|
Name |
Accession |
Description |
Interval |
E-value |
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-325 |
2.76e-172 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 481.91 E-value: 2.76e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMV 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 161 LSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGNYNLL 240
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 241 DA------DKATQLLQRPISSR------------IAIRPEAIELSRTGE---LDALVRSHSLLGNVIRYRIE-ARGVELV 298
Cdd:COG3842 243 PGtvlgdeGGGVRTGGRTLEVPadaglaaggpvtVAIRPEDIRLSPEGPengLPGTVEDVVFLGSHVRYRVRlGDGQELV 322
|
330 340
....*....|....*....|....*..
gi 545130686 299 VDVLNRSADDLHPdGQRLALSIDPSAL 325
Cdd:COG3842 323 VRVPNRAALPLEP-GDRVGLSWDPEDV 348
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-325 |
8.31e-143 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 407.15 E-value: 8.31e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMV 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 161 LSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGNY--N 238
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPpmN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 239 LLDADKATQLLQR-----PISSR----------IAIRPEAIELSRTGE--LDALVRSHSLLGNVIRYRIEARGVELVVDV 301
Cdd:COG3839 241 LLPGTVEGGGVRLggvrlPLPAAlaaaaggevtLGIRPEHLRLADEGDggLEATVEVVEPLGSETLVHVRLGGQELVARV 320
|
330 340
....*....|....*....|....
gi 545130686 302 lnrSADDLHPDGQRLALSIDPSAL 325
Cdd:COG3839 321 ---PGDTRLRPGDTVRLAFDPERL 341
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-325 |
1.06e-132 |
|
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: 381.69 E-value: 1.06e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMV 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 161 LSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGNYNLL 240
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 241 DA---------------DKATQLLQRPISSRIAIRPEAIELSRTGE----LDALVRSHSLLGNviRYRIEAR-----GVE 296
Cdd:TIGR03265 242 PGtrgggsrarvggltlACAPGLAQPGASVRLAVRPEDIRVSPAGNaanlLLARVEDMEFLGA--FYRLRLRleglpGQA 319
|
330 340 350
....*....|....*....|....*....|.
gi 545130686 297 LVVDVLnRSADDLHPD--GQRLALSIDPSAL 325
Cdd:TIGR03265 320 LVADVS-ASEVERLGIraGQPIWIELPAERL 349
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-325 |
2.63e-130 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 375.25 E-value: 2.63e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSfVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI-VPLSPQKRHIGM 79
Cdd:COG1118 1 MS-IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDE 159
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 160 PLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGNYNL 239
Cdd:COG1118 160 PFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 240 LD---------ADKATQLLQRPISSRIA---IRPEAIELSRTGE----LDALVRSHSLLGNVIRYRIEARGVE---LVVD 300
Cdd:COG1118 240 LRgrviggqleADGLTLPVAEPLPDGPAvagVRPHDIEVSREPEgentFPATVARVSELGPEVRVELKLEDGEgqpLEAE 319
|
330 340
....*....|....*....|....*.
gi 545130686 301 VLNRSADDLHPD-GQRLALSIDPSAL 325
Cdd:COG1118 320 VTKEAWAELGLApGDPVYLRPRPARV 345
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-235 |
1.69e-124 |
|
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: 356.16 E-value: 1.69e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMVFQS 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 YALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545130686 164 LDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIG 235
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-242 |
1.06e-121 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 354.64 E-value: 1.06e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMV 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 161 LSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGNYNLL 240
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIF 251
|
..
gi 545130686 241 DA 242
Cdd:PRK09452 252 DA 253
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-216 |
3.68e-115 |
|
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: 331.79 E-value: 3.68e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMVFQS 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 YALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545130686 164 LDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-323 |
6.13e-109 |
|
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: 320.21 E-value: 6.13e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 34 LLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMVFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKR 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 114 VQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHD 193
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 194 QEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGNYNLLDA-------------------DKATQLLQRPIS 254
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEAtvierkseqvvlagvegrrCDIYTDVPVEKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 255 SR--IAIRPEAIELSRTGE------LDALVRSHSLLGNVIRY--RIEARGVELVVDVLNrsADDLHPD---GQRLALSID 321
Cdd:TIGR01187 241 QPlhVVLRPEKIVIEEEDEanssnaIIGHVIDITYLGMTLEVhvRLETGQKVLVSEFFN--EDDPHMSpsiGDRVGLTWH 318
|
..
