFQSY-ALFPHMTVEQN 106
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWdiRHKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 107 IAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLE 186
Cdd:PRK13650 103 VAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2485516087 187 LVDILEKVGVTCLMVTHDQEEaMTMASRIAIMSYGRIAQVGSP 229
Cdd:PRK13650 183 IKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTP 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
25-229 |
9.00e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 145.69 E-value: 9.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 25 DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP-YLRpTN--MMFQSYALFpHM 101
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLeSLR-RQigVVPQDTFLF-SG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 102 TVEQNIAMGlkqdklpKNEITD-RVAAMLKLVKMEPYARRKPQ-----------QLSGGQQQRVALARSLAKRPKLLLLD 169
Cdd:COG1132 429 TIRENIRYG-------RPDATDeEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 170 EPMGALDkkLRTEMQLElvDILEKV--GVTCLMVTH------DqeeamtmASRIAIMSYGRIAQVGSP 229
Cdd:COG1132 502 EATSALD--TETEALIQ--EALERLmkGRTTIVIAHrlstirN-------ADRILVLDDGRIVEQGTH 558
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
14-237 |
1.72e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 138.67 E-value: 1.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSF-DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDI----TALPPYLRPT 88
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 89 NMMFQSY--ALFPHmTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLL 166
Cdd:PRK13639 81 GIVFQNPddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485516087 167 LLDEPMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPN 237
Cdd:PRK13639 160 VLDEPTSGLDPMGASQI-MKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
29-223 |
1.86e-38 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 137.31 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP----PYLR-PTNMMFQSYALFPHMTV 103
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnrevPFLRrQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 104 EQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLrTEM 183
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL-SEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2485516087 184 QLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:PRK10908 176 ILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
29-236 |
8.69e-38 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 138.17 E-value: 8.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP----YLRPT-NMMFQS-YA-LFPHM 101
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqkLLRQKiQIVFQNpYGsLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 102 TVEQNIAMGLK-QDKLPKNEITDRVAAMLKLVKMEP-YARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKL 179
Cdd:PRK11308 110 KVGQILEEPLLiNTSLSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2485516087 180 RTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESP 236
Cdd:PRK11308 190 QAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
11-245 |
1.19e-37 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 136.25 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 11 AEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP------- 83
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 84 -------YLRPT-NMMFQSYALFPHMTVEQNIAMGLKQD-KLPKNEITDRVAAMLKLVKMEPYARRK-PQQLSGGQQQRV 153
Cdd:PRK10619 82 adknqlrLLRTRlTMVFQHFNLWSHMTVLENVMEAPIQVlGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 154 ALARSLAKRPKLLLLDEPMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIY 233
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEV-LRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
250
....*....|..
gi 2485516087 234 ESPNSRMTAEFI 245
Cdd:PRK10619 241 GNPQSPRLQQFL 252
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
7-250 |
2.17e-37 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 137.53 E-value: 2.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 7 TSAQAEVLLSIKGISKSFD------------STL-AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVL 73
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDikdgkqwfwqppKTLkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 74 DGQDITALPP-YLRPT----NMMFQS--YALFPHMTVEQNIAMGLK--QDKLPKNEITDRVAAMLKLVKMEP-YARRKPQ 143
Cdd:PRK15079 81 LGKDLLGMKDdEWRAVrsdiQMIFQDplASLNPRMTIGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLLPnLINRYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 144 QLSGGQQQRVALARSLAKRPKLLLLDEPMGALD-----------KKLRTEMQLELVDILEKVGVtclmVTHdqeeamtMA 212
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDvsiqaqvvnllQQLQREMGLSLIFIAHDLAV----VKH-------IS 229
|
250 260 270
....*....|....*....|....*....|....*...
gi 2485516087 213 SRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSVNI 250
Cdd:PRK15079 230 DRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVPI 267
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
26-225 |
8.82e-37 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 133.02 E-value: 8.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 26 STLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPT------NMMFQSYALFP 99
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqklGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 100 HMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKL 179
Cdd:PRK11629 101 DFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2485516087 180 RTEMQLELVDILEKVGVTCLMVTHDQEEAMTMaSRIAIMSYGRIAQ 225
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-223 |
1.75e-36 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 131.94 E-value: 1.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 18 KGISKSFDS--TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMF--Q 93
Cdd:cd03245 6 RNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYvpQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SYALFpHMTVEQNIAMGlkqdklpKNEITD-RVAAMLKLVKMEPYARRKP-----------QQLSGGQQQRVALARSLAK 161
Cdd:cd03245 86 DVTLF-YGTLRDNITLG-------APLADDeRILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 162 RPKLLLLDEPMGALDKklRTEMQleLVDILEKV--GVTCLMVTHDQeEAMTMASRIAIMSYGRI 223
Cdd:cd03245 158 DPPILLLDEPTSAMDM--NSEER--LKERLRQLlgDKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-237 |
2.14e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 133.61 E-value: 2.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 27 TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITA------LPPYLRPTNMMFQsyalFP- 99
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknkkLKPLRKKVGIVFQ----FPe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 100 HM----TVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKM-EPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGA 174
Cdd:PRK13634 96 HQlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 175 LDKKLRTEMqLELVDILEK-VGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPN 237
Cdd:PRK13634 176 LDPKGRKEM-MEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
10-234 |
3.98e-36 |
|
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: 137.63 E-value: 3.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 10 QAEVLLSIKGISKSFDST-----LAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSG----RIVLDGQDITA 80
Cdd:TIGR03269 275 VGEPIIKVRNVSKRYISVdrgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvRVGDEWVDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 81 LPPYLRP-----TNMMFQSYALFPHMTVEQNI--AMGLKqdkLPKNEITDRVAAMLKLVKM-EPYAR----RKPQQLSGG 148
Cdd:TIGR03269 355 PGPDGRGrakryIGILHQEYDLYPHRTVLDNLteAIGLE---LPDELARMKAVITLKMVGFdEEKAEeildKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 149 QQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGS 228
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
....*.
gi 2485516087 229 PIDIYE 234
Cdd:TIGR03269 512 PEEIVE 517
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-245 |
4.18e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 131.96 E-value: 4.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGF-----ETPDSGRIVLDGQDITALPPYL--RP 87
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIElrRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 88 TNMMFQSYALFPHMTVEQNIAMGLKQDKLPKN--EITDRVAAMLKLVKMEPYARRK----PQQLSGGQQQRVALARSLAK 161
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSkkELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 162 RPKLLLLDEPMGALDKKLRTEMQ---LELvdileKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNS 238
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIEslfLEL-----KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
....*..
gi 2485516087 239 RMTAEFI 245
Cdd:PRK14247 239 ELTEKYV 245
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-224 |
5.13e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 136.69 E-value: 5.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 7 TSAQAEVLLSIKGISksfdSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP--- 83
Cdd:COG1129 249 AAAPGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrda 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 84 ------YL---RptnmmfQSYALFPHMTVEQNIAMGLkQDKLPKN---------EITDRVAAMLKlVKMePYARRKPQQL 145
Cdd:COG1129 325 iragiaYVpedR------KGEGLVLDLSIRENITLAS-LDRLSRGglldrrrerALAEEYIKRLR-IKT-PSPEQPVGNL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 146 SGGQQQRVALARSLAKRPKLLLLDEP-----MGAldkklRTEMQlELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSY 220
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPtrgidVGA-----KAEIY-RLIRELAAEGKAVIVISSELPELLGLSDRILVMRE 469
|
....
gi 2485516087 221 GRIA 224
Cdd:COG1129 470 GRIV 473
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
32-338 |
5.14e-36 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 134.23 E-value: 5.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 32 DVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQ---DI---TALPPYLRPTNMMFQSYALFPHMTVEQ 105
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAekgICLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 106 NIAMGLKQDKLPKneiTDRVAAMLKLvkmEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALD---KKlrte 182
Cdd:PRK11144 96 NLRYGMAKSMVAQ---FDKIVALLGI---EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlprKR---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 183 mqlELVDILEK----VGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSVNIFEANILED 258
Cdd:PRK11144 166 ---ELLPYLERlareINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMRPWLPKEEQSSILKVTVLEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 259 NSDSLSLASELLDAPVFIDRgvtTPAETTETL-IALRPEKIYLTTEKPEGDS--NWSCGTVDNIAYLGDitSYYVKLASG 335
Cdd:PRK11144 243 HPHYAMTALALGDQHLWVNK---LDAPLGTALrIRIQASDVSLVLQPPQQSSirNILRAKVVEIYDDNG--QVEVKLEVG 317
|
...
gi 2485516087 336 KRV 338
Cdd:PRK11144 318 GKT 320
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
25-223 |
5.78e-36 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 138.85 E-value: 5.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 25 DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMF--QSYALFpHMT 102
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYvpQDPRLF-YGT 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 103 VEQNIAMGLKQdklpkneITD-RVAAMLKLVKMEPYARRKPQ-----------QLSGGQQQRVALARSLAKRPKLLLLDE 170
Cdd:TIGR03375 555 LRDNIALGAPY-------ADDeEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDE 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2485516087 171 PMGALDKklRTEMQleLVDILEKV--GVTCLMVTHDQeEAMTMASRIAIMSYGRI 223
Cdd:TIGR03375 628 PTSAMDN--RSEER--FKDRLKRWlaGKTLVLVTHRT-SLLDLVDRIIVMDNGRI 677
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
25-229 |
1.41e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 131.01 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 25 DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPY-LRP-TNMMFQSY--ALFPh 100
Cdd:PRK13647 16 DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSkVGLVFQDPddQVFS- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 101 MTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLR 180
Cdd:PRK13647 95 STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2485516087 181 TEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSP 229
Cdd:PRK13647 175 ETL-MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
25-233 |
3.11e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 130.35 E-value: 3.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 25 DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDI----TALPPYLRPTNMMFQS--YALF 98
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMKLRESVGMVFQDpdNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 99 PhMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKK 178
Cdd:PRK13636 97 S-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2485516087 179 LRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIY 233
Cdd:PRK13636 176 GVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
29-236 |
4.38e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 129.92 E-value: 4.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDS---GRIVLDGQDITALPPY-LRP-TNMMFQSY-ALFPHMT 102
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWdIREkVGIVFQNPdNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 103 VEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTE 182
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 183 MQLELVDILEKVGVTCLMVTHDQEEAmTMASRIAIMSYGRIAQVGSPIDIYESP 236
Cdd:PRK13640 182 ILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
15-235 |
6.11e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 130.31 E-value: 6.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRP-TNMMFQ 93
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMG 173
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 174 ALDKKLRTEMQLELVDILEKvGVTCLMVTHDQEEAMTMASRIAIMSYGR-IAQvGSPIDIYES 235
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRkIAE-GAPHALIES 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-209 |
6.65e-35 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 126.58 E-value: 6.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 23 SFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPylrptnmmfQSYAL---FP 99
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVP---------QRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 100 hMTVEQNIAMGLKQDKLPKNEIT--DR--VAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGAL 175
Cdd:NF040873 72 -LTVRDLVAMGRWARRGLWRRLTrdDRaaVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|....
gi 2485516087 176 DKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAM 209
Cdd:NF040873 151 DAESRERI-IALLAEEHARGATVVVVTHDLELVR 183
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-239 |
1.26e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 128.57 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSF-DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIV---LDGQDITALPPYLRPTN 89
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 MMFQS-YALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLL 168
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485516087 169 DEPMGALDKKlRTEMQLELVDILEKVGVTCLMVTHDQEEaMTMASRIAIMSYGRIAQVGSPIDIYESPNSR 239
Cdd:PRK13644 161 DEVTSMLDPD-SGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
16-255 |
1.70e-34 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 127.51 E-value: 1.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 16 SIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP--------YLRp 87
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSrelakrlaILR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 88 tnmmfQSYALFPHMTVEQNIAMG---------LKQDKlpknEITDRVAAMLKLvkmEPYARRKPQQLSGGQQQRVALARS 158
Cdd:COG4604 82 -----QENHINSRLTVRELVAFGrfpyskgrlTAEDR----EIIDEAIAYLDL---EDLADRYLDELSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 159 LAKRPKLLLLDEPMGALDKKLRTEM--QL-ELVDILEKvgvTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIyes 235
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMmkLLrRLADELGK---TVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI--- 223
|
250 260
....*....|....*....|
gi 2485516087 236 pnsrMTAEFIGSvnIFEANI 255
Cdd:COG4604 224 ----ITPEVLSD--IYDTDI 237
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
25-235 |
3.03e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 127.17 E-value: 3.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 25 DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITA--LPPYLRPTNMMFQS-YALFPHM 101
Cdd:PRK13648 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdnFEKLRKHIGIVFQNpDNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 102 TVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRT 181
Cdd:PRK13648 100 IVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2485516087 182 EMqLELVDIL-EKVGVTCLMVTHDQEEAMTmASRIAIMSYGRIAQVGSPIDIYES 235
Cdd:PRK13648 180 NL-LDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
25-228 |
1.02e-33 |
|
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: 124.91 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 25 DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDI-TALPPYLR-PTNMMFQSYALFpHMT 102
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRrQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 103 VEQNIAMGlkqDKLPKNEitdRVAAMLKLVKMEPYARRKPQ-----------QLSGGQQQRVALARSLAKRPKLLLLDEP 171
Cdd:cd03252 92 IRDNIALA---DPGMSME---RVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2485516087 172 MGALDKKLRTEMQLELVDILEkvGVTCLMVTHDQEEAMTmASRIAIMSYGRIAQVGS 228
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGS 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
14-223 |
2.54e-33 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 131.00 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSF---DSTLAV-DDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP----YL 85
Cdd:PRK10535 4 LLELKDIRRSYpsgEEQVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalaQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 86 RPTNM--MFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRP 163
Cdd:PRK10535 84 RREHFgfIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 164 KLLLLDEPMGALDKKLRTEMQLELVDILEKvGVTCLMVTHDQEEAmTMASRIAIMSYGRI 223
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEI 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
30-258 |
4.84e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 124.43 E-value: 4.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 30 VDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPY--LRPTNMMFQSY-ALFPHMTVEQN 106
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWnlRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 107 IAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLE 186
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485516087 187 LVDILEKVGVTCLMVTHDQEEAMTmASRIAIMSYGRIAQVGSPIDIYESPNSRMTaefIGSVNIFEANILED 258
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVE---IGLDVPFSSNLMKD 250
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-232 |
5.05e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 125.20 E-value: 5.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 17 IKGISKSFDSTL-----AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIV----------------LDG 75
Cdd:PRK13651 5 VKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekeKVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 76 QDITALPPYLRP----------TNMMFQ--SYALFpHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKM-EPYARRKP 142
Cdd:PRK13651 85 EKLVIQKTRFKKikkikeirrrVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 143 QQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGR 222
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEI-LEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
250
....*....|
gi 2485516087 223 IAQVGSPIDI 232
Cdd:PRK13651 243 IIKDGDTYDI 252
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-236 |
6.97e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 124.96 E-value: 6.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 11 AEVLLSIKGISKSFDST-----LAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRI----VLDGQDITAL 81
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 82 PPYLRPT--------------NMMFQ--SYALFPHmTVEQNIAMGLKQDKLPKNEITDRvaAMLKLVKM---EPYARRKP 142
Cdd:PRK13631 98 ELITNPYskkiknfkelrrrvSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKL--AKFYLNKMgldDSYLERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 143 QQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGR 222
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
250
....*....|....
