|
Name |
Accession |
Description |
Interval |
E-value |
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-377 |
0e+00 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 850.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 1 MNDAIPRPQAKTRKALTPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDG 80
Cdd:PRK11607 1 MNDAIPRPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 81 VDLSQVPPYLRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVAL 160
Cdd:PRK11607 81 VDLSHVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 161 ARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 241 PTTRYSAEFIGSVNVFEGVLKERQEDGLVLDSPGLVHPLKVDADASVVDNVPVHVALRPEKIMLCEEPPANGCNFAVGEV 320
Cdd:PRK11607 241 PTTRYSAEFIGSVNVFEGVLKERQEDGLVIDSPGLVHPLKVDADASVVDNVPVHVALRPEKIMLCEEPPADGCNFAVGEV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 321 IHIAYLGDLSVYHVRLKSGQMISAQLQNAHRHRKGLPTWGDEVRLCWEVDSCVVLTV 377
Cdd:PRK11607 321 IHIAYLGDLSIYHVRLKSGQMISAQLQNAHRYRKGLPTWGDEVRLCWEADSCVVLTV 377
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
17-376 |
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: 551.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMM 96
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVF 256
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 257 EGVLKERQEDGlvLDSPGlvHPLKVDADASVVDNVPVHVALRPEKIMLCEEPPANGcnfAVGEVIHIAYLGDLSVYHVRL 336
Cdd:COG3842 243 PGTVLGDEGGG--VRTGG--RTLEVPADAGLAAGGPVTVAIRPEDIRLSPEGPENG---LPGTVEDVVFLGSHVRYRVRL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1314858832 337 KSGQMISAQLQNAHRHRkglPTWGDEVRLCWEVDSCVVLT 376
Cdd:COG3842 316 GDGQELVVRVPNRAALP---LEPGDRVGLSWDPEDVVVLP 352
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
50-375 |
0e+00 |
|
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: 550.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 50 LLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASR 129
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 130 VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHD 209
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 210 QEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGVLKERQEDGLVLDSpGLVHPLKVDADASVVD 289
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAG-VEGRRCDIYTDVPVEK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 290 NVPVHVALRPEKIMLCEEPPANGCNFAVGEVIHIAYLGDLSVYHVRLKSGQ--MISAQLQNAHRHRKglPTWGDEVRLCW 367
Cdd:TIGR01187 240 DQPLHVVLRPEKIVIEEEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQkvLVSEFFNEDDPHMS--PSIGDRVGLTW 317
|
....*...
gi 1314858832 368 EVDSCVVL 375
Cdd:TIGR01187 318 HPGSEVVL 325
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
20-374 |
1.97e-146 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 418.32 E-value: 1.97e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQS 99
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:COG3839 84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVFE 257
Cdd:COG3839 164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppMNLLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 258 GVLKerqEDGLVLDSpglvHPLKVDADASVVDNVPVHVALRPEKIMLCEEPPANgcnfAVGEVIHIAYLGDLSVYHVRLk 337
Cdd:COG3839 244 GTVE---GGGVRLGG----VRLPLPAALAAAAGGEVTLGIRPEHLRLADEGDGG----LEATVEVVEPLGSETLVHVRL- 311
|
330 340 350
....*....|....*....|....*....|....*..
gi 1314858832 338 SGQMISAQLQNAHRHRKglptwGDEVRLCWEVDSCVV 374
Cdd:COG3839 312 GGQELVARVPGDTRLRP-----GDTVRLAFDPERLHL 343
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
20-367 |
4.75e-138 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 396.82 E-value: 4.75e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDL-SQVPPYLRPINMMFQ 98
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEG 258
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 259 vlkERQEDGLVLDSPGLvhplkvdADASVVDNVPVHVALRPEKIMLCEEPpaNGCNFAVGEVIHIAYLGDLSVYHVRL-- 336
Cdd:COG1118 243 ---RVIGGQLEADGLTL-------PVAEPLPDGPAVAGVRPHDIEVSREP--EGENTFPATVARVSELGPEVRVELKLed 310
|
330 340 350
....*....|....*....|....*....|.
gi 1314858832 337 KSGQMISAQLqNAHRHRKGLPTWGDEVRLCW 367
Cdd:COG1118 311 GEGQPLEAEV-TKEAWAELGLAPGDPVYLRP 340
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
17-344 |
4.80e-137 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 395.47 E-value: 4.80e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMM 96
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVF 256
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 257 EGVLKERQEDGLVL-DSPGLVHPLKVDADASVVDNvpVHVALRPEKI---MLCEEPPANGcnfAVGEVIHIAYLG---DL 329
Cdd:PRK09452 252 DATVIERLDEQRVRaNVEGRECNIYVNFAVEPGQK--LHVLLRPEDLrveEINDDEHAEG---LIGYVRERNYKGmtlDS 326
|
330
....*....|....*
gi 1314858832 330 SvyhVRLKSGQMISA 344
Cdd:PRK09452 327 V---VELENGKMVMV 338
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-251 |
5.25e-137 |
|
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: 389.67 E-value: 5.25e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQS 99
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG 251
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
18-356 |
7.30e-123 |
|
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: 358.58 E-value: 7.30e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMF 97
Cdd:TIGR03265 3 PYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
Cdd:TIGR03265 83 QSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 178 GALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFE 257
Cdd:TIGR03265 163 SALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 258 GvlkERQEDGLVLDSPGLVHPLKVDADASvvdnVPVHVALRPEKIMLceEPPANGCNFAVGEVIHIAYLGdlSVYHVRLK 337
Cdd:TIGR03265 243 G---TRGGGSRARVGGLTLACAPGLAQPG----ASVRLAVRPEDIRV--SPAGNAANLLLARVEDMEFLG--AFYRLRLR 311
|
330 340
....*....|....*....|...
gi 1314858832 338 ----SGQMISAQLQNAHRHRKGL 356
Cdd:TIGR03265 312 leglPGQALVADVSASEVERLGI 334
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
20-232 |
1.64e-119 |
|
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: 344.50 E-value: 1.64e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQS 99
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1314858832 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
20-252 |
1.27e-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: 302.72 E-value: 1.27e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQS 99
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 YALFPHMTVEQNIAFGLK----QDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
18-249 |
3.51e-102 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 302.39 E-value: 3.51e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSY----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPylrPI 93
Cdd:COG1116 6 PALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---DR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKfvqiGEPEEIYE-------HPTTRYS 246
Cdd:COG1116 163 DEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARP----GRIVEEIDvdlprprDRELRTS 238
|
...
gi 1314858832 247 AEF 249
Cdd:COG1116 239 PEF 241
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
20-232 |
1.74e-100 |
|
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: 296.47 E-value: 1.74e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQS 99
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1314858832 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
20-355 |
2.68e-100 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 300.99 E-value: 2.68e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQ 98
Cdd:PRK11650 4 LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:PRK11650 84 NYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVF 256
Cdd:PRK11650 164 NLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpaMNLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 257 EGvlkERQEDGLVLDSPGLVhPLKVDADASVVDNVPVHVALRPEKImlceEPPANGCNFAVgEVIHIAYLGDLSVYHVRL 336
Cdd:PRK11650 244 DG---RVSADGAAFELAGGI-ALPLGGGYRQYAGRKLTLGIRPEHI----ALSSAEGGVPL-TVDTVELLGADNLAHGRW 314
|
330
....*....|....*....
gi 1314858832 337 kSGQMISAQLQNAHRHRKG 355
Cdd:PRK11650 315 -GGQPLVVRLPHQERPAAG 332
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
20-255 |
2.39e-98 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 291.70 E-value: 2.39e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQS 99
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNV 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
20-225 |
1.75e-97 |
|
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: 288.99 E-value: 1.75e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDG----QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPylrPINM 95
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314858832 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNR 225
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-327 |
1.76e-94 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 286.23 E-value: 1.76e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQS 99
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGV 259
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPAT 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314858832 260 LKERQedglvLDSPGLVHPLKvDADASVVDNVPVHVALRPEKIMLCEE-PPANGCnfavgEVIHIAYLG 327
Cdd:PRK11432 247 LSGDY-----VDIYGYRLPRP-AAFAFNLPDGECTVGVRPEAITLSEQgEESQRC-----TIKHVAYMG 304
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
21-252 |
2.64e-94 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 283.91 E-value: 2.64e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 21 EIRNLTKSY-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYL--RPINMMF 97
Cdd:COG1125 3 EFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM--QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
19-329 |
8.82e-91 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 276.57 E-value: 8.82e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHaVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQ 98
Cdd:NF040840 1 MIRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:NF040840 80 NYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEG 258
Cdd:NF040840 160 ALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEG 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 259 VLKErQEDGLVLDSPGLVHPLKVDADAsvvdnvPVHVALRPEKIMLCEEPPANGC-NFAVGEVIHIAYLGDL 329
Cdd:NF040840 240 VAEK-GGEGTILDTGNIKIELPEEKKG------KVRIGIRPEDITISTEKVKTSArNEFKGKVEEIEDLGPL 304
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
20-252 |
3.29e-90 |
|
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: 271.48 E-value: 3.29e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP--YLRPINMM 96
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPveLRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM--QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
22-377 |
6.26e-89 |
|
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: 272.25 E-value: 6.26e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 22 IRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSA--GQIMLDGVDLSQVPPYLRPINMMFQS 99
Cdd:TIGR03258 8 IDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGltGRIAIADRDLTHAPPHKRGLALLFQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:TIGR03258 88 YALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 180 LDKKLRDRMQLEVVDILERV-GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEG 258
Cdd:TIGR03258 168 LDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANILPA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 259 VLKERQEDGLVLDSPGLVHPLKVDADAS--VVDNVpvhVALRPEKIMLCEEPPanGCNFAVGEVIHIAYLGDLSVYHVRL 336
Cdd:TIGR03258 248 IALGITEAPGLVDVSCGGAVIFAFGDGRhdGRDKL---ACIRPEHLALTPRPA--GEGRFHATIASVEWHGAALHLLCDL 322
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1314858832 337 KSGQMISAqLQNAHRHRKGLPTWGDEVRLCWEVDSCVVLTV 377
Cdd:TIGR03258 323 DAACDEPM-LVTMLRGRGPAPERGAKLALDCEADDAVLIEP 362
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
20-264 |
4.71e-87 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 267.33 E-value: 4.71e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQS 99
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 YALFPHMTVEQNIAFGLK----QDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTvlprRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNR 242
|
....*....
gi 1314858832 256 FEGVLKERQ 264
Cdd:PRK10851 243 LQGTIRGGQ 251
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-255 |
9.82e-86 |
|
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: 259.58 E-value: 9.82e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYdGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQS 99
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
22-252 |
4.84e-84 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 259.96 E-value: 4.84e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 22 IRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQSYA 101
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 102 LFPHMTVEQNIAFGLKQDKLPKAEIASRVN---EMLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:PRK11000 86 LYPHLSVAENMSFGLKLAGAKKEEINQRVNqvaEVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
Cdd:PRK11000 163 NLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGS 236
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
34-255 |
1.14e-83 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 259.65 E-value: 1.14e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP----YLR--PINMMFQSYALFPHMT 107
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKkelrELRrkKMSMVFQHFALLPHRT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 108 VEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
Cdd:COG4175 122 VLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRRE 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 188 MQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
Cdd:COG4175 202 MQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDVDR 269
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
17-250 |
2.83e-82 |
|
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: 251.05 E-value: 2.83e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVP-----PYLR 91
Cdd:COG1127 3 EPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekelyELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 92 PINMMFQSYALFPHMTVEQNIAFGLKQ-DKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 171 LLLDEP--------MGALD---KKLRDRMqlevvdilervGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY- 238
Cdd:COG1127 163 LLYDEPtagldpitSAVIDeliRELRDEL-----------GLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLa 231
|
250
....*....|...
gi 1314858832 239 -EHPTTRysaEFI 250
Cdd:COG1127 232 sDDPWVR---QFL 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-253 |
9.21e-82 |
|
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: 258.68 E-value: 9.21e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 3 DAIPRPQAKTRKALTPLLEIRNLTKSY-----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIM 77
Cdd:COG1123 244 GAARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 78 LDGVDLSQVP-----PYLRPINMMFQ--SYALFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQ-EFAKRKPH 148
Cdd:COG1123 324 FDGKDLTKLSrrslrELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRlHGLLSRAERRERVAELLERVGLPpDLADRYPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 149 QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMN 224
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSV----QAQILNLLrdlqRELGLTYLFISHDLAVVRYIADRVAVMY 479
|
250 260
....*....|....*....|....*....
gi 1314858832 225 RGKFVQIGEPEEIYEHPTTRYSAEFIGSV 253
Cdd:COG1123 480 DGRIVEDGPTEEVFANPQHPYTRALLAAV 508
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
27-274 |
3.76e-78 |
|
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: 244.76 E-value: 3.76e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 27 KSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP------YLRPINMMFQSY 100
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 101 ALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 181 DKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFE--- 257
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQvfd 240
|
250
....*....|....*...
gi 1314858832 258 -GVLKERQEDGLVLDSPG 274
Cdd:TIGR01186 241 aERIAQRMNTGPITKTAD 258
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
34-255 |
5.09e-78 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 241.01 E-value: 5.09e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVP-PYLRP-----INMMFQSYALFPHMT 107
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrKELRElrrkkISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 108 VEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 188 MQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVDR 266
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
19-253 |
4.87e-77 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 237.58 E-value: 4.87e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLS----QVPPYLRPIN 94
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 95 MMFQSYALFPHMTVEQNIAFGLKQ-DKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 174 DEPMGALDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
Cdd:COG1126 161 DEPTSALDPELVG----EVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFL 236
|
...
gi 1314858832 251 GSV 253
Cdd:COG1126 237 SKV 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
20-271 |
5.56e-77 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 240.75 E-value: 5.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPY-LRP-- 92
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSEReLRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 --INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
Cdd:COG1135 82 rkIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 171 LLLDEPMGALD-----------KKLRDRMqlevvdilervGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
Cdd:COG1135 162 LLCDEATSALDpettrsildllKDINREL-----------GLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 1314858832 240 HPTTRYSAEFIGSVNVFE------GVLKERQEDGLVLD 271
Cdd:COG1135 231 NPQSELTRRFLPTVLNDElpeellARLREAAGGGRLVR 268
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
20-251 |
6.36e-77 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 236.96 E-value: 6.36e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAvdDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQS 99
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 YALFPHMTVEQNIAFGLKQD-KLPKAEIAsRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLA-KRPkLLLLDEPM 177
Cdd:COG3840 80 NNLFPHLTVAQNIGLGLRPGlKLTAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDEPF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 178 GALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG 251
Cdd:COG3840 158 SALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
17-229 |
4.34e-76 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 234.55 E-value: 4.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSY-DGQ---HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPY--- 89
Cdd:COG1136 2 SPLLELRNLTKSYgTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 90 ---LRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 167 RPKLLLLDEPMGALDKKLRDrmqlEVVDILERV----GVTCVMVTHDqEEAMTMAGRIAIMNRGKFV 229
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGE----EVLELLRELnrelGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
20-227 |
4.92e-76 |
|
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: 232.85 E-value: 4.92e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDL----SQVPPYLRPINM 95
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdleDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYALFPHMTVEQNIAFGlkqdklpkaeiasrvnemlglvhmqefakrkphqLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
20-241 |
6.42e-76 |
|
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: 234.15 E-value: 6.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQV-PPYLRP-INMM 96
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnLRELRRkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQS--YALFpHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:COG1122 81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 175 EPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:COG1122 160 EPTAGLDPRGRREL-LELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
20-237 |
6.41e-75 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 231.88 E-value: 6.41e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP-INMMFQ 98
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 SYALFPHMTVEQNIAF--GLKqdKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:COG1131 81 EPALYPDLTVRENLRFfaRLY--GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314858832 177 MGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-258 |
2.73e-73 |
|
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: 228.15 E-value: 2.73e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSY----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP--YLRP 92
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkaFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 INMMFQSY--ALFPHMTVEQNIAFGLKQDKLPkaEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 170 LLLLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
Cdd:COG1124 159 LLLLDEPTSALDVS----VQAEILNLLKDLreerGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
250
....*....|...
gi 1314858832 246 SAEFIGSVNVFEG 258
Cdd:COG1124 235 TRELLAASLAFER 247
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
20-236 |
1.63e-72 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 225.32 E-value: 1.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVP----PYLR-PI 93
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreiPYLRrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 174 DEPMGALDKKLRdrmqLEVVDILE---RVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
Cdd:COG2884 162 DEPTGNLDPETS----WEIMELLEeinRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
20-227 |
1.79e-72 |
|
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: 225.06 E-value: 1.79e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP------Y 89
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaafR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 90 LRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 170 LLLLDEPMGALDKKLRDrmqlEVVDILERV----GVTCVMVTHDQEEAMtMAGRIAIMNRGK 227
Cdd:cd03255 161 IILADEPTGNLDSETGK----EVMELLRELnkeaGTTIVVVTHDPELAE-YADRIIELRDGK 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-223 |
4.17e-72 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 225.51 E-value: 4.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDG----QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQvPPYLRPI 93
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 nmMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:COG4525 81 --VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314858832 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIM 223
Cdd:COG4525 159 DEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
20-237 |
3.15e-71 |
|
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: 222.38 E-value: 3.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQV-PPYLRPI----N 94
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLsEAELYRLrrrmG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 95 MMFQSYALFPHMTVEQNIAFGLKQD-KLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
19-241 |
2.25e-70 |
|
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: 220.15 E-value: 2.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPY-LRP- 92
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKeLRKa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 ---INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
Cdd:cd03258 81 rrrIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 170 LLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
37-232 |
3.71e-70 |
|
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: 219.09 E-value: 3.71e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 37 DVSLTIyKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGV---DLSQ---VPPYLRPINMMFQSYALFPHMTVEQ 110
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkinLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 111 NIAFGLKqdKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQL 190
Cdd:cd03297 95 NLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1314858832 191 EVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
17-244 |
1.93e-68 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 218.45 E-value: 1.93e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQ-----------HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQ 85
Cdd:COG4608 5 EPLLEVRDLKKHFPVRgglfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 86 VP-----PYLRPINMMFQ-SYA-LFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQ 156
Cdd:COG4608 85 LSgrelrPLRRRMQMVFQdPYAsLNPRMTVGDIIAEPLRiHGLASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 157 RVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILE----RVGVTCVMVTHDQeeAMT--MAGRIAIMNRGKFVQ 230
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVS----IQAQVLNLLEdlqdELGLTYLFISHDL--SVVrhISDRVAVMYLGKIVE 238
|
250
....*....|....*..
gi 1314858832 231 IGEPEEIYE---HPTTR 244
Cdd:COG4608 239 IAPRDELYArplHPYTQ 255
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
19-232 |
2.58e-67 |
|
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: 212.37 E-value: 2.58e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP-- 92
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 ---INMMFQSY--ALFPHMTVEQNIAFGLK-QDKLPKAEIASRVnEMLGLVHMQ---EFAKRKPHQLSGGQRQRVALARS 163
Cdd:cd03257 81 rkeIQMVFQDPmsSLNPRMTIGEQIAEPLRiHGKLSKKEARKEA-VLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314858832 164 LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
21-227 |
1.16e-66 |
|
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: 210.02 E-value: 1.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 21 EIRNLTKSYDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP--YLRPINMM 96
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkeLRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQsyalFP-HM----TVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
Cdd:cd03225 81 FQ----NPdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 172 LLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:cd03225 157 LLDEPTAGLDPAGRREL-LELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
37-311 |
1.34e-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: 212.27 E-value: 1.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQ------VPPYLRPINMMFQSYALFPHMTVEQ 110
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 111 NIAFGLKQDKLPKAEIA-SRVNEMLGLVHMqefAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDrmq 189
Cdd:COG4148 97 NLLYGRKRAPRAERRISfDEVVELLGIGHL---LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 190 lEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGVLKERQE 265
Cdd:COG4148 171 -EILPYLERLrdelDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVAAHDP 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1314858832 266 D-GLV-LDSPGlvHPLKVdADASVVDNVPVHVALRPEKIMLCEEPPAN 311
Cdd:COG4148 250 DyGLTrLALGG--GRLWV-PRLDLPPGTRVRVRIRARDVSLALEPPEG 294
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
20-227 |
1.33e-64 |
|
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: 204.69 E-value: 1.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLS----QVPPYLRPINM 95
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYALFPHMTVEQNIAFGLKQ-DKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 175 EPMGALDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:cd03262 161 EPTSALDPELVG----EVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
17-291 |
1.87e-64 |
|
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: 213.61 E-value: 1.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSA---GQIMLDGVDLSQVPPYLR 91
Cdd:COG1123 2 TPLLEVRDLSVRYPGGdvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 92 P--INMMFQS--YALFPhMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKR 167
Cdd:COG1123 82 GrrIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 168 PKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSA 247
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1314858832 248 EFIGSVNVFEGVLKERQEDGLVLDSPGLVHPLKVDADASVVDNV 291
Cdd:COG1123 241 PRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKGGVRAVDDV 284
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-220 |
3.22e-64 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 203.48 E-value: 3.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP---SAGQIMLDGVDLSQVPPYLRPINMM 96
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFPHMTVEQNIAFGLKqDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:COG4136 82 FQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1314858832 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRI 220
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA-AGRV 203
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
21-253 |
9.30e-64 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 206.96 E-value: 9.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 21 EIRNLTKSYDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP-----YLR 91
Cdd:PRK11153 3 ELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrkARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 92 PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 172 LLDEPMGALD-KKLRDRMQLeVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
Cdd:PRK11153 163 LCDEATSALDpATTRSILEL-LKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFI 241
|
...
gi 1314858832 251 GSV 253
Cdd:PRK11153 242 QST 244
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
35-244 |
1.42e-63 |
|
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: 202.70 E-value: 1.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRpinMMFQSYALFPHMTVEQNIAF 114
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---VVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 115 GLKQ--DKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
Cdd:TIGR01184 78 AVDRvlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1314858832 193 VDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI-YEHPTTR 244
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRDR 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
17-241 |
4.05e-63 |
|
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: 202.19 E-value: 4.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP---I 93
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSYALFPHMTVEQNIA---------------FGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRV 158
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVR 241
|
...