gi 545130686 322 PS 323
Cdd:TIGR01187 319 PG 320
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-322 |
5.31e-107 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 316.28 E-value: 5.31e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 2 SFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMVF 81
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 82 QSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPL 161
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 162 SALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGNYNLLD 241
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 242 ADKATQ-------LLQRPI---------SSRIAIRPEAIELSRTGELD--ALVRSHSLLGNVIRYRIEARGVELvvdVLN 303
Cdd:PRK11432 245 ATLSGDyvdiygyRLPRPAafafnlpdgECTVGVRPEAITLSEQGEESqrCTIKHVAYMGPQYEVTVDWHGQEL---LLQ 321
|
330 340
....*....|....*....|
gi 545130686 304 RSADDLHPD-GQRLALSIDP 322
Cdd:PRK11432 322 VNATQLQPDlGEHYYLEIHP 341
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-236 |
1.57e-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: 300.80 E-value: 1.57e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSfVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMV 80
Cdd:cd03296 1 MS-IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPNMTVEQNVAFGLRMQKV----NADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLL 156
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 157 LDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGN 236
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-207 |
3.45e-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: 300.47 E-value: 3.45e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYA----GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPqkrH 76
Cdd:COG1116 5 APALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 77 IGMVFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLL 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 545130686 157 LDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLM 207
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
1.43e-99 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 292.24 E-value: 1.43e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMVFQS 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 YALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545130686 164 LDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-325 |
1.76e-99 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 297.14 E-value: 1.76e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAG-TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGM 79
Cdd:PRK11650 1 MAGLKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDE 159
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 160 PLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGN--Y 237
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpaM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 238 NLLDADKATQLLQRPISSRIA------------------IRPEAIELSR-TGELDALVRSHSLLG--NVIRYRIEarGVE 296
Cdd:PRK11650 241 NLLDGRVSADGAAFELAGGIAlplgggyrqyagrkltlgIRPEHIALSSaEGGVPLTVDTVELLGadNLAHGRWG--GQP 318
|
330 340
....*....|....*....|....*....
gi 545130686 297 LVVDVLNRSAddlHPDGQRLALSIDPSAL 325
Cdd:PRK11650 319 LVVRLPHQER---PAAGSTLWLHLPANQL 344
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-214 |
1.66e-96 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 284.75 E-value: 1.66e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAG----TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQdivPLSPQKRHIGM 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE---PVTGPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDE 159
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 160 PLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQ--GKIVQ 214
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-240 |
5.05e-96 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 284.00 E-value: 5.05e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMVFQS 83
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 YALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 164 LDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGNYNLL 240
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-241 |
6.71e-94 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 283.65 E-value: 6.71e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 6 VQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMVFQSYA 85
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 86 LFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALD 165
Cdd:PRK11607 102 LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 166 ARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGNYNLLD 241
Cdd:PRK11607 182 KKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFE 257
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-276 |
1.09e-91 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 275.43 E-value: 1.09e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 7 QHLQKSYA-GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGMVFQS 83
Cdd:COG1125 5 ENVTKRYPdGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVIQQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 YALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVEL--KDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPL 161
Cdd:COG1125 85 IGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 162 SALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIG---NYN 238
Cdd:COG1125 165 GALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGadrGLR 244
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 545130686 239 LLDADKATQLLQRPIssrIAIRP-----EAIELSRTGELDALV 276
Cdd:COG1125 245 RLSLLRVEDLMLPEP---PTVSPdaslrEALSLMLERGVDWLL 284
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-273 |
1.65e-91 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 276.96 E-value: 1.65e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSfVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMV 80
Cdd:PRK10851 1 MS-IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPNMTVEQNVAFGLRM----QKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLL 156
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 157 LDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGN 236
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 545130686 237 YNLLDAD-KATQLL----QRPISSRIA--------IRPEAIELSRTGELD 273
Cdd:PRK10851 240 VNRLQGTiRGGQFHvgahRWPLGYTPAyqgpvdlfLRPWEVDISRRTSLD 289
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-239 |
3.61e-90 |
|
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: 269.21 E-value: 3.61e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 6 VQHLQKSYaGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMVFQSYA 85
Cdd:cd03299 3 VENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 86 LFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALD 165
Cdd:cd03299 82 LFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545130686 166 ARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGNYNL 239
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
6-309 |
4.15e-90 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 273.10 E-value: 4.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 6 VQHLQKSYAGTPVfSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMVFQSYA 85
Cdd:NF040840 4 IENLSKDWKEFKL-RDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 86 LFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALD 165
Cdd:NF040840 83 LFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 166 ARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGNYNLLD--AD 243
Cdd:NF040840 163 VQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEgvAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 244 KATQL---------LQRPISS----RIAIRPEAIELSRTG-------ELDALVRSHSLLGNVIRYRIEArGVELVVDVLN 303
Cdd:NF040840 243 KGGEGtildtgnikIELPEEKkgkvRIGIRPEDITISTEKvktsarnEFKGKVEEIEDLGPLVKLTLDV-GIILVAFITR 321
|
....*.