gi 2485516087 223 IAQVGSPIDIYESP 236
Cdd:PRK13631 254 ILKTGTPYEIFTDQ 267
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-231 |
1.14e-32 |
|
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: 122.50 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 12 EVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIV------LDGQDITALppyl 85
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWEL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 86 RP-----TNMMFQSYAlfPHMTVEQNIA------MGLKQDklPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVA 154
Cdd:COG1119 77 RKriglvSPALQLRFP--RDETVLDVVLsgffdsIGLYRE--PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 155 LARSLAKRPKLLLLDEPMGALDKKLRTEMqLELVDIL-EKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGsPID 231
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELL-LALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG-PKE 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-222 |
3.12e-32 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 126.58 E-value: 3.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 11 AEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFeTPD---SGRIVLDGQDITAlpPYLRP 87
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQA--SNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 88 TN-----MMFQSYALFPHMTVEQNIAMGlkqdklpkNEITD-----------RVAAMLKLVKMEPYARRKPQQLSGGQQQ 151
Cdd:PRK13549 79 TEragiaIIHQELALVKELSVLENIFLG--------NEITPggimdydamylRAQKLLAQLKLDINPATPVGNLGLGQQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485516087 152 RVALARSLAKRPKLLLLDEPMGALDKKlRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGR 222
Cdd:PRK13549 151 LVEIAKALNKQARLLILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
12-222 |
3.38e-32 |
|
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: 120.62 E-value: 3.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 12 EVLLSIKGISKSFdsTL---------AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQ----DI 78
Cdd:COG4778 2 TTLLEVENLSKTF--TLhlqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 79 TALPP----YLRPTNMMFQSYAL--FPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLklvkmepyAR-RKPQQL------ 145
Cdd:COG4778 80 AQASPreilALRRRTIGYVSQFLrvIPRVSALDVVAEPLLERGVDREEARARARELL--------ARlNLPERLwdlppa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 146 --SGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRtEMQLELVDILEKVGVTCLMVTHDqEEAM-TMASRIAIMSYGR 222
Cdd:COG4778 152 tfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANR-AVVVELIEEAKARGTAIIGIFHD-EEVReAVADRVVDVTPFS 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-245 |
6.12e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 120.72 E-value: 6.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 24 FDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGF-----ETPDSGRIVLDGQDITAlpPYLRP------TNMMF 92
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYS--PDVDPievrreVGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 93 QSYALFPHMTVEQNIAMGLKQDKL--PKNEITDRVAAMLKLVKM--EPYARRK--PQQLSGGQQQRVALARSLAKRPKLL 166
Cdd:PRK14267 92 QYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdEVKDRLNdyPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 167 LLDEPMGALD----KKLRtEMQLELvdileKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTA 242
Cdd:PRK14267 172 LMDEPTANIDpvgtAKIE-ELLFEL-----KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTE 245
|
...
gi 2485516087 243 EFI 245
Cdd:PRK14267 246 KYV 248
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
14-248 |
9.93e-32 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 120.32 E-value: 9.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQD-----ITALPPYLRpT 88
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAER-R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 89 NMMFQSYALfphmtVEQNIAMGLKQDKLPKNEITDRVAAM---------------LKLVKMEPyAR--RKPQQLSGGQQQ 151
Cdd:TIGR02323 82 RLMRTEWGF-----VHQNPRDGLRMRVSAGANIGERLMAIgarhygnirataqdwLEEVEIDP-TRidDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 152 RVALARSLAKRPKLLLLDEPMGALDkklrTEMQLELVDILEKV----GVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLD----VSVQARLLDLLRGLvrdlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
250 260
....*....|....*....|.
gi 2485516087 228 SPIDIYESPNSRMTAEFIGSV 248
Cdd:TIGR02323 232 LTDQVLDDPQHPYTQLLVSSI 252
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
25-228 |
1.08e-31 |
|
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: 119.64 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 25 DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDIT--ALPPYLRPTNMMFQSYALFpHMT 102
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdyTLASLRRQIGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 103 VEQNIAMGLkqdklpKNEITDRVAAMLKLVKMEPYARRKPQ-----------QLSGGQQQRVALARSLAKRPKLLLLDEP 171
Cdd:cd03251 92 VAENIAYGR------PGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516087 172 MGALDkkLRTEMQLElvDILEK--VGVTCLMVTHdQEEAMTMASRIAIMSYGRIAQVGS 228
Cdd:cd03251 166 TSALD--TESERLVQ--AALERlmKNRTTFVIAH-RLSTIENADRIVVLEDGKIVERGT 219
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
14-227 |
1.13e-31 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 120.03 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITalppyLRPTNMMFQ 93
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQ-----LRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SYALFPHMT----VEQNIAMGLKQDKLPKNEITDRV-------------AAMLKLVKMEPYARR---KPQQLSGGQQQRV 153
Cdd:PRK11701 81 AERRRLLRTewgfVHQHPRDGLRMQVSAGGNIGERLmavgarhygdiraTAGDWLERVEIDAARiddLPTTFSGGMQQRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 154 ALARSLAKRPKLLLLDEPMGALDkklrTEMQLELVDIL----EKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLD----VSVQARLLDLLrglvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
29-246 |
1.16e-31 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 119.40 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKST----LLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMFQS--YALFPHMT 102
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 103 VEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYAR---RKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKL 179
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEvlkKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485516087 180 RTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIG 246
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
29-235 |
1.21e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 120.88 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITA-------LPPYLRPTNMMFQ--SYALFP 99
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkikeVKRLRKEIGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 100 HmTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKM-EPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKK 178
Cdd:PRK13645 106 E-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2485516087 179 LRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYES 235
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
14-232 |
1.44e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 119.61 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPY---LRPTNM 90
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 91 MFQSYALFPHMTVEQNIAMGLK-QDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLD 169
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 170 EPMGALDKKLRTEMQlELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDI 232
Cdd:PRK10895 163 EPFAGVDPISVIDIK-RIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
29-234 |
1.45e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 120.62 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITA------LPPYLRPTNMMFQsyalFPHM- 101
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIKQIRKKVGLVFQ----FPESq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 102 ----TVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKM-EPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALD 176
Cdd:PRK13649 98 lfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 177 KKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYE 234
Cdd:PRK13649 178 PKGRKEL-MTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-246 |
2.34e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 123.98 E-value: 2.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 12 EVLLSIKGIS-KSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPY-LRPTN 89
Cdd:COG3845 255 EVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPReRRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 MMF-----QSYALFPHMTVEQNIAMG-LKQDKLPKNEITDRvAAMLKLVK--MEPYARRKP------QQLSGGQQQRVAL 155
Cdd:COG3845 335 VAYipedrLGRGLVPDMSVAENLILGrYRRPPFSRGGFLDR-KAIRAFAEelIEEFDVRTPgpdtpaRSLSGGNQQKVIL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 156 ARSLAKRPKLLLLDEPMGALD--------KKLrtemqLELVDilEKVGVtcLMVTHDQEEAMTMASRIAIMSYGRIaqvg 227
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDvgaiefihQRL-----LELRD--AGAAV--LLISEDLDEILALSDRIAVMYEGRI---- 480
|
250
....*....|....*....
gi 2485516087 228 spidIYESPNSRMTAEFIG 246
Cdd:COG3845 481 ----VGEVPAAEATREEIG 495
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-248 |
2.37e-31 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 124.97 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP-----PYLRPTNMMFQS-YA-LFPHM 101
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgklqALRRDIQFIFQDpYAsLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 102 TVEQNIAMGLK-QDKLPKNEITDRVAAMLKLVKMEP-YARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKL 179
Cdd:PRK10261 419 TVGDSIMEPLRvHGLLPGKAAAARVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516087 180 RTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEFIGSV 248
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
31-228 |
2.79e-31 |
|
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: 118.41 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 31 DDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMF--QSYALFPhMTVEQNIA 108
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLvsQEPVLFD-GTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 109 MGLKQDKLPKNEITDRVAAMLKLVKMEPYARR-----KPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEM 183
Cdd:cd03249 99 YGKPDATDEEVEEAAKKANIHDFIMSLPDGYDtlvgeRGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLV 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2485516087 184 QLELVDILEkvGVTCLMVTHdQEEAMTMASRIAIMSYGRIAQVGS 228
Cdd:cd03249 179 QEALDRAMK--GRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGT 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-223 |
2.90e-31 |
|
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: 116.55 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDST--LAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITAL-PPYLRPT-NM 90
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWdPNELGDHvGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 91 MFQSYALFPHmTVEQNIamglkqdklpkneitdrvaamlklvkmepyarrkpqqLSGGQQQRVALARSLAKRPKLLLLDE 170
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 171 PMGALDKKlRTEMQLELVDILEKVGVTCLMVTHdQEEAMTMASRIAIMSYGRI 223
Cdd:cd03246 123 PNSHLDVE-GERALNQAIAALKAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-234 |
5.25e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 120.32 E-value: 5.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 2 AVTNNTSAQAEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITAL 81
Cdd:PRK13536 29 AKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 82 PPYLRP-TNMMFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLA 160
Cdd:PRK13536 109 ARLARArIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALI 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 161 KRPKLLLLDEPMGALDKKLRTEMQLELVDILEKvGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYE 234
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
15-239 |
5.42e-31 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 121.49 E-value: 5.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYL--RPTNMMF 92
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 93 QSYALFPHMTVEQNIAMGLK--QDKLPKNEITDRVA---AMLKlVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLL 167
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMGRTphRSRFDTWTETDRAAverAMER-TGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 168 LDEPMGALD--KKLRTemqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSR 239
Cdd:PRK09536 163 LDEPTASLDinHQVRT---LELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLR 233
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
33-208 |
5.84e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 117.57 E-value: 5.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 33 VSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP----PYLRPTNM--MFQSYALFPHMTVEQN 106
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearAKLRAKHVgfVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 107 IAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLE 186
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180
....*....|....*....|..
gi 2485516087 187 LVDILEKVGVTCLMVTHDQEEA 208
Cdd:PRK10584 189 LFSLNREHGTTLILVTHDLQLA 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-222 |
1.02e-30 |
|
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: 122.24 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDS--GRIVLDGQDITAlpPYLRPTN-- 89
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKA--SNIRDTEra 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 ---MMFQSYALFPHMTVEQNIAMG----LKQDKLPKNEITDRVAAMLKLVKMEPYARRKP-QQLSGGQQQRVALARSLAK 161
Cdd:TIGR02633 79 givIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485516087 162 RPKLLLLDEPMGALDKKlRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGR 222
Cdd:TIGR02633 159 QARLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
29-235 |
4.78e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 115.56 E-value: 4.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQdITALppyLRpTNMMFQsyalfPHMTVEQNI- 107
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSAL---LE-LGAGFH-----PELTGRENIy 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 108 ----AMGlkqdkLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALD----KKL 179
Cdd:COG1134 111 lngrLLG-----LSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDaafqKKC 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516087 180 RTEMQlelvDILEKvGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSP---IDIYES 235
Cdd:COG1134 186 LARIR----ELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPeevIAAYEA 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-245 |
5.47e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 120.58 E-value: 5.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 8 SAQAEVLLSIKGISKSF-----------DSTLAVDDVSLDIHKGEIFALLGGSGSGKST----LLRMLAGfetpdSGRIV 72
Cdd:PRK15134 269 PEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 73 LDGQDI-----TALPPYLRPTNMMFQ--SYALFPHMTVEQNIAMGLK--QDKLPKNEITDRVAAMLKLVKMEPYAR-RKP 142
Cdd:PRK15134 344 FDGQPLhnlnrRQLLPVRHRIQVVFQdpNSSLNPRLNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLDPETRhRYP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 143 QQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGR 222
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGE 503
|
250 260
....*....|....*....|...
gi 2485516087 223 IAQVGSPIDIYESPNSRMTAEFI 245
Cdd:PRK15134 504 VVEQGDCERVFAAPQQEYTRQLL 526
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-218 |
6.08e-30 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 120.47 E-value: 6.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSF-DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP--YLRPTNMM 91
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAdsWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 FQSYALFPHmTVEQNIAMGlkqdklpKNEITD-RVAAMLKLVKMEPYARRKPQQ-----------LSGGQQQRVALARSL 159
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLA-------RPDASDaEIREALERAGLDEFVAALPQGldtpigeggagLSGGQAQRLALARAF 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485516087 160 AKRPKLLLLDEPMGALDKklrtEMQLELVDILEKV--GVTCLMVTHDqEEAMTMASRIAIM 218
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDA----ETEAEVLEALRALaqGRTVLLVTHR-LALAALADRIVVL 529
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
30-227 |
6.31e-30 |
|
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: 120.62 E-value: 6.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 30 VDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP--------YLrPtnmmfQSYALFPHm 101
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDReelgrhigYL-P-----QDVELFDG- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 102 TVEQNIA-MGlkqdklpknEITDR--VAAmlklvkmepyAR---------RKPQ-----------QLSGGQQQRVALARS 158
Cdd:COG4618 421 TIAENIArFG---------DADPEkvVAA----------AKlagvhemilRLPDgydtrigeggaRLSGGQRQRIGLARA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 159 LAKRPKLLLLDEPMGALD----KKLRtemqlELVDILEKVGVTCLMVTHDQeEAMTMASRIAIMSYGRIAQVG 227
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDdegeAALA-----AAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFG 548
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-228 |
7.42e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 115.50 E-value: 7.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 12 EVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDS---GRIVLDGQDITALPPYLRP- 87
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGRLARDi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 88 ------TNMMFQSYALFPHMTVEQNIAMG-LKQDKLPKN-------EITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRV 153
Cdd:PRK09984 82 rksranTGYIFQQFNLVNRLSVLENVLIGaLGSTPFWRTcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485516087 154 ALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGS 228
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-245 |
7.63e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 115.14 E-value: 7.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 11 AEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGF-ETPDS-----GRIVLDGQDITALPP- 83
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSkikvdGKVLYFGKDIFQIDAi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 84 -YLRPTNMMFQSYALFPHMTVEQNIAMGLKQDKLP-KNEITDRVAAMLKLVKM--EPYAR--RKPQQLSGGQQQRVALAR 157
Cdd:PRK14246 87 kLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkEVYDRlnSPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 158 SLAKRPKLLLLDEPMGALD-------KKLRTEMQLElvdilekvgVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPI 230
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDivnsqaiEKLITELKNE---------IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSN 237
|
250
....*....|....*
gi 2485516087 231 DIYESPNSRMTAEFI 245
Cdd:PRK14246 238 EIFTSPKNELTEKYV 252
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
29-227 |
9.48e-30 |
|
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: 114.17 E-value: 9.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGqditalppylRPTNMMFQSYALFPHMTVEQNIA 108
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----------RVSSLLGLGGGFNPELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 109 -----MGLKQDklpknEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEM 183
Cdd:cd03220 107 lngrlLGLSRK-----EIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2485516087 184 QLELVDILEKvGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:cd03220 182 QRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-245 |
1.52e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 114.49 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 7 TSAQAEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLR-------MLAGFETpdSGRIVLDGQDIT 79
Cdd:PRK14243 3 TLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 80 AlpPYLRPT------NMMFQSYALFPHmTVEQNIAMGLKQDKLPKN-----EITDRVAAMLKLVKMEpyARRKPQQLSGG 148
Cdd:PRK14243 81 A--PDVDPVevrrriGMVFQKPNPFPK-SIYDNIAYGARINGYKGDmdelvERSLRQAALWDEVKDK--LKQSGLSLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 149 QQQRVALARSLAKRPKLLLLDEPMGALD--KKLRTEmqlELVDILeKVGVTCLMVTHDqeeaMTMASRIAIMS------- 219
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDpiSTLRIE---ELMHEL-KEQYTIIIVTHN----MQQAARVSDMTaffnvel 227
|
250 260 270
....*....|....*....|....*....|..