gi 1314858832 239 EHP 241
Cdd:COG0411 242 ADP 244
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-240 |
1.05e-62 |
|
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: 201.89 E-value: 1.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDL---SQVPPYLRPIN 94
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 95 MMFQSyalfPH-----MTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
Cdd:TIGR04520 81 MVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 170 LLLLDEPMGALDKKLRDrmqlEVVDILERV----GVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:TIGR04520 157 IIILDEATSMLDPKGRK----EVLETIRKLnkeeGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-241 |
1.34e-62 |
|
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: 202.98 E-value: 1.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP---SAGQIMLDGVDLSQVPP--- 88
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 89 ---YLRPINMMFQ-SY-ALFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHM---QEFAKRKPHQLSGGQRQRVA 159
Cdd:COG0444 81 rkiRGREIQMIFQdPMtSLNPVMTVGDQIAEPLRiHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 160 LARSLAKRPKLLLLDEPMGALDKklrdRMQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDV----TIQAQILNLLkdlqRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVE 236
|
....*.
gi 1314858832 236 EIYEHP 241
Cdd:COG0444 237 ELFENP 242
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-241 |
2.00e-61 |
|
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: 197.27 E-value: 2.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP---INMM 96
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFPHMTVEQNI----------AFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
Cdd:cd03219 81 FQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 167 RPKLLLLDEPMGALDKKLRDRMqlevVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEEL----AELIRELrerGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
19-237 |
2.17e-61 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 197.96 E-value: 2.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP--YLRPINMM 96
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRreLARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFPHMTVEQNIAFG----LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314858832 173 LDEPMGALDkkLrdRMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG1120 161 LDEPTSHLD--L--AHQLEVLELLRRLarerGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
19-239 |
2.61e-61 |
|
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: 197.39 E-value: 2.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP-INMMF 97
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRqIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 178 GALDkkLRDRMQLevVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
Cdd:COG4555 161 NGLD--VMARRLL--REILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
32-232 |
4.68e-61 |
|
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: 195.40 E-value: 4.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQSYALFPHMTVEQN 111
Cdd:cd03298 11 GEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 112 IAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLE 191
Cdd:cd03298 91 VGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1314858832 192 VVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
20-228 |
1.17e-60 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 194.26 E-value: 1.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP--YLRPINMMF 97
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpeWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 98 QSYALFPhMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHmqEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:COG4619 81 QEPALWG-GTVRDNLPFPFQlRERKFDRERALELLERLGLPP--DILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
20-237 |
4.87e-60 |
|
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: 193.55 E-value: 4.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-----EQPSAGQIMLDGVDL--SQVPPYL-- 90
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIydLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 91 RPINMMFQSYALFPhMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQEFAKRKPH--QLSGGQRQRVALARSLAKR 167
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRlHGIKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 168 PKLLLLDEPMGALD-----------KKLRDRMqlevvdilervgvTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
Cdd:cd03260 160 PEVLLLDEPTSALDpistakieeliAELKKEY-------------TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 1314858832 237 I 237
Cdd:cd03260 227 I 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
20-228 |
1.39e-59 |
|
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: 190.30 E-value: 1.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP-INMMFQ 98
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 SYALFPHMTVEQNIafglkqdklpkaeiasrvnemlglvhmqefakrkphQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314858832 179 ALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
Cdd:cd03230 125 GLDPESRREF-WELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-240 |
2.21e-59 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 193.69 E-value: 2.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQ--VPPYLRPI 93
Cdd:PRK13635 4 EIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSY-ALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:PRK13635 84 GMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314858832 173 LDEPMGALDKKLRDRMqLEVVDIL-ERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:PRK13635 164 LDEATSMLDPRGRREV-LETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
18-237 |
8.82e-59 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 191.04 E-value: 8.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSY-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP-----YLR 91
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralrrLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 92 PINMMFQSYALFPHMTVEQNI-------------AFGLkqdkLPKAEIAsRVNEMLGLVHMQEFAKRKPHQLSGGQRQRV 158
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVlagrlgrtstwrsLLGL----FPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 159 ALARSLAKRPKLLLLDEPMGALDKKL-RDRMQLeVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-237 |
6.97e-58 |
|
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: 187.71 E-value: 6.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP-INMM 96
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQsLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFPHMTVEQNIAF--GLKqdKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:cd03263 81 PQFDALFDELTVREHLRFyaRLK--GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 175 EPMGALDKKLRDrmqlEVVDILERV--GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:cd03263 159 EPTSGLDPASRR----AIWDLILEVrkGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
19-227 |
1.05e-57 |
|
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: 187.07 E-value: 1.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYD-GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLS-----QVPPYLRP 92
Cdd:TIGR02673 1 MIEFHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNrlrgrQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 173 LDEPMGALDkklrDRMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:TIGR02673 161 ADEPTGNLD----PDLSERILDLLKRLnkrGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
17-242 |
3.35e-57 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 186.83 E-value: 3.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP---YLrPi 93
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRrigYV-P- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 nmmfQSYAL---FPhMTVEQNIAFGLKQD----KLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
Cdd:COG1121 82 ----QRAEVdwdFP-ITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314858832 167 RPKLLLLDEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKfVQIGEPEEIYEHPT 242
Cdd:COG1121 157 DPDLLLLDEPFAGVDAA----TEEALYELLRELrreGKTILVVTHDLGAVREYFDRVLLLNRGL-VAHGPPEEVLTPEN 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
19-237 |
1.00e-56 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 185.17 E-value: 1.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHAvdDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQ 98
Cdd:PRK10771 1 MLKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 SYALFPHMTVEQNIAFGL-------KQDKLPKAEIASRVnemlGLvhmQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
Cdd:PRK10771 79 ENNLFSHLTVAQNIGLGLnpglklnAAQREKLHAIARQM----GI---EDLLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 172 LLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK10771 152 LLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
19-226 |
1.86e-56 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 185.29 E-value: 1.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQvPPYLRPInmMFQ 98
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1314858832 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
19-253 |
1.98e-56 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 184.53 E-value: 1.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYdGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPI---- 93
Cdd:PRK09493 1 MIEFKNVSKHF-GPTQVlHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSYALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 173 LDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
Cdd:PRK09493 160 FDEPTSALDPELRHEV-LKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQH 238
|
.
gi 1314858832 253 V 253
Cdd:PRK09493 239 V 239
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-242 |
4.40e-56 |
|
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: 184.96 E-value: 4.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDG-----QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDL-SQVPPYLRPI 93
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 ----NMMFQ--SYALFpHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAK 166
Cdd:TIGR04521 81 rkkvGLVFQfpEHQLF-EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 167 RPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPT 242
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
20-240 |
3.98e-55 |
|
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: 181.23 E-value: 3.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP-----YLRPI 93
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSYALFPHMTVEQNIAFGLKQDK---------LPKAEIAsRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSL 164
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRstwrslfglFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 165 AKRPKLLLLDEPMGALDKKL-RDRMQLeVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:cd03256 160 MQQPKLILADEPVASLDPASsRQVMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
22-220 |
1.32e-54 |
|
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: 178.58 E-value: 1.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 22 IRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVD-----LSQVPPYLRP-INM 95
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQEtpplnSKKASKFRREkLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1314858832 176 PMGALDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAmTMAGRI 220
Cdd:TIGR03608 161 PTGSLDPKNRD----EVLDLLLELndeGKTIIIVTHDPEVA-KQADRV 203
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
34-275 |
2.35e-54 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 184.08 E-value: 2.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP------YLRPINMMFQSYALFPHMT 107
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 108 VEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 188 MQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGV----LKER 263
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFsakdIARR 282
|
250
....*....|..
gi 1314858832 264 QEDGLVLDSPGL 275
Cdd:PRK10070 283 TPNGLIRKTPGF 294
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
17-227 |
5.54e-54 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 178.72 E-value: 5.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLeIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRpinMM 96
Cdd:PRK11247 11 TPLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---LM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEiasrvnEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1314858832 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-245 |
1.18e-53 |
|
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: 185.27 E-value: 1.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 3 DAIPRPQAKTRKAL-TPLLEIRNLTKSYDGQ-----------HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQ 70
Cdd:COG4172 258 AAEPRGDPRPVPPDaPPLLEARDLKVWFPIKrglfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-I 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 71 PSAGQIMLDGVDLSQVP-----PYLRPINMMFQS-YA-LFPHMTVEQNIAFGLK--QDKLPKAEIASRVNEMLGLVHMQ- 140
Cdd:COG4172 337 PSEGEIRFDGQDLDGLSrralrPLRRRMQVVFQDpFGsLSPRMTVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDp 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 141 EFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdRMQLEVVDIL----ERVGVTCVMVTHDQEEAMTM 216
Cdd:COG4172 417 AARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV----SVQAQILDLLrdlqREHGLAYLFISHDLAVVRAL 492
|
250 260
....*....|....*....|....*....
gi 1314858832 217 AGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
Cdd:COG4172 493 AHRVMVMKDGKVVEQGPTEQVFDAPQHPY 521
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
39-232 |
1.54e-53 |
|
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: 176.21 E-value: 1.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 39 SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQSYALFPHMTVEQNIAFGLKQ 118
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 119 DKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILER 198
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....
gi 1314858832 199 VGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-250 |
3.97e-53 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 175.97 E-value: 3.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDG--VDLSQVPP-----YLR- 91
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqFDFSQKPSekairLLRq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 92 PINMMFQSYALFPHMTVEQN-IAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 171 LLLDEPMGALDKKLRDrmqlEVVDI---LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpEEIYEHPTTRYSA 247
Cdd:COG4161 163 LLFDEPTAALDPEITA----QVVEIireLSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFA 237
|
...
gi 1314858832 248 EFI 250
Cdd:COG4161 238 HYL 240
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
20-244 |
5.28e-53 |
|
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: 175.42 E-value: 5.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP---INMM 96
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRArlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314858832 177 MGALDKKLRDRMQlEVVDILERVGVTcVMVT-HDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
Cdd:cd03218 161 FAGVDPIAVQDIQ-KIIKILKDRGIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-240 |
1.19e-52 |
|
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: 185.81 E-value: 1.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPY-LRP-INM 95
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAsLRRqIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYALFpHMTVEQNIAFGlkqdkLPKAEIAsRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSL 164
Cdd:COG2274 554 VLQDVFLF-SGTIRENITLG-----DPDATDE-EIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 165 AKRPKLLLLDEPMGALDKKLRDRmqleVVDILERV--GVTCVMVTHDqEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAI----ILENLRRLlkGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
17-220 |
2.09e-51 |
|
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: 171.46 E-value: 2.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSY-DGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVP----P 88
Cdd:COG4181 6 APIIELRGLTKTVgTGAGELtilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 89 YLRPINM--MFQSYALFPHMTVEQNIAfglkqdkLPkAEIASRVN------EMLGLVHMQEFAKRKPHQLSGGQRQRVAL 160
Cdd:COG4181 86 RLRARHVgfVFQSFQLLPTLTALENVM-------LP-LELAGRRDarararALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314858832 161 ARSLAKRPKLLLLDEPMGALDKKLRDRmqleVVDIL----ERVGVTCVMVTHDQEEA------MTM-AGRI 220
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQ----IIDLLfelnRERGTTLVLVTHDPALAarcdrvLRLrAGRL 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-227 |
3.63e-51 |
|
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: 170.28 E-value: 3.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVP----PYLR-PI 93
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraiPYLRrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 174 DEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:cd03292 161 DEPTGNLDPD----TTWEIMNLLKKInkaGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-250 |
5.59e-51 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 170.58 E-value: 5.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDG--VDLSQVPP-----YLR- 91
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPSdkairELRr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 92 PINMMFQSYALFPHMTVEQN-IAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 171 LLLDEPMGALDKKLRDrmqlEVVDI---LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpEEIYEHPTTRYSA 247
Cdd:PRK11124 163 LLFDEPTAALDPEITA----QIVSIireLAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFK 237
|
...
gi 1314858832 248 EFI 250
Cdd:PRK11124 238 NYL 240
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
20-232 |
5.84e-51 |
|
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: 169.30 E-value: 5.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGeIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP-INMMFQ 98
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 179 ALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
21-232 |
7.76e-51 |
|
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: 168.00 E-value: 7.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 21 EIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRpinmmfqsy 100
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 101 AlfphmtveQNIAFglkqdkLPKAeiasrvnemLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
Cdd:cd03214 72 A--------RKIAY------VPQA---------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 181 DKKlrdrMQLEVVDILER----VGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03214 129 DIA----HQIELLELLRRlareRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-244 |
1.49e-50 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 169.44 E-value: 1.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLR------ 91
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlgig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 92 --PinmmfQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
Cdd:COG1137 82 ylP-----QEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 170 LLLLDEPMGALD-----------KKLRDRmqlevvDIlervGvtcVMVT-HDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG1137 157 FILLDEPFAGVDpiavadiqkiiRHLKER------GI----G---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
....*..
gi 1314858832 238 YEHPTTR 244
Cdd:COG1137 224 LNNPLVR 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-237 |
1.63e-50 |
|
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: 168.70 E-value: 1.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP-INMMFQ 98
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRrIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1314858832 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
35-176 |
2.54e-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: 165.51 E-value: 2.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQ--VPPYLRPINMMFQSYALFPHMTVEQNI 112
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 113 AFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRK----PHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
18-213 |
4.72e-50 |
|
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: 166.89 E-value: 4.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP-YLRPINMM 96
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIasRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1314858832 177 MGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEA 213
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLEL 194
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-237 |
7.45e-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: 166.84 E-value: 7.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP---INMM 96
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFPHMTVEQNIAFGLKqdKLPKAEIASRVNEMLGLV-HMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAY--ARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 176 PMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:cd03224 159 PSEGLAPKIVEEI-FEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
20-229 |
1.22e-49 |
|
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: 165.85 E-value: 1.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQS 99
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 YALFPHMTVEQNIAFGLKQDKLPKaeiaSRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 180 LD----KKLRDRMQLevvdiLERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:cd03268 157 LDpdgiKELRELILS-----LRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
17-239 |
1.57e-49 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 167.86 E-value: 1.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVP-PYLRP- 92
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIRKk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 INMMFQSY-ALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
Cdd:PRK13632 85 IGIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 172 LLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPEEIYE 239
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
17-244 |
1.59e-49 |
|
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: 166.70 E-value: 1.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP---I 93
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSYALFPHMTVEQNIAFGLKQDKlPKAEIASRVNEMLGLV-HMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 173 LDEP-MGaLDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
Cdd:COG0410 160 LDEPsLG-LAPLIVE----EIFEIIRRLnreGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVR 230
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
37-268 |
2.15e-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: 169.91 E-value: 2.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLS------QVPPYLRPINMMFQSYALFPHMTVEQ 110
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdsrkgiFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 111 NIAFGLKQDKLPKAEIA-SRVNEMLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDrmq 189
Cdd:TIGR02142 95 NLRYGMKRARPSERRISfERVIELLGIGHLLG---RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 190 lEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYsAEFIGSVNVFEGVLKE-RQ 264
Cdd:TIGR02142 169 -EILPYLERLhaefGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW-LAREDQGSLIEGVVAEhDQ 246
|
....
gi 1314858832 265 EDGL 268
Cdd:TIGR02142 247 HYGL 250
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
19-240 |
2.75e-49 |
|
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: 166.32 E-value: 2.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSY-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVP-----PYLRP 92
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkklrKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 INMMFQSYALFPHMTVEQNI---AFGLKQ------DKLPKAEIAsRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARS 163
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgRLGYKPtwrsllGRFSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 164 LAKRPKLLLLDEPMGALDKKLRDRmqleVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQ----VMDYLKRInkedGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
.
gi 1314858832 240 H 240
Cdd:TIGR02315 236 E 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
20-227 |
1.03e-48 |
|
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: 162.17 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP-YLRP-INM 95
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLeSLRKnIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYALFpHMTVEQNIafglkqdklpkaeiasrvnemlglvhmqefakrkphqLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 176 PMGALDKKLRDRmqleVVDILERV--GVTCVMVTHDqEEAMTMAGRIAIMNRGK 227
Cdd:cd03228 123 ATSALDPETEAL----ILEALRALakGKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-237 |
4.71e-48 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 169.81 E-value: 4.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSqvppYLRP---- 92
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR----FRSPrdaq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 ---INMMFQSYALFPHMTVEQNIAFGLKQDKLP---KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
Cdd:COG1129 78 aagIAIIHQELNLVPNLSVAENIFLGREPRRGGlidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314858832 167 RPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG1129 158 DARVLILDEPTASLTEREVERL-FRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-238 |
4.79e-48 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 164.45 E-value: 4.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYD-----GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPIN 94
Cdd:PRK13637 3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 95 ----MMFQ--SYALFPHmTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM--QEFAKRKPHQLSGGQRQRVALARSLAK 166
Cdd:PRK13637 83 kkvgLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 167 RPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
21-227 |
5.36e-48 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 160.10 E-value: 5.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 21 EIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPylrpinmmfqsy 100
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 101 alfphmtveqniafglkqdklpkaeiaSRVNEMLGLVhmqefakrkpHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
Cdd:cd00267 69 ---------------------------EELRRRIGYV----------PQLSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1314858832 181 DKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:cd00267 112 DPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-271 |
5.72e-48 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 164.51 E-value: 5.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP----YL---Rp 92
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRrrigYLpeeR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 inmmfqsyALFPHMTV-EQNIAFG-LKQdkLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
Cdd:COG4152 81 --------GLYPKMKVgEQLVYLArLKG--LSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 171 LLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE-HPTTRYSAEF 249
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRqFGRNTLRLEA 229
|
250 260
....*....|....*....|....*.
gi 1314858832 250 IGSVNVFE---GVLK-ERQEDGLVLD 271
Cdd:COG4152 230 DGDAGWLRalpGVTVvEEDGDGAELK 255
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-241 |
7.16e-48 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 162.90 E-value: 7.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 10 AKTRKALTPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLL----RMLAgfEQPSA---GQIMLDGVD 82
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMND--LIPGArveGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 83 L--SQVPPYL--RPINMMFQSYALFPhMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQ----LSGG 153
Cdd:COG1117 80 IydPDVDVVElrRRVGMVFQKPNPFP-KSIYDNVAYGLRlHGIKSKSELDEIVEESLRKAALWDEVKDRLKKsalgLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 154 QRQRVALARSLAKRPKLLLLDEPMGALD-----------KKLRDRMqlevvdilervgvTCVMVTHDQEEAMTMAGRIAI 222
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDpistakieeliLELKKDY-------------TIVIVTHNMQQAARVSDYTAF 225
|
250
....*....|....*....
gi 1314858832 223 MNRGKFVQIGEPEEIYEHP 241
Cdd:COG1117 226 FYLGELVEFGPTEQIFTNP 244
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-229 |
7.58e-48 |
|
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: 159.52 E-value: 7.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGvdlsqvppylRPINmmFQS 99
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG----------KEVS--FAS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 yalfphmtveqniafglkqdklPKAEIASRVnemlGLVhmqefakrkpHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:cd03216 69 ----------------------PRDARRAGI----AMV----------YQLSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314858832 180 LDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:cd03216 113 LTPAEVERL-FKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-246 |
1.58e-47 |
|
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: 169.09 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDG----QHAVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLAGFEQPSAGQIMLDGVDLSQVPP 88
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 89 Y-LR-----PINMMFQ--SYALFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQEFAKR---KPHQLSGGQRQ 156
Cdd:COG4172 84 ReLRrirgnRIAMIFQepMTSLNPLHTIGKQIAEVLRlHRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 157 RVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDIL----ERVGVTCVMVTHDqeeaMT----MAGRIAIMNRGKF 228
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTV----QAQILDLLkdlqRELGMALLLITHD----LGvvrrFADRVAVMRQGEI 235
|
250
....*....|....*...
gi 1314858832 229 VQIGEPEEIYEHPTTRYS 246
Cdd:COG4172 236 VEQGPTAELFAAPQHPYT 253
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-238 |
2.30e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 162.21 E-value: 2.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDG---QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQ--VPPYLRPI 93
Cdd:PRK13650 4 IIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSY-ALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:PRK13650 84 GMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 173 LDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEaMTMAGRIAIMNRGKFVQIGEPEEIY 238
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
21-228 |
3.54e-47 |
|
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: 159.62 E-value: 3.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 21 EIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYlrpINMMFQSY 100
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR---IGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 101 AL---FPhMTVEQNIAFGLKQD----KLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:cd03235 78 SIdrdFP-ISVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 174 DEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
Cdd:cd03235 157 DEPFAGVDPK----TQEDIYELLRELrreGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-232 |
6.19e-47 |
|
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: 159.46 E-value: 6.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYD----GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVP-PYLRPI 93
Cdd:cd03266 1 MITADALTKRFRdvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSYALFPHMTVEQNIAF-----GLKQDklpkaEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYfaglyGLKGD-----ELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 169 KLLLLDEPMGALDkKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03266 156 PVLLLDEPTTGLD-VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-240 |
6.54e-47 |
|
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: 168.01 E-value: 6.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 3 DAIPRPQAKTRKALTPLLEIRNLTKSY-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGV 81
Cdd:COG4988 320 PAAPAGTAPLPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 82 DLSQVPP--YLRPINMMFQSYALFpHMTVEQNIAFGlkqdkLPKAEIAsRVNEMLGLVHMQEFAKRKPH----------- 148
Cdd:COG4988 400 DLSDLDPasWRRQIAWVPQNPYLF-AGTIRENLRLG-----RPDASDE-ELEAALEAAGLDEFVAALPDgldtplgeggr 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 149 QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrMQLE--VVDILERV--GVTCVMVTHDqEEAMTMAGRIAIMN 224
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLD------AETEaeILQALRRLakGRTVILITHR-LALLAQADRILVLD 545
|
250
....*....|....*.
gi 1314858832 225 RGKFVQIGEPEEIYEH 240
Cdd:COG4988 546 DGRIVEQGTHEELLAK 561
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
17-252 |
1.53e-46 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 159.58 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYdGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDG--------------- 80
Cdd:COG4598 6 PPALEVRDLHKSF-GDLEVlKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdrdgelvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 81 VDLSQVPPYLRPINMMFQSYALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVA 159
Cdd:COG4598 85 ADRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 160 LARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPELVGEV-LKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFG 243
|
250
....*....|...
gi 1314858832 240 HPTTRYSAEFIGS 252
Cdd:COG4598 244 NPKSERLRQFLSS 256
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-244 |
4.15e-46 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 160.52 E-value: 4.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQ----------HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQV 86
Cdd:PRK11308 3 QPLLQAIDLKKHYPVKrglfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 87 PPYL-----RPINMMFQS-YA-LFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQR 157
Cdd:PRK11308 83 DPEAqkllrQKIQIVFQNpYGsLNPRKKVGQILEEPLLiNTSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 158 VALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK11308 163 IAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
250
....*....|
gi 1314858832 238 YE---HPTTR 244
Cdd:PRK11308 243 FNnprHPYTQ 252
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-236 |
6.13e-46 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 157.97 E-value: 6.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPY----LRPIn 94
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarRRAV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 95 mMFQSYAL-FPhMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLA-------K 166
Cdd:COG4559 80 -LPQHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 167 RPKLLLLDEPMGALDKKLrdrmQLEVVDIL-----ERVGVTCVMvtHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
Cdd:COG4559 158 GPRWLFLDEPTSALDLAH----QHAVLRLArqlarRGGGVVAVL--HDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-230 |
6.33e-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: 158.04 E-value: 6.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYD-----GQHA----VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP- 88
Cdd:TIGR02769 2 LLEVRDVTHTYRtgglfGAKQrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 89 ----YLRPINMMFQ-SYALF-PHMTVEQNIAFGLKQ-DKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVAL 160
Cdd:TIGR02769 82 qrraFRRDVQLVFQdSPSAVnPRMTVRQIIGEPLRHlTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 161 ARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILE----RVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVL----QAVILELLRklqqAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-241 |
1.88e-45 |
|
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: 164.17 E-value: 1.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 4 AIPRPQAKTRKALTPLLEIRNLTKSYDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGV 81
Cdd:COG4987 318 AVTEPAEPAPAPGGPSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGV 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 82 DLSQVPP--YLRPINMMFQSYALFpHMTVEQNIAFGlkqdklpkAEIAS--RVNEMLGLVHMQEFAKRKPH--------- 148
Cdd:COG4987 398 DLRDLDEddLRRRIAVVPQRPHLF-DTTLRENLRLA--------RPDATdeELWAALERVGLGDWLAALPDgldtwlgeg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 149 --QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR-MQlevvDILERV-GVTCVMVTHDqEEAMTMAGRIAIMN 224
Cdd:COG4987 469 grRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAlLA----DLLEALaGRTVLLITHR-LAGLERMDRILVLE 543
|
250
....*....|....*..
gi 1314858832 225 RGKFVQIGEPEEIYEHP 241
Cdd:COG4987 544 DGRIVEQGTHEELLAQN 560
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-244 |
7.99e-45 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 155.23 E-value: 7.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDG---------QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVP 87
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 88 -----PYLRPINMMFQSY--ALFPHMTVEQNIAFGLKQ-DKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQRV 158
Cdd:PRK10419 81 raqrkAFRRDIQMVFQDSisAVNPRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 159 ALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ---I 231
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVL----QAGVIRLLKKLqqqfGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqpV 236
|
250
....*....|...
gi 1314858832 232 GEPEEiYEHPTTR 244
Cdd:PRK10419 237 GDKLT-FSSPAGR 248
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
19-227 |
3.36e-44 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 152.12 E-value: 3.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSY-DGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP----YL 90
Cdd:TIGR02211 1 LLKCENLGKRYqEGKLDTRvlkGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSneraKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 91 RPINMMF--QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
Cdd:TIGR02211 81 RNKKLGFiyQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 169 KLLLLDEPMGALDKklrdRMQLEVVDILERV----GVTCVMVTHDqeeaMTMAGRIAI---MNRGK 227
Cdd:TIGR02211 161 SLVLADEPTGNLDN----NNAKIIFDLMLELnrelNTSFLVVTHD----LELAKKLDRvleMKDGQ 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-236 |
3.79e-44 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 153.39 E-value: 3.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYL--RPINM 95
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYAL-FPhMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLA------KRP 168
Cdd:PRK13548 81 LPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 169 KLLLLDEPMGALDKklrdRMQLEVVDILER------VGVTCVMvtHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
Cdd:PRK13548 160 RWLLLDEPTSALDL----AHQHHVLRLARQlahergLAVIVVL--HDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-236 |
6.27e-44 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 158.65 E-value: 6.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDG--VDLSQvppylrP-- 92
Cdd:COG3845 3 PPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRS------Prd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 -----INMMFQSYALFPHMTVEQNIAFGLKQDK---LPKAEIASRVNEMlglvhMQEF-----AKRKPHQLSGGQRQRVA 159
Cdd:COG3845 77 aialgIGMVHQHFMLVPNLTVAENIVLGLEPTKggrLDRKAARARIREL-----SERYgldvdPDAKVEDLSVGEQQRVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 160 LARSLAKRPKLLLLDEP------------MGALdKKLRDRmqlevvdilervGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:COG3845 152 ILKALYRGARILILDEPtavltpqeadelFEIL-RRLAAE------------GKSIIFITHKLREVMAIADRVTVLRRGK 218
|
....*....
gi 1314858832 228 FVQIGEPEE 236
Cdd:COG3845 219 VVGTVDTAE 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-250 |
2.19e-43 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 151.06 E-value: 2.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQI-----MLDG-VDLSQVPPYLRP- 92
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTaRSLSQQKGLIRQl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 ---INMMFQSYALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
Cdd:PRK11264 84 rqhVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 169 KLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAE 248
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEV-LNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
..
gi 1314858832 249 FI 250
Cdd:PRK11264 243 FL 244
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
20-232 |
2.27e-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: 2.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPylRPINMMFQS 99
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR--NRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 YALFPHMTV-EQNIAFG-LKqdKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
Cdd:cd03269 79 RGLYPKMKViDQLVYLAqLK--GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 178 GALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03269 157 SGLDPVNVELL-KDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-247 |
3.31e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 151.38 E-value: 3.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSY-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYL----RPI 93
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLlevrKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSY--ALFPHmTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
Cdd:PRK13639 81 GIVFQNPddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 172 LLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSA 247
Cdd:PRK13639 160 VLDEPTSGLDPMGASQI-MKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKA 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-242 |
1.07e-42 |
|
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: 155.73 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDGQ-----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIML----DGVDLSQVPP 88
Cdd:TIGR03269 278 PIIKVRNVSKRYISVdrgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 89 YLRP-----INMMFQSYALFPHMTVEQNI--AFGLKqdkLPKaEIASR----VNEMLGLV--HMQEFAKRKPHQLSGGQR 155
Cdd:TIGR03269 358 DGRGrakryIGILHQEYDLYPHRTVLDNLteAIGLE---LPD-ELARMkaviTLKMVGFDeeKAEEILDKYPDELSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 156 QRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
....*..
gi 1314858832 236 EIYEHPT 242
Cdd:TIGR03269 514 EIVEELT 520
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-237 |
1.29e-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: 148.44 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP---INMM 96
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAragIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHmqEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVLK--EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314858832 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-229 |
1.60e-42 |
|
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: 147.74 E-value: 1.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYL--RPINM 95
Cdd:cd03245 3 IEFRNVSFSYPNQeiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYALFpHMTVEQNIAFGlkqdkLPKAEIAS--RVNEMLGLvhmQEFAKRKPH-----------QLSGGQRQRVALAR 162
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLG-----APLADDERilRAAELAGV---TDFVNKHPNgldlqigergrGLSGGQRQAVALAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314858832 163 SLAKRPKLLLLDEPMGALD----KKLRDRMQLEVVDIlervgvTCVMVTHDQeEAMTMAGRIAIMNRGKFV 229
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDmnseERLKERLRQLLGDK------TLIIITHRP-SLLDLVDRIIVMDSGRIV 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
21-229 |
6.97e-42 |
|
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: 145.48 E-value: 6.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 21 EIRNLTKSY-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQvPPYLRPINMMFQS 99
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 --YALFPHmTVEQNIAFGLKqdklPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
Cdd:cd03226 80 vdYQLFTD-SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 178 GALDkklRDRMQL--EVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:cd03226 155 SGLD---YKNMERvgELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-236 |
1.60e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 153.40 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 7 RPQAKTRKALTPLLEIRNLTKSYDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQ 85
Cdd:COG1132 327 PPGAVPLPPVRGEIEFENVSFSYPGDRPVlKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 86 VPP--YLRPINMMFQSYALFpHMTVEQNIAFGlkqdkLPKAEIAsRVNEMLGLVHMQEFAKRKPH-----------QLSG 152
Cdd:COG1132 407 LTLesLRRQIGVVPQDTFLF-SGTIRENIRYG-----RPDATDE-EVEEAAKAAQAHEFIEALPDgydtvvgergvNLSG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 153 GQRQRVALARSLAKRPKLLLLDEPMGALD--------KKLRDRMQlevvdilervGVTCVMVTH--------Dqeeamtm 216
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDtetealiqEALERLMK----------GRTTIVIAHrlstirnaD------- 542
|
250 260
....*....|....*....|
gi 1314858832 217 agRIAIMNRGKFVQIGEPEE 236
Cdd:COG1132 543 --RILVLDDGRIVEQGTHEE 560
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
34-238 |
2.05e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 146.77 E-value: 2.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLS---QVPPYLRPINMMFQSyalfPH----- 105
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeeNLWDIRNKAGMVFQN----PDnqiva 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 106 MTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
Cdd:PRK13633 101 TIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1314858832 186 DRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIY 238
Cdd:PRK13633 181 REVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-245 |
5.98e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 145.52 E-value: 5.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSY-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVD---LSQVPPYLRPIN 94
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDtgdFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 95 MMFQS-YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 174 DEPMGALDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEaMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
Cdd:PRK13644 161 DEVTSMLDPD-SGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-235 |
1.23e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 144.49 E-value: 1.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPY-LRP-INMM 96
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSkVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSY--ALFPhMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:PRK13647 85 FQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314858832 175 EPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
Cdd:PRK13647 164 EPMAYLDPRGQETL-MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-253 |
2.79e-40 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 145.23 E-value: 2.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDGQ-------------HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDL- 83
Cdd:PRK15079 7 VLLEVADLKVHFDIKdgkqwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 84 ----SQVPPYLRPINMMFQS--YALFPHMTVEQNIAFGLK--QDKLPKAEIASRVNEML---GLvhMQEFAKRKPHQLSG 152
Cdd:PRK15079 87 gmkdDEWRAVRSDIQMIFQDplASLNPRMTIGEIIAEPLRtyHPKLSRQEVKDRVKAMMlkvGL--LPNLINRYPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
Cdd:PRK15079 165 GQCQRIGIARALILEPKLIICDEPVSALDVSI----QAQVVNLLQQLqremGLSLIFIAHDLAVVKHISDRVLVMYLGHA 240
|
250 260
....*....|....*....|....*
gi 1314858832 229 VQIGEPEEIYEHPTTRYSAEFIGSV 253
Cdd:PRK15079 241 VELGTYDEVYHNPLHPYTKALMSAV 265
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
20-237 |
3.27e-40 |
|
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: 150.79 E-value: 3.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPY-LRP-INM 95
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdLRRnIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYALFpHMTVEQNIAFGL----KQDKLPKAEIAsrvnemlGLvhmQEFAKRKPH-----------QLSGGQRQRVAL 160
Cdd:TIGR03375 544 VPQDPRLF-YGTLRDNIALGApyadDEEILRAAELA-------GV---TEFVRRHPDgldmqigergrSLSGGQRQAVAL 612
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314858832 161 ARSLAKRPKLLLLDEPMGALDkklrDRMQLEVVDILERV--GVTCVMVTHDQeEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:TIGR03375 613 ARALLRDPPILLLDEPTSAMD----NRSEERFKDRLKRWlaGKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPKDQV 686
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
17-237 |
1.30e-39 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 140.99 E-value: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIM------LDGVDLSQvppyL 90
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWE----L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 91 RPiNMMFQSYALF----PHMTVEQNIA------FGLKQDklPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVAL 160
Cdd:COG1119 77 RK-RIGLVSPALQlrfpRDETVLDVVLsgffdsIGLYRE--PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 161 ARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDIL-ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELL-LALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
19-244 |
2.73e-39 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 141.06 E-value: 2.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDL-----SQVPPYLRPI 93
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSYALFPHMTVEQNIAFGLKQ-DKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 173 LDEP--------MGALDKklrdrmqleVVDILER-VGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTT 243
Cdd:PRK11831 167 FDEPfvgqdpitMGVLVK---------LISELNSaLGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP 237
|
.
gi 1314858832 244 R 244
Cdd:PRK11831 238 R 238
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
34-242 |
3.17e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 141.31 E-value: 3.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIML------DGVDLSQVPPYLRPINMMFQsyalFP-HM 106
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKPLRKKVGIVFQ----FPeHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 107 ----TVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
Cdd:PRK13634 98 lfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 182 KKLRdrmqLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPT 242
Cdd:PRK13634 178 PKGR----KEMMEMFYKLhkekGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-241 |
4.84e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 140.32 E-value: 4.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQ--VPPYLRPINM 95
Cdd:PRK13652 3 LIETRDLCYSYSGSkEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSY--ALFPhMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:PRK13652 83 VFQNPddQIFS-PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
21-237 |
6.81e-39 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 139.06 E-value: 6.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 21 EIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP--YLRPINMMFQ 98
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSreLAKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 SYALFPHMTVEQNIAFG---LKQDKLpKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:COG4604 83 ENHINSRLTVRELVAFGrfpYSKGRL-TAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 176 PMGALD-KKLRDRMQL--EVVDILERvgvTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG4604 162 PLNNLDmKHSVQMMKLlrRLADELGK---TVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-275 |
7.07e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 140.37 E-value: 7.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSY-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDG--VDLSQ--VPPYLRPI 93
Cdd:PRK13636 5 ILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRkgLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQS--YALFPhMTVEQNIAFGLKQDKLPKAEIASRVNEML---GLVHMqefaKRKP-HQLSGGQRQRVALARSLAKR 167
Cdd:PRK13636 85 GMVFQDpdNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALkrtGIEHL----KDKPtHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 168 PKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEhpttrySA 247
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA------EK 233
|
250 260 270
....*....|....*....|....*....|....*
gi 1314858832 248 EFIGSVNV-------FEGVLKERqeDGLVLDSPGL 275
Cdd:PRK13636 234 EMLRKVNLrlprighLMEILKEK--DGFVFDELDL 266
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
17-241 |
1.09e-38 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 138.97 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLrpINMM 96
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ--IARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 -----FQSYALFPHMTVEQNIAFGLKQD----------KLP-----KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQ 156
Cdd:PRK11300 81 gvvrtFQHVRLFREMTVIENLLVAQHQQlktglfsgllKTPafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
....*
gi 1314858832 237 IYEHP 241
Cdd:PRK11300 241 IRNNP 245
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-220 |
1.70e-38 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 137.64 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSY-DGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYL-- 90
Cdd:PRK11629 3 KILLQCDNLCKRYqEGSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 91 ----RPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
Cdd:PRK11629 83 elrnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 167 RPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDqeeaMTMAGRI 220
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHD----LQLAKRM 212
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-229 |
2.26e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 138.29 E-value: 2.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY-----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP-- 92
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 INMMFQSYAL--FPHMTVEQNIA------------FGLKQDKlpKAEIASRVNEM-LGLV-HMQEFAKrkphQLSGGQRQ 156
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrrglrRGLTKKR--RELFRELLATLgLGLEnRLDTKVG----LLSGGQRQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDR-MQLeVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALvLEL-TEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
20-227 |
3.01e-38 |
|
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: 135.04 E-value: 3.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY-DGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQV-PPYLRP-INM 95
Cdd:cd03246 1 LEVENVSFRYpGAEPPVlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWdPNELGDhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYALFPHmTVEQNIafglkqdklpkaeiasrvnemlglvhmqefakrkphqLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 176 PMGALDKKlRDRMQLEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRGK 227
Cdd:cd03246 123 PNSHLDVE-GERALNQAIAALKAAGATRIVIAH-RPETLASADRILVLEDGR 172
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
16-238 |
7.42e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 137.53 E-value: 7.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 16 LTPLLEIRNLTKSYDGQHAVDD---VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLS--QVPPYL 90
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 91 RPINMMFQSY-ALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
Cdd:PRK13642 81 RKIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314858832 170 LLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIY 238
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-239 |
1.09e-37 |
|
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: 135.44 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQV--PPYLRPINM 95
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYtlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYALFpHMTVEQNIAFGlkqdkLPKAEIAsRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSL 164
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYG-----RPGATRE-EVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 165 AKRPKLLLLDEPMGALDKKLRDRMQlevvDILER--VGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQ----AALERlmKNRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-240 |
1.54e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 136.42 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHA--VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIM-----LDGVDLSQVPPY 89
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFynnqaITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 90 lrpINMMFQS-YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
Cdd:PRK13648 85 ---IGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 169 KLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-229 |
2.38e-37 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 134.23 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSY-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLS-----QVPPYLRP 92
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 173 LDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:PRK10908 161 ADEPTGNLDDALSEGI-LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-245 |
3.29e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 134.97 E-value: 3.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-----EQPSAGQIMLDGVDL--SQVPP--YL 90
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIysPDVDPieVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 91 RPINMMFQSYALFPHMTVEQNIAFGLKQDKL--PKAEIASRVNEMLGLVHMQEFAKRK----PHQLSGGQRQRVALARSL 164
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRlndyPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 165 AKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP--- 241
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPehe 242
|
....*
gi 1314858832 242 -TTRY 245
Cdd:PRK14267 243 lTEKY 247
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
34-242 |
5.94e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 134.93 E-value: 5.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSA---GQIMLDGVDLSQ--VPPYLRPINMMFQSY-ALFPHMT 107
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAktVWDIREKVGIVFQNPdNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 108 VEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 188 MQLEVVDILERVGVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPEEIYEHPT 242
Cdd:PRK13640 182 ILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-229 |
2.24e-36 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 139.86 E-value: 2.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 16 LTPLLEIRNLTKSY---DGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP--- 88
Cdd:PRK10535 1 MTALLELKDIRRSYpsgEEQVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 89 -YLRP--INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLA 165
Cdd:PRK10535 81 aQLRRehFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 166 KRPKLLLLDEPMGALDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAmTMAGRIAIMNRGKFV 229
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGE----EVMAILHQLrdrGHTVIIVTHDPQVA-AQAERVIEIRDGEIV 222
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-237 |
2.73e-36 |
|
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: 138.73 E-value: 2.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 4 AIPRPQAKtrkaltplLEIRNLTKSYDGQHA--VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGV 81
Cdd:COG4618 323 PLPRPKGR--------LSVENLTVVPPGSKRpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 82 DLSQVPP--------YLrPinmmfQSYALFPHmTVEQNIA-FG-LKQDKLPKAEIASRVNEM-LGLvhmqefakrkP--- 147
Cdd:COG4618 395 DLSQWDReelgrhigYL-P-----QDVELFDG-TIAENIArFGdADPEKVVAAAKLAGVHEMiLRL----------Pdgy 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 148 --------HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD-----------KKLRDRmqlevvdilervGVTCVMVTH 208
Cdd:COG4618 458 dtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalaaaiRALKAR------------GATVVVITH 525
|
250 260
....*....|....*....|....*....
gi 1314858832 209 DQeEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG4618 526 RP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
28-214 |
3.45e-36 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 130.43 E-value: 3.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 28 SYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIML-DGVDLSQVPpylrpinmmfQSYAL---F 103
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRaGGARVAYVP----------QRSEVpdsL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 104 PhMTVEQNIAFGLKQDKLP----KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:NF040873 71 P-LTVRDLVAMGRWARRGLwrrlTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*
gi 1314858832 180 LDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAM 214
Cdd:NF040873 150 LDAESRERI-IALLAEEHARGATVVVVTHDLELVR 183
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-239 |
6.19e-36 |
|
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: 131.12 E-value: 6.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 21 EIRNLTKSYD---GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP--YLRPINM 95
Cdd:cd03249 2 EFKNVSFRYPsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLrwLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYALFPhMTVEQNIAFGLKQDKLPKAEIASRVNEmlglVHmqEFAKRKPH-----------QLSGGQRQRVALARSL 164
Cdd:cd03249 82 VSQEPVLFD-GTIAENIRYGKPDATDEEVEEAAKKAN----IH--DFIMSLPDgydtlvgergsQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 165 AKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
Cdd:cd03249 155 LRNPKILLLDEATSALDAE----SEKLVQEALDRAmkGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMA 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-278 |
9.09e-36 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 137.68 E-value: 9.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 6 PRPQAKTRKALTPLLEIRNLTKSYDGQ-----------HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAG 74
Cdd:PRK10261 300 PPIEQDTVVDGEPILQVRNLVTRFPLRsgllnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGG 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 75 QIMLDG--VDL---SQVPPYLRPINMMFQS-YA-LFPHMTVEQNIAFGLKQDKLPKAEIA-SRVNEMLGLVHMQ-EFAKR 145
Cdd:PRK10261 380 EIIFNGqrIDTlspGKLQALRRDIQFIFQDpYAsLDPRQTVGDSIMEPLRVHGLLPGKAAaARVAWLLERVGLLpEHAWR 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 146 KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNR 225
Cdd:PRK10261 460 YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYL 539
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1314858832 226 GKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGVLKERQEDGLVLDSPGLVHP 278
Cdd:PRK10261 540 GQIVEIGPRRAVFENPQHPYTRKLMAAVPVADPSRQRPQRVLLSDDLPSNIHL 592
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
16-236 |
2.33e-35 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 137.01 E-value: 2.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 16 LTPLLEIRNLTKSY--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLS--QVPPYLR 91
Cdd:TIGR03797 448 LSGAIEVDRVTFRYrpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAglDVQAVRR 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 92 PINMMFQSYALFPHmTVEQNIAFG--LKQDKlpkaeiASRVNEMLGLvhmQEFAKRKP---H--------QLSGGQRQRV 158
Cdd:TIGR03797 528 QLGVVLQNGRLMSG-SIFENIAGGapLTLDE------AWEAARMAGL---AEDIRAMPmgmHtvisegggTLSGGQRQRL 597
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 159 ALARSLAKRPKLLLLDEPMGALDkklrDRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEE 236
Cdd:TIGR03797 598 LIARALVRKPRILLFDEATSALD----NRTQAIVSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDE 670
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
20-250 |
2.89e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 130.09 E-value: 2.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYdGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP---------- 88
Cdd:PRK10619 6 LNVIDLHKRY-GEHEVlKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 89 ----YLRP-INMMFQSYALFPHMTVEQNIAFGLKQD-KLPKAEIASRVNEMLGLVHMQEFAKRK-PHQLSGGQRQRVALA 161
Cdd:PRK10619 85 nqlrLLRTrLTMVFQHFNLWSHMTVLENVMEAPIQVlGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 162 RSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEV-LRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
....*....