gi 2485516087 220 ------YGRIAQVGSPIDIYESPNSRMTAEFI 245
Cdd:PRK14243 228 tegggrYGYLVEFDRTEKIFNSPQQQATRDYV 259
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-207 |
2.15e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 113.27 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP--YLRPTNMM 91
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 FQSYALFPHmTV----------------EQNIAMGLKQDKLPKNEITDRVAAmlklvkmepyarrkpqqLSGGQQQRVAL 155
Cdd:PRK10247 87 AQTPTLFGD-TVydnlifpwqirnqqpdPAIFLDDLERFALPDTILTKNIAE-----------------LSGGEKQRISL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2485516087 156 ARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEE 207
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-245 |
2.35e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 113.72 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 12 EVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGF-----ETPDSGRIVLDGQDI----TALP 82
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysprTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 83 PYLRPTNMMFQSYALFPhMTVEQNIAMGLKQDKLPKNEITDRV-------AAMLKLVKMEPYArrKPQQLSGGQQQRVAL 155
Cdd:PRK14239 83 DLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAvekslkgASIWDEVKDRLHD--SALGLSGGQQQRVCI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 156 ARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKvgVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYES 235
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMN 237
|
250
....*....|
gi 2485516087 236 PNSRMTAEFI 245
Cdd:PRK14239 238 PKHKETEDYI 247
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
29-237 |
2.40e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.51 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITA--LPPYLRPTNMMFQSY--ALFPhMTVE 104
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenIREVRKFVGLVFQNPddQIFS-PTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 105 QNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQ 184
Cdd:PRK13652 98 QDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 185 LELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPN 237
Cdd:PRK13652 178 DFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
26-234 |
3.07e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 114.45 E-value: 3.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 26 STLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITA------LPPYLRPTNMMFQsyalFP 99
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStskqkeIKPVRKKVGVVFQ----FP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 100 HM-----TVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKM-EPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMG 173
Cdd:PRK13643 94 ESqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485516087 174 ALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYE 234
Cdd:PRK13643 174 GLDPKARIEM-MQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
12-247 |
4.71e-29 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 113.35 E-value: 4.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 12 EVLLSIKGISKSF---------DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP 82
Cdd:PRK15112 2 ETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 83 PYLRPT--NMMFQ--SYALFPHMTVEQNIAMGLKQD-KLPKNEITDRVAAMLKLVKMEP-YARRKPQQLSGGQQQRVALA 156
Cdd:PRK15112 82 YSYRSQriRMIFQdpSTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 157 RSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVThdQEEAMT--MASRIAIMSYGRIAQVGSPIDIYE 234
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT--QHLGMMkhISDQVLVMHQGEVVERGSTADVLA 239
|
250
....*....|...
gi 2485516087 235 SPNSRMTAEFIGS 247
Cdd:PRK15112 240 SPLHELTKRLIAG 252
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
15-258 |
7.09e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.41 E-value: 7.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPylrptNMMFQS 94
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-----RQLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 YALFP--HMT-----VEQNIAMG----------LKQDklpKNEITDRvaAMLKLvKMEPYARRKPQQLSGGQQQRVALAR 157
Cdd:PRK11231 78 LALLPqhHLTpegitVRELVAYGrspwlslwgrLSAE---DNARVNQ--AMEQT-RINHLADRRLTDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 158 SLAKRPKLLLLDEPMGALDkklrTEMQLELVDILEKV---GVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIye 234
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLD----INHQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV-- 225
|
250 260
....*....|....*....|....
gi 2485516087 235 spnsrMTAEFIGSVNIFEANILED 258
Cdd:PRK11231 226 -----MTPGLLRTVFDVEAEIHPE 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-228 |
1.12e-28 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 116.69 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 5 NNTSAQAEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP- 83
Cdd:PRK15439 2 QTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 84 -------YLRPtnmmfQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYArrkpQQLSGGQQQRVALA 156
Cdd:PRK15439 82 kahqlgiYLVP-----QEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSA----GSLEVADRQIVEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485516087 157 RSLAKRPKLLLLDEPMGALdKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGS 228
Cdd:PRK15439 153 RGLMRDSRILILDEPTASL-TPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
31-229 |
1.47e-28 |
|
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: 111.17 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 31 DDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP-PYLRPT-NMMFQSYALFpHMTVEQNIA 108
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTlDSLRRAiGVVPQDTVLF-NDTIGYNIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 109 MGlkqdKLPKNEITDRVAAmlKLVKMEPYARRKPQQ-----------LSGGQQQRVALARSLAKRPKLLLLDEPMGALDk 177
Cdd:cd03253 97 YG----RPDATDEEVIEAA--KAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALD- 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 178 klrTEMQLELVDILEKV--GVTCLMVTHDQEEAMTmASRIAIMSYGRIAQVGSP 229
Cdd:cd03253 170 ---THTEREIQAALRDVskGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTH 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
13-223 |
2.51e-28 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 110.74 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 13 VLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPpylrPTNMMF 92
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQ----TAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 93 QSYALFPH-------MTVEQNIAM-GLKQDKLPKNEITDRVAAMLKLVkmepYARR--KPQQLSGGQQQRVALARSLAKR 162
Cdd:PRK11614 80 EAVAIVPEgrrvfsrMTVEENLAMgGFFAERDQFQERIKWVYELFPRL----HERRiqRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485516087 163 PKLLLLDEPMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQI-FDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-204 |
2.94e-28 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 115.54 E-value: 2.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 7 TSAQAEVLLSIKGISKSF-DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYL 85
Cdd:TIGR02868 327 AVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 86 RPTNMMF--QSYALFpHMTVEQNIAMGlkqdklpKNEITD-RVAAMLKLVKMEPYARRKP-----------QQLSGGQQQ 151
Cdd:TIGR02868 407 VRRRVSVcaQDAHLF-DTTVRENLRLA-------RPDATDeELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 152 RVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEkvGVTCLMVTHD 204
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-245 |
6.06e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 110.13 E-value: 6.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDS-----GRIVLDGQDI----TALPPYL 85
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 86 RPTNMMFQSYALFPhMTVEQNIAMGLKQDKL-PKNEITDRVAAMLKLVKMEPYARRKPQQ----LSGGQQQRVALARSLA 160
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 161 KRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIM--SYGRIAQV---GSPIDIYES 235
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRIGQLvefGLTKKIFNS 246
|
250
....*....|
gi 2485516087 236 PNSRMTAEFI 245
Cdd:PRK14258 247 PHDSRTREYV 256
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
27-237 |
1.05e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 110.30 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 27 TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITA------LPPYLRPTNMMFQsyalFPH 100
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnknLKKLRKKVSLVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 101 M-----TVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKM-EPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGA 174
Cdd:PRK13641 96 AqlfenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 175 LDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPN 237
Cdd:PRK13641 176 LDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
17-223 |
1.05e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 113.62 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 17 IKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITAlppYLRptnmmfQSYA 96
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIG---YLP------QEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 97 LFPHMTVEQNIAMG---LKQDKLPKNEITDRVAAMLKLvkMEPYAR--------------------------------RK 141
Cdd:COG0488 72 LDDDLTVLDTVLDGdaeLRALEAELEELEAKLAEPDED--LERLAElqeefealggweaearaeeilsglgfpeedldRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 142 PQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDkklrTEMQLELVDILEKVGVTCLMVTHDQE--EAmtMASRIAIMS 219
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSHDRYflDR--VATRILELD 223
|
....
gi 2485516087 220 YGRI 223
Cdd:COG0488 224 RGKL 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-228 |
1.06e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 114.15 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 4 TNNTSAQAEVLLSIKGISKSF--DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITAL 81
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 82 P-PYLRptNMMF---QSYALFPHmTVEQNIAMGlkqdklpKNEITD-RVAAMLKLVKMEPYARRKP----------QQLS 146
Cdd:PRK11160 408 SeAALR--QAISvvsQRVHLFSA-TLRDNLLLA-------APNASDeALIEVLQQVGLEKLLEDDKglnawlgeggRQLS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 147 GGQQQRVALARSLAKRPKLLLLDEPMGALDKklRTEMQ-LELvdiLEKV--GVTCLMVTHdQEEAMTMASRIAIMSYGRI 223
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDA--ETERQiLEL---LAEHaqNKTVLMITH-RLTGLEQFDRICVMDNGQI 551
|
....*
gi 2485516087 224 AQVGS 228
Cdd:PRK11160 552 IEQGT 556
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-204 |
1.71e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 113.24 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 13 VLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLdGQDITalppylrptnmmf 92
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK------------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 93 QSY------ALFPHMTVEQNIAMGlkQDKLPKNEITDRVAAML-------KLVKmepyarrkpqQLSGGQQQRVALARSL 159
Cdd:COG0488 380 IGYfdqhqeELDPDKTVLDELRDG--APGGTEQEVRGYLGRFLfsgddafKPVG----------VLSGGEKARLALAKLL 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2485516087 160 AKRPKLLLLDEPMGALDkklrTEMQLELVDILEKVGVTCLMVTHD 204
Cdd:COG0488 448 LSPPNVLLLDEPTNHLD----IETLEALEEALDDFPGTVLLVSHD 488
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-229 |
2.49e-27 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 113.68 E-value: 2.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 18 KGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITalppylrPTNM------- 90
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD-------AGDIatrrrvg 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 91 -MFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLD 169
Cdd:NF033858 343 yMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILD 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 170 EPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTmASRIAIMSYGRIAQVGSP 229
Cdd:NF033858 423 EPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTP 481
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
15-234 |
3.36e-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: 112.20 E-value: 3.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFET--PDSGRIV-------------------- 72
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 73 --------LDGQDITALPP-------YLRPTNMMFQ-SYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEP 136
Cdd:TIGR03269 81 pcpvcggtLEPEEVDFWNLsdklrrrIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 137 YARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALD---KKLRTEMQLELVdilEKVGVTCLMVTHDQEEAMTMAS 213
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVHNALEEAV---KASGISMVLTSHWPEVIEDLSD 237
|
250 260
....*....|....*....|.
gi 2485516087 214 RIAIMSYGRIAQVGSPIDIYE 234
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVA 258
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
15-246 |
3.42e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 112.31 E-value: 3.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDitalppyLRPTNMM--- 91
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-------MRFASTTaal 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 -------FQSYALFPHMTVEQNIAMGlkqdKLPK-----NEITDRVAAMLKL----VKMEPYARRKpqQLSGGQQQRVAL 155
Cdd:PRK11288 78 aagvaiiYQELHLVPEMTVAENLYLG----QLPHkggivNRRLLNYEAREQLehlgVDIDPDTPLK--YLSIGQRQMVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 156 ARSLAKRPKLLLLDEPMGALDKKlRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRiaQVGSPIDIYES 235
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSAR-EIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGR--YVATFDDMAQV 228
|
250
....*....|.
gi 2485516087 236 PNSRMTAEFIG 246
Cdd:PRK11288 229 DRDQLVQAMVG 239
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
4-236 |
3.60e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 109.81 E-value: 3.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 4 TNNTSAQAEVLLSIKGISKSF-----DSTlAVDDVSLDIHKGEIFALLGGSGSGKS----TLLRMLAGfetpdSGRI--- 71
Cdd:PRK09473 2 VPLAQQQADALLDVKDLRVTFstpdgDVT-AVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-----NGRIggs 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 72 -VLDGQDITALPPY----LRP--TNMMFQS--YALFPHMTVEQNIAMGLKQDK-LPKNEITDRVAAMLKLVKMePYARRK 141
Cdd:PRK09473 76 aTFNGREILNLPEKelnkLRAeqISMIFQDpmTSLNPYMRVGEQLMEVLMLHKgMSKAEAFEESVRMLDAVKM-PEARKR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 142 ----PQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAI 217
Cdd:PRK09473 155 mkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLV 234
|
250
....*....|....*....
gi 2485516087 218 MSYGRIAQVGSPIDIYESP 236
Cdd:PRK09473 235 MYAGRTMEYGNARDVFYQP 253
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-223 |
6.55e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 106.65 E-value: 6.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 13 VLLSIKGISK-SFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGqditaLPPYLRPTN-- 89
Cdd:cd03267 19 LIGSLKSLFKrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVPWKRRKKfl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 -----MMFQSYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPK 164
Cdd:cd03267 94 rrigvVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516087 165 LLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
33-248 |
6.96e-27 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 106.85 E-value: 6.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 33 VSLDIHKGEIFALLGGSGSGKSTLLRMLAGFeTPDSGRIVLDGQDITALPP--------YLRPtnmmfQSYALFPhMTVE 104
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAaelarhraYLSQ-----QQSPPFA-MPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 105 QNIAMGLkQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAK-------RPKLLLLDEPMGALDk 177
Cdd:COG4138 88 QYLALHQ-PAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 178 klrTEMQLELVDILEKV---GVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIyespnsrMTAEFIGSV 248
Cdd:COG4138 166 ---VAQQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV-------MTPENLSEV 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
10-232 |
8.52e-27 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 111.35 E-value: 8.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 10 QAEVLLSIKGISKSF--DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDIT--ALPPYL 85
Cdd:TIGR02203 326 RARGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdyTLASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 86 RPTNMMFQSYALFPHmTVEQNIAMGlKQDKLPKNEITDRVAA--MLKLVKMEPYARRKP-----QQLSGGQQQRVALARS 158
Cdd:TIGR02203 406 RQVALVSQDVVLFND-TIANNIAYG-RTEQADRAEIERALAAayAQDFVDKLPLGLDTPigengVLLSGGQRQRLAIARA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 159 LAKRPKLLLLDEPMGALDkklrTEMQLELVDILEKV--GVTCLMVTHdQEEAMTMASRIAIMSYGRIAQVGSPIDI 232
Cdd:TIGR02203 484 LLKDAPILILDEATSALD----NESERLVQAALERLmqGRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-229 |
9.14e-27 |
|
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: 106.16 E-value: 9.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 17 IKGISKSFDST-LAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPY-LRptNMM--- 91
Cdd:cd03254 5 FENVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKsLR--SMIgvv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 FQSYALFPHmTVEQNIAMGlkqdklpKNEITD-RVAAMLKLVKMEPYARRKP-----------QQLSGGQQQRVALARSL 159
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLG-------RPNATDeEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 160 AKRPKLLLLDEPMGALDKKLRTEMQLELVDILEkvGVTCLMVTHdQEEAMTMASRIAIMSYGRIAQVGSP 229
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTH 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
29-237 |
1.57e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 107.17 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP--YLRP----TNMMFQsyalFPHM- 101
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkYIRPvrkrIGMVFQ----FPESq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 102 ----TVEQNIAMGLKQDKLPKNEITDRVAAMLklvkME-PYAR----RKPQQLSGGQQQRVALARSLAKRPKLLLLDEPM 172
Cdd:PRK13646 98 lfedTVEREIIFGPKNFKMNLDEVKNYAHRLL----MDlGFSRdvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485516087 173 GALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPN 237
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
32-227 |
5.01e-26 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 103.89 E-value: 5.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 32 DVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPD---SGRIVLDGQditALPPYLRPTNMMF--QSYALFPHMTVEQN 106
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQ---PRKPDQFQKCVAYvrQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 107 I---AMGLKQDKLPKNEITDRVAAM-LKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTE 182
Cdd:cd03234 102 LtytAILRLPRKSSDAIRKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2485516087 183 MQLELVDILEKvGVTCLMVTHD-QEEAMTMASRIAIMSYGRIAQVG 227
Cdd:cd03234 182 LVSTLSQLARR-NRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-229 |
1.09e-25 |
|
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: 102.22 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFE--TPDSGRIVLDGQDITALPPYLRPTN--- 89
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 MMFQSYALFPhmtveqniamGlkqdklpkneitdrvaamlklVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLD 169
Cdd:cd03217 81 LAFQYPPEIP----------G---------------------VKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485516087 170 EPMGALDKKlRTEMQLELVDILEKVGVTCLMVTHDQEEAMTM-ASRIAIMSYGRIAQVGSP 229
Cdd:cd03217 130 EPDSGLDID-ALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-223 |
2.03e-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: 101.24 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFD--STLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPT-NMM 91
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLiSVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 FQSYALFpHMTVEQNIAmglkqdklpkneitdrvaamlklvkmepyarrkpQQLSGGQQQRVALARSLAKRPKLLLLDEP 171
Cdd:cd03247 81 NQRPYLF-DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 172 MGALDKKlrTEMQ-LELV-DILEkvGVTCLMVTHdQEEAMTMASRIAIMSYGRI 223
Cdd:cd03247 126 TVGLDPI--TERQlLSLIfEVLK--DKTLIWITH-HLTGIEHMDKILFLENGKI 174
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
27-223 |
2.35e-25 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 102.16 E-value: 2.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 27 TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP-PYL-RPTNMMFQSYALFPHmTVE 104
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEhKYLhSKVSLVGQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 105 QNIAMGLKQDKLPK-NEITDRVAAMLKLVKME--PY--ARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKL 179
Cdd:cd03248 106 DNIAYGLQSCSFECvKEAAQKAHAHSFISELAsgYDteVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2485516087 180 RTEMQLELVDILEKvgVTCLMVTHdQEEAMTMASRIAIMSYGRI 223
Cdd:cd03248 186 EQQVQQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-249 |
2.85e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 103.25 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 20 ISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRML-------AGFETpdSGRIVLDGQDI---TALPPYLRPTN 89
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRY--SGDVLLGGRSIfnyRDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 MMFQSYALFPhMTVEQNIAMGLKQDKL-PKNEITDRVAAMLKLVKMEPYARRK----PQQLSGGQQQRVALARSLAKRPK 164
Cdd:PRK14271 105 MLFQRPNPFP-MSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 165 LLLLDEPMGALDKKLRTEMQLELVDILEKvgVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMTAEF 244
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARY 261
|
....*
gi 2485516087 245 IGSVN 249
Cdd:PRK14271 262 VAGLS 266
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
11-221 |
3.38e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 106.41 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 11 AEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTN- 89
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 --MMFQSYALFPHMTVEQNIAMGlkqdKLPK-----------NEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALA 156
Cdd:PRK09700 82 igIIYQELSVIDELTVLENLYIG----RHLTkkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485516087 157 RSLAKRPKLLLLDEPMGALDKKlRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYG 221
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNK-EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
31-228 |
4.70e-25 |
|
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: 106.44 E-value: 4.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 31 DDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP-YLR------PtnmmfQSYALFpHMTV 103
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQaSLRaaigivP-----QDTVLF-NDTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 104 EQNIAMGlkqdklpKNEITDR-VAAMLKLVKMEPYARRKPQQ-----------LSGGQQQRVALARSLAKRPKLLLLDEP 171
Cdd:COG5265 449 AYNIAYG-------RPDASEEeVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEA 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 172 MGALDKKLRTEMQLELVDILEkvGVTCLMVTH------DqeeamtmASRIAIMSYGRIAQVGS 228
Cdd:COG5265 522 TSALDSRTERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGRIVERGT 575
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
30-232 |
1.73e-24 |
|
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: 104.74 E-value: 1.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 30 VDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITAL-PPYLRPT-NMMFQSYALFPHmTVEQNI 107
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWdRETFGKHiGYLPQDVELFPG-TVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 108 AmglkqdKLPKNEITDRVAAMLKLVKMEPYARRKPQ-----------QLSGGQQQRVALARSLAKRPKLLLLDEPMGALD 176
Cdd:TIGR01842 413 A------RFGENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 177 KKLRTEMQLELVDiLEKVGVTCLMVTHdQEEAMTMASRIAIMSYGRIAQVGSPIDI 232
Cdd:TIGR01842 487 EEGEQALANAIKA-LKARGITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
15-206 |
1.91e-24 |
|
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: 97.52 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGrIVLDGQDITalPPYLrptnmmfqs 94
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-IVTWGSTVK--IGYF--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 yalfphmtveqniamglkqdklpkneitdrvaamlklvkmepyarrkpQQLSGGQQQRVALARSLAKRPKLLLLDEPMGA 174
Cdd:cd03221 69 ------------------------------------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190
....*....|....*....|....*....|..
gi 2485516087 175 LDkklrTEMQLELVDILEKVGVTCLMVTHDQE 206
Cdd:cd03221 101 LD----LESIEALEEALKEYPGTVILVSHDRY 128
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
15-229 |
2.08e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.14 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFE--TPDSGRIVLDGQDITALPPYLRPTN--- 89
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERARAgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 MMFQSYALFPHMTVEQ--NIAMG-LKQDKLPKNEITDRVAAMLKLVKMEP-YARRkpqQL----SGGQQQRVALARSLAK 161
Cdd:COG0396 81 LAFQYPVEIPGVSVSNflRTALNaRRGEELSAREFLKLLKEKMKELGLDEdFLDR---YVnegfSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 162 RPKLLLLDEPMGALD-----------KKLRTEmqlelvdilekvGVTCLMVTHDQE--EAMTmASRIAIMSYGRIAQVGS 228
Cdd:COG0396 158 EPKLAILDETDSGLDidalrivaegvNKLRSP------------DRGILIITHYQRilDYIK-PDFVHVLVDGRIVKSGG 224
|
.
gi 2485516087 229 P 229
Cdd:COG0396 225 K 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
25-236 |
2.57e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 100.25 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 25 DSTLAVDDV-------------SLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITAL--PPYLRPTN 89
Cdd:PRK10575 9 DTTFALRNVsfrvpgrtllhplSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWssKAFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 MMFQSYALFPHMTVEQNIAMGLK--QDKLPKNEITDR--VAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKL 165
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVAIGRYpwHGALGRFGAADRekVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485516087 166 LLLDEPMGALDKKLRTEMqLELVDILEKV-GVTCLMVTHDqeeaMTMASR-----IAIMSYGRIAQvGSPIDIYESP 236
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDV-LALVHRLSQErGLTVIAVLHD----INMAARycdylVALRGGEMIAQ-GTPAELMRGE 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-230 |
2.94e-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: 104.71 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 17 IKGISKSFDST--LAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDI-TALPPYLRPTNMMFQ 93
Cdd:TIGR01257 931 VKNLVKIFEPSgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMG 173
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516087 174 ALDKKLRTEMQlelvDILEKV--GVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPI 230
Cdd:TIGR01257 1091 GVDPYSRRSIW----DLLLKYrsGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPL 1145
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-228 |
4.83e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.39 E-value: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 23 SFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFeTPDSGRIVLDGQDITALPP--YLRPTNMMFQSYALFpH 100
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPesWRKHLSWVGQNPQLP-H 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 101 MTVEQNIAMGlkqdklpKNEITD-RVAAMLKLVKMEPYARRKPQ-----------QLSGGQQQRVALARSLAKRPKLLLL 168
Cdd:PRK11174 437 GTLRDNVLLG-------NPDASDeQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 169 DEPMGALDKK--------LRTEMQlelvdilekvGVTCLMVTHdQEEAMTMASRIAIMSYGRIAQVGS 228
Cdd:PRK11174 510 DEPTASLDAHseqlvmqaLNAASR----------RQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGD 566
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-222 |
4.96e-24 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 102.95 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAG------FEtpdsGRIVLDGQ-----DItalp 82
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphgsYE----GEILFDGEvcrfkDI---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 83 pylRPTN-----MMFQSYALFPHMTVEQNIAMGLKQDK---LPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVA 154
Cdd:NF040905 73 ---RDSEalgivIIHQELALIPYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485516087 155 LARSLAKRPKLLLLDEPMGALD----KKLrtemqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGR 222
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALNeedsAAL-----LDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
32-225 |
5.31e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 103.21 E-value: 5.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 32 DVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP---------YLrPTNMmfQSYALFPHMT 102
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlarglvYL-PEDR--QSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 103 VEQNIA------MGLKQDKLPKNEITDRVAAML--KLVKMEPYARRkpqqLSGGQQQRVALARSLAKRPKLLLLDEPMGA 174
Cdd:PRK15439 358 LAWNVCalthnrRGFWIKPARENAVLERYRRALniKFNHAEQAART----LSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2485516087 175 LDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQ 225
Cdd:PRK15439 434 VDVSARNDI-YQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISG 483
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
32-203 |
5.35e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 95.33 E-value: 5.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 32 DVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP-----YLRPTNmmfqsyALFPHMTVEQN 106
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeachYLGHRN------AMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 107 IAM--GLKQDKLPkneitdRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSL-AKRPkLLLLDEPMGALDKKlRTEM 183
Cdd:PRK13539 94 LEFwaAFLGGEEL------DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLvSNRP-IWILDEPTAALDAA-AVAL 165
|
170 180
....*....|....*....|
gi 2485516087 184 QLELVDILEKVGVTCLMVTH 203
Cdd:PRK13539 166 FAELIRAHLAQGGIVIAATH 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
31-178 |
6.69e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 94.87 E-value: 6.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 31 DDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP-YLRptNMMF---QSyALFPHMTVEQN 106
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeYHQ--DLLYlghQP-GIKTELTALEN 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 107 IAMGLKQDKLPKNEITDRVAAMLKLVKME--PyARrkpqQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKK 178
Cdd:PRK13538 95 LRFYQRLHGPGDDEALWEALAQVGLAGFEdvP-VR----QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
32-236 |
8.55e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.18 E-value: 8.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 32 DVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP-PYL-RPTNMMFQSYALFPHmTVEQNIAM 109
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhHYLhRQVALVGQEPVLFSG-SVRENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 110 GLkqDKLPKNEIT---------DRVAAMLKLVKMEpyARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDkklr 180
Cdd:TIGR00958 578 GL--TDTPDEEIMaaakaanahDFIMEFPNGYDTE--VGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD---- 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 181 TEMQLELVDILEKVGVTCLMVTHdQEEAMTMASRIAIMSYGRIAQVGSPIDIYESP 236
Cdd:TIGR00958 650 AECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
29-236 |
1.13e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 97.12 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKS-TLLRMLAGFETPdsGRIV-----LDGQDITALPPYLR------PTNMMFQS-- 94
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMaekleFNGQDLQRISEKERrnlvgaEVAMIFQDpm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 YALFPHMTVEQNIAMGLK-QDKLPKNEITDRVAAMLKLVKMEPYARR---KPQQLSGGQQQRVALARSLAKRPKLLLLDE 170
Cdd:PRK11022 100 TSLNPCYTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 171 PMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESP 236
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
15-225 |
2.29e-22 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 98.51 E-value: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSF-DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP--YLRPTNMM 91
Cdd:PRK10522 323 LELRNVTFAYqDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPedYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 FQSYALFPHMtveqniamgLKQDKLPKNEitDRVAAMLKLVKMEPYARRKPQ-----QLSGGQQQRVALARSLAKRPKLL 166
Cdd:PRK10522 403 FTDFHLFDQL---------LGPEGKPANP--ALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516087 167 LLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDqEEAMTMASRIAIMSYGRIAQ 225
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSE 529
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-247 |
2.40e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.24 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSF----DSTLAVDDVSLDIHKGEIFALLGGSGSGKS-TLLRMLAGFETPD----SGRIVLDGQDIT-ALPP 83
Cdd:PRK15134 5 LLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLhASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 84 YLRPTN-----MMFQS--YALFPHMTVEQNIA------MGLKQDKlPKNEITDrvaaMLKLVKMEPYARRK---PQQLSG 147
Cdd:PRK15134 85 TLRGVRgnkiaMIFQEpmVSLNPLHTLEKQLYevlslhRGMRREA-ARGEILN----CLDRVGIRQAAKRLtdyPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 148 GQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQN 239
|
250 260
....*....|....*....|
gi 2485516087 228 SPIDIYESPNSRMTAEFIGS 247
Cdd:PRK15134 240 RAATLFSAPTHPYTQKLLNS 259
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
15-241 |
2.48e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 94.77 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLaVDDVSLDIHKGEIFALLGGSGSGKS----TLLRMLAGFETPDSGRIVLDGQDITA--LPPYLRPT 88
Cdd:PRK10418 5 IELRNIALQAAQPL-VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPcaLRGRKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 89 NMMFQSYALFPHMTVEQNIAMGLKQDKLPKNEitDRVAAMLKLVKMEPYAR---RKPQQLSGGQQQRVALARSLAKRPKL 165
Cdd:PRK10418 84 IMQNPRSAFNPLHTMHTHARETCLALGKPADD--ATLTAALEAVGLENAARvlkLYPFEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 166 LLLDEPMGALDkklrTEMQLELVDILEKV----GVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYESPNSRMT 241
Cdd:PRK10418 162 IIADEPTTDLD----VVAQARILDLLESIvqkrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVT 237
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
14-204 |
2.56e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 94.41 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQ-DITALPP--YLRPTnm 90
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlRIGYVPQklYLDTT-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 91 mfqsyalFPhMTVEQniAMGLKqdklPKNEITDRVAAmLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDE 170
Cdd:PRK09544 82 -------LP-LTVNR--FLRLR----PGTKKEDILPA-LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 2485516087 171 PMGALDkklrTEMQLELVDILEKV----GVTCLMVTHD 204
Cdd:PRK09544 147 PTQGVD----VNGQVALYDLIDQLrrelDCAVLMVSHD 180
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-236 |
3.01e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 96.13 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDS----TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFeTPDSGRI-----VLDGQDITALPPY 84
Cdd:COG4170 3 LLDIRNLTIEIDTpqgrVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVtadrfRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 85 LR------PTNMMFQ--SYALFPHMTVEQNIAMGLKQDKLP------KNEITDRVAAMLKLVK-------MEPYarrkPQ 143
Cdd:COG4170 82 ERrkiigrEIAMIFQepSSCLDPSAKIGDQLIEAIPSWTFKgkwwqrFKWRKKRAIELLHRVGikdhkdiMNSY----PH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 144 QLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKlrTEMQ-LELVDILEKV-GVTCLMVTHDQEEAMTMASRIAIMSYG 221
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMEST--TQAQiFRLLARLNQLqGTSILLISHDLESISQWADTITVLYCG 235
|
250
....*....|....*
gi 2485516087 222 RIAQVGSPIDIYESP 236
Cdd:COG4170 236 QTVESGPTEQILKSP 250
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
25-229 |
3.07e-22 |
|
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: 93.71 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 25 DSTLAVDDVSLDIHKGEIFALLGGSGSGKST----LLRMLagfeTPDSGRIVLDGQDITALPP-YLRpTNMMF--QSYAL 97
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLhDLR-SRISIipQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 98 FPHmTVEQNIAmglkqdklPKNEITD-RVAAMLKLVKMEPYARRKP-----------QQLSGGQQQRVALARSLAKRPKL 165
Cdd:cd03244 90 FSG-TIRSNLD--------PFGEYSDeELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485516087 166 LLLDEPMGALD--------KKLRTEMqlelvdilekVGVTCLMVTHdQEEAMTMASRIAIMSYGRIAQVGSP 229
Cdd:cd03244 161 LVLDEATASVDpetdaliqKTIREAF----------KDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
30-203 |
3.12e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.96 E-value: 3.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 30 VDDVSLDIHKGEifALL--GGSGSGKSTLLRMLAGFETPDSGRIVL-DGQDITALP--PY-----LRptnmmfqSYALFP 99
Cdd:COG4178 379 LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPqrPYlplgtLR-------EALLYP 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 100 HmtveqniamglkqdklPKNEITD-RVAAMLKLVKMEPYA------RRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPM 172
Cdd:COG4178 450 A----------------TAEAFSDaELREALEAVGLGHLAerldeeADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190
....*....|....*....|....*....|..