gi 1314858832 242 TTRYSAEFI 250
Cdd:PRK10619 244 QSPRLQQFL 252
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-236 |
8.54e-35 |
|
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: 127.73 E-value: 8.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 21 EIRNLTKSYDGQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPY-LRP-INMMF 97
Cdd:cd03254 4 EFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKsLRSmIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 98 QSYALFPHmTVEQNIAFGlkqDKLPKAEiasRVNEMLGLVHMQEFAKRKP-----------HQLSGGQRQRVALARSLAK 166
Cdd:cd03254 84 QDTFLFSG-TIMENIRLG---RPNATDE---EVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 167 RPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDE 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-223 |
1.05e-34 |
|
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: 133.95 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 3 DAIPRPQAKTRKALT---PLLEIRNLTKSYDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIML 78
Cdd:TIGR02857 302 DAAPRPLAGKAPVTAapaSSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 79 DGVDLSQVPP--YLRPINMMFQSYALFPHmTVEQNIAFGLK-------QDKLPKAEIASRVNEmLGLVHMQEFAKRkPHQ 149
Cdd:TIGR02857 382 NGVPLADADAdsWRDQIAWVPQHPFLFAG-TIAENIRLARPdasdaeiREALERAGLDEFVAA-LPQGLDTPIGEG-GAG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrDRMQLEVVDILERV--GVTCVMVTHDqEEAMTMAGRIAIM 223
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLD----AETEAEVLEALRALaqGRTVLLVTHR-LALAALADRIVVL 529
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-245 |
1.27e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 128.11 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-----EQPSAGQIMLDGVDLSQVPPYL--RP 92
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIElrRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 INMMFQSYALFPHMTVEQNIAFGLKQDKL--PKAEIASRVNEMLGLVHMQEFAKRK----PHQLSGGQRQRVALARSLAK 166
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 167 RPKLLLLDEPMGALDKKlrDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP----T 242
Cdd:PRK14247 164 QPEVLLADEPTANLDPE--NTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPrhelT 241
|
...
gi 1314858832 243 TRY 245
Cdd:PRK14247 242 EKY 244
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
34-240 |
1.44e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 128.97 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGV-------DLSQVPPYLRPINMMFQ--SYALFP 104
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipanlkKIKEVKRLRKEIGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 105 HmTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
Cdd:PRK13645 106 E-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314858832 184 LRDrmqlEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:PRK13645 185 GEE----DFINLFERLnkeyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
15-240 |
1.49e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 129.15 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 15 ALTPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP-I 93
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 174 DEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-237 |
2.02e-34 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 127.32 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPY---LRPINM 95
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYALFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314858832 175 EPMGALDKklrdrmqLEVVDI------LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK10895 163 EPFAGVDP-------ISVIDIkriiehLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-237 |
4.11e-34 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 126.67 E-value: 4.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPylrpiNMMFQS 99
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-----RQLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 YALFP--HMT-----VEQNIAFG----------LKQDKlpkaeiASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALAR 162
Cdd:PRK11231 78 LALLPqhHLTpegitVRELVAYGrspwlslwgrLSAED------NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 163 SLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDIN----HQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-240 |
5.88e-34 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 125.96 E-value: 5.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSY----------------------DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAG 74
Cdd:COG1134 2 SSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 75 QIMLDGvdlsQVPPylrPINMM--FQsyalfPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSG 152
Cdd:COG1134 82 RVEVNG----RVSA---LLELGagFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 153 GQRQRVALARSLAKRPKLLLLDEPMGALD----KKLRDRMQlevvDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
Cdd:COG1134 150 GMRARLAFAVATAVDPDILLVDEVLAVGDaafqKKCLARIR----ELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
250
....*....|..
gi 1314858832 229 VQIGEPEEIYEH 240
Cdd:COG1134 225 VMDGDPEEVIAA 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-250 |
9.22e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 125.92 E-value: 9.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 16 LTPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSaGQIMLDG-VDLSQVPPYLRPIN 94
Cdd:PRK14258 4 LIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrVEFFNQNIYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 95 ---------MMFQSYALFPhMTVEQNIAFGLKQDKL-PKAEIASRVNEMLGLVHMQEFAKRKPHQ----LSGGQRQRVAL 160
Cdd:PRK14258 83 lnrlrrqvsMVHPKPNLFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 161 ARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIM----NR-GKFVQIGEPE 235
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgneNRiGQLVEFGLTK 241
|
250
....*....|....*
gi 1314858832 236 EIYEHPTTRYSAEFI 250
Cdd:PRK14258 242 KIFNSPHDSRTREYV 256
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-242 |
1.88e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 126.50 E-value: 1.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 11 KTRKALTPL-----LEIRNLTKSYDGQH-----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIML-- 78
Cdd:PRK13631 8 KKLKVPNPLsddiiLRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 79 ----DGVDLSQVPPYLRP------------INMMFQ--SYALFPHmTVEQNIAFG---LKQDKLPKAEIASRVNEMLGLv 137
Cdd:PRK13631 88 iyigDKKNNHELITNPYSkkiknfkelrrrVSMVFQfpEYQLFKD-TIEKDIMFGpvaLGVKKSEAKKLAKFYLNKMGL- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 138 hMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMA 217
Cdd:PRK13631 166 -DDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAKANNKTVFVITHTMEHVLEVA 243
|
250 260
....*....|....*....|....*
gi 1314858832 218 GRIAIMNRGKFVQIGEPEEIYEHPT 242
Cdd:PRK13631 244 DEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-228 |
4.26e-33 |
|
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: 121.77 E-value: 4.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTksydGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPY-LRPINMM 96
Cdd:cd03215 3 PVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 F-----QSYALFPHMTVEQNIAFglkqdklpkaeiasrvnemlglvhmqefakrkPHQLSGGQRQRVALARSLAKRPKLL 171
Cdd:cd03215 79 YvpedrKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 172 LLDEPMGALD--------KKLRDrmqlevvdiLERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
Cdd:cd03215 127 ILDEPTRGVDvgakaeiyRLIRE---------LADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-244 |
4.72e-33 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 126.14 E-value: 4.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIrNLTKSYdGQHAVDdVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDG---VDLSQ---VPPYLRPI 93
Cdd:PRK11144 2 LEL-NFKQQL-GDLCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgicLPPEKRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSYALFPHMTVEQNIAFGLKQDKlpKAEIASRVnEMLGLVHMqefAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:PRK11144 79 GYVFQDARLFPHYKVRGNLRYGMAKSM--VAQFDKIV-ALLGIEPL---LDRYPGSLSGGEKQRVAIGRALLTAPELLLM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 174 DEPMGALDKKlRDRmqlEVVDILER----VGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
Cdd:PRK11144 153 DEPLASLDLP-RKR---ELLPYLERlareINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-237 |
1.22e-32 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 129.47 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 5 IPRPQAKTRKAltPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDG--VD 82
Cdd:NF033858 254 IPPRPADDDDE--PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVD 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 83 lsqvppylrPINM--------MFQSYALFPHMTVEQNIA-----FGlkqdkLPKAEIASRVNEMLGLVHMQEFAKRKPHQ 149
Cdd:NF033858 332 ---------AGDIatrrrvgyMSQAFSLYGELTVRQNLElharlFH-----LPAAEIAARVAEMLERFDLADVADALPDS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFV 229
Cdd:NF033858 398 LPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVL 476
|
....*...
gi 1314858832 230 QIGEPEEI 237
Cdd:NF033858 477 ASDTPAAL 484
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
20-236 |
1.42e-32 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 121.95 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYD-GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVP-PYLR-PINMM 96
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTlDSLRrAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFpHMTVEQNIAFG----LKQDKLPKAEIAsrvnemlglvHMQEFAKRKPHQ-----------LSGGQRQRVALA 161
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYGrpdaTDEEVIEAAKAA----------QIHDKIMRFPDGydtivgerglkLSGGEKQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 162 RSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV--GVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEE 236
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTH----TEREIQAALRDVskGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-237 |
2.19e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 123.27 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQ-----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVD------------ 82
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 83 --------------LSQVPPYLRPINMMFQ--SYALFpHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM-QEFAKR 145
Cdd:PRK13651 83 vleklviqktrfkkIKKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 146 KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNR 225
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEI-LEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250
....*....|..
gi 1314858832 226 GKFVQIGEPEEI 237
Cdd:PRK13651 241 GKIIKDGDTYDI 252
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-209 |
2.83e-32 |
|
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: 127.09 E-value: 2.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 8 PQAKTRKALTPLLEIRNLTKSYDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQV 86
Cdd:TIGR02868 323 PAAGAVGLGKPTLELRDLSAGYPGAPPVlDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 87 PPYL--RPINMMFQSYALFpHMTVEQNIAFGLKQ-------DKLPKAEIASRVNEMLGLVH--MQEFAKRkphqLSGGQR 155
Cdd:TIGR02868 403 DQDEvrRRVSVCAQDAHLF-DTTVRENLRLARPDatdeelwAALERVGLADWLRALPDGLDtvLGEGGAR----LSGGER 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 156 QRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHD 209
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
30-237 |
3.99e-32 |
|
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: 121.05 E-value: 3.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP--YLRPINMMFQSYALFpHMT 107
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPawLRRQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 108 VEQNIAFGlkqDKLPKAEiasRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:cd03252 92 IRDNIALA---DPGMSME---RVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314858832 177 MGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEI 237
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
19-213 |
4.13e-32 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 120.65 E-value: 4.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSY-DGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP-- 92
Cdd:PRK10584 6 IVEVHHLKKSVgQGEHELSiltGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAkl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 ----INMMFQSYALFPHMTVEQNIafglkqdKLP-----KAEIASRVN--EMLGLVHMQEFAKRKPHQLSGGQRQRVALA 161
Cdd:PRK10584 86 rakhVGFVFQSFMLIPTLNALENV-------ELPallrgESSRQSRNGakALLEQLGLGKRLDHLPAQLSGGEQQRVALA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 162 RSLAKRPKLLLLDEPMGALDKKLRDRmqleVVDIL----ERVGVTCVMVTHDQEEA 213
Cdd:PRK10584 159 RAFNGRPDVLFADEPTGNLDRQTGDK----IADLLfslnREHGTTLILVTHDLQLA 210
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-240 |
5.17e-32 |
|
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: 126.75 E-value: 5.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 3 DAIPRPQAKTR--KALTPLLEIRNLTKSY--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIML 78
Cdd:TIGR02203 312 DSPPEKDTGTRaiERARGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 79 DGVDLSQvppYL-----RPINMMFQSYALFPHmTVEQNIAFGlKQDKLPKAEIasrvNEMLGLVHMQEFAKRKP---HQ- 149
Cdd:TIGR02203 392 DGHDLAD---YTlaslrRQVALVSQDVVLFND-TIANNIAYG-RTEQADRAEI----ERALAAAYAQDFVDKLPlglDTp 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 150 -------LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQlevvDILERV--GVTCVMVTHdQEEAMTMAGRI 220
Cdd:TIGR02203 463 igengvlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQ----AALERLmqGRTTLVIAH-RLSTIEKADRI 537
|
250 260
....*....|....*....|
gi 1314858832 221 AIMNRGKFVQIGEPEEIYEH 240
Cdd:TIGR02203 538 VVMDDGRIVERGTHNELLAR 557
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
17-253 |
6.29e-32 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 120.80 E-value: 6.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSqvppyLRPINMM 96
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQ-----LRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFPHMT----VEQNIAFGLKQDKLPKAEIASRVneM-LGLVH-----------MQEF---AKR---KPHQLSGGQ 154
Cdd:PRK11701 79 SEAERRRLLRTewgfVHQHPRDGLRMQVSAGGNIGERL--MaVGARHygdiratagdwLERVeidAARiddLPTTFSGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 155 RQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqlevVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARL----LDLLRGLvrelGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
250 260
....*....|....*....|...
gi 1314858832 231 IGEPEEIYEHPTTRYSAEFIGSV 253
Cdd:PRK11701 233 SGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
16-239 |
6.32e-32 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 126.98 E-value: 6.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 16 LTPLLEIRNLTKSYD--GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYL--R 91
Cdd:TIGR03796 474 LSGYVELRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVlaN 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 92 PINMMFQSYALFpHMTVEQNIAfgLKQDKLPKAEI--ASRVNEMLGLVhmqefaKRKPHQ-----------LSGGQRQRV 158
Cdd:TIGR03796 554 SVAMVDQDIFLF-EGTVRDNLT--LWDPTIPDADLvrACKDAAIHDVI------TSRPGGydaelaegganLSGGQRQRL 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 159 ALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERVGVTCVMVTH------DQEEamtmagrIAIMNRGKFVQIG 232
Cdd:TIGR03796 625 EIARALVRNPSILILDEATSALDPE----TEKIIDDNLRRRGCTCIIVAHrlstirDCDE-------IIVLERGKVVQRG 693
|
....*..
gi 1314858832 233 EPEEIYE 239
Cdd:TIGR03796 694 THEELWA 700
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
34-239 |
1.14e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 120.99 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLS------QVPPYLRPINMMFQsyalFPHM- 106
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQ----FPESq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 107 ----TVEQNIAFGLKQDKLPKAE---IASRVNEMLGLvhMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:PRK13643 97 lfeeTVLKDVAFGPQNFGIPKEKaekIAAEKLEMVGL--ADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 180 LDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
Cdd:PRK13643 175 LDPKARIEM-MQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-241 |
1.18e-31 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 120.66 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSY-------DGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPY 89
Cdd:PRK15112 4 LLEVRNLSKTFryrtgwfRRQTveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 90 LRP--INMMFQ--SYALFPHMTVEQNIAFGLKQD-KLPKAEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARS 163
Cdd:PRK15112 84 YRSqrIRMIFQdpSTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 164 LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVThdQEEAMT--MAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT--QHLGMMkhISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-250 |
1.89e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 119.50 E-value: 1.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-----EQPSAGQIMLDG----------VD 82
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGhniysprtdtVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 83 LSqvppylRPINMMFQSYALFPhMTVEQNIAFGLKQDKLP-KAEIASRVNEMLGLVHMQEFAKRKPHQ----LSGGQRQR 157
Cdd:PRK14239 84 LR------KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKdKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 158 VALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
250
....*....|...
gi 1314858832 238 YEHPTTRYSAEFI 250
Cdd:PRK14239 235 FMNPKHKETEDYI 247
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
34-240 |
4.06e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 119.46 E-value: 4.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLS------QVPPYLRPINMMFQsyalFPHM- 106
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQIRKKVGLVFQ----FPESq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 107 ----TVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
Cdd:PRK13649 98 lfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1314858832 182 KKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:PRK13649 178 PKGRKEL-MTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-250 |
5.16e-31 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 123.66 E-value: 5.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSY-----------DGQHAVDDVSLTIYKGEIFALLGASGCGKST----LLRMLAgfeqpSAGQIMLDGV 81
Cdd:PRK15134 273 SPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 82 DL-----SQVPPYLRPINMMFQ--SYALFPHMTVEQNIAFGLK--QDKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLS 151
Cdd:PRK15134 348 PLhnlnrRQLLPVRHRIQVVFQdpNSSLNPRLNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTV----QAQILALLkslqQKHQLAYLFISHDLHVVRALCHQVIVLRQGE 503
|
250 260
....*....|....*....|...
gi 1314858832 228 FVQIGEPEEIYEHPTTRYSAEFI 250
Cdd:PRK15134 504 VVEQGDCERVFAAPQQEYTRQLL 526
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-226 |
7.06e-31 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 117.15 E-value: 7.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSY-----DGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLD----GVDLSQ 85
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 86 VPP----YLRPINMMFQSYAL--FPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEfakR----KPHQLSGGQR 155
Cdd:COG4778 82 ASPreilALRRRTIGYVSQFLrvIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPE---RlwdlPPATFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 156 QRVALARSLAKRPKLLLLDEPMGALDKKLRDRmqleVVDILERV---GVTCVMVTHDqEEAM-TMAGRIAIMNRG 226
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAV----VVELIEEAkarGTAIIGIFHD-EEVReAVADRVVDVTPF 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
18-295 |
7.98e-31 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 121.10 E-value: 7.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYL--RPINM 95
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYALFPHMTVEQNIAFGLK--QDKLPKAEIASR--VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGRTphRSRFDTWTETDRaaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 172 LLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRysAEFIG 251
Cdd:PRK09536 162 LLDEPTASLDINHQVRT-LELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLR--AAFDA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1314858832 252 SVNVFEgvlkerqedGLVLDSPgLVHPLKVDADASVVDNVPVHV 295
Cdd:PRK09536 239 RTAVGT---------DPATGAP-TVTPLPDPDRTEAAADTRVHV 272
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
34-251 |
2.37e-30 |
|
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: 115.93 E-value: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP----SAGQIMLDGVDLSQVPPYLRPINMMFQS--YALFPHMT 107
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 108 VEQNIAFGLKQ----DKLPKAEIASRVnEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
Cdd:TIGR02770 81 MGNHAIETLRSlgklSKQARALILEAL-EAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 184 lrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG 251
Cdd:TIGR02770 160 ----NQARVLKLLRELrqlfGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
27-232 |
2.43e-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: 115.71 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 27 KSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGvdlsQVPPYLRpINMMFQsyalfPHM 106
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----RVSSLLG-LGGGFN-----PEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 107 TVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
Cdd:cd03220 100 TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1314858832 187 RMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03220 180 KCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-237 |
2.84e-30 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 121.04 E-value: 2.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP---I 93
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAqlgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSYALFPHMTVEQNIAFGlkqdKLPK-----------AEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALAR 162
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIG----RHLTkkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 163 SLAKRPKLLLLDEPMGALDKKLRDRMQLeVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFL-IMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-240 |
3.38e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 118.39 E-value: 3.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 6 PRPQAKTRKALtpllEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVdlsQ 85
Cdd:PRK13536 32 SIPGSMSTVAI----DLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV---P 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 86 VPPYLRP----INMMFQSYALFPHMTVEQN-IAFGlKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVAL 160
Cdd:PRK13536 105 VPARARLararIGVVPQFDNLDLEFTVRENlLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 161 ARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE-IYE 239
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAlIDE 262
|
.
gi 1314858832 240 H 240
Cdd:PRK13536 263 H 263
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
17-212 |
4.30e-30 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 115.20 E-value: 4.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP--YLRPIN 94
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 95 MMFQSYALFPHmTVEQNIAF----------------GLKQDKLPKAEIASRVNEmlglvhmqefakrkphqLSGGQRQRV 158
Cdd:PRK10247 85 YCAQTPTLFGD-TVYDNLIFpwqirnqqpdpaifldDLERFALPDTILTKNIAE-----------------LSGGEKQRI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRmqleVVDILERV----GVTCVMVTHDQEE 212
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESNKHN----VNEIIHRYvreqNIAVLWVTHDKDE 200
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-257 |
4.45e-30 |
|
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: 120.68 E-value: 4.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQ--PSAGQIM-------------------- 77
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 78 -------------LDGVDLSQVPPY--LRPINMMFQ-SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQE 141
Cdd:TIGR03269 81 pcpvcggtlepeeVDFWNLSDKLRRriRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 142 FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIA 221
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 1314858832 222 IMNRGKFVQIGEPEEIyehpttrySAEFIGSVNVFE 257
Cdd:TIGR03269 241 WLENGEIKEEGTPDEV--------VAVFMEGVSEVE 268
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-240 |
4.73e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.51 E-value: 4.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 10 AKTRKALTPLLEIRNLTksydGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP- 88
Cdd:COG1129 247 KRAAAPGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPr 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 89 --------YL---RpinmmfQSYALFPHMTVEQNIA---------FGLkqdkLPKAEIASRVNEMlglvhMQEFAKRKPH 148
Cdd:COG1129 323 dairagiaYVpedR------KGEGLVLDLSIRENITlasldrlsrGGL----LDRRRERALAEEY-----IKRLRIKTPS 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 149 ------QLSGGQRQRVALARSLAKRPKLLLLDEP-----MGAldKKlrdrmqlEVVDILERV---GVTCVMVTHDQEEAM 214
Cdd:COG1129 388 peqpvgNLSGGNQQKVVLAKWLATDPKVLILDEPtrgidVGA--KA-------EIYRLIRELaaeGKAVIVISSELPELL 458
|
250 260
....*....|....*....|....*.
gi 1314858832 215 TMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:COG1129 459 GLSDRILVMREGRIVGELDREEATEE 484
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-246 |
6.37e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 121.37 E-value: 6.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 5 IPRPQAKTRKALTPLLEIRNLTKSYDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGV 81
Cdd:TIGR00958 464 IPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVpvlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 82 DLSQVP-PYL-RPINMMFQSYALFPHmTVEQNIAFGLkqDKLPKAEIASRVNEMLGLVHMQEFAK-------RKPHQLSG 152
Cdd:TIGR00958 544 PLVQYDhHYLhRQVALVGQEPVLFSG-SVRENIAYGL--TDTPDEEIMAAAKAANAHDFIMEFPNgydtevgEKGSQLSG 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKklrdRMQLEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMG 695
|
250
....*....|....
gi 1314858832 233 EPEEIYEHPTTRYS 246
Cdd:TIGR00958 696 THKQLMEDQGCYKH 709
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-266 |
8.11e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 120.33 E-value: 8.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLT-KSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPSAGQIMLDGVDLSQVPP--YLRPINMM 96
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPesWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFpHMTVEQNIAFGlkqdklpKAEIA-SRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSL 164
Cdd:PRK11174 429 GQNPQLP-HGTLRDNVLLG-------NPDASdEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARAL 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 165 AKRPKLLLLDEPMGALDKKLRDRmqleVVDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPt 242
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQL----VMQALNAAsrRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG- 574
|
250 260
....*....|....*....|....
gi 1314858832 243 trysaefigsvNVFEGVLKERQED 266
Cdd:PRK11174 575 -----------GLFATLLAHRQEE 587
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-232 |
1.89e-29 |
|
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: 112.02 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRP-INMM 96
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFpHMTVEQNiafglkqdklpkaeiasrvnemLGLvhmqefakrkphQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:cd03247 81 NQRPYLF-DTTLRNN----------------------LGR------------RFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 177 MGALDKKlRDRMQLEVV-DILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03247 126 TVGLDPI-TERQLLSLIfEVLK--DKTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-253 |
1.92e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 114.81 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 15 ALTPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRML-------AGFEQpsAGQIMLDG---VDLS 84
Cdd:PRK14271 17 AAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRY--SGDVLLGGrsiFNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 85 QVPPYLRPINMMFQSYALFPhMTVEQNIAFGLKQDKL-PKAEIASRVNEMLGLVHMQEFAKRK----PHQLSGGQRQRVA 159
Cdd:PRK14271 95 DVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 160 LARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
250
....*....|....*...