gi 2485516087 173 GALDKKLRTEM-QLeLVDILEkvGVTCLMVTH 203
Cdd:COG4178 514 SALDEENEAALyQL-LREELP--GTTVISVGH 542
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-206 |
3.24e-22 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 93.48 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 6 NTSAQAEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFE--TPDSGRIVLDGQDITalpp 83
Cdd:COG2401 22 DLSERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 84 ylrptnmmfqsyalfphmtVEQNIAmglkqDKLPKNEITDRVAAMLKLVKM-EPYA-RRKPQQLSGGQQQRVALARSLAK 161
Cdd:COG2401 98 -------------------REASLI-----DAIGRKGDFKDAVELLNAVGLsDAVLwLRRFKELSTGQKFRFRLALLLAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2485516087 162 RPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQE 206
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-224 |
3.76e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 97.67 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 9 AQAEVLLSIKGISKSfdsTLAvDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP----- 83
Cdd:PRK11288 252 PLGEVRLRLDGLKGP---GLR-EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrdair 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 84 ---YLRPTNMMFQsyALFPHMTVEQNIAMGLKQDKLP---------KNEITDRVAAMLKlVKMePYARRKPQQLSGGQQQ 151
Cdd:PRK11288 328 agiMLCPEDRKAE--GIIPVHSVADNINISARRHHLRagclinnrwEAENADRFIRSLN-IKT-PSREQLIMNLSGGNQQ 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 152 RVALARSLAKRPKLLLLDEPMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIA 224
Cdd:PRK11288 404 KAILGRWLSEDMKVILLDEPTRGIDVGAKHEI-YNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
31-258 |
6.32e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.90 E-value: 6.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 31 DDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDIT--ALPPYLRPTNMMFQSYALFPHMTVEQNIA 108
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyASKEVARRIGLLAQNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 109 MGlKQDKLP-----KNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDkklrTEM 183
Cdd:PRK10253 104 RG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD----ISH 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516087 184 QLELVDILEKV----GVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIyespnsrMTAEFIGSVNIFEANILED 258
Cdd:PRK10253 179 QIDLLELLSELnrekGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI-------VTAELIERIYGLRCMIIDD 250
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-265 |
2.32e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 93.23 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDG-----------QDITA-----------LPPYlr 86
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrrkefaRRIGVvfgqrsqlwwdLPAI-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 87 ptnmmfQSYALFPHMTveqniamglkqdKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLL 166
Cdd:COG4586 115 ------DSFRLLKAIY------------RIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 167 LLDEPMGALD----KKLRTemqlELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIYE--SPNSRM 240
Cdd:COG4586 177 FLDEPTIGLDvvskEAIRE----FLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKErfGPYKTI 252
|
250 260
....*....|....*....|....*....
gi 2485516087 241 TAEFIGSVNIFE----ANILEDNSDSLSL 265
Cdd:COG4586 253 VLELAEPVPPLElprgGEVIEREGNRVRL 281
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-203 |
2.63e-21 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 90.50 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPyLRPTNMMFQS 94
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 Y--ALFPHMTVEQNI----AMGLKQDKLPKNeitdrvaaMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLL 168
Cdd:TIGR01189 80 HlpGLKPELSALENLhfwaAIHGGAQRTIED--------ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....*
gi 2485516087 169 DEPMGALDKKLRTEMQLELVDILEKVGVTcLMVTH 203
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGGIV-LLTTH 185
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-204 |
2.83e-21 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 91.70 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 36 DIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTnmmfqsyalFPhMTVEQ---NIAMGLK 112
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKAD---------YE-GTVRDllsSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 113 QDKLPKNEItdrvaamLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILE 192
Cdd:cd03237 91 THPYFKTEI-------AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170
....*....|..
gi 2485516087 193 KVGVTCLMVTHD 204
Cdd:cd03237 164 NNEKTAFVVEHD 175
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-204 |
4.69e-21 |
|
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: 94.62 E-value: 4.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 12 EVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLdGQdiTALPPYLRptnmm 91
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GE--TVKLAYVD----- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 fQSY-ALFPHMTVEQNIAMGLKQDKLPKNEITDRV---------AAMLKLVKmepyarrkpqQLSGGQQQRVALARSLAK 161
Cdd:TIGR03719 392 -QSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAyvgrfnfkgSDQQKKVG----------QLSGGERNRVHLAKTLKS 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2485516087 162 RPKLLLLDEPMGALD-KKLRTemqLElvDILEKVGVTCLMVTHD 204
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDvETLRA---LE--EALLNFAGCAVVISHD 499
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-227 |
4.93e-21 |
|
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: 89.53 E-value: 4.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLaVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAG--FETPDSGRIVLDGQDITALPPYLRpTNMMF 92
Cdd:cd03213 11 VTVKSSPSKSGKQL-LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKI-IGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 93 QSYALFPHMTVEQNIamglkqdklpkneitdRVAAMLKlvkmepyarrkpqQLSGGQQQRVALARSLAKRPKLLLLDEPM 172
Cdd:cd03213 89 QDDILHPTLTVRETL----------------MFAAKLR-------------GLSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2485516087 173 GALDKklRTEMQ-LELVDILEKVGVTCLMVTHD-QEEAMTMASRIAIMSYGRIAQVG 227
Cdd:cd03213 140 SGLDS--SSALQvMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
33-255 |
6.24e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 90.76 E-value: 6.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 33 VSLDIHKGEIFALLGGSGSGKSTLLRMLAGFeTPDSGRIVLDGQDITALPP--------YL----RPTNMM--FQSYALF 98
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAaelarhraYLsqqqTPPFAMpvFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 99 -PHMTVEQNIAMGLkqdklpkneitDRVAAMLKLVKMEPyarRKPQQLSGGQQQRVALA-------RSLAKRPKLLLLDE 170
Cdd:PRK03695 94 qPDKTRTEAVASAL-----------NEVAEALGLDDKLG---RSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 171 PMGALDKKLRTEMQLeLVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIyespnsrMTAEFIGSVni 250
Cdd:PRK03695 160 PMNSLDVAQQAALDR-LLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV-------LTPENLAQV-- 229
|
....*
gi 2485516087 251 FEANI 255
Cdd:PRK03695 230 FGVNF 234
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-228 |
1.00e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 93.49 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 20 ISKSFD-STLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDIT--ALPPYLRPTNMMFQSYA 96
Cdd:PRK13657 340 VSFSYDnSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRtvTRASLRRNIAVVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 97 LFpHMTVEQNIAMGlKQDKLPKN--EITDRVAA----MLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDE 170
Cdd:PRK13657 420 LF-NRSIEDNIRVG-RPDATDEEmrAAAERAQAhdfiERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516087 171 PMGALDkkLRTEMQLEL-VDILEKvGVTCLMVTHdQEEAMTMASRIAIMSYGRIAQVGS 228
Cdd:PRK13657 498 ATSALD--VETEAKVKAaLDELMK-GRTTFIIAH-RLSTVRNADRILVFDNGRVVESGS 552
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
33-233 |
1.67e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.07 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 33 VSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDIT----ALPPYLRPTNMMFQ--SYALFpHMTVEQN 106
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQdpEQQIF-YTDIDSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 107 IAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMqLE 186
Cdd:PRK13638 99 IAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM-IA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2485516087 187 LVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDIY 233
Cdd:PRK13638 178 IIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
7-204 |
3.61e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 91.79 E-value: 3.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 7 TSAQAEVLLSIKGISKSFDS-TLAVDdvSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDgQDITALPPYL 85
Cdd:PRK13409 333 DESERETLVEYPDLTKKLGDfSLEVE--GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKPQYI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 86 RPTnmmfqsyalfPHMTVEQNIAMGLKQ--DKLPKNEITDRvaamLKLVK-MEpyarRKPQQLSGGQQQRVALARSLAKR 162
Cdd:PRK13409 410 KPD----------YDGTVEDLLRSITDDlgSSYYKSEIIKP----LQLERlLD----KNVKDLSGGELQRVAIAACLSRD 471
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2485516087 163 PKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHD 204
Cdd:PRK13409 472 ADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD 513
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-204 |
6.06e-20 |
|
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: 91.38 E-value: 6.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 8 SAQAEVLLSIKGISKSFDS-TLAVDdvSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDgQDITALPPYLR 86
Cdd:COG1245 335 EKEEETLVEYPDLTKSYGGfSLEVE--GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISYKPQYIS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 87 PTNmmfqsyalfpHMTVEQNIAMGLKqDKLP----KNEITDRvaamLKLVK-MEPYARrkpqQLSGGQQQRVALARSLAK 161
Cdd:COG1245 412 PDY----------DGTVEEFLRSANT-DDFGssyyKTEIIKP----LGLEKlLDKNVK----DLSGGELQRVAIAACLSR 472
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2485516087 162 RPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHD 204
Cdd:COG1245 473 DADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD 515
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-223 |
6.51e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 90.83 E-value: 6.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 9 AQAEVLLSIKGISKSfdstlAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPP----- 83
Cdd:PRK10762 252 APGEVRLKVDNLSGP-----GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqdgla 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 84 ----YL---RPTNmmfqsyALFPHMTVEQNiaMGL--------KQDKLPKNEITDRVAAMLKLVKMEPYARRKP-QQLSG 147
Cdd:PRK10762 327 ngivYIsedRKRD------GLVLGMSVKEN--MSLtalryfsrAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAiGLLSG 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 148 GQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:PRK10762 399 GNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEI-YQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-248 |
7.37e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.07 E-value: 7.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 11 AEVLLSIKGISKSFD----STLAVDDVSLDIHKGEIFALLGGSGSGKS----TLLRML--AGFETpDSGRIVLD------ 74
Cdd:PRK10261 9 ARDVLAVENLNIAFMqeqqKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLV-QCDKMLLRrrsrqv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 75 ---GQDITALPPYLRPTN--MMFQS--YALFPHMTVEQNIAMGLK-QDKLPKNEITDRVAAMLKLVKM---EPYARRKPQ 143
Cdd:PRK10261 88 ielSEQSAAQMRHVRGADmaMIFQEpmTSLNPVFTVGEQIAESIRlHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 144 QLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMqLELVDILEK---VGVtcLMVTHDQEEAMTMASRIAIMSY 220
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQI-LQLIKVLQKemsMGV--IFITHDMGVVAEIADRVLVMYQ 244
|
250 260
....*....|....*....|....*...
gi 2485516087 221 GRIAQVGSPIDIYESPNSRMTAEFIGSV 248
Cdd:PRK10261 245 GEAVETGSVEQIFHAPQHPYTRALLAAV 272
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
30-232 |
8.54e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 87.96 E-value: 8.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 30 VDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGfETPDS---------GRIVLDGQDITALPPY----LRPTnMMFQSYA 96
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPrlarLRAV-LPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 97 LFPhMTVEQNIAMGLKQDKLPKNEITDR----VAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAK---------RP 163
Cdd:PRK13547 95 AFA-FSAREIVLLGRYPHARRAGALTHRdgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 164 KLLLLDEPMGALDkklrTEMQLELVDILEKVG----VTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDI 232
Cdd:PRK13547 174 RYLLLDEPTAALD----LAHQHRLLDTVRRLArdwnLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
30-226 |
3.91e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.69 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 30 VDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRPTNMMF------QSYALFPHMTV 103
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAyitesrRDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 104 EQNIA-------------MGLKQDKLPKNEITDRVAAM-LKLVKMEpyarRKPQQLSGGQQQRVALARSLAKRPKLLLLD 169
Cdd:PRK09700 359 AQNMAisrslkdggykgaMGLFHEVDEQRTAENQRELLaLKCHSVN----QNITELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2485516087 170 EPMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQV 226
Cdd:PRK09700 435 EPTRGIDVGAKAEI-YKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
29-228 |
4.07e-19 |
|
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: 89.03 E-value: 4.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQ-----DITALPPYLrptNMMFQSYALFPHmTV 103
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkdiDRHTLRQFI---NYLPQEPYIFSG-SI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 104 EQNIAMGLKQdklpkNEITDRVAAMLKLVKMEPYARRKPQ-----------QLSGGQQQRVALARSLAKRPKLLLLDEPM 172
Cdd:TIGR01193 565 LENLLLGAKE-----NVSQDEIWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 173 GALDKKLRTEMQLELVDILEKvgvTCLMVTHDQEEAmTMASRIAIMSYGRIAQVGS 228
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGS 691
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-222 |
5.49e-19 |
|
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: 84.06 E-value: 5.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 21 SKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQD-ITALPPYLRPTnmmfqsyalfp 99
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIaYVSQEPWIQNG----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 100 hmTVEQNIAMGLKQDKlpkneitDRVAAMLKLVKMEPYARRKPQQ-----------LSGGQQQRVALARSLAKRPKLLLL 168
Cdd:cd03250 81 --TIRENILFGKPFDE-------ERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485516087 169 DEPMGALDKKLRTemqlelvDILEKV-------GVTCLMVTHdQEEAMTMASRIAIMSYGR 222
Cdd:cd03250 152 DDPLSAVDAHVGR-------HIFENCilglllnNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
32-229 |
6.60e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.18 E-value: 6.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 32 DVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPD---SGRIVLDGQDITAlpPYLRPTNMMFQSYALF-PHMTVEQNI 107
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDA--KEMRAISAYVQQDDLFiPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 108 ---AMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQ------LSGGQQQRVALARSLAKRPKLLLLDEPMGALDkk 178
Cdd:TIGR00955 121 mfqAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD-- 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2485516087 179 lrTEMQLELVDILEKV---GVTCLMVTHD-QEEAMTMASRIAIMSYGRIAQVGSP 229
Cdd:TIGR00955 199 --SFMAYSVVQVLKGLaqkGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSP 251
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
27-228 |
6.97e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.15 E-value: 6.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 27 TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDIT--ALPPYLRPTNMMFQSYALFpHMTVE 104
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLRNQVALVSQNVHLF-NDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 105 QNIAMGlKQDKLPKNEITD--RVA-AMLKLVKME----PYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDK 177
Cdd:PRK11176 435 NNIAYA-RTEQYSREQIEEaaRMAyAMDFINKMDngldTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2485516087 178 KLRTEMQLELvDILEKvGVTCLMVTHdQEEAMTMASRIAIMSYGRIAQVGS 228
Cdd:PRK11176 514 ESERAIQAAL-DELQK-NRTSLVIAH-RLSTIEKADEILVVEDGEIVERGT 561
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-175 |
3.23e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 12 EVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPylRPT--- 88
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGP--KSSqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 89 --NMMFQSYALFPHMTVEQNIAMGlkqdklpkNEITDRVA------------AMLKLVKMEPYARRKPQQLSGGQQQRVA 154
Cdd:PRK10762 80 giGIIHQELNLIPQLTIAENIFLG--------REFVNRFGridwkkmyaeadKLLARLNLRFSSDKLVGELSIGEQQMVE 151
|
170 180
....*....|....*....|.
gi 2485516087 155 LARSLAKRPKLLLLDEPMGAL 175
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDAL 172
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
25-203 |
3.77e-18 |
|
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: 80.66 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 25 DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVL-DGQDITALP--PYLRPTNMMFQSyaLFPHM 101
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLPqrPYLPLGTLREQL--IYPWD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 102 TVeqniamglkqdklpkneitdrvaamlklvkmepyarrkpqqLSGGQQQRVALARSLAKRPKLLLLDEPMGALDkklrT 181
Cdd:cd03223 90 DV-----------------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD----E 124
|
170 180
....*....|....*....|..
gi 2485516087 182 EMQLELVDILEKVGVTCLMVTH 203
Cdd:cd03223 125 ESEDRLYQLLKELGITVISVGH 146
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
29-204 |
5.52e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.01 E-value: 5.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITA-----LPPYLRPTNMMFQSyalFPhMTV 103
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQalqknLVAYVPQSEEVDWS---FP-VLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 104 EQNIAMG----LKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKL 179
Cdd:PRK15056 98 EDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180
....*....|....*....|....*
gi 2485516087 180 RTEMqLELVDILEKVGVTCLMVTHD 204
Cdd:PRK15056 178 EARI-ISLLRELRDEGKTMLVSTHN 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
33-177 |
6.58e-18 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 81.00 E-value: 6.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 33 VSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLRpTNMMFQSYA--LFPHMTVEQNIAMg 110
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIA-RGLLYLGHApgIKTTLSVLENLRF- 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485516087 111 lkqdkLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDK 177
Cdd:cd03231 97 -----WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
18-176 |
7.63e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 84.79 E-value: 7.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 18 KGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLdGQdiTALPPYLRptnmmfQSY-A 96
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE--TVKLAYVD------QSRdA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 97 LFPHMTVEQNIAMGLKQDKLPKNEITDR--VAAM-------LKLVKmepyarrkpqQLSGGQQQRVALARSLAKRPKLLL 167
Cdd:PRK11819 399 LDPNKTVWEEISGGLDIIKVGNREIPSRayVGRFnfkggdqQKKVG----------VLSGGERNRLHLAKTLKQGGNVLL 468
|
....*....