gi 1314858832 240 HP----TTRYSAEFIGSV 253
Cdd:PRK14271 252 SPkhaeTARYVAGLSGDV 269
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-227 |
2.31e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 118.63 E-value: 2.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 22 IRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLD-GVDLSQVPpylrpinmmfQSY 100
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLP----------QEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 101 ALFPHMTVEQNIAFGLK-----QDKLPKAEIA---------------------------SRVNEML-GLVHMQEFAKRKP 147
Cdd:COG0488 71 PLDDDLTVLDTVLDGDAelralEAELEELEAKlaepdedlerlaelqeefealggweaeARAEEILsGLGFPEEDLDRPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 148 HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVVDILERV-----GvTCVMVTHDQE--EAmtMAGRI 220
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--------LESIEWLEEFlknypG-TVLVVSHDRYflDR--VATRI 219
|
....*..
gi 1314858832 221 AIMNRGK 227
Cdd:COG0488 220 LELDRGK 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-240 |
2.31e-29 |
|
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: 112.24 E-value: 2.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE--QPSAGQIMLDGVDLSQVPPYLRP---IN 94
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERArlgIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 95 MMFQSYALFPHMTVEQNIAFglkqdklpkaeiasrVNEmlglvhmqefakrkphQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:cd03217 81 LAFQYPPEIPGVKNADFLRY---------------VNE----------------GFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 175 EPMGALDKklrDRMQL--EVVDILERVGVTCVMVTHDQEEAMTM-AGRIAIMNRGKFVQIGEPE---EIYEH 240
Cdd:cd03217 130 EPDSGLDI---DALRLvaEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKElalEIEKK 198
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
4-240 |
2.76e-29 |
|
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: 118.60 E-value: 2.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 4 AIPRPQAKtrkaltplLEIRNLTKSYDGQHA--VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGV 81
Cdd:TIGR01842 309 PLPEPEGH--------LSVENVTIVPPGGKKptLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGA 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 82 DLSQV-PPYL-RPINMMFQSYALFPHmTVEQNIA-FG--LKQDKLPKAEIASRVNEMLglvhmqefaKRKPH-------- 148
Cdd:TIGR01842 381 DLKQWdRETFgKHIGYLPQDVELFPG-TVAENIArFGenADPEKIIEAAKLAGVHELI---------LRLPDgydtvigp 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 149 ---QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNR 225
Cdd:TIGR01842 451 ggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQD 528
|
250
....*....|....*
gi 1314858832 226 GKFVQIGEPEEIYEH 240
Cdd:TIGR01842 529 GRIARFGERDEVLAK 543
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-209 |
2.86e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 118.24 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLdGVDLSQVppYLRpinmmf 97
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIG--YFD------ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 98 QSYALF-PHMTVEQNIAFGlkQDKLPKAEIASRVNEMLglvhmqeF----AKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:COG0488 385 QHQEELdPDKTVLDELRDG--APGGTEQEVRGYLGRFL-------FsgddAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1314858832 173 LDEPMGALDkklrdrmqLEVVDILERV-----GvTCVMVTHD 209
Cdd:COG0488 456 LDEPTNHLD--------IETLEALEEAlddfpG-TVLLVSHD 488
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
38-237 |
3.14e-29 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 113.40 E-value: 3.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPSAGQIMLDGVDLSQVPP--------YLRPinmmfQSYALFPhMTVE 109
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAaelarhraYLSQ-----QQSPPFA-MPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 110 QNIAFGLkQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK-------RPKLLLLDEPMGALDK 182
Cdd:COG4138 88 QYLALHQ-PAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 183 klrdRMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG4138 167 ----AQQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-237 |
3.57e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.82 E-value: 3.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 5 IPRPQAKTRKaltPLLEIRNLT-KSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDL 83
Cdd:COG3845 246 VEKAPAEPGE---VVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 84 SQVPPY-LRPINMMF-----QSYALFPHMTVEQNIAFGlKQDKLP--------KAEIASRVNEMlglvhMQEFAKRKPH- 148
Cdd:COG3845 323 TGLSPReRRRLGVAYipedrLGRGLVPDMSVAENLILG-RYRRPPfsrggfldRKAIRAFAEEL-----IEEFDVRTPGp 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 149 -----QLSGGQRQRVALARSLAKRPKLLLLDEPMGALD-----------KKLRDRmqlevvdilervGVTCVMVTHDQEE 212
Cdd:COG3845 397 dtparSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDvgaiefihqrlLELRDA------------GAAVLLISEDLDE 464
|
250 260
....*....|....*....|....*
gi 1314858832 213 AMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG3845 465 ILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
40-237 |
4.21e-29 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 112.25 E-value: 4.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 40 LTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGvdlSQVPPYLRPINMMFQSYAL---FPhMTVEQNIAFG- 115
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG---ASPGKGWRHIGYVPQRHEFawdFP-ISVAHTVMSGr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 116 ---LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEV 192
Cdd:TIGR03771 77 tghIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL-TEL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1314858832 193 VDILERVGVTCVMVTHDQEEAMTMAGRIAIMNrGKFVQIGEPEEI 237
Cdd:TIGR03771 156 FIELAGAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQL 199
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
34-238 |
4.93e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 113.72 E-value: 4.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP--YLRPIN----MMFQsyalFPHM- 106
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkYIRPVRkrigMVFQ----FPESq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 107 ----TVEQNIAFGLKQDKLPKAEIASRVNEML-GLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
Cdd:PRK13646 98 lfedTVEREIIFGPKNFKMNLDEVKNYAHRLLmDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 182 KKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-238 |
2.21e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 111.64 E-value: 2.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYL----RPIN 94
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLlalrQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 95 MMFQ--SYALFpHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:PRK13638 81 TVFQdpEQQIF-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314858832 173 LDEPMGALDKKLRDRMqlevVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
Cdd:PRK13638 160 LDEPTAGLDPAGRTQM----IAIIRRIvaqGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
11-237 |
2.25e-28 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 115.92 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 11 KTRKALTPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP-- 88
Cdd:PRK15439 3 TSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPak 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 89 ------YLRPinmmfQSYALFPHMTVEQNIAFGlkqdkLPK-AEIASRVNEMLGLVHMQefakRKPHQLSG----GQRQR 157
Cdd:PRK15439 83 ahqlgiYLVP-----QEPLLFPNLSVKENILFG-----LPKrQASMQKMKQLLAALGCQ----LDLDSSAGslevADRQI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 158 VALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-241 |
3.20e-28 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 112.69 E-value: 3.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPS----AGQIMLDGVDLSQVPPY 89
Cdd:COG4170 2 PLLDIRNLTIEIDTPQgrvkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 90 LR------PINMMFQ--SYALFPHMTVEQNIAFGLKQDKLP---------KAEIASRVNEMLGLVHMQEFAKRKPHQLSG 152
Cdd:COG4170 82 ERrkiigrEIAMIFQepSSCLDPSAKIGDQLIEAIPSWTFKgkwwqrfkwRKKRAIELLHRVGIKDHKDIMNSYPHELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMEST----TQAQIFRLLARLnqlqGTSILLISHDLESISQWADTITVLYCGQT 237
|
250
....*....|...
gi 1314858832 229 VQIGEPEEIYEHP 241
Cdd:COG4170 238 VESGPTEQILKSP 250
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
10-250 |
4.36e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 110.64 E-value: 4.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 10 AKTRKALTPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLR-------MLAGFEqpSAGQIMLDGVD 82
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 83 L--SQVPP--YLRPINMMFQSYALFPHmTVEQNIAFGlkqdklpkaeiaSRVNEMLGlvHMQEFAKRKPHQ--------- 149
Cdd:PRK14243 79 LyaPDVDPveVRRRIGMVFQKPNPFPK-SIYDNIAYG------------ARINGYKG--DMDELVERSLRQaalwdevkd 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 150 --------LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHDQEEAMTMAGRIA 221
Cdd:PRK14243 144 klkqsglsLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTA 221
|
250 260 270
....*....|....*....|....*....|....*...
gi 1314858832 222 IMN---------RGKFVQIGEPEEIYEHPTTRYSAEFI 250
Cdd:PRK14243 222 FFNveltegggrYGYLVEFDRTEKIFNSPQQQATRDYV 259
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-229 |
4.55e-28 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 115.03 E-value: 4.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPSA---GQIMLDGVDLsqVPPYLRP-- 92
Cdd:PRK13549 4 YLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEEL--QASNIRDte 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 ---INMMFQSYALFPHMTVEQNIAFG---LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
Cdd:PRK13549 81 ragIAIIHQELALVKELSVLENIFLGneiTPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314858832 167 RPKLLLLDEPMGALDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:PRK13549 161 QARLLILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-229 |
1.22e-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: 108.96 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQH---------------------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIML 78
Cdd:cd03267 1 IEVSNLSKSYRVYSkepgligslkslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 79 DG-VDLSQVPPYLRPINMMF-QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQ 156
Cdd:cd03267 81 AGlVPWKRRKKFLRRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314858832 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-250 |
2.61e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 108.60 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 21 EIRNLTKSY---DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGV------DLSQVPP--Y 89
Cdd:PRK14246 9 DVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAikL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 90 LRPINMMFQSYALFPHMTVEQNIAFGLKQDKLP-KAEIASRVNEMLGLVHM-QEFAKR---KPHQLSGGQRQRVALARSL 164
Cdd:PRK14246 89 RKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 165 AKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNE 246
|
....*.
gi 1314858832 245 YSAEFI 250
Cdd:PRK14246 247 LTEKYV 252
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-232 |
3.07e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 113.00 E-value: 3.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 8 PQAKTRKALTPLLEIRNLTKSYDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQ 85
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 86 VP-PYLRpiNMMF---QSYALFPHmTVEQNIAFGlkqdkLPKA--EIASRVNEMLGLVHMQEFAK----------RkphQ 149
Cdd:PRK11160 407 YSeAALR--QAISvvsQRVHLFSA-TLRDNLLLA-----APNAsdEALIEVLQQVGLEKLLEDDKglnawlgeggR---Q 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdRMQLEVVDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGK 227
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA----ETERQILELLAEHaqNKTVLMITH-RLTGLEQFDRICVMDNGQ 550
|
....*
gi 1314858832 228 FVQIG 232
Cdd:PRK11160 551 IIEQG 555
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-289 |
3.80e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 109.41 E-value: 3.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 21 EIRNLTKSYDGQ---------------------HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLD 79
Cdd:COG4586 3 EVENLSKTYRVYekepglkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 80 GVDlsqvpP------YLRPINMMF-QSYALFPHMTVEQNiaFGLKQD--KLPKAEIASRVNEMLGLVHMQEFAKRKPHQL 150
Cdd:COG4586 83 GYV-----PfkrrkeFARRIGVVFgQRSQLWWDLPAIDS--FRLLKAiyRIPDAEYKKRLDELVELLDLGELLDTPVRQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALD----KKLRDRmqleVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDvvskEAIREF----LKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 227 KFVQIGEPEEIYEH--PTTRYSAEFIGSVNVFEgvLkerQEDGLVLDSPGLVHPLKVDADASVVD 289
Cdd:COG4586 232 RIIYDGSLEELKERfgPYKTIVLELAEPVPPLE--L---PRGGEVIEREGNRVRLEVDPRESLAE 291
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-227 |
1.27e-26 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 105.63 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 16 LTPLLEIRNLTKSYDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVP-PYL- 90
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRPDTlvlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEhKYLh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 91 RPINMMFQSYALFPHmTVEQNIAFGLKQDKLPK-AEIASRVNE---MLGLVH-MQEFAKRKPHQLSGGQRQRVALARSLA 165
Cdd:cd03248 88 SKVSLVGQEPVLFAR-SLQDNIAYGLQSCSFECvKEAAQKAHAhsfISELASgYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 166 KRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgvTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPER---RTVLVIAHRLSTVERADQILVLDGGR 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
8-253 |
1.41e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 108.27 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 8 PQAKTRKALTPLLEIRNLT---KSYDGQ-HAVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLAGFEQPSaGQIMLD 79
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRvtfSTPDGDvTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIG-GSATFN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 80 GVDLSQVPPY----LRP--INMMFQS--YALFPHMTVEQNIAFGLKQDK-LPKAEIASRVNEMLGLVHMQEFAKRK---P 147
Cdd:PRK09473 80 GREILNLPEKelnkLRAeqISMIFQDpmTSLNPYMRVGEQLMEVLMLHKgMSKAEAFEESVRMLDAVKMPEARKRMkmyP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 148 HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILER-VGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
Cdd:PRK09473 160 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQI-MTLLNELKReFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
250 260
....*....|....*....|....*..
gi 1314858832 227 KFVQIGEPEEIYEHPTTRYSAEFIGSV 253
Cdd:PRK09473 239 RTMEYGNARDVFYQPSHPYSIGLLNAV 265
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-230 |
1.61e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 110.39 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDL---SQVPPYLRPI 93
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSYALFPHMTVEQNIAFGlkqdKLP-------KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLG----QLPhkggivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 167 RPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQL-FRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-226 |
2.52e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 105.87 E-value: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF---EQPSAGQIMLDGVDLSQVPPYLRPI-- 93
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 -----NMMFQSYALFPHMTVEQNIAFG-LKQDKLPKA-------EIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVAL 160
Cdd:PRK09984 84 srantGYIFQQFNLVNRLSVLENVLIGaLGSTPFWRTcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 161 ARSLAKRPKLLLLDEPMGALDKKlRDRMQLEVV-DILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPE-SARIVMDTLrDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-208 |
2.85e-26 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 103.98 E-value: 2.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP-YLRPINMMFQ 98
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDePHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 SYALFPHMTVEQNIAFglKQDKLPKAEIAsrVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:TIGR01189 81 LPGLKPELSALENLHF--WAAIHGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|
gi 1314858832 179 ALDKKLRDRMQLEVVDILERVGVTcVMVTH 208
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIV-LLTTH 185
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1-232 |
4.72e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 109.67 E-value: 4.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 1 MNDAIP----RPQAKTRKALTPLLEIRNLTKSYDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQ 75
Cdd:PRK13657 312 VEDAVPdvrdPPGAIDLGRVKGAVEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 76 IMLDGVDLSQV--PPYLRPINMMFQSYALFpHMTVEQNIAFGlKQDKLPkAEIAsrvnEMLGLVHMQEFAKRKPH----- 148
Cdd:PRK13657 392 ILIDGTDIRTVtrASLRRNIAVVFQDAGLF-NRSIEDNIRVG-RPDATD-EEMR----AAAERAQAHDFIERKPDgydtv 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 149 ------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQlEVVDILeRVGVTCVMVTHdQEEAMTMAGRIAI 222
Cdd:PRK13657 465 vgergrQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVK-AALDEL-MKGRTTFIIAH-RLSTVRNADRILV 541
|
250
....*....|
gi 1314858832 223 MNRGKFVQIG 232
Cdd:PRK13657 542 FDNGRVVESG 551
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-242 |
5.36e-26 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 105.25 E-value: 5.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 22 IRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQ--VPPYLRPINMMFQS 99
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 YALFPHMTVEQNIAFGlkqdKLP--------KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
Cdd:PRK10575 94 LPAAEGMTVRELVAIG----RYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 172 LLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPT 242
Cdd:PRK10575 170 LLDEPTSALDIA----HQVDVLALVHRLsqerGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
38-237 |
7.43e-26 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 104.24 E-value: 7.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPSAGQIMLDGVDLSQVPP--------YL----RPINMM--FQSYALF 103
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAaelarhraYLsqqqTPPFAMpvFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 104 phmtveqniafglKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALA-------RSLAKRPKLLLLDEP 176
Cdd:PRK03695 94 -------------QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 177 MGALD---KKLRDRmqleVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK03695 161 MNSLDvaqQAALDR----LLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-229 |
1.12e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 103.42 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP---YLRPIN 94
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakiMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 95 MMFQSYALFPHMTVEQNIAF-GLKQDKLPKAEIASRVNEMLGlvHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMgGFFAERDQFQERIKWVYELFP--RLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 174 DEP-MGaldkkLRDRMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:PRK11614 162 DEPsLG-----LAPIIIQQIFDTIEQLreqGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-208 |
1.18e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.36 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 3 DAIPRPQAKTRKALTPLLEIRNLT-KSYDGQHAVDDVSLTIYKGEifALL--GASGCGKSTLLRMLAGFEQPSAGQImld 79
Cdd:COG4178 346 DALPEAASRIETSEDGALALEDLTlRTPDGRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRI--- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 80 gvdlsQVPPylrPINMMF---QSYalFPHMTVEQNIAFGLKQDKLPKAEIAsrvnEMLGLVHMQEFAKR------KPHQL 150
Cdd:COG4178 421 -----ARPA---GARVLFlpqRPY--LPLGTLREALLYPATAEAFSDAELR----EALEAVGLGHLAERldeeadWDQVL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRM-QLevvdILERV-GVTCVMVTH 208
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALyQL----LREELpGTTVISVGH 542
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-229 |
2.62e-25 |
|
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: 106.83 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPSA---GQIMLDGVDL--SQVPPYLRP- 92
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLkaSNIRDTERAg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 INMMFQSYALFPHMTVEQNIAFG----LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKP-HQLSGGQRQRVALARSLAKR 167
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 168 PKLLLLDEPMGALDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:TIGR02633 160 ARLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
35-241 |
2.67e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 103.76 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLS------QVPPYLRPINMMFQsyalFPHM-- 106
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQ----FPEAql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 107 ---TVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQE-FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
Cdd:PRK13641 99 fenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1314858832 183 KLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:PRK13641 179 EGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
32-211 |
2.97e-25 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 101.96 E-value: 2.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE--QPSAGQIMLDGVDLSQVPPYLRpinmmfqsyalfphmtve 109
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREASLID------------------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 110 qniAFGLKQDKLPKAEIASRVnemlGLVHMQEFaKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQ 189
Cdd:COG2401 105 ---AIGRKGDFKDAVELLNAV----GLSDAVLW-LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170 180
....*....|....*....|..
gi 1314858832 190 LEVVDILERVGVTCVMVTHDQE 211
Cdd:COG2401 177 RNLQKLARRAGITLVVATHHYD 198
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
7-181 |
3.79e-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: 106.83 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 7 RPQAKTRKALTPLLEIRNLTKSYDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQ 85
Cdd:COG5265 345 APDAPPLVVGGGEVRFENVSFGYDPERPIlKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRD 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 86 VPP-YLR-PINMMFQSYALFpHMTVEQNIAFGlkqdklpKAEiASR--VNEMLGLVHMQEFAKRKPHQ-----------L 150
Cdd:COG5265 425 VTQaSLRaAIGIVPQDTVLF-NDTIAYNIAYG-------RPD-ASEeeVEAAARAAQIHDFIESLPDGydtrvgerglkL 495
|
170 180 190
....*....|....*....|....*....|.
gi 1314858832 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
20-237 |
5.13e-25 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 106.75 E-value: 5.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP--YLRPINM 95
Cdd:TIGR01846 456 ITFENIRFRYapDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPawLRRQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYALFPHmTVEQNIAFGLKQDKLPKAEIASRvnemlgLVHMQEFAKRKPH-----------QLSGGQRQRVALARSL 164
Cdd:TIGR01846 536 VLQENVLFSR-SIRDNIALCNPGAPFEHVIHAAK------LAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARAL 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314858832 165 AKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-208 |
5.54e-25 |
|
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: 100.65 E-value: 5.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP-YLRPINMMFQ 98
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDsIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 SYALFPHMTVEQNIAFglkqdkLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:cd03231 81 APGIKTTLSVLENLRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|
gi 1314858832 179 ALDKKLRDRMQLEVVDILERVGVTcVMVTH 208
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMV-VLTTH 183
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-183 |
8.59e-25 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 100.26 E-value: 8.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP-YLRpiNMMF 97
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeYHQ--DLLY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 98 QSYA--LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLvhmQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:PRK13538 79 LGHQpgIKTELTALENLRFYQRLHGPGDDEALWEALAQVGL---AGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
....*...
gi 1314858832 176 PMGALDKK 183
Cdd:PRK13538 156 PFTAIDKQ 163
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
20-211 |
1.47e-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: 97.90 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQImldgvdlsQVPPYLRPinmmfqs 99
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------TWGSTVKI------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 yALFPhmtveqniafglkqdklpkaeiasrvnemlglvhmqefakrkphQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:cd03221 66 -GYFE--------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190
....*....|....*....|....*....|..
gi 1314858832 180 LDkkLRDRMQLEvvDILERVGVTCVMVTHDQE 211
Cdd:cd03221 101 LD--LESIEALE--EALKEYPGTVILVSHDRY 128
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
37-232 |
1.52e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 100.04 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSA---GQIMLDGVDLSqvpPYLRPINMMF--QSYALFPHMTVEQN 111
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRK---PDQFQKCVAYvrQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 112 IAFGLK---QDKLPKAEIASRVNEM-LGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdR 187
Cdd:cd03234 102 LTYTAIlrlPRKSSDAIRKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS----F 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314858832 188 MQLEVVDILERVGVT--CVMVTHDQ--EEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03234 178 TALNLVSTLSQLARRnrIVILTIHQprSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-209 |
1.95e-24 |
|
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: 104.63 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIML-DGVDLSQVPpylrpinmmfQ 98
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVD----------Q 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 SY-ALFPHMTVEQNIAFGLKQDKLPKAEIASRvnemlglVHMQEFA------KRKPHQLSGGQRQRVALARSLAKRPKLL 171
Cdd:TIGR03719 393 SRdALDPNKTVWEEISGGLDIIKLGKREIPSR-------AYVGRFNfkgsdqQKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190
....*....|....*....|....*....|....*....