gi 2485516087 168 LDEPMGALD 176
Cdd:PRK11819 469 LDEPTNDLD 477
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
15-229 |
1.62e-17 |
|
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: 80.15 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTL--AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP-PYLRptnmm 91
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPlEDLR----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 fQSYALFPHmtvEQNIAMGLKQDKL-PKNEITDR-VAAMLKLvkmepyaRRKPQQLSGGQQQRVALARSLAKRPKLLLLD 169
Cdd:cd03369 82 -SSLTIIPQ---DPTLFSGTIRSNLdPFDEYSDEeIYGALRV-------SEGGLNLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 170 EPMGALD--------KKLRTEMQlelvdilekvGVTCLMVTHdqeEAMTMA--SRIAIMSYGRIAQVGSP 229
Cdd:cd03369 151 EATASIDyatdaliqKTIREEFT----------NSTILTIAH---RLRTIIdyDKILVMDAGEVKEYDHP 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-228 |
1.80e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 84.29 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 26 STLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDI-TALPPYLRPTNMMFQSYALFPHMTVE 104
Cdd:TIGR01257 1951 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQNMGYCPQFDAIDDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 105 QNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQ 184
Cdd:TIGR01257 2031 EHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 2110
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2485516087 185 LELVDILEKvGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGS 228
Cdd:TIGR01257 2111 NTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
33-170 |
3.98e-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: 82.54 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 33 VSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITA--LPPYlRptNMM---FQSYALFPHMtveqni 107
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAdnREAY-R--QLFsavFSDFHLFDRL------ 421
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 108 aMGLKQDKLPkneitDRVAAMLKLVKMEpyarRKPQ---------QLSGGQQQRVALARSLA-KRPkLLLLDE 170
Cdd:COG4615 422 -LGLDGEADP-----ARARELLERLELD----HKVSvedgrfsttDLSQGQRKRLALLVALLeDRP-ILVFDE 483
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-204 |
5.25e-17 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 82.29 E-value: 5.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 11 AEVLLSIKGISKSFDSTLAV-DDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVL-DGQDITALP--PYLR 86
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKVGYLPqePQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 87 PTnmmfqsyalfphMTVEQNIAMGL--KQDKLPK-NEITDRVAA----MLKLVK------------------------ME 135
Cdd:TIGR03719 81 PT------------KTVRENVEEGVaeIKDALDRfNEISAKYAEpdadFDKLAAeqaelqeiidaadawdldsqleiaMD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 136 pyARRKP------QQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKklrtemqlELVDILEKV-----GvTCLMVTHD 204
Cdd:TIGR03719 149 --ALRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA--------ESVAWLERHlqeypG-TVVAVTHD 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-204 |
1.41e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 80.93 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 11 AEVLLSIKGISKSFDSTLAV-DDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVL-DGQDITALP--PYLR 86
Cdd:PRK11819 3 AQYIYTMNRVSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKVGYLPqePQLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 87 PTNmmfqsyalfphmTVEQNIAMGL--KQDKLPK-NEITDRVAA----MLKLVK------------------------ME 135
Cdd:PRK11819 83 PEK------------TVRENVEEGVaeVKAALDRfNEIYAAYAEpdadFDALAAeqgelqeiidaadawdldsqleiaMD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 136 pyARRKP------QQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKklrtemqlELVDILEKV-----GvTCLMVTHD 204
Cdd:PRK11819 151 --ALRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--------ESVAWLEQFlhdypG-TVVAVTHD 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-223 |
3.74e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.48 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 30 VDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAG-FETPDSGRIVLDGQ--DITALPPYLRPTNMMF----QSYALFPHMT 102
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKpvDIRNPAQAIRAGIAMVpedrKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 103 VEQNIAMGLKQ--------DKLPKNEITDRVAAMLKLVKMEPYArrKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGA 174
Cdd:TIGR02633 356 VGKNITLSVLKsfcfkmriDAAAELQIIGSAIQRLKVKTASPFL--PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2485516087 175 LDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:TIGR02633 434 VDVGAKYEI-YKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-222 |
3.85e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 79.39 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 17 IKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDI---TALPPYLRPTNMMFQ 93
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SYALFPHMTVEQNIAMG--------LKQDKLPKNeiTDRVAAMLKlVKMEPyaRRKPQQLSGGQQQRVALARSLAKRPKL 165
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGryptkgmfVDQDKMYRD--TKAIFDELD-IDIDP--RAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2485516087 166 LLLDEPMGALDKKlRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGR 222
Cdd:PRK10982 156 VIMDEPTSSLTEK-EVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
15-228 |
4.10e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 79.76 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSF-DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALppylrptnmmfq 93
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL------------ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 syalfPHMTVEQNIAMgLKQD------------KLPKNEITDRVAAMLKLVKMEPYARRKPQ-----------QLSGGQQ 150
Cdd:PRK10790 409 -----SHSVLRQGVAM-VQQDpvvladtflanvTLGRDISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQK 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 151 QRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKvgvTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGS 228
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-223 |
4.21e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.59 E-value: 4.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 30 VDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAG-FETPDSGRIVLDGQDIT------------ALPPYLRptnmmfQSYA 96
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKPVKirnpqqaiaqgiAMVPEDR------KRDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 97 LFPHMTVEQNIAMG-LKQ-------DKLPKNEITDRVAAMLKLVKMEPYARRKpqQLSGGQQQRVALARSLAKRPKLLLL 168
Cdd:PRK13549 352 IVPVMGVGKNITLAaLDRftggsriDDAAELKTILESIQRLKVKTASPELAIA--RLSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2485516087 169 DEPMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:PRK13549 430 DEPTRGIDVGAKYEI-YKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
14-203 |
8.31e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 75.37 E-value: 8.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITA-LPPYLRPTNMMF 92
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 93 QSYALFPHMTVEQNIAMGLKQDKlPKNEITDrvaaMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPM 172
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDIHFSP-GAVGITE----LCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|.
gi 2485516087 173 GALDkKLRTEMQLELVDILEKVGVTCLMVTH 203
Cdd:PRK13540 156 VALD-ELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
40-227 |
1.87e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 77.61 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 40 GEIFALLGGSGSGKSTLLRMLAGFETPDS--GRIVLDGQDITAlpPYLRPTNMMFQSYALFPHMTVEQNIAMG------- 110
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK--QILKRTGFVTQDDILYPHLTVRETLVFCsllrlpk 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 111 --LKQDKLpknEITDRVAAMLKLVKMEP--YARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLE 186
Cdd:PLN03211 172 slTKQEKI---LVAESVISELGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2485516087 187 LVDILEKvGVTCLMVTHD-QEEAMTMASRIAIMSYGRIAQVG 227
Cdd:PLN03211 249 LGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
291-370 |
2.30e-15 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.
Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 70.34 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 291 IALRPEKIYLttekpEGDSNWSCGTVDNIAYLGDITSYYVKLASGKRVQATMANVERRgeRPTWGDRVYVSWEASSPILL 370
Cdd:pfam08402 1 LAIRPEKIRL-----AAAANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHAR--PPAPGDRVGLGWDPEDAHVL 73
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
8-227 |
2.34e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 76.31 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 8 SAQAEVLLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLG--GSGSGKSTLLRMLAGfetPDSGRIVLDGQDITALPPYL 85
Cdd:NF000106 7 SNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGp*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 86 RPTNMMFQ--SYALFPHMTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRP 163
Cdd:NF000106 84 RRTIG*HRpvR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485516087 164 KLLLLDEPMGALDKKLRTEMQLELVDILEKvGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-215 |
3.19e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.91 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDgQDITAL-----PP----- 83
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVArlqqdPPrnveg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 84 ---------------YLRPTNMMFQSYALFPHmtvEQNIA-MGLKQDKLPKN---EITDRVAAMLKLVKMEPYArrKPQQ 144
Cdd:PRK11147 82 tvydfvaegieeqaeYLKRYHDISHLVETDPS---EKNLNeLAKLQEQLDHHnlwQLENRINEVLAQLGLDPDA--ALSS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485516087 145 LSGGQQQRVALARSLAKRPKLLLLDEPMGALDkklrtemqLELVDILEKV----GVTCLMVTHDQEEAMTMASRI 215
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD--------IETIEWLEGFlktfQGSIIFISHDRSFIRNMATRI 223
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
14-176 |
1.76e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 71.80 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPpylRPTNMMFQ 93
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD---RSRFMAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 94 SY--ALFPHMTVEQNIAM-----GLKQDKLPKNEITdrvaamlkLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLL 166
Cdd:PRK13543 88 GHlpGLKADLSTLENLHFlcglhGRRAKQMPGSALA--------IVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLW 159
|
170
....*....|
gi 2485516087 167 LLDEPMGALD 176
Cdd:PRK13543 160 LLDEPYANLD 169
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-206 |
4.63e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.45 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 25 DSTLaVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDgqdiTALP-PYlrptnmmFQSY--ALFPHM 101
Cdd:PRK11147 331 GKQL-VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLEvAY-------FDQHraELDPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 102 TVEQNIAMGlkqdklpKNEIT----DR-VAAMLKLVKMEPYARRKP-QQLSGGQQQRVALARSLAKRPKLLLLDEPMGAL 175
Cdd:PRK11147 399 TVMDNLAEG-------KQEVMvngrPRhVLGYLQDFLFHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
170 180 190
....*....|....*....|....*....|..
gi 2485516087 176 DkkLRTemqLELV-DILEKVGVTCLMVTHDQE 206
Cdd:PRK11147 472 D--VET---LELLeELLDSYQGTVLLVSHDRQ 498
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
27-176 |
9.98e-14 |
|
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: 73.02 E-value: 9.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 27 TLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQdITALP--PYLRPTnmmfqsyalfphmTVE 104
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISFSPqtSWIMPG-------------TIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 105 QNIAMGLKQDKLpkneitdRVAAMLKLVKMEPYARRKPQQ-----------LSGGQQQRVALARSLAKRPKLLLLDEPMG 173
Cdd:TIGR01271 505 DNIIFGLSYDEY-------RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
...
gi 2485516087 174 ALD 176
Cdd:TIGR01271 578 HLD 580
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
32-185 |
1.07e-13 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 70.66 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 32 DVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQdITALPpylrptnmmfQSYALFPHmTVEQNIAMGL 111
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSS----------QFSWIMPG-TIKENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 112 KQDKLpkneitdRVAAMLKLVKMEPYARRKPQQ-----------LSGGQQQRVALARSLAKRPKLLLLDEPMGALDkkLR 180
Cdd:cd03291 123 SYDEY-------RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD--VF 193
|
....*
gi 2485516087 181 TEMQL 185
Cdd:cd03291 194 TEKEI 198
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
14-228 |
1.46e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.67 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFetPD----SGRIVLDGQDITALPPYLRPTN 89
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAykilEGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 ---MMFQSYALFPHMTVEQ--NIAMGLKQDKLPKNEIT-----DRVAAMLKLVKMEPY--ARRKPQQLSGGQQQRVALAR 157
Cdd:CHL00131 85 gifLAFQYPIEIPGVSNADflRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPSflSRNVNEGFSGGEKKRNEILQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 158 SLAKRPKLLLLDEPMGALD-KKLRTEMqlELVDILEKVGVTCLMVTHDQE-EAMTMASRIAIMSYGRIAQVGS 228
Cdd:CHL00131 165 MALLDSELAILDETDSGLDiDALKIIA--EGINKLMTSENSIILITHYQRlLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
14-251 |
1.63e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 70.60 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDST----LAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFeTPDSGRIV-----LDGQDITALPPY 84
Cdd:PRK15093 3 LLDIRNLTIEFKTSdgwvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTadrmrFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 85 LR------PTNMMFQ--SYALFPHMTVEQNIAMGL-------------KQDKLPKNEITDRVAAMLKLVKMEPYarrkPQ 143
Cdd:PRK15093 82 ERrklvghNVSMIFQepQSCLDPSERVGRQLMQNIpgwtykgrwwqrfGWRKRRAIELLHRVGIKDHKDAMRSF----PY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 144 QLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
250 260
....*....|....*....|....*...
gi 2485516087 224 AQVGSPIDIYESPNSRMTAEFIGSVNIF 251
Cdd:PRK15093 238 VETAPSKELVTTPHHPYTQALIRAIPDF 265
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
16-171 |
3.78e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.92 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 16 SIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRI-VLDGqDI------TALPP---Yl 85
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGG-DMadarhrRAVCPriaY- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 86 rptnmMFQSYA--LFPHMTVEQNIAM-----GlkqdkLPKNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARS 158
Cdd:NF033858 81 -----MPQGLGknLYPTLSVFENLDFfgrlfG-----QDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCA 150
|
170
....*....|...
gi 2485516087 159 LAKRPKLLLLDEP 171
Cdd:NF033858 151 LIHDPDLLILDEP 163
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
43-203 |
4.24e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.83 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 43 FALLGGSGSGKSTLLrmlagFEtpDSGRIVLDGQDITALPpyLRPTNMMF----QSYALFpHMTVEQNIAMGLKQDKLPK 118
Cdd:PTZ00265 1258 FSLTKEGGSGEDSTV-----FK--NSGKILLDGVDICDYN--LKDLRNLFsivsQEPMLF-NMSIYENIKFGKEDATRED 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 119 NEITDRVAAMLKLVK---------MEPYARrkpqQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVD 189
Cdd:PTZ00265 1328 VKRACKFAAIDEFIEslpnkydtnVGPYGK----SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1403
|
170
....*....|....
gi 2485516087 190 ILEKVGVTCLMVTH 203
Cdd:PTZ00265 1404 IKDKADKTIITIAH 1417
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
39-217 |
1.08e-12 |
|
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: 65.09 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 39 KGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVldgqditalppYLRPTNMMFQSYALFPHMTVEQNIAMGlkqdklpk 118
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI-----------YIDGEDILEEVLDQLLLIIVGGKKASG-------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 119 neitdrvaamlklvkmepyarrkpqqlSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVD-----ILEK 193
Cdd:smart00382 62 ---------------------------SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKSE 114
|
170 180
....*....|....*....|....