gi 1314858832 172 LLDEPMGALD-KKLRdrmQLEvvDILERVGVTCVMVTHD 209
Cdd:TIGR03719 466 LLDEPTNDLDvETLR---ALE--EALLNFAGCAVVISHD 499
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
34-282 |
2.03e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 102.13 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 34 AVDDVSLTIYKGEIFALLGASGCGKS-TLLRMLAGFEQP---SAGQIMLDGVDLSQVPPYLR------PINMMFQS--YA 101
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 102 LFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQEFAKR---KPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 178 GALDKKLrdrmQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSv 253
Cdd:PRK11022 182 TALDVTI----QAQIIELLlelqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRA- 256
|
250 260 270
....*....|....*....|....*....|
gi 1314858832 254 nvfegvLKERQEDGLVLDS-PGLVhPLKVD 282
Cdd:PRK11022 257 ------LPEFAQDKARLASlPGVV-PGKYD 279
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-234 |
3.87e-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: 3.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 15 ALTPLLEIRNLTKSYD--GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLR- 91
Cdd:TIGR01257 924 GLVPGVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRq 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 92 PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
Cdd:TIGR01257 1004 SLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 172 LLDEPMGALDKKLRDrmqlEVVDIL--ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRR----SIWDLLlkYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-237 |
4.30e-24 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 104.05 E-value: 4.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYD-GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPY-LRP-INMM 96
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHtLRQfINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFPHmTVEQNIAFGLK----QDKLPKA----EIASRVNEM-LGLvhmQEFAKRKPHQLSGGQRQRVALARSLAKR 167
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAKenvsQDEIWAAceiaEIKDDIENMpLGY---QTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 168 PKLLLLDEPMGALDKKLRDRMQLEVVDILERvgvTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-181 |
5.46e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 103.56 E-value: 5.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQvppY----LR-P 92
Cdd:PRK11176 342 IEFRNVTFTYPGKEvpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRD---YtlasLRnQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 INMMFQSYALFpHMTVEQNIAFGlKQDKLPKAEI--ASRvnemlgLVHMQEFAKRKPH-----------QLSGGQRQRVA 159
Cdd:PRK11176 419 VALVSQNVHLF-NDTIANNIAYA-RTEQYSREQIeeAAR------MAYAMDFINKMDNgldtvigengvLLSGGQRQRIA 490
|
170 180
....*....|....*....|..
gi 1314858832 160 LARSLAKRPKLLLLDEPMGALD 181
Cdd:PRK11176 491 IARALLRDSPILILDEATSALD 512
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-252 |
6.45e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 102.86 E-value: 6.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQ----HAVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLagfeqPS------AGQIMLDGVD 82
Cdd:PRK15134 3 QPLLAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 83 LSQVP-PYLR-----PINMMFQS--YALFPHMTVEQNIA------FGLKQDKlPKAEIASrvneMLGLVHMQEFAKR--- 145
Cdd:PRK15134 78 LLHASeQTLRgvrgnKIAMIFQEpmVSLNPLHTLEKQLYevlslhRGMRREA-ARGEILN----CLDRVGIRQAAKRltd 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 146 KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNR 225
Cdd:PRK15134 153 YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQN 232
|
250 260
....*....|....*....|....*..
gi 1314858832 226 GKFVQIGEPEEIYEHPTTRYSAEFIGS 252
Cdd:PRK15134 233 GRCVEQNRAATLFSAPTHPYTQKLLNS 259
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-234 |
7.79e-24 |
|
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: 97.95 E-value: 7.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY--DGQHAVDDVSLTIYKGEIFALLGASGCGKST----LLRMLagfeQPSAGQIMLDGVDLSQVPP-YLRP 92
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLhDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 -INMMFQSYALFPHmTVEQNIA-FGLKQDklpkaeiaSRVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVA 159
Cdd:cd03244 79 rISIIPQDPVLFSG-TIRSNLDpFGEYSD--------EELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 160 LARSLAKRPKLLLLDEPMGALDKKLRDRMQlEVVDiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEP 234
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQ-KTIR-EAFKDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
24-237 |
1.12e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 98.91 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 24 NLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP--YLRPINMMFQSYA 101
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASkeVARRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 102 LFPHMTVEQNIAFGlkqdKLPKAEIASR--------VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:PRK10253 92 TPGDITVQELVARG----RYPHQPLFTRwrkedeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 174 DEPMGALDKKLRDRMqLEVVDILERV-GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK10253 168 DEPTTWLDISHQIDL-LELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-253 |
2.42e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 101.47 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSY--DGQH--AVDDVSLTIYKGEIFALLGASGCGKS-TLLRMLAGFEQpSAGQIMLDG----------VDL 83
Cdd:PRK10261 12 VLAVENLNIAFmqEQQKiaAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKmllrrrsrqvIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 84 S-QVPPYLRPIN-----MMFQS--YALFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHM---QEFAKRKPHQLS 151
Cdd:PRK10261 91 SeQSAAQMRHVRgadmaMIFQEpmTSLNPVFTVGEQIAESIRlHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILER---VGVtcVMVTHDQEEAMTMAGRIAIMNRGKF 228
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQI-LQLIKVLQKemsMGV--IFITHDMGVVAEIADRVLVMYQGEA 247
|
250 260
....*....|....*....|....*
gi 1314858832 229 VQIGEPEEIYEHPTTRYSAEFIGSV 253
Cdd:PRK10261 248 VETGSVEQIFHAPQHPYTRALLAAV 272
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-235 |
4.80e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 96.29 E-value: 4.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE--QPSAGQIMLDGVDLSQVPPYLRP---IN 94
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERAragIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 95 MMFQSYALFPHMTVEQ--NIAFG-LKQDKLPKAEIASRVNEMLGLVHM-QEFAKRKPHQ-LSGGQRQRVALARSLAKRPK 169
Cdd:COG0396 81 LAFQYPVEIPGVSVSNflRTALNaRRGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 170 LLLLDEPMGALDkklRDRMQLeVVDILERV---GVTCVMVTHDQeeamtmagRI---------AIMNRGKFVQIGEPE 235
Cdd:COG0396 161 LAILDETDSGLD---IDALRI-VAEGVNKLrspDRGILIITHYQ--------RIldyikpdfvHVLVDGRIVKSGGKE 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-244 |
6.97e-23 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 96.31 E-value: 6.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQhAVDDVSLTIYKGEIFALLGASGCGKS----TLLRML-AGFEQpSAGQIMLDGVDLSqvPPYLRPIN 94
Cdd:PRK10418 5 IELRNIALQAAQP-LVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQ-TAGRVLLDGKPVA--PCALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 95 ----MMFQSYALFPHMT-----VEQNIAFGlkqdKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLA 165
Cdd:PRK10418 81 iatiMQNPRSAFNPLHTmhthaRETCLALG----KPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 166 KRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY--- 238
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVV----AQARILDLLESIvqkrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFnap 232
|
....*.
gi 1314858832 239 EHPTTR 244
Cdd:PRK10418 233 KHAVTR 238
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-208 |
8.93e-23 |
|
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: 94.54 E-value: 8.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLT---KSYDGQHA---VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG--FEQPSAGQIMLDGVDLSQVPPYLR 91
Cdd:cd03213 4 LSFRNLTvtvKSSPSKSGkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 92 pINMMFQSYALFPHMTVEQNIAFGlkqdklpkAEIASrvnemlglvhmqefakrkphqLSGGQRQRVALARSLAKRPKLL 171
Cdd:cd03213 84 -IGYVPQDDILHPTLTVRETLMFA--------AKLRG---------------------LSGGERKRVSIALELVSNPSLL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1314858832 172 LLDEPMGALDKklrdRMQLEVVDILERV---GVTCVMVTH 208
Cdd:cd03213 134 FLDEPTSGLDS----SSALQVMSLLRRLadtGRTIICSIH 169
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-230 |
1.81e-22 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 98.71 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG------FEqpsaGQIMLDGV-----DLSQVP 87
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphgsYE----GEILFDGEvcrfkDIRDSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 88 PylRPINMMFQSYALFPHMTVEQNIAFGLKQDK---LPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSL 164
Cdd:NF040905 77 A--LGIVIIHQELALIPYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 165 AKRPKLLLLDEPMGALD----KKLRDRMqLEvvdiLERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
Cdd:NF040905 155 SKDVKLLILDEPTAALNeedsAALLDLL-LE----LKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-227 |
2.45e-22 |
|
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: 93.30 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQH-----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGvDLSQVP--PYLRP 92
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-SIAYVSqePWIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 inmmfqsyalfphMTVEQNIAFG----------------LKQD--KLPKA---EIASR-VNemlglvhmqefakrkphqL 150
Cdd:cd03250 80 -------------GTIRENILFGkpfdeeryekvikacaLEPDleILPDGdltEIGEKgIN------------------L 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRmqlevvdILERV-------GVTCVMVTHdQEEAMTMAGRIAIM 223
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRH-------IFENCilglllnNKTRILVTH-QLQLLPHADQIVVL 200
|
....
gi 1314858832 224 NRGK 227
Cdd:cd03250 201 DNGR 204
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-227 |
2.66e-22 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 98.12 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDG--VDLSQVPPYLRPINMM 96
Cdd:PRK10522 323 LELRNVTFAYqDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkpVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 FQSYALFPHMTVEQNIAfglkqdklPKAEIASRVNEMLGLVHMQEFAKRK--PHQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:PRK10522 403 FTDFHLFDQLLGPEGKP--------ANPALVEKWLERLKMAHKLELEDGRisNLKLSKGQKKRLALLLALAEERDILLLD 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1314858832 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDqEEAMTMAGRIAIMNRGK 227
Cdd:PRK10522 475 EWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
11-209 |
3.41e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 95.26 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 11 KTRKALTPLLEIRNLTKSYDgqhavdDVSL-----TIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDgVDLSQ 85
Cdd:PRK13409 332 RDESERETLVEYPDLTKKLG------DFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 86 VPPYLRPInmmfqsyalfPHMTVEQNI-----AFGlkqDKLPKAEIASRvnemLGLVHMQEfakRKPHQLSGGQRQRVAL 160
Cdd:PRK13409 405 KPQYIKPD----------YDGTVEDLLrsitdDLG---SSYYKSEIIKP----LQLERLLD---KNVKDLSGGELQRVAI 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1314858832 161 ARSLAKRPKLLLLDEPMGALDKKLRdrmqLEVVDILERV----GVTCVMVTHD 209
Cdd:PRK13409 465 AACLSRDADLYLLDEPSAHLDVEQR----LAVAKAIRRIaeerEATALVVDHD 513
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-208 |
5.37e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.93 E-value: 5.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDG--VDLSQVPP---YLRP 92
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdIDDPDVAEachYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 INmmfqsyALFPHMTVEQNIAF--GLKQDKLPKAEIAsrvnemLGLVHMQEFAKRKPHQLSGGQRQRVALARSL-AKRPk 169
Cdd:PRK13539 81 RN------AMKPALTVAENLEFwaAFLGGEELDIAAA------LEAVGLAPLAHLPFGYLSAGQKRRVALARLLvSNRP- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1314858832 170 LLLLDEPMGALDKKlRDRMQLEVVDI-LERVGvTCVMVTH 208
Cdd:PRK13539 148 IWILDEPTAALDAA-AVALFAELIRAhLAQGG-IVIAATH 185
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
20-209 |
8.08e-21 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 94.03 E-value: 8.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIML-DGVDLSQVPpylrpinmmfQ 98
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKLAYVD----------Q 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 SY-ALFPHMTVEQNIAFGLKQDKLPKAEIASRVnemlglvHMQEFAKRKPHQ------LSGGQRQRVALARSLAKRPKLL 171
Cdd:PRK11819 395 SRdALDPNKTVWEEISGGLDIIKVGNREIPSRA-------YVGRFNFKGGDQqkkvgvLSGGERNRLHLAKTLKQGGNVL 467
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1314858832 172 LLDEPMGALD-KKLRdrmQLEVVdILERVGvtCVMV-THD 209
Cdd:PRK11819 468 LLDEPTNDLDvETLR---ALEEA-LLEFPG--CAVViSHD 501
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-209 |
8.70e-21 |
|
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: 93.70 E-value: 8.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDGqhavddVSLT-----IYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDgVDLSQVPPYLRP 92
Cdd:COG1245 340 TLVEYPDLTKSYGG------FSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISYKPQYISP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 INmmfqsyalfpHMTVEQNIAFGLKqDKLP----KAEIASRvnemLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRP 168
Cdd:COG1245 413 DY----------DGTVEEFLRSANT-DDFGssyyKTEIIKP----LGLEKLLD---KNVKDLSGGELQRVAIAACLSRDA 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1314858832 169 KLLLLDEPMGALDkkLRDRMqlEVVDILERV----GVTCVMVTHD 209
Cdd:COG1245 475 DLYLLDEPSAHLD--VEQRL--AVAKAIRRFaenrGKTAMVVDHD 515
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-209 |
1.16e-20 |
|
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: 89.77 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 22 IRNLTKSYDGqhavDDVSL-----TIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPInmm 96
Cdd:cd03237 1 YTYPTMKKTL----GEFTLeveggSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKAD--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 97 fqsyalFPhMTVEQnIAFGLKQDKLPKAEIASRVNEMLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:cd03237 74 ------YE-GTVRD-LLSSITKDFYTHPYFKTEIAKPLQIEQILD---REVPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190
....*....|....*....|....*....|...
gi 1314858832 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHD 209
Cdd:cd03237 143 SAYLDVEQRLMASKVIRRFAENNEKTAFVVEHD 175
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-232 |
1.94e-20 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 93.54 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLsqvppyLRPIN 94
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI------LTNIS 2008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 95 MMFQSYALFPH-------MTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKR 167
Cdd:TIGR01257 2009 DVHQNMGYCPQfdaiddlLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 168 PKLLLLDEPMGALDKKLRdRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQAR-RMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLG 2152
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-256 |
4.09e-20 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 89.86 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLT---KSYDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP----SAGQIMLDGVDLSQVPPY 89
Cdd:PRK15093 2 PLLDIRNLTiefKTSDGWvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 90 LR------PINMMFQSyalfPHMTVE--QNIAFGLKQdKLP----KAEIASRVN-------EML---GLVHMQEFAKRKP 147
Cdd:PRK15093 82 ERrklvghNVSMIFQE----PQSCLDpsERVGRQLMQ-NIPgwtyKGRWWQRFGwrkrraiELLhrvGIKDHKDAMRSFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 148 HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIM 223
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPT----TQAQIFRLLTRLnqnnNTTILLISHDLQMLSQWADKINVL 232
|
250 260 270
....*....|....*....|....*....|...
gi 1314858832 224 NRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVF 256
Cdd:PRK15093 233 YCGQTVETAPSKELVTTPHHPYTQALIRAIPDF 265
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-209 |
3.23e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.48 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSY-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVppyLRP--I 93
Cdd:PRK15056 4 QAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA---LQKnlV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSYAL---FPhMTVEQNIAFG----LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
Cdd:PRK15056 81 AYVPQSEEVdwsFP-VLVEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1314858832 167 RPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHD 209
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARI-ISLLRELRDEGKTMLVSTHN 201
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
33-236 |
4.18e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.95 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPS---AGQIMLDG--VDLSQvppyLRPINMMFQSYALF-PHM 106
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGmpIDAKE----MRAISAYVQQDDLFiPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 107 TVEQNIAFG--LK-QDKLPKAEIASRVNE---MLGLVHMQEFAKRKPHQ---LSGGQRQRVALARSLAKRPKLLLLDEPM 177
Cdd:TIGR00955 115 TVREHLMFQahLRmPRRVTKKEKRERVDEvlqALGLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314858832 178 GALDKKlrdrMQLEVVDILERV---GVTCVMVTHD-QEEAMTMAGRIAIMNRGKFVQIGEPEE 236
Cdd:TIGR00955 195 SGLDSF----MAYSVVQVLKGLaqkGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-228 |
4.40e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.57 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTksydGQHAVDdVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP-------- 88
Cdd:PRK15439 266 APVLTVEDLT----GEGFRN-ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlargl 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 89 -YL---RpinmmfQSYALFPHMTVEQNIAfGLKQDKL-----PKAEIA--SRVNEMLG--LVHMQEFAKRkphqLSGGQR 155
Cdd:PRK15439 341 vYLpedR------QSSGLYLDAPLAWNVC-ALTHNRRgfwikPARENAvlERYRRALNikFNHAEQAART----LSGGNQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 156 QRVALARSLAKRPKLLLLDEPMGALDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
Cdd:PRK15439 410 QKVLIAKCLEASPQLLIVDEPTRGVDVSARN----DIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-211 |
7.56e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 88.08 E-value: 7.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 21 EIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLdGVDLSQVppYlrpinmmFQSY 100
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVA--Y-------FDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 101 --ALFPHMTVEQNIAFGlKQDklpkAEIASRVNEMLGlvHMQEF------AKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:PRK11147 391 raELDPEKTVMDNLAEG-KQE----VMVNGRPRHVLG--YLQDFlfhpkrAMTPVKALSGGERNRLLLARLFLKPSNLLI 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1314858832 173 LDEPMGALDkklrdrmqLEVVDILERV-----GvTCVMVTHDQE 211
Cdd:PRK11147 464 LDEPTNDLD--------VETLELLEELldsyqG-TVLLVSHDRQ 498
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-237 |
1.35e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 84.88 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG-FEQPSA-------GQIMLDGVDLSQVPPY- 89
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 90 ---LRPInMMFQSYALFPhMTVEQNIAFGlkqdKLPKA-----------EIASRVnemLGLVHMQEFAKRKPHQLSGGQR 155
Cdd:PRK13547 81 larLRAV-LPQAAQPAFA-FSAREIVLLG----RYPHArragalthrdgEIAWQA---LALAGATALVGRDVTTLSGGEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 156 QRVALARSLAK---------RPKLLLLDEPMGALDKKLRDRMqLEVVDILER---VGVtcVMVTHDQEEAMTMAGRIAIM 223
Cdd:PRK13547 152 ARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRL-LDTVRRLARdwnLGV--LAIVHDPNLAARHADRIAML 228
|
250
....*....|....
gi 1314858832 224 NRGKFVQIGEPEEI 237
Cdd:PRK13547 229 ADGAIVAHGAPADV 242
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-186 |
1.53e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 82.61 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVP-PYLRPINmmfQSYALFPHMTVEQNIAFG 115
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkPYCTYIG---HNLGLKLEMTVFENLKFW 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 116 lkqdklpkAEIASRVNEMLGLVH---MQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
Cdd:PRK13541 95 --------SEIYNSAETLYAAIHyfkLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
16-250 |
2.33e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.62 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 16 LTPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQImldgvdlsQVPPYLRpINM 95
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLR-IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYALFPHM--TVEQNIAF--GLK-QDKLPKAEiasRVNEmlglVHMQEFAKRKphqLSGGQRQRVALARSLAKRPKL 170
Cdd:PRK09544 72 VPQKLYLDTTLplTVNRFLRLrpGTKkEDILPALK---RVQA----GHLIDAPMQK---LSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 171 LLLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRgKFVQIGEPEEIYEHPttrys 246
Cdd:PRK09544 142 LVLDEPTQGVDVN----GQVALYDLIDQLrrelDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHP----- 211
|
....
gi 1314858832 247 aEFI 250
Cdd:PRK09544 212 -EFI 214
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-234 |
3.77e-18 |
|
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: 82.07 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVP--PYLRPINM 95
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPleDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYALFPHmTVEQNIAfglKQDKLPKAEI--ASRVNEMlGLvhmqefakrkphQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:cd03369 87 IPQDPTLFSG-TIRSNLD---PFDEYSDEEIygALRVSEG-GL------------NLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314858832 174 DEPMGALDKKLRDRMQLEVVDilERVGVTCVMVTHDQEEAMTMAgRIAIMNRGKFVQIGEP 234
Cdd:cd03369 150 DEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDYD-KILVMDAGEVKEYDHP 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-227 |
4.85e-18 |
|
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: 85.37 E-value: 4.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 22 IRNLTKSYDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDgvdlsqvPPYlrPINMMFQSY 100
Cdd:TIGR03719 7 MNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-------PGI--KVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 101 ALFPHMTVEQNIAFGL--KQDKL------------PKAEIASRVNEMLGL---------------VHMQEFAKRKP---- 147
Cdd:TIGR03719 78 QLDPTKTVRENVEEGVaeIKDALdrfneisakyaePDADFDKLAAEQAELqeiidaadawdldsqLEIAMDALRCPpwda 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 148 --HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdrmqlEVVDILERV-----GvTCVMVTHDQEEAMTMAGRI 220
Cdd:TIGR03719 158 dvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA--------ESVAWLERHlqeypG-TVVAVTHDRYFLDNVAGWI 228
|
....*..
gi 1314858832 221 AIMNRGK 227
Cdd:TIGR03719 229 LELDRGR 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-227 |
6.01e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.96 E-value: 6.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 6 PRPQAKTRkaltplLEIRNLtksyDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLsq 85
Cdd:PRK11288 250 PRPLGEVR------LRLDGL----KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 86 vpPYLRPINMMFQSYAL----------FPHMTVEQNIA---------FGLKQDKLPKAEIASRvnemlglvHMQEFAKRK 146
Cdd:PRK11288 318 --DIRSPRDAIRAGIMLcpedrkaegiIPVHSVADNINisarrhhlrAGCLINNRWEAENADR--------FIRSLNIKT 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 147 PH------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDrmqlEVVDI---LERVGVTCVMVTHDQEEAMTMA 217
Cdd:PRK11288 388 PSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKH----EIYNViyeLAAQGVAVLFVSSDLPEVLGVA 463
|
250
....*....|
gi 1314858832 218 GRIAIMNRGK 227
Cdd:PRK11288 464 DRIVVMREGR 473
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-233 |
9.26e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.67 E-value: 9.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP---YLRPI 93
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkssQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSYALFPHMTVEQNI--------AFGLKQDKLPKAEiASRVNEMLGLVHMqefAKRKPHQLSGGQRQRVALARSLA 165
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIflgrefvnRFGRIDWKKMYAE-ADKLLARLNLRFS---SDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 166 KRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFvqIGE 233
Cdd:PRK10762 158 FESKVIIMDEPTDALTDTETESL-FRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF--IAE 222
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
295-375 |
1.03e-17 |
|
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: 76.89 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 295 VALRPEKIMLCEeppanGCNFAVGEVIHIAYLGDLSVYHVRLKSGQMISAQLQNAHRHRkglPTWGDEVRLCWEVDSCVV 374
Cdd:pfam08402 1 LAIRPEKIRLAA-----AANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHARP---PAPGDRVGLGWDPEDAHV 72
|
.
gi 1314858832 375 L 375
Cdd:pfam08402 73 L 73
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-183 |
2.03e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 79.61 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQ-VPPYLRPINMMF 97
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 98 QSYALFPHMTVEQNIAFGLKqdklpKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDIH-----FSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
....*.
gi 1314858832 178 GALDKK 183
Cdd:PRK13540 156 VALDEL 161
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-231 |
3.83e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.52 E-value: 3.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDGQhaVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMF 97
Cdd:PRK09700 264 TVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 98 ------QSYALFPHMTVEQNIAFgLKQDKLpkaeiaSRVNEMLGLVHMQEFAKRKPHQ-----------------LSGGQ 154
Cdd:PRK09700 342 yitesrRDNGFFPNFSIAQNMAI-SRSLKD------GGYKGAMGLFHEVDEQRTAENQrellalkchsvnqniteLSGGN 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 155 RQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
Cdd:PRK09700 415 QQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEI-YKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-227 |
5.74e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.97 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSydgqhAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPP---------Yl 90
Cdd:PRK10762 258 LKVDNLSGP-----GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqdglangivY- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 91 rpINMMFQSYALFPHMTVEQNIA------FGLKQDKLPKAEIASRVNEMLGLvhmqeFAKRKPHQ------LSGGQRQRV 158
Cdd:PRK10762 332 --ISEDRKRDGLVLGMSVKENMSltalryFSRAGGSLKHADEQQAVSDFIRL-----FNIKTPSMeqaiglLSGGNQQKV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 159 ALARSLAKRPKLLLLDEPMGALD---KKlrdrmqlEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVDvgaKK-------EIYQLINQFkaeGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-209 |
8.78e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 81.70 E-value: 8.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 23 RNLTKSYDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIML-DGVD---LSQVPPylrpinmmf 97
Cdd:PRK11819 10 NRVSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKvgyLPQEPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 98 qsyaLFPHMTVEQNI--AFGLKQDKLPK-----AEIASRVNEMLGLvhMQEFAK------------------------RK 146
Cdd:PRK11819 81 ----LDPEKTVRENVeeGVAEVKAALDRfneiyAAYAEPDADFDAL--AAEQGElqeiidaadawdldsqleiamdalRC 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 147 PH------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdrmqlEVVDILERV-----GvTCVMVTHD 209
Cdd:PRK11819 155 PPwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--------ESVAWLEQFlhdypG-TVVAVTHD 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-208 |
1.48e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.42 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLT-KSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQI-MLDGVDLSQVP--PYlrpinm 95
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgMPEGEDLLFLPqrPY------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 mfqsyalFPHMTVEQNIAFGLKQdklpkaeiasrvnemlglvhmqefakrkphQLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:cd03223 75 -------LPLGTLREQLIYPWDD------------------------------VLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|...
gi 1314858832 176 PMGALDKKLRDRMqlevVDILERVGVTCVMVTH 208
Cdd:cd03223 118 ATSALDEESEDRL----YQLLKELGITVISVGH 146
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-175 |
2.23e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 80.61 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQH-----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDG--VDLSQVPPYLRP 92
Cdd:COG4615 328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGqpVTADNREAYRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 INMMFQSYALFPHMtveqniaFGLKQDKLPKaeiasRVNEMLGLVHMQE--------FAKRKphqLSGGQRQRVALARSL 164
Cdd:COG4615 408 FSAVFSDFHLFDRL-------LGLDGEADPA-----RARELLERLELDHkvsvedgrFSTTD---LSQGQRKRLALLVAL 472
|
170
....*....|..
gi 1314858832 165 A-KRPkLLLLDE 175
Cdd:COG4615 473 LeDRP-ILVFDE 483
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-208 |
3.26e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 80.31 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 22 IRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPS--AGQIMLDGVDLSQvpPYLRPINMMFQS 99
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK--QILKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 YALFPHMTVEQNIAFG---------LKQDKLPKAEiaSRVNEmLGLVHMQE--FAKRKPHQLSGGQRQRVALARSLAKRP 168
Cdd:PLN03211 149 DILYPHLTVRETLVFCsllrlpkslTKQEKILVAE--SVISE-LGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINP 225
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1314858832 169 KLLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTH 208
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMH 264
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
12-237 |
3.36e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 79.01 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 12 TRKALTP----LLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCG--KSTLLRMLAGfeqPSAGQ-------IML 78
Cdd:NF000106 2 TRKTISNgarnAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRrpwrf*tWCA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 79 DGVDLSQVPPYLRPINMMFQSyalfpHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRV 158
Cdd:NF000106 79 NRRALRRTIG*HRPVR*GRRE-----SFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314858832 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILeRVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:NF000106 154 DLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
37-288 |
6.89e-16 |
|
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: 79.57 E-value: 6.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDG-VDLSQVPPYLRPinmmfqsyalfphMTVEQNIAFG 115
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGrISFSPQTSWIMP-------------GTIKDNIIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 116 LKQDKLpkaeiasRVNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKLLLLDEPMGALD--- 181
Cdd:TIGR01271 511 LSYDEY-------RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDvvt 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 182 -KKLRDRMQLEVVDILERVGVTCVMvthdqeEAMTMAGRIAIMNRGKFVQIGEPEEIY-EHPTtrYSAEFIGSVNvFEGV 259
Cdd:TIGR01271 584 eKEIFESCLCKLMSNKTRILVTSKL------EHLKKADKILLLHEGVCYFYGTFSELQaKRPD--FSSLLLGLEA-FDNF 654
|
250 260
....*....|....*....|....*....
gi 1314858832 260 LKERQEDGLVldspGLVHPLKVDADASVV 288
Cdd:TIGR01271 655 SAERRNSILT----ETLRRVSIDGDSTVF 679
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
35-226 |
9.80e-16 |
|
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: 75.45 E-value: 9.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGV-DLSQVPPYLRPINMMFQSYA----LFPHMTVE 109
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnESEPSFEATRSRNRYSVAYAaqkpWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 110 QNIAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACSlqpdiDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1314858832 185 RDR-MQLEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRG 226
Cdd:cd03290 176 SDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
72-237 |
1.18e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.92 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 72 SAGQIMLDGVDLSQVPpyLRPINMMF----QSYALFpHMTVEQNIAFGLKQDKLPKAEIASRvnemlgLVHMQEFAKRKP 147
Cdd:PTZ00265 1275 NSGKILLDGVDICDYN--LKDLRNLFsivsQEPMLF-NMSIYENIKFGKEDATREDVKRACK------FAAIDEFIESLP 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 148 HQ-----------LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHdQEEAMTM 216
Cdd:PTZ00265 1346 NKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKR 1424
|
170 180
....*....|....*....|....*.
gi 1314858832 217 AGRIAIMNR----GKFVQI-GEPEEI 237
Cdd:PTZ00265 1425 SDKIVVFNNpdrtGSFVQAhGTHEEL 1450
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
37-264 |
1.96e-15 |
|
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: 75.66 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGvdlsqvppylrPINMMFQSYALFPHmTVEQNIAFGL 116
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------RISFSSQFSWIMPG-TIKENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 117 KQDKLpkaeiasRVNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKLLLLDEPMGALD---- 181
Cdd:cd03291 123 SYDEY-------RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDvfte 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 182 KKLRDRMQLEVVDILERVGVTCVMvthdqeEAMTMAGRIAIMNRGKFVQIGEPEEIyEHPTTRYSAEFIGsVNVFEGVLK 261
Cdd:cd03291 196 KEIFESCVCKLMANKTRILVTSKM------EHLKKADKILILHEGSSYFYGTFSEL-QSLRPDFSSKLMG-YDTFDQFSA 267
|
...
gi 1314858832 262 ERQ 264
Cdd:cd03291 268 ERR 270
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-176 |
2.67e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.47 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 21 EIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQ------VPPYlrpIN 94
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADarhrraVCPR---IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 95 MMFQSYA--LFPHMTVEQNIAF-----GLkqdklPKAEIASRVNEML---GLvhmQEFAKRKPHQLSGGQRQRVALARSL 164
Cdd:NF033858 80 YMPQGLGknLYPTLSVFENLDFfgrlfGQ-----DAAERRRRIDELLratGL---APFADRPAGKLSGGMKQKLGLCCAL 151
|
170
....*....|..
gi 1314858832 165 AKRPKLLLLDEP 176
Cdd:NF033858 152 IHDPDLLILDEP 163
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
17-235 |
2.91e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 74.68 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfeQPS----AGQIMLDGVDLSQVPPYLRP 92
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 ---INMMFQSYALFPHMTVEQ--NIAFGLKQDKLPKAEIA-----SRVNEMLGLVHMQE-FAKRKPHQ-LSGGQRQRVAL 160
Cdd:CHL00131 83 hlgIFLAFQYPIEIPGVSNADflRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 161 ARSLAKRPKLLLLDEPMGALDKklrDRMQL--EVVDILERVGVTCVMVTHDQeeamtmagR---------IAIMNRGKFV 229
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDI---DALKIiaEGINKLMTSENSIILITHYQ--------RlldyikpdyVHVMQNGKII 231
|
....*.
gi 1314858832 230 QIGEPE 235
Cdd:CHL00131 232 KTGDAE 237
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-239 |
3.78e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.68 E-value: 3.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGvdlsqvppylRPInmmfq 98
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG----------RPL----- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 syALFPHMTVEQNIAFgLKQDKLPKAEI------------ASRVNEMLGLVHMQEFAKRKP-----------HQLSGGQR 155
Cdd:PRK10790 406 --SSLSHSVLRQGVAM-VQQDPVVLADTflanvtlgrdisEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQK 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 156 QRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPE 235
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAH-RLSTIVEADTILVLHRGQAVEQGTHQ 559
|
....
gi 1314858832 236 EIYE 239
Cdd:PRK10790 560 QLLA 563
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-229 |
4.32e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 76.31 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 22 IRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDG--VDLSQVPPYLRP-INMMFQ 98
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSKEALENgISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 SYALFPHMTVEQNIAFG--------LKQDKLPKAEIAsrVNEMLGLvhmQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGryptkgmfVDQDKMYRDTKA--IFDELDI---DIDPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1314858832 171 LLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHL-FTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-227 |
6.85e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.63 E-value: 6.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTkSYDGQHA----VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG-FEQPSAGQIMLDG--VDLSQVPPYLR 91
Cdd:TIGR02633 257 ILEARNLT-CWDVINPhrkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGkpVDIRNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 92 PINMMF----QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPH------QLSGGQRQRVALA 161
Cdd:TIGR02633 336 AGIAMVpedrKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpflpigRLSGGNQQKAVLA 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 162 RSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:TIGR02633 416 KMLLTNPRVLILDEPTRGVDVGAKYEI-YKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-246 |
2.78e-14 |
|
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: 74.60 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPY-LR-PINM 95
Cdd:TIGR00957 1285 VEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHdLRfKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MFQSYALFPHmTVEQNI-AFGLKQDKlpkaeiasRVNEMLGLVHMQEFAKRKP----HQ-------LSGGQRQRVALARS 163
Cdd:TIGR00957 1365 IPQDPVLFSG-SLRMNLdPFSQYSDE--------EVWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 164 LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvgvTCVMVT--HDQEEAMTMAgRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDNLIQSTIRTQFE----DCTVLTiaHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQR 1510
|
....*
gi 1314858832 242 TTRYS 246
Cdd:TIGR00957 1511 GIFYS 1515
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
33-240 |
2.80e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 72.16 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGvdlsqvppylrPINMMFQSYALFPHMTVEQNI 112
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------EVSVIAISAGLSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 113 AFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKI 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1314858832 193 VDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:PRK13546 187 YEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
35-181 |
5.22e-14 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 69.98 E-value: 5.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG----FEQPSaGQIMLDGVDLSQ-VPPYLRPINMMFQSYALFPHMTVE 109
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtegNVSVE-GDIHYNGIPYKEfAEKYPGEIIYVSEEDVHFPTLTVR 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 110 QNIAFGLKqdklpkaeiaSRVNEMLglvhmqefakRKphqLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
Cdd:cd03233 102 ETLDFALR----------CKGNEFV----------RG---ISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-183 |
6.06e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.52 E-value: 6.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIML-DGVDLSQV--PPYLRPI 93
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDInlKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSYALFPHmTVEQNIAFGL-------------------KQDKLPK-----AEIASRVNEML------GLVHMQ--- 140
Cdd:PTZ00265 463 GVVSQDPLLFSN-SIKNNIKYSLyslkdlealsnyynedgndSQENKNKrnscrAKCAGDLNDMSnttdsnELIEMRkny 541
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 141 ------------------EFAKRKP-----------HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
Cdd:PTZ00265 542 qtikdsevvdvskkvlihDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-210 |
9.93e-14 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 72.51 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIML-DGVDLSQVP----PYLR 91
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAqhqlEFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 92 PINMMFQSYALFPHMTVEQNI-----AFGLKQDKLpkAEIASRvnemlglvhmqefakrkphqLSGGQRQRVALARSLAK 166
Cdd:PRK10636 390 ADESPLQHLARLAPQELEQKLrdylgGFGFQGDKV--TEETRR--------------------FSGGEKARLVLALIVWQ 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1314858832 167 RPKLLLLDEPMGALDKKLRDRMQLEVVDILERVgvtcVMVTHDQ 210
Cdd:PRK10636 448 RPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDR 487
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-227 |
1.74e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.50 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTkSYD----GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG-FEQPSAGQIMLDG--VDLSQVPPYLRP 92
Cdd:PRK13549 260 LEVRNLT-AWDpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGkpVKIRNPQQAIAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 -INMMFQS---YALFPHMTVEQNIAFGLkqdkLPKAEIASRVNEMLGLVHMQEFAKR------KPHQ----LSGGQRQRV 158
Cdd:PRK13549 339 gIAMVPEDrkrDGIVPVMGVGKNITLAA----LDRFTGGSRIDDAAELKTILESIQRlkvktaSPELaiarLSGGNQQKA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 159 ALARSLAKRPKLLLLDEPMGALD-------KKLrdrmqlevVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:PRK13549 415 VLAKCLLLNPKILILDEPTRGIDvgakyeiYKL--------INQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-229 |
3.84e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.75 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQP-SAGQIMLDGvD-----LSQVPP---- 88
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-EVLlDDGRIIYEQ-DlivarLQQDPPrnve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 89 ----------------YLRPINMMFQSYALFPHmtvEQNIA-FGLKQDKLPKA---EIASRVNEMLGLVHMQefAKRKPH 148
Cdd:PRK11147 81 gtvydfvaegieeqaeYLKRYHDISHLVETDPS---EKNLNeLAKLQEQLDHHnlwQLENRINEVLAQLGLD--PDAALS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 149 QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMN 224
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD--------IETIEWLEGFlktfQGSIIFISHDRSFIRNMATRIVDLD 227
|
....*
gi 1314858832 225 RGKFV 229
Cdd:PRK11147 228 RGKLV 232
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-181 |
5.93e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.18 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPpylRPINMMF 97
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD---RSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 98 QSY--ALFPHMTVEQNIAF-----GLKQDKLPKAEIAsrvnemlgLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
Cdd:PRK13543 87 LGHlpGLKADLSTLENLHFlcglhGRRAKQMPGSALA--------IVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPL 158
|
170
....*....|.
gi 1314858832 171 LLLDEPMGALD 181
Cdd:PRK13543 159 WLLDEPYANLD 169
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
20-220 |
6.34e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.92 E-value: 6.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDgvDLSQVPPYLRPINMMF-Q 98
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS--ENANIGYYAQDHAYDFeN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 SYALFPHMTveqniafglkQDKLPKAEIASrVNEMLG-LVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
Cdd:PRK15064 398 DLTLFDWMS----------QWRQEGDDEQA-VRGTLGrLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1314858832 178 GALDkklrdrMQ-LEVVDI-LERVGVTCVMVTHDQEEAMTMAGRI 220
Cdd:PRK15064 467 NHMD------MEsIESLNMaLEKYEGTLIFVSHDREFVSSLATRI 505
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
44-217 |
1.76e-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: 64.32 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 44 KGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLdgvdlsqvppylrpINMmfqsyalfphmtveqniafglkqdklpk 123
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------IDG---------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 124 aeiaSRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVD-----ILER 198
Cdd:smart00382 39 ----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKSE 114
|
170
....*....|....*....
gi 1314858832 199 VGVTCVMVTHDQEEAMTMA 217
Cdd:smart00382 115 KNLTVILTTNDEKDLGPAL 133
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
38-268 |
1.97e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.85 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQ--VPPYLRPINMMFQSYALFPHmTVEQNI-AF 114
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFSG-TVRFNIdPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 115 GLKQDklpkaeiaSRVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
Cdd:PLN03232 1334 SEHND--------ADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 184 LRDRMQLEVVDilERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS--AEFIGSVNV--FEGV 259
Cdd:PLN03232 1406 TDSLIQRTIRE--EFKSCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFrmVHSTGPANAqyLSNL 1482
|
....*....
gi 1314858832 260 LKERQEDGL 268
Cdd:PLN03232 1483 VFERRENGM 1491
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
36-181 |
7.18e-12 |
|
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: 63.80 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 36 DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPS--AGQIMLDGvdlsqvppylRPINMMFQSYALFphmtVEQNIA 113
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILING----------RPLDKNFQRSTGY----VEQQDV 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 114 FglkqdkLPKaeiaSRVNEMLglvhmqEFAKrKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
Cdd:cd03232 90 H------SPN----LTVREAL------RFSA-LLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-237 |
1.14e-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: 66.51 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 8 PQAKTRKALTP----LLEIRNLTKSY--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGv 81
Cdd:TIGR00957 621 PDSIERRTIKPgegnSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 82 DLSQVPpylrpinmmfqSYALFPHMTVEQNIAFGlKQDKLPKAEIASRVNEMLGLVHMQEFAKR-----KPHQLSGGQRQ 156
Cdd:TIGR00957 700 SVAYVP-----------QQAWIQNDSLRENILFG-KALNEKYYQQVLEACALLPDLEILPSGDRteigeKGVNLSGGQKQ 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVV---DILErvGVTCVMVTHDQeEAMTMAGRIAIMNRGKFVQIGE 233
Cdd:TIGR00957 768 RVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpeGVLK--NKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGS 844
|
....
gi 1314858832 234 PEEI 237
Cdd:TIGR00957 845 YQEL 848
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-241 |
1.47e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 65.50 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 21 EIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQV--PPYLRPINMMFQ 98
Cdd:PRK10789 317 NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqlDSWRSRLAVVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 99 SYALFPHmTVEQNIAFGLKQDKLPKAEIASRvnemLGLVHmqEFAKRKPH-----------QLSGGQRQRVALARSLAKR 167
Cdd:PRK10789 397 TPFLFSD-TVANNIALGRPDATQQEIEHVAR----LASVH--DDILRLPQgydtevgergvMLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 168 PKLLLLDEPMGALDkklrDRMQLEVVDILERVGVT-CVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:PRK10789 470 AEILILDDALSAVD----GRTEHQILHNLRQWGEGrTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-230 |
3.24e-11 |
|
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: 63.33 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY-DGQHAV-DDVSLTIYKGEIFALLGASGCGKSTL----LRMLAgfeqpSAGQIMLDGVDLSQVP--PYLR 91
Cdd:cd03289 3 MTVKDLTAKYtEGGNAVlENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVPlqKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 92 PINMMFQSYALFPHmTVEQNI-AFGLKQDKlpkaEIAsRVNEMLGLVH-MQEFAKRKPHQ-------LSGGQRQRVALAR 162
Cdd:cd03289 78 AFGVIPQKVFIFSG-TFRKNLdPYGKWSDE----EIW-KVAEEVGLKSvIEQFPGQLDFVlvdggcvLSHGHKQLMCLAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 163 SLAKRPKLLLLDEPMGALDKklrdrMQLEVV-DILERVGVTC-VMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDP-----ITYQVIrKTLKQAFADCtVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
37-241 |
3.27e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.19 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDgvdlsqvppylRPINMMFQSyALFPHMTVEQNIAFGL 116
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-----------RSIAYVPQQ-AWIMNATVRGNILFFD 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 117 KQD--KLPKAEIASRVNEMLGLVH--MQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
Cdd:PTZ00243 746 EEDaaRLADAVRVSQLEADLAQLGggLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEEC 825
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314858832 193 vdILERV-GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:PTZ00243 826 --FLGALaGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
49-210 |
5.94e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.11 E-value: 5.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 49 ALLGASGCGKSTLLRMLAGFEQPSAGQIM--------------LDGVDLSQVPPylrpINMMfqsyALFPhmtveqniaf 114
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDLSSNPL----LYMM----RCFP---------- 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 115 GLKQDKLpKAEIAS-RVNEMLGLVHMqefakrkpHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVV 193
Cdd:PLN03073 601 GVPEQKL-RAHLGSfGVTGNLALQPM--------YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD--------LDAV 663
|
170 180
....*....|....*....|...
gi 1314858832 194 D------ILERVGVtcVMVTHDQ 210
Cdd:PLN03073 664 EaliqglVLFQGGV--LMVSHDE 684
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-181 |
6.40e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.16 E-value: 6.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSY--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAgfeqpSAGQIMLDGVDLSQVppylrPI 93
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLlsalLRLLS-----TEGEIQIDGVSWNSV-----TL 1287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSYALFPHMTVEQNIAFGLKQDklPKAEIAS----RVNEMLGLVHM-QEFAKRKPHQ-------LSGGQRQRVALA 161
Cdd:TIGR01271 1288 QTWRKAFGVIPQKVFIFSGTFRKNLD--PYEQWSDeeiwKVAEEVGLKSViEQFPDKLDFVlvdggyvLSNGHKQLMCLA 1365
|
170 180
....*....|....*....|
gi 1314858832 162 RSLAKRPKLLLLDEPMGALD 181
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLD 1385
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-181 |
6.83e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.97 E-value: 6.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 23 RNLTKS--YDGQHAV--DDVSLTIYKGEIFALLGASGCGKSTLLRMLAgfEQPSAGqIMLDGVDLSQVPP----YLRPIN 94
Cdd:TIGR00956 763 RNLTYEvkIKKEKRVilNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTG-VITGGDRLVNGRPldssFQRSIG 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 95 MMFQSYALFPHMTVEQNIAFG--LKQDK-LPKAEIASRVNEMLGLVHMQEFAKR---KPHQ-LSGGQRQRVALARSLAKR 167
Cdd:TIGR00956 840 YVQQQDLHLPTSTVRESLRFSayLRQPKsVSKSEKMEYVEEVIKLLEMESYADAvvgVPGEgLNVEQRKRLTIGVELVAK 919
|
170
....*....|....*
gi 1314858832 168 PKLLL-LDEPMGALD 181
Cdd:TIGR00956 920 PKLLLfLDEPTSGLD 934
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
11-250 |
9.59e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.21 E-value: 9.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 11 KTRKALTPLLEIRNLTKSydGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPyL 90
Cdd:PRK10982 242 KENKPGEVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNA-N 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 91 RPINMMF-------QSYALFPHMTVEQN--IA--------FGLKQDKLPKAEIASRVNEMLglvhmqefAKRKPHQ---- 149
Cdd:PRK10982 319 EAINHGFalvteerRSTGIYAYLDIGFNslISnirnyknkVGLLDNSRMKSDTQWVIDSMR--------VKTPGHRtqig 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 150 -LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDiLERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
Cdd:PRK10982 391 sLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAE-LAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
250 260
....*....|....*....|..