gi 2485516087 194 VGVTCLMVTHDQEEAMTMASRIAI 217
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
29-227 |
2.00e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.20 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITA--LPPYLRPTNMMFQSYALFPHmTVEQN 106
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqLDSWRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 107 IAMGlKQDKLPKnEItDRVAamlKLVKMEPYARRKPQ-----------QLSGGQQQRVALARSLAKRPKLLLLDEPMGAL 175
Cdd:PRK10789 409 IALG-RPDATQQ-EI-EHVA---RLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2485516087 176 DKklRTEMQlelvdILEKV-----GVTCLMVTHdQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:PRK10789 483 DG--RTEHQ-----ILHNLrqwgeGRTVIISAH-RLSALTEASEILVMQHGHIAQRG 531
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-224 |
4.89e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 7 TSAQAEVLLSIKGISKSfdSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPyLR 86
Cdd:PRK10982 243 ENKPGEVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNA-NE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 87 PTNMMF-------QSYALFPHMTVEQN--IA--------MGLKQDKLPKNEITDRVAAMLklVKMePYARRKPQQLSGGQ 149
Cdd:PRK10982 320 AINHGFalvteerRSTGIYAYLDIGFNslISnirnyknkVGLLDNSRMKSDTQWVIDSMR--VKT-PGHRTQIGSLSGGN 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485516087 150 QQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIA 224
Cdd:PRK10982 397 QQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEI-YQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-205 |
5.83e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 67.12 E-value: 5.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLD-----GQDITALPPYLRPT 88
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkgiklGYFAQHQLEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 89 NMMFQSYALFPHMTVEQNI-----AMGLKQDKLpkNEITDRvaamlklvkmepyarrkpqqLSGGQQQRVALARSLAKRP 163
Cdd:PRK10636 392 ESPLQHLARLAPQELEQKLrdylgGFGFQGDKV--TEETRR--------------------FSGGEKARLVLALIVWQRP 449
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2485516087 164 KLLLLDEPMGALDKKLRTEMQLELVDILEKVGVtclmVTHDQ 205
Cdd:PRK10636 450 NLLLLDEPTNHLDLDMRQALTEALIDFEGALVV----VSHDR 487
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
15-215 |
7.45e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.45 E-value: 7.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLD--------GQDITAlppylr 86
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenanigyyAQDHAY------ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 87 ptnmMF-QSYALFPHMTveqniamglkQDKLPKNEITdRVAAML-KLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPK 164
Cdd:PRK15064 394 ----DFeNDLTLFDWMS----------QWRQEGDDEQ-AVRGTLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPN 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 165 LLLLDEPMGALDkklrteMQ-LE-LVDILEKVGVTCLMVTHDQEEAMTMASRI 215
Cdd:PRK15064 459 VLVMDEPTNHMD------MEsIEsLNMALEKYEGTLIFVSHDREFVSSLATRI 505
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-312 |
7.83e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.11 E-value: 7.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 32 DVSLDIHKGEIFALLGGSGSGKSTLLRMLAG-FETpDSGRiVLDGQDITALPPylrptnmmfQSYALfpHMTVEQNIAMG 110
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSqFEI-SEGR-VWAERSIAYVPQ---------QAWIM--NATVRGNILFF 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 111 LKQDklpkneiTDRVAAMLKLVKMEPYARR-----------KPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKL 179
Cdd:PTZ00243 745 DEED-------AARLADAVRVSQLEADLAQlgggleteigeKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 180 rTEMQLELVDILEKVGVTCLMVTHdQEEAMTMASRIAIMSYGRIAQVGSPIDIYESP-NSRMTAEFIGSVNIFEAniled 258
Cdd:PTZ00243 818 -GERVVEECFLGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTSlYATLAAELKENKDSKEG----- 890
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516087 259 NSDSLSLASELLDA-PVFIDRGVTTPAETTE--TLIALRPEKIYLTT--EKPEGDSNWS 312
Cdd:PTZ00243 891 DADAEVAEVDAAPGgAVDHEPPVAKQEGNAEggDGAALDAAAGRLMTreEKASGSVPWS 949
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
14-176 |
1.50e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 63.66 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 14 LLSIKGISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFE--TPDSGRIVLDGQDITALPPYLRPTN-- 89
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 90 -MMFQSYALFPHMTVEQNIAMGL-------KQDKLPKNEITDRVAAMLKLVKMEP--YARRKPQQLSGGQQQRVALARSL 159
Cdd:PRK09580 81 fMAFQYPVEIPGVSNQFFLQTALnavrsyrGQEPLDRFDFQDLMEEKIALLKMPEdlLTRSVNVGFSGGEKKRNDILQMA 160
|
170
....*....|....*..
gi 2485516087 160 AKRPKLLLLDEPMGALD 176
Cdd:PRK09580 161 VLEPELCILDESDSGLD 177
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
28-180 |
1.73e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 62.58 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 28 LAVDDVSLDIHKGEIFALL------------GGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP-PYLrptNMMFQS 94
Cdd:PRK13541 2 LSLHQLQFNIEQKNLFDLSitflpsaityikGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkPYC---TYIGHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 YALFPHMTVEQNIAMGlkqdklpkNEITDRVA---AMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEP 171
Cdd:PRK13541 79 LGLKLEMTVFENLKFW--------SEIYNSAEtlyAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEV 150
|
....*....
gi 2485516087 172 MGALDKKLR 180
Cdd:PRK13541 151 ETNLSKENR 159
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
31-176 |
1.81e-11 |
|
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: 62.65 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 31 DDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPD--SGRIVLDGQDITalPPYLRPTNMMFQSYALFPHMTVEQNIa 108
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLD--KNFQRSTGYVEQQDVHSPNLTVREAL- 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 109 mglkqdklpkneitdRVAAMLKlvkmepyarrkpqQLSGGQQQRVALARSLAKRPKLLLLDEPMGALD 176
Cdd:cd03232 101 ---------------RFSALLR-------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
36-217 |
2.32e-11 |
|
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: 61.82 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 36 DIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYLrptnmmfqsyalfphmtveqniamglkqdk 115
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 116 lpkneitdrvaamlklvkmepyarrkpqQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVG 195
Cdd:cd03222 71 ----------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|..
gi 2485516087 196 VTCLMVTHDQEEAMTMASRIAI 217
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHV 144
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-223 |
3.92e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 61.89 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 20 ISKSFDSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAG----FETPdSGRIVLDGQDIT-ALPPYLRPTNMMFQS 94
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtegNVSV-EGDIHYNGIPYKeFAEKYPGEIIYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 95 YALFPHMTVEQNIAMGLKqdkLPKNEITdrvaamlklvkmepyarRKpqqLSGGQQQRVALARSLAKRPKLLLLDEPMGA 174
Cdd:cd03233 92 DVHFPTLTVRETLDFALR---CKGNEFV-----------------RG---ISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 175 LD--------KKLRTemqleLVDILekvGVTCLM-VTHDQEEAMTMASRIAIMSYGRI 223
Cdd:cd03233 149 LDsstaleilKCIRT-----MADVL---KTTTFVsLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
40-204 |
4.56e-11 |
|
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: 62.38 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 40 GEIFALLGGSGSGKSTLLRMLAG--------FETPDSGRIVLDGQDITALPPY--------LRPTnMMFQSYALFPHmTV 103
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGklkpnlgkFDDPPDWDEILDEFRGSELQNYftkllegdVKVI-VKPQYVDLIPK-AV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 104 EQNIAMGLKQ--DKLPKNEITDRVaamlklvKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRT 181
Cdd:cd03236 104 KGKVGELLKKkdERGKLDELVDQL-------ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|...
gi 2485516087 182 EMQlELVDILEKVGVTCLMVTHD 204
Cdd:cd03236 177 NAA-RLIRELAEDDNYVLVVEHD 198
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-228 |
6.57e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.20 E-value: 6.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 33 VSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQdITALPpylrptnmmfqSYALFPHMTVEQNIAMGlK 112
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVP-----------QQAWIQNDSLRENILFG-K 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 113 QDKLPKNEITDRVAAMLKLVKMEPYARR-----KPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEmqlel 187
Cdd:TIGR00957 724 ALNEKYYQQVLEACALLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH----- 798
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2485516087 188 vdILEKV--------GVTCLMVTHDQeEAMTMASRIAIMSYGRIAQVGS 228
Cdd:TIGR00957 799 --IFEHVigpegvlkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGS 844
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-203 |
9.31e-11 |
|
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: 61.19 E-value: 9.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 23 SFDSTLA-VDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP-PYLRPTNMMFQSYA---- 96
Cdd:cd03290 9 SWGSGLAtLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSfEATRSRNRYSVAYAaqkp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 97 LFPHMTVEQNIAMGLKQDKLPKNEITDrVAAMLKLVKMEPYARR-----KPQQLSGGQQQRVALARSLAKRPKLLLLDEP 171
Cdd:cd03290 89 WLLNATVEENITFGSPFNKQRYKAVTD-ACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190
....*....|....*....|....*....|...
gi 2485516087 172 MGALDKKLRTE-MQLELVDILEKVGVTCLMVTH 203
Cdd:cd03290 168 FSALDIHLSDHlMQEGILKFLQDDKRTLVLVTH 200
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-232 |
1.43e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.04 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 25 DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALPPYlrptNMMFQsYALFPHMTVE 104
Cdd:TIGR00957 1297 DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLH----DLRFK-ITIIPQDPVL 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 105 QNIAMGLKQDklPKNEITDR-VAAMLKLVKMEPYARRKP-----------QQLSGGQQQRVALARSLAKRPKLLLLDEPM 172
Cdd:TIGR00957 1372 FSGSLRMNLD--PFSQYSDEeVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 173 GALDKKLRTEMQLELVDILEKvgVTCLMVTHDQEEAMTMaSRIAIMSYGRIAQVGSPIDI 232
Cdd:TIGR00957 1450 AAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
29-227 |
2.79e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 60.21 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQditalppylrpTNMMFQSYALFPHMTVEQNI- 107
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAGLSGQLTGIENIe 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 108 ----AMGLKQdklpkNEITDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLrTEM 183
Cdd:PRK13546 108 fkmlCMGFKR-----KEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF-AQK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2485516087 184 QLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:PRK13546 182 CLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
40-176 |
5.68e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 40 GEIFALLGGSGSGKSTLLRMLAGFETpdsGRIVLDGQDITALPP----YLRPTNMMFQSYALFPHMTVEQNI--AMGLKQ 113
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVT---TGVITGGDRLVNGRPldssFQRSIGYVQQQDLHLPTSTVRESLrfSAYLRQ 865
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485516087 114 DK-LPKNEITDRVAAMLKLVKMEPYARR----KPQQLSGGQQQRVALARSLAKRPKLLL-LDEPMGALD 176
Cdd:TIGR00956 866 PKsVSKSEKMEYVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-244 |
6.35e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 6.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 33 VSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDIT--ALPPYLRPTNMMFQSYALFPHmTVEQNIamg 110
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfGLTDLRRVLSIIPQSPVLFSG-TVRFNI--- 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 111 lkqDKLPKNEITDRVAAmLKLVKMEPYARRKP-----------QQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDkkL 179
Cdd:PLN03232 1331 ---DPFSEHNDADLWEA-LERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASVD--V 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485516087 180 RTEMQLELVDILEKVGVTCLMVTHdQEEAMTMASRIAIMSYGRIAQVGSPIDIYespnSRMTAEF 244
Cdd:PLN03232 1405 RTDSLIQRTIREEFKSCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELL----SRDTSAF 1464
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-218 |
9.83e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 27 TLAVDdvSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDITALP----------PYLRPTNMMFQSYA 96
Cdd:PRK10938 18 TLQLP--SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSfeqlqklvsdEWQRNNTDMLSPGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 97 LFPHMTVEQNIamglkQDKLPKNEITDRVAAMLKLvkmEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALD 176
Cdd:PRK10938 96 DDTGRTTAEII-----QDEVKDPARCEQLAQQFGI---TALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2485516087 177 KKLRTEMQlELVDILEKVGVTCLMVTHDQEEAMTMASRIAIM 218
Cdd:PRK10938 168 VASRQQLA-ELLASLHQSGITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
29-227 |
1.07e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.90 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 29 AVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQditalppylrpTNMMFQSYALFPHMTVEQNIA 108
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 109 -----MGLKQDKLpkNEITDRVAAMLKLVKmepYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLrTEM 183
Cdd:PRK13545 108 lkglmMGLTKEKI--KEIIPEIIEFADIGK---FIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTF-TKK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2485516087 184 QLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVG 227
Cdd:PRK13545 182 CLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-235 |
1.16e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTLA---VDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVldgqDITALPPYLRPTNMM 91
Cdd:PLN03232 615 ISIKNGYFSWDSKTSkptLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSV----VIRGSVAYVPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 FQSyalfphmTVEQNIAMGLKQDKLPKNEITDRVAAMLKLVKMEPYAR----RKPQQLSGGQQQRVALARSLAKRPKLLL 167
Cdd:PLN03232 691 FNA-------TVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLteigERGVNISGGQKQRVSMARAVYSNSDIYI 763
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 168 LDEPMGALDKKLRTEMQLELVDiLEKVGVTCLMVThDQEEAMTMASRIAIMSYGRIAQVGSPIDIYES 235
Cdd:PLN03232 764 FDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
15-238 |
1.53e-09 |
|
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: 58.00 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTL--AVDDVSLDIHKGEIFALLGGSGSGKSTL----LRMLAGFEtpdsGRIVLDGQDITALPPY-LRP 87
Cdd:cd03288 20 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 88 T-NMMFQSYALFphmtvEQNIAMGLKqdklPKNEITD-RVAAMLKLVKMEPYARRKP-----------QQLSGGQQQRVA 154
Cdd:cd03288 96 RlSIILQDPILF-----SGSIRFNLD----PECKCTDdRLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 155 LARSLAKRPKLLLLDEPMGALDkkLRTEmqlelvDILEKVgvtcLMVTHDQEEAMTMASRIA---------IMSYGRIAQ 225
Cdd:cd03288 167 LARAFVRKSSILIMDEATASID--MATE------NILQKV----VMTAFADRTVVTIAHRVStildadlvlVLSRGILVE 234
|
250
....*....|...
gi 2485516087 226 VGSPIDIYESPNS 238
Cdd:cd03288 235 CDTPENLLAQEDG 247
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
30-203 |
3.96e-09 |
|
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: 58.22 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 30 VDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDG-QDITALP--PYLrpTNMMFQSYALFPhMTVEQN 106
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAkGKLFYVPqrPYM--TLGTLRDQIIYP-DSSEDM 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 107 IAMGLKQDKLPKneitdrvaaMLKLVKMEPYARRK---------PQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDk 177
Cdd:TIGR00954 545 KRRGLSDKDLEQ---------ILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS- 614
|
170 180
....*....|....*....|....*.
gi 2485516087 178 klrTEMQLELVDILEKVGVTCLMVTH 203
Cdd:TIGR00954 615 ---VDVEGYMYRLCREFGITLFSVSH 637
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-204 |
4.16e-09 |
|
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: 57.87 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 39 KGEIFALLGGSGSGKSTLLRMLAGFETPDSGRI--------VLD---GqdiTALPPYLRptnmmfqsyalfphMTVEQNI 107
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdeVLKrfrG---TELQDYFK--------------KLANGEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 108 AMGLK-Q--DKLPK------NEITDRV---AAMLKLVK---MEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPM 172
Cdd:COG1245 161 KVAHKpQyvDLIPKvfkgtvRELLEKVderGKLDELAEklgLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|..
gi 2485516087 173 GALDKKLRTEMQlELVDILEKVGVTCLMVTHD 204
Cdd:COG1245 241 SYLDIYQRLNVA-RLIRELAEEGKYVLVVEHD 271
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
44-224 |
1.00e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.79 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 44 ALLGGSGSGKSTLLRMLAGFETPDSGRIV--------------LDGQDITALPpylrptnMMFQSYAlFPhmtveqniam 109
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDLSSNP-------LLYMMRC-FP---------- 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 110 GLKQDKLPKNEITDRVAAMLKLVKMepyarrkpQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVd 189
Cdd:PLN03073 601 GVPEQKLRAHLGSFGVTGNLALQPM--------YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV- 671
|
170 180 190
....*....|....*....|....*....|....*
gi 2485516087 190 iLEKVGVtcLMVTHDQEEAMTMASRIAIMSYGRIA 224
Cdd:PLN03073 672 -LFQGGV--LMVSHDEHLISGSVDELWVVSEGKVT 703
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-229 |
1.77e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.28 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 33 VSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDGQDIT--ALPPYLRPTNMMFQSYALFPHmTVEQNIAmg 110
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISkfGLMDLRKVLGIIPQAPVLFSG-TVRFNLD-- 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 111 lkqdklPKNEITD-RVAAMLKLVKMEPYARRKPQQL-----------SGGQQQRVALARSLAKRPKLLLLDEPMGALDkk 178
Cdd:PLN03130 1335 ------PFNEHNDaDLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVD-- 1406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2485516087 179 LRTEMQLELVDILEKVGVTCLMVTHdQEEAMTMASRIAIMSYGRIAQVGSP 229
Cdd:PLN03130 1407 VRTDALIQKTIREEFKSCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTP 1456
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
39-204 |
3.27e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 39 KGEIFALLGGSGSGKSTLLRMLAG--------FETPDSGRIVLDgqditalppYLRPTNMmfQSYalFpHMTVEQNIAMG 110
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVLK---------RFRGTEL--QNY--F-KKLYNGEIKVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 111 LK-Q--DKLPK------NEI---TDRVAAMLKLVK---MEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGAL 175
Cdd:PRK13409 164 HKpQyvDLIPKvfkgkvRELlkkVDERGKLDEVVErlgLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180
....*....|....*....|....*....
gi 2485516087 176 DKKLRTEMQLELVDILEKVGVtcLMVTHD 204
Cdd:PRK13409 244 DIRQRLNVARLIRELAEGKYV--LVVEHD 270
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
32-215 |
8.04e-08 |
|
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: 51.55 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 32 DVSLDIHKGEIFALLGGSGSGKSTLLrmLAGFETPDSGRIvldgqdITALPPYLR-PTNMMFQSYALfphmtveqnIAMG 110
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKARL------ISFLPKFSRnKLIFIDQLQFL---------IDVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 111 LkqdklpkneitdrvaAMLKLvkmepyaRRKPQQLSGGQQQRVALARSLAKRPK--LLLLDEPMGALDKKlRTEMQLELV 188
Cdd:cd03238 76 L---------------GYLTL-------GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ-DINQLLEVI 132
|
170 180
....*....|....*....|....*..
gi 2485516087 189 DILEKVGVTCLMVTHDqEEAMTMASRI 215
Cdd:cd03238 133 KGLIDLGNTVILIEHN-LDVLSSADWI 158
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
32-178 |
9.74e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.26 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 32 DVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDG----QDITaLPPYLRPTNMMFQSYALFPHmTVEQNI 107
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDIN-LKWWRSKIGVVSQDPLLFSN-SIKNNI 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 108 AMGL--------------------KQDKLPKNEITDRVAAMLKLV----------------------------------- 132
Cdd:PTZ00265 481 KYSLyslkdlealsnyynedgndsQENKNKRNSCRAKCAGDLNDMsnttdsneliemrknyqtikdsevvdvskkvlihd 560
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2485516087 133 -------KMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKK 178
Cdd:PTZ00265 561 fvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-234 |
1.34e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 30 VDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFET---PDSGRIV-----LDGQDITALPPYL-----RPTNMMFQSYA 96
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIdgiPKNCQILhveqeVVGDDTTALQCVLntdieRTQLLEEEAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 97 LFPHMTVEQNIAMGLKQ----DKLPKNEITDRVAAMLK-LVKMEPYA-------------------RRKPQQLSGGQQQR 152
Cdd:PLN03073 273 VAQQRELEFETETGKGKgankDGVDKDAVSQRLEEIYKrLELIDAYTaearaasilaglsftpemqVKATKTFSGGWRMR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 153 VALARSLAKRPKLLLLDEPMGALDkkLRTEMQLElvDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRIAQVGSPIDI 232
Cdd:PLN03073 353 IALARALFIEPDLLLLDEPTNHLD--LHAVLWLE--TYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDT 428
|
..
gi 2485516087 233 YE 234
Cdd:PLN03073 429 FE 430
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
143-208 |
2.72e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 2.72e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485516087 143 QQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDkKLRTEMQLELVDILEKVGVTCLM-VTHDQEEA 208
Cdd:PRK10938 400 HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD-PLNRQLVRRFVDVLISEGETQLLfVSHHAEDA 465
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-176 |
3.61e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.43 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGISKSFDSTL---AVDDVSLDIHKGEIFALLGGSGSGKSTLLR-MLAGFETPDSGRIVLDGQditalPPYLRPTNM 90
Cdd:PLN03130 615 ISIKNGYFSWDSKAerpTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-----VAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 91 MFQSyalfphmTVEQNIAMGLKQDKlPKNEITDRVAAMLKLVKMEPYAR-----RKPQQLSGGQQQRVALARSLAKRPKL 165
Cdd:PLN03130 690 IFNA-------TVRDNILFGSPFDP-ERYERAIDVTALQHDLDLLPGGDlteigERGVNISGGQKQRVSMARAVYSNSDV 761
|
170
....*....|.
gi 2485516087 166 LLLDEPMGALD 176
Cdd:PLN03130 762 YIFDDPLSALD 772
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
32-215 |
3.91e-07 |
|
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: 50.33 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 32 DVSLDIHKGEIFALLGGSGSGKSTLlrmlaGFETpdsgrIVLDGQD--ITALPPYLRptnmmfqsyALFPHMTVEQ--NI 107
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSL-----AFDT-----IYAEGQRryVESLSAYAR---------QFLGQMDKPDvdSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 108 -----AMGLKQDKLPKN---------EITD-------RVA-----AMLKLVKMEpYAR--RKPQQLSGGQQQRVALARSL 159
Cdd:cd03270 74 eglspAIAIDQKTTSRNprstvgtvtEIYDylrllfaRVGirerlGFLVDVGLG-YLTlsRSAPTLSGGEAQRIRLATQI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2485516087 160 AKRPK--LLLLDEPMGALDKKlRTEMQLELVDILEKVGVTCLMVTHDqEEAMTMASRI 215
Cdd:cd03270 153 GSGLTgvLYVLDEPSIGLHPR-DNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADHV 208
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-238 |
4.50e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.09 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 28 LAVDDVSLDIHKGEIFALLGGSGSGKSTLL----RMLagfETPdSGRIVLDGQDITA--LPPYLRPTNMMFQSYALFPHm 101
Cdd:PTZ00243 1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLLltfmRMV---EVC-GGEIRVNGREIGAygLRELRRQFSMIPQDPVLFDG- 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 102 TVEQNIAmglkqdklPKNEITD-RVAAMLKLVKMEPYARRKPQQL-----------SGGQQQRVALARSLAKR-PKLLLL 168
Cdd:PTZ00243 1399 TVRQNVD--------PFLEASSaEVWAALELVGLRERVASESEGIdsrvleggsnySVGQRQLMCMARALLKKgSGFILM 1470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485516087 169 DEPMGALDKKLRTEMQLELVDILEkvGVTCLMVTHdqeEAMTMAS--RIAIMSYGRIAQVGSPIDIYESPNS 238
Cdd:PTZ00243 1471 DEATANIDPALDRQIQATVMSAFS--AYTVITIAH---RLHTVAQydKIIVMDHGAVAEMGSPRELVMNRQS 1537
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-248 |
1.09e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 32 DVSLDIHKGEIFALLGGSGSGKSTLLRMLA----GFETPDSGRIVLDGQDITALPPYLRPTNMMF-QSYALFPHMTVE-- 104
Cdd:TIGR00956 79 PMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNaETDVHFPHLTVGet 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 105 ----------QNIAMGLKQDKLpKNEITDRVAAMLKL--VKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPM 172
Cdd:TIGR00956 159 ldfaarcktpQNRPDGVSREEY-AKHIADVYMATYGLshTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNAT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 173 GALD--------KKLRTemqleLVDILEkvgVTCLMVTHD-QEEAMTMASRIAIMSYGRIAQVGsPIDI---------YE 234
Cdd:TIGR00956 238 RGLDsatalefiRALKT-----SANILD---TTPLVAIYQcSQDAYELFDKVIVLYEGYQIYFG-PADKakqyfekmgFK 308
|
250
....*....|....
gi 2485516087 235 SPNSRMTAEFIGSV 248
Cdd:TIGR00956 309 CPDRQTTADFLTSL 322
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
30-223 |
1.95e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 30 VDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAG--FETPDSGRIVLDGQDITalppyLRptnmmfqsyalfphmTVEQNI 107
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGKEVD-----VS---------------TVSDAI 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 108 AMGL-------KQ------------------DKLPKNEITD-----RVAamlklvkmEPYARR----------KPQQLSG 147
Cdd:NF040905 336 DAGLayvtedrKGyglnliddikrnitlanlGKVSRRGVIDeneeiKVA--------EEYRKKmniktpsvfqKVGNLSG 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 148 GQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMqLELVDILEKVGVTCLMVTHDQEEAMTMASRIAIMSYGRI 223
Cdd:NF040905 408 GNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEI-YTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
76-238 |
4.90e-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: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 76 QDITALPpyLRPTNMMFQSYALFPhmtVEQNIAmglkqDKLPKnEITDRVAaMLKLVKME-PYARRKPQQLSGGQQQRVA 154
Cdd:TIGR00630 431 ADVSELS--IREAHEFFNQLTLTP---EEKKIA-----EEVLK-EIRERLG-FLIDVGLDyLSLSRAAGTLSGGEAQRIR 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 155 LARSLAKRPK--LLLLDEPMGALDKKlRTEMQLELVDILEKVGVTCLMVTHDqEEAMTMASRIAIMSY------GRIAQV 226
Cdd:TIGR00630 499 LATQIGSGLTgvLYVLDEPSIGLHQR-DNRRLINTLKRLRDLGNTLIVVEHD-EDTIRAADYVIDIGPgagehgGEVVAS 576
|
170
....*....|..
gi 2485516087 227 GSPIDIYESPNS 238
Cdd:TIGR00630 577 GTPEEILANPDS 588
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-176 |
5.21e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.75 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 30 VDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDsGRIVLDG--QDITALPPYLRPTNMMFQSYALFPHmTVEQNI 107
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvsWNSVTLQTWRKAFGVIPQKVFIFSG-TFRKNL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 108 AmglkqdklPKNEITD----RVAAMLKLVKM-EPYARRKPQQL-------SGGQQQRVALARSLAKRPKLLLLDEPMGAL 175
Cdd:TIGR01271 1313 D--------PYEQWSDeeiwKVAEEVGLKSViEQFPDKLDFVLvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
.
gi 2485516087 176 D 176
Cdd:TIGR01271 1385 D 1385
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
30-206 |
7.10e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 30 VDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDSGRIVLDG--------QDITALP----PYLRPTNMMFQSYAL 97
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPqpalEYVIDGDREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 98 FPHMTVEQN----IA-MGLKQDKLPKNEITDRVAAMLK-LVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEP 171
Cdd:PRK10636 97 QLHDANERNdghaIAtIHGKLDAIDAWTIRSRAASLLHgLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 2485516087 172 MGALDkklrtemqLELVDILEK----VGVTCLMVTHDQE 206
Cdd:PRK10636 177 TNHLD--------LDAVIWLEKwlksYQGTLILISHDRD 207
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
15-206 |
3.76e-05 |
|
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: 44.14 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 15 LSIKGIsKSFDstlavDDVSLDIHKGeIFALLGGSGSGKSTLLRML--AGF-ETPDSGRIVLDGQDITalppylRPTNMM 91
Cdd:cd03240 4 LSIRNI-RSFH-----ERSEIEFFSP-LTLIVGQNGAGKTTIIEALkyALTgELPPNSKGGAHDPKLI------REGEVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 92 FQSYALFPH-----MTVEQNIAMGLKQDKLPKNEITDRVAAMLKlvkmepyarrkpqQLSGGQQQ------RVALARSLA 160
Cdd:cd03240 71 AQVKLAFENangkkYTITRSLAILENVIFCHQGESNWPLLDMRG-------------RCSGGEKVlasliiRLALAETFG 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2485516087 161 KRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVTCLMV-THDQE 206
Cdd:cd03240 138 SNCGILALDEPTTNLDEENIEESLAEIIEERKSQKNFQLIViTHDEE 184
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
25-176 |
4.37e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 44.85 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 25 DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLAGFETPDsGRIVLDG--QDITALPPYLRPTNMMFQSYALFPHmT 102
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGvsWNSVPLQKWRKAFGVIPQKVFIFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 103 VEQNIAMGLKQDKLPKNEITDRVAamLKLVkMEPYarrkPQQL-----------SGGQQQRVALARSLAKRPKLLLLDEP 171
Cdd:cd03289 93 FRKNLDPYGKWSDEEIWKVAEEVG--LKSV-IEQF----PGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEP 165
|
....*
gi 2485516087 172 MGALD 176
Cdd:cd03289 166 SAHLD 170
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
41-243 |
9.07e-05 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 43.12 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 41 EIFALLGGSGSGKSTLLRMLAGFETPDSGRIVldGQDITALPpylrptnmMFQSYALFPHMTVEQNIAMGLKQDKLPKNE 120
Cdd:PRK15177 14 EHIGILAAPGSGKTTLTRLLCGLDAPDEGDFI--GLRGDALP--------LGANSFILPGLTGEENARMMASLYGLDGDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 121 ITDRVaamLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLRTEMQLELVDILEKVGVtcLM 200
Cdd:PRK15177 84 FSHFC---YQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAALACQLQQKGL--IV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2485516087 201 VTHDQEEAMTMASRIAIMSYGRI------AQVGSPIDIYESPNSRMTAE 243
Cdd:PRK15177 159 LTHNPRLIKEHCHAFGVLLHGKItmcedlAQATALFEQYQSNQATIQTE 207
|
|
| COG3911 |
COG3911 |
Predicted ATPase [General function prediction only]; |
43-82 |
1.34e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443117 Cd Length: 180 Bit Score: 42.11 E-value: 1.34e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2485516087 43 FALLGGSGSGKSTLLRMLA--GFET-PDSGR-IVLDGQ--DITALP 82
Cdd:COG3911 6 IVITGGPGSGKTTLLNALArrGYACvPEAGReIIREQQaiGGDALP 51
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
31-57 |
5.23e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.96 E-value: 5.23e-04
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
145-171 |
5.46e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 5.46e-04
10 20 30
....*....|....*....|....*....|
gi 2485516087 145 LSGGQQQRVALARSLAKRPK---LLLLDEP 171
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEP 856
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-245 |
1.03e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 145 LSGGQQQRVALARSLAKRPK--LLLLDEPMGALDKKlRTEMQLELVDILEKVGVTCLMVTHDqEEAMTMASRI------A 216
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQ-DTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRIidigpgA 554
|
90 100
....*....|....*....|....*....
gi 2485516087 217 IMSYGRIAQVGSPIDIYESPNSrMTAEFI 245
Cdd:PRK00635 555 GIFGGEVLFNGSPREFLAKSDS-LTAKYL 582
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-203 |
1.20e-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: 41.15 E-value: 1.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485516087 145 LSGGQQQRVALARSLAKR---PKLLLLDEPMGALD----KKLrtemqLELVDILEKVGVTCLMVTH 203
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHfddiKKL-----LEVLQRLVDKGNTVVVIEH 890
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
145-171 |
2.00e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 2.00e-03
10 20 30
....*....|....*....|....*....|
gi 2485516087 145 LSGGQQQRVALARSLAKRPK---LLLLDEP 171
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEP 860
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
31-218 |
2.13e-03 |
|
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: 38.49 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 31 DDVSLDIHKGEIFALLGGSGSGKSTLLRMLAgfetpdsgrivldgqditalppylrptnmmfqsYALFPHMtveqniamg 110
Cdd:cd03227 12 VPNDVTFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LALGGAQ--------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485516087 111 LKQDKLPKNEITDRVAAmlklVKMEPYARRKpqQLSGGQQQRVALARSLA----KRPKLLLLDEPMGALDkklrTEMQLE 186
Cdd:cd03227 50 SATRRRSGVKAGCIVAA----VSAELIFTRL--QLSGGEKELSALALILAlaslKPRPLYILDEIDRGLD----PRDGQA 119
|
170 180 190
....*....|....*....|....*....|....*
gi 2485516087 187 LVDILEKV---GVTCLMVTHDqEEAMTMASRIAIM 218
Cdd:cd03227 120 LAEAILEHlvkGAQVIVITHL-PELAELADKLIHI 153
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
25-61 |
2.46e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 40.17 E-value: 2.46e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2485516087 25 DSTLAVDDVSLDIHKGEIFALLGGSGSGKSTLLRMLA 61
Cdd:COG5635 165 ERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLA 201
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
145-204 |
4.20e-03 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 38.36 E-value: 4.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485516087 145 LSGGQQQRVALARSLAKR---PKLLLLDEPMGALD----KKLrtemqLELVDILEKVGVTCLMVTHD 204
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHfhdvKKL-----LEVLQRLVDKGNTVVVIEHN 231
|
|
| AAA_28 |
pfam13521 |
AAA domain; |
43-87 |
4.26e-03 |
|
AAA domain;
Pssm-ID: 433278 [Multi-domain] Cd Length: 164 Bit Score: 37.63 E-value: 4.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2485516087 43 FALLGGSGSGKSTLLRMLA---GFET-PDSGRIVLDGQDIT---ALPPYLRP 87
Cdd:pfam13521 2 IVITGGPSTGKTTLAEALAarfGYPVvPEAAREILEELGADggdALPWVEDL 53
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
145-206 |
9.89e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.12 E-value: 9.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485516087 145 LSGGQQQ------RVALARSLAKRPKLLLLDEPMGALDKKLRTemqlELVDILEK-------VgvtcLMVTHDQE 206
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRR----KLVDIMERylrkipqV----IIVSHDEE 855
|
|
| |