gi 1314858832 229 VQIGEPEEIYEHPTTRYSAEFI 250
Cdd:PRK10982 470 AGIVDTKTTTQNEILRLASLHL 491
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
20-240 |
1.13e-10 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 61.46 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAGFEqpsaGQIMLDGVDLSQVPPY-LRP 92
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 -INMMFQSYALFphmtvEQNIAFGLKqdklPKAEIA-SRVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVA 159
Cdd:cd03288 96 rLSIILQDPILF-----SGSIRFNLD----PECKCTdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 160 LARSLAKRPKLLLLDEPMGALDkklrdrMQLEvvDILERVgvtcVMVTHDQEEAMTMAGRIA---------IMNRGKFVQ 230
Cdd:cd03288 167 LARAFVRKSSILIMDEATASID------MATE--NILQKV----VMTAFADRTVVTIAHRVStildadlvlVLSRGILVE 234
|
250
....*....|
gi 1314858832 231 IGEPEEIYEH 240
Cdd:cd03288 235 CDTPENLLAQ 244
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
17-213 |
1.55e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.34 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG-FEQPSAGQIMLDGV---------DLSQV 86
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQGYSNDLTLFGRrrgsgetiwDIKKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 87 PPYLrpinmmfqSYALfpHM------TVEQNI------AFGLKQ---DKLPKaeiasRVNEMLGLVHMQEFAKRKP-HQL 150
Cdd:PRK10938 338 IGYV--------SSSL--HLdyrvstSVRNVIlsgffdSIGIYQavsDRQQK-----LAQQWLDILGIDKRTADAPfHSL 402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 151 SGGQrQRVAL-ARSLAKRPKLLLLDEPMGALD---KKLRDRMqlevVDILERVGVTCVM-VTHDQEEA 213
Cdd:PRK10938 403 SWGQ-QRLALiVRALVKHPTLLILDEPLQGLDplnRQLVRRF----VDVLISEGETQLLfVSHHAEDA 465
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
38-271 |
3.62e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.68 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPY-LRPI-NMMFQSYALFPHmTVEQNI-AF 114
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMdLRKVlGIIPQAPVLFSG-TVRFNLdPF 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 115 GLKQDklpkAEIAsrvnEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLLDEPMGALD-- 181
Cdd:PLN03130 1337 NEHND----ADLW----ESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVDvr 1408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 182 ------KKLRDRMQlevvdilervgvTCVM--VTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS------- 246
Cdd:PLN03130 1409 tdaliqKTIREEFK------------SCTMliIAH-RLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSkmvqstg 1475
|
250 260
....*....|....*....|....*...
gi 1314858832 247 ---AEFIGSVNVFEGVLKERQEDGLVLD 271
Cdd:PLN03130 1476 aanAQYLRSLVFGGDEDRLAREESKALD 1503
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
42-222 |
5.26e-10 |
|
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: 57.97 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 42 IYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLrpinmmfqsyalfphmtveqniafglkqdkl 121
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 122 pkaeiasrvnemlglvhmqefakrkphQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGV 201
Cdd:cd03222 71 ---------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180
....*....|....*....|.
gi 1314858832 202 TCVMVTHDQEEAMTMAGRIAI 222
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHV 144
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
19-181 |
6.18e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.03 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE--QPSAGQIMLDGVDLSQVPPYLRP---I 93
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAgegI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQ--------SYALFPHMTVEQNIAFgLKQDKLPKAEIASRVNEMLGLVHMQE--FAKRKPHQLSGGQRQRVALARS 163
Cdd:PRK09580 81 FMAFQypveipgvSNQFFLQTALNAVRSY-RGQEPLDRFDFQDLMEEKIALLKMPEdlLTRSVNVGFSGGEKKRNDILQM 159
|
170
....*....|....*...
gi 1314858832 164 LAKRPKLLLLDEPMGALD 181
Cdd:PRK09580 160 AVLEPELCILDESDSGLD 177
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
45-209 |
6.26e-10 |
|
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: 59.30 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 45 GEIFALLGASGCGKSTLLRMLAGFEQPSAGQImldgvdlsQVPPYLRPINMMFQSYALFPHMT--VEQNIAFGLKQ---D 119
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--------DDPPDWDEILDEFRGSELQNYFTklLEGDVKVIVKPqyvD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 120 KLPKA------EIASRVNE---------MLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
Cdd:cd03236 98 LIPKAvkgkvgELLKKKDErgkldelvdQLELRHVLD---RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|....*
gi 1314858832 185 RDRMQlEVVDILERVGVTCVMVTHD 209
Cdd:cd03236 175 RLNAA-RLIRELAEDDNYVLVVEHD 198
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-242 |
6.95e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.76 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 17 TPLLEIRNLTKSYDGQHA---VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPSAGQimlDGVDLSQVPPYLRPI 93
Cdd:PLN03232 612 APAISIKNGYFSWDSKTSkptLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-ELSHAET---SSVVIRGSVAYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQSyalfphmTVEQNIAFG--LKQDKLPKAEIASRVNEMLGLV---HMQEFAKRKPHqLSGGQRQRVALARSLAKRP 168
Cdd:PLN03232 688 SWIFNA-------TVRENILFGsdFESERYWRAIDVTALQHDLDLLpgrDLTEIGERGVN-ISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 169 KLLLLDEPMGALDKKLRDRMQLEVVDiLERVGVTCVMVThDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPT 242
Cdd:PLN03232 760 DIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGS 831
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
32-209 |
1.69e-09 |
|
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: 56.56 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLrmLAGFEqpSAGQIMLdgVDLSQVPPYlRPINMMFQSYALfphmtveqn 111
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLY--ASGKARL--ISFLPKFSR-NKLIFIDQLQFL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 112 IAFGLKQDKLpkaeiasrvnemlglvhmqefaKRKPHQLSGGQRQRVALARSLAKRPK--LLLLDEPMGALDKKLRDRMq 189
Cdd:cd03238 72 IDVGLGYLTL----------------------GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQL- 128
|
170 180
....*....|....*....|
gi 1314858832 190 LEVVDILERVGVTCVMVTHD 209
Cdd:cd03238 129 LEVIKGLIDLGNTVILIEHN 148
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
31-208 |
2.19e-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: 58.99 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF--------EQPSAGQIMLdgvdlsqVP--PYLRpiNMMFQSY 100
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFY-------VPqrPYMT--LGTLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 101 ALFPhMTVEQNIAFGLKQDKLpkaeiasrvNEMLGLVHMQEFAKRK---------PHQLSGGQRQRVALARSLAKRPKLL 171
Cdd:TIGR00954 535 IIYP-DSSEDMKRRGLSDKDL---------EQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190
....*....|....*....|....*....|....*..
gi 1314858832 172 LLDEPMGALDKKLRDRMqlevVDILERVGVTCVMVTH 208
Cdd:TIGR00954 605 ILDECTSAVSVDVEGYM----YRLCREFGITLFSVSH 637
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
35-211 |
2.69e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.64 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDG----VDLSQVPPYL-RP-INMMFQSYALFPHMTV 108
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlAWVNQETPALpQPaLEYVIDGDREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 109 EQNIA-----------FGLKQDKLPKAEIASRVNEML-GLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:PRK10636 97 QLHDAnerndghaiatIHGKLDAIDAWTIRSRAASLLhGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1314858832 177 MGALDkklrdrmqLEVVDILER----VGVTCVMVTHDQE 211
Cdd:PRK10636 177 TNHLD--------LDAVIWLEKwlksYQGTLILISHDRD 207
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-181 |
3.57e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.33 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLA--------------GFEQPSAG------QIMLD 79
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncqilHVEQEVVGddttalQCVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 80 gVDLSQVPPYLRPINMMFQSYAL-FPHMTVEQNIAF--GLKQDKLPK--AEIASRVNE-------------MLGLVHMQE 141
Cdd:PLN03073 258 -TDIERTQLLEEEAQLVAQQRELeFETETGKGKGANkdGVDKDAVSQrlEEIYKRLELidaytaearaasiLAGLSFTPE 336
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1314858832 142 FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
44-209 |
4.19e-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: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 44 KGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMlDGVDLSQVPPYlrpinmmFQSYALFPHMT--VEQNIAFGLK-Q-- 118
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYD-EEPSWDEVLKR-------FRGTELQDYFKklANGEIKVAHKpQyv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 119 DKLPKA------EIASRVNE---------MLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
Cdd:COG1245 170 DLIPKVfkgtvrELLEKVDErgkldelaeKLGLENILD---RDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246
|
170 180
....*....|....*....|....*.
gi 1314858832 184 LRDRMQlEVVDILERVGVTCVMVTHD 209
Cdd:COG1245 247 QRLNVA-RLIRELAEEGKYVLVVEHD 271
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-181 |
4.68e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.20 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 15 ALTPLLEIRNLTKSYDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLA----GFEQPSAGQIMLDGVDLSQVP 87
Cdd:TIGR00956 54 LLKILTRGFRKLKKFRDTKTFDilkPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 88 PYLR-PINMMFQSYALFPHMTVEQNIAF-------GLKQDKLPKAEIASRVNEM----LGLVHMQ------EFAKrkphQ 149
Cdd:TIGR00956 134 KHYRgDVVYNAETDVHFPHLTVGETLDFaarcktpQNRPDGVSREEYAKHIADVymatYGLSHTRntkvgnDFVR----G 209
|
170 180 190
....*....|....*....|....*....|..
gi 1314858832 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
Cdd:TIGR00956 210 VSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
39-237 |
1.44e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 39 SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDgvdlsqvppYLRPINMMFQSYA--------------LFP 104
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ---------FSHITRLSFEQLQklvsdewqrnntdmLSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 105 H-----MTVEQNIafglkQDKLPKAEIASRVNEMLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:PRK10938 94 GeddtgRTTAEII-----QDEVKDPARCEQLAQQFGITALLD---RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1314858832 180 LDkkLRDRMQL-EVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK10938 166 LD--VASRQQLaELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-237 |
1.50e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.67 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PLLEIRNLTKSYDG---QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQP--SAGQIMLDGvDLSQVPPylrp 92
Cdd:PLN03130 613 PAISIKNGYFSWDSkaeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPprSDASVVIRG-TVAYVPQ---- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 93 INMMFQSyalfphmTVEQNIAFGLKQDKlPKAEIASRVNEM---LGLV---HMQEFAKRKPHqLSGGQRQRVALARSLAK 166
Cdd:PLN03130 687 VSWIFNA-------TVRDNILFGSPFDP-ERYERAIDVTALqhdLDLLpggDLTEIGERGVN-ISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 167 RPKLLLLDEPMGALD---------KKLRDRMQlevvdilervGVTCVMVThDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PLN03130 758 NSDVYIFDDPLSALDahvgrqvfdKCIKDELR----------GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-240 |
2.61e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.67 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 27 KSYDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGvdlsqvppylrPINMMFQSYALFP 104
Cdd:PRK13545 30 RSKDGEyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----------SAALIAISSGLNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 105 HMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
Cdd:PRK13545 99 QLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 185 RDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:PRK13545 179 TKKC-LDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
45-181 |
8.31e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 45 GEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLD-GVDLSqvppYLRPINMMFQS------------------------ 99
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLG----KLRQDQFAFEEftvldtvimghtelwevkqerdri 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 100 YALfPHMTVEQniafGLKQDKLpKAEIA--------SRVNEML-----------GLvhMQEFAkrkPhqlsgGQRQRVAL 160
Cdd:PRK15064 103 YAL-PEMSEED----GMKVADL-EVKFAemdgytaeARAGELLlgvgipeeqhyGL--MSEVA---P-----GWKLRVLL 166
|
170 180
....*....|....*....|.
gi 1314858832 161 ARSLAKRPKLLLLDEPMGALD 181
Cdd:PRK15064 167 AQALFSNPDILLLDEPTNNLD 187
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-233 |
1.09e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 19 LLEIRNLTkSYDGQHA----VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG--FEQPSAGQIMLDG--VDLSQVPpyl 90
Cdd:NF040905 257 VFEVKNWT-VYHPLHPerkvVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGkeVDVSTVS--- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 91 RPINMMF-------QSYALFPHMTVEQNIAFGlkqdKLPKaeIASR--VNEMLGLVHMQEFAKR----------KPHQLS 151
Cdd:NF040905 333 DAIDAGLayvtedrKGYGLNLIDDIKRNITLA----NLGK--VSRRgvIDENEEIKVAEEYRKKmniktpsvfqKVGNLS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 152 GGQRQRVALARSLAKRPKLLLLDEP-----MGAldkklrdrmQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIM 223
Cdd:NF040905 407 GGNQQKVVLSKWLFTDPDVLILDEPtrgidVGA---------KYEIYTIINELaaeGKGVIVISSELPELLGMCDRIYVM 477
|
250
....*....|
gi 1314858832 224 NRGKFVqiGE 233
Cdd:NF040905 478 NEGRIT--GE 485
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
18-223 |
3.77e-07 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 50.35 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 18 PL-LEIRNLTkSYDGQHAVDDVSLTiyKGEIFALLGASGCGKSTLLR--MLAGF-EQPSAGQIMLDGVDLSQVPPYLRpI 93
Cdd:cd03279 3 PLkLELKNFG-PFREEQVIDFTGLD--NNGLFLICGPTGAGKSTILDaiTYALYgKTPRYGRQENLRSVFAPGEDTAE-V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 94 NMMFQ----SYALF--PHMTVEQ--NIAFglkqdkLPKAEIAsrvnemlglvhmqEFAKRKPHQLSGGQRQRVALARSLA 165
Cdd:cd03279 79 SFTFQlggkKYRVErsRGLDYDQftRIVL------LPQGEFD-------------RFLARPVSTLSGGETFLASLSLALA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 166 ----------KRPKLLLLDEPMGALDKKLRDRMQlEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIM 223
Cdd:cd03279 140 lsevlqnrggARLEALFIDEGFGTLDPEALEAVA-TALELIRTENRMVGVISHVEELKERIPQRLEVI 206
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
44-209 |
4.24e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 44 KGEIFALLGASGCGKSTLLRMLAGFEQPSAGqimldgvDLSQVPPYLRPINMmFQSYALFPHMT--VEQNIAFGLK-Q-- 118
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLG-------DYEEEPSWDEVLKR-FRGTELQNYFKklYNGEIKVVHKpQyv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 119 DKLPKA------EIASRVNE---------MLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkk 183
Cdd:PRK13409 170 DLIPKVfkgkvrELLKKVDErgkldevveRLGLENILD---RDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD-- 244
|
170 180
....*....|....*....|....*...
gi 1314858832 184 LRDRMqlEVVDILERV--GVTCVMVTHD 209
Cdd:PRK13409 245 IRQRL--NVARLIRELaeGKYVLVVEHD 270
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
37-261 |
3.43e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGfeQPSAGQIMLDgVDLSQVPP----YLRPINMMFQSYALFPHMTVEQNI 112
Cdd:PLN03140 898 EVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGD-IRISGFPKkqetFARISGYCEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 113 ---AFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKR-----KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK- 183
Cdd:PLN03140 975 iysAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARa 1054
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 184 --LRDRMQLEVVDilerVGVTCVMVTH----DQEEAMTmagRIAIMNRGKFVqigepeeIYEHPTTRYSAEFIGSVNVFE 257
Cdd:PLN03140 1055 aaIVMRTVRNTVD----TGRTVVCTIHqpsiDIFEAFD---ELLLMKRGGQV-------IYSGPLGRNSHKIIEYFEAIP 1120
|
....
gi 1314858832 258 GVLK 261
Cdd:PLN03140 1121 GVPK 1124
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
137-211 |
4.02e-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: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 137 VHMQEFAK---RKPHQLSGGQRQ------RVALARSLAKRPKLLLLDEPMGALDkklRDRMQLEVVDILERVGVTCVM-- 205
Cdd:cd03240 100 CHQGESNWpllDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD---EENIEESLAEIIEERKSQKNFql 176
|
....*...
gi 1314858832 206 --VTHDQE 211
Cdd:cd03240 177 ivITHDEE 184
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
150-241 |
8.92e-05 |
|
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: 44.62 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 150 LSGGQRQRVALARSLAKRPK--LLLLDEPMGALDKklRDRMQL-EVVDILERVGVTCVMVTHDqEEAMTMAGRI------ 220
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQ--RDNRRLiNTLKRLRDLGNTLIVVEHD-EDTIRAADYVidigpg 565
|
90 100
....*....|....*....|.
gi 1314858832 221 AIMNRGKFVQIGEPEEIYEHP 241
Cdd:TIGR00630 566 AGEHGGEVVASGTPEEILANP 586
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
32-220 |
1.41e-04 |
|
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: 42.63 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLlrmlaGFEQPSA-GQIMLdgvdLSQVPPYLRP-INMMFQSY-----ALFP 104
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSL-----AFDTIYAeGQRRY----VESLSAYARQfLGQMDKPDvdsieGLSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 105 HMTVEQNIA-------FGLKQ---DKL----PKAEIASRVNEM--LGLVHMQefAKRKPHQLSGGQRQRVALARSLAKRP 168
Cdd:cd03270 79 AIAIDQKTTsrnprstVGTVTeiyDYLrllfARVGIRERLGFLvdVGLGYLT--LSRSAPTLSGGEAQRIRLATQIGSGL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 169 K--LLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDqEEAMTMAGRI 220
Cdd:cd03270 157 TgvLYVLDEPSIGLHPRDNDRL-IETLKRLRDLGNTVLVVEHD-EDTIRAADHV 208
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
150-211 |
1.68e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 1.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 150 LSGGQRQ------RVALARSLAKRPKLLLLDEPMGALDKKLRDRMqlevVDILER-------VgvtcVMVTHDQE 211
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKL----VDIMERylrkipqV----IIVSHDEE 855
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
38-246 |
1.90e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.61 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQ--VPPYLRPINMMFQSYALFPHmTVEQNIafg 115
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVLFDG-TVRQNV--- 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 116 lkqDKLPKAEIAsRVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKR-PKLLLLDEPMGALDKK 183
Cdd:PTZ00243 1405 ---DPFLEASSA-EVWAALELVGLRERVASESEGIdsrvleggsnySVGQRQLMCMARALLKKgSGFILMDEATANIDPA 1480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314858832 184 LRDRMQLEVVDILErvGVTCVMVTHdqeEAMTMA--GRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
Cdd:PTZ00243 1481 LDRQIQATVMSAFS--AYTVITIAH---RLHTVAqyDKIIVMDHGAVAEMGSPRELVMNRQSIFH 1540
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
150-208 |
1.95e-04 |
|
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: 43.46 E-value: 1.95e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314858832 150 LSGGQRQRVALARSLAKR---PKLLLLDEPMGALD----KKLrdrmqLEVVDILERVGVTCVMVTH 208
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHfddiKKL-----LEVLQRLVDKGNTVVVIEH 890
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
20-209 |
2.38e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.92 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 20 LEIRNLtKSYDGQHAVDdvsltiYKGEIFALLGASGCGKSTLLR----MLAGfEQPSAGQIMLDGVDLSQVPPYLRpinM 95
Cdd:COG0419 5 LRLENF-RSYRDTETID------FDDGLNLIVGPNGAGKSTILEairyALYG-KARSRSKLRSDLINVGSEEASVE---L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 96 MF----QSYALfphmTVEQNiafglKQDKLPKAEIASR---VNEMLGLVHMQEFAKR----------------------- 145
Cdd:COG0419 74 EFehggKRYRI----ERRQG-----EFAEFLEAKPSERkeaLKRLLGLEIYEELKERlkeleealesaleelaelqklkq 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314858832 146 ----------KPHQLSGGQRQRVALARSLAkrpklLLLDepMGALDKKLRDRMqlevVDILERVGVtcvmVTHD 209
Cdd:COG0419 145 eilaqlsgldPIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERL----LDALEELAI----ITHV 203
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
150-187 |
4.23e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 4.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1314858832 150 LSGGQRQRVALARSLAKRPK---LLLLDEP------------MGALDkKLRDR 187
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPttglhfhdirklLEVLH-RLVDK 878
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
148-211 |
5.74e-04 |
|
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: 40.04 E-value: 5.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314858832 148 HQLSGGQRQRVALARSLA----KRPKLLLLDEPMGALDkkLRDRMQLEVVdILERVGVTCVM--VTHDQE 211
Cdd:cd03227 76 LQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLD--PRDGQALAEA-ILEHLVKGAQVivITHLPE 142
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
150-209 |
1.02e-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: 40.29 E-value: 1.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314858832 150 LSGGQRQRVALARSLAKR---PKLLLLDEPMGALD----KKLrdrmqLEVVDILERVGVTCVMVTHD 209
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHfhdvKKL-----LEVLQRLVDKGNTVVVIEHN 231
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
150-176 |
2.47e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 2.47e-03
10 20 30
....*....|....*....|....*....|
gi 1314858832 150 LSGGQRQRVALARSLAKRPK---LLLLDEP 176
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEP 860
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
147-211 |
3.82e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 3.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314858832 147 PHQLSGGQRQ------RVALARSLAK-----RP-KLLLLDEPMGALDKKLRDRMqLEVVDILERVGV-TCVMVTHDQE 211
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAEgiegdAPlPPLILDEPTVFLDSGHVSQL-VDLVESMRRLGVeQIVVVSHDDE 855
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
15-66 |
5.83e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 39.02 E-value: 5.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1314858832 15 ALTPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLA 66
Cdd:COG5635 150 LLVSLDDLYVPLNLLERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLA 201
|
|
| |