gi 545130686 304 RSADDL 309
Cdd:NF040840 322 SSFLDL 327
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-235 |
1.78e-88 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 269.59 E-value: 1.78e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 161 LSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIG 235
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIG 235
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-225 |
7.78e-87 |
|
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: 260.68 E-value: 7.78e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK-----RHIG 78
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 79 MVFQSYALFPNMTVEQNVAFGLRMQ-KVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLL 157
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545130686 158 DEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
4-242 |
5.31e-86 |
|
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: 263.01 E-value: 5.31e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVD--SGKILLDGQDIVPLSPQKRHIGMVF 81
Cdd:TIGR03258 6 IRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAglTGRIAIADRDLTHAPPHKRGLALLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 82 QSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPL 161
Cdd:TIGR03258 86 QNYALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 162 SALDARIRKHLREQIRQIQREL-GLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGNYNLL 240
Cdd:TIGR03258 166 SALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANIL 245
|
..
gi 545130686 241 DA 242
Cdd:TIGR03258 246 PA 247
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-225 |
1.12e-83 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 252.61 E-value: 1.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVP----LSPQKRHIGM 79
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskkdINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPNMTVEQNVAFGLRM-QKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLD 158
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 159 EPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:COG1126 162 EPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENP 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-235 |
1.51e-82 |
|
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: 249.91 E-value: 1.51e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAG-TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGMV 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVEL--KDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLD 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 159 EPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIG 235
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-213 |
5.28e-82 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 248.03 E-value: 5.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSY----AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKR---- 75
Cdd:COG1136 5 LELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 76 --HIGMVFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPR 153
Cdd:COG1136 85 rrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 154 LLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDqEEALTMSDRIFLMNQGKIV 213
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-225 |
1.34e-81 |
|
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: 256.37 E-value: 1.34e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYA-----GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK---- 74
Cdd:COG1123 261 LEVRNLSKRYPvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 75 -RHIGMVFQ--SYALFPNMTVEQNVAFGLRMQKV-NADDSHKRVQEVLQLVEL-KDLAGRYPHQMSGGQCQRVALARSLV 149
Cdd:COG1123 341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 150 TRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-234 |
1.39e-79 |
|
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: 243.32 E-value: 1.39e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSP------QKRHIGMVFQSYALFPNMTVEQ 94
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelrelRRKKISMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 95 NVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLRE 174
Cdd:cd03294 122 NVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQD 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 175 QIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFI 234
Cdd:cd03294 202 ELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-212 |
1.37e-77 |
|
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: 236.62 E-value: 1.37e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAG----TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKR---- 75
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 76 --HIGMVFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPR 153
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545130686 154 LLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALtMSDRIFLMNQGKI 212
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-221 |
1.13e-76 |
|
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: 234.70 E-value: 1.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK-----RHIG 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 79 MVFQSYALFPNMTVEQNVAFGLRMQ-KVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLL 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 158 DEPLSALDArIRKHLREQ-IRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:cd03261 161 DEPTAGLDP-IASGVIDDlIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-225 |
1.66e-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: 1.66e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYA-GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGMV 80
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQS--YALFpNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLD 158
Cdd:COG1122 81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 159 EPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-216 |
1.76e-75 |
|
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: 231.03 E-value: 1.76e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 26 VAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKI------LLDGQDIVPLSPQKRHIGMVFQSYALFPNMTVEQNVAFG 99
Cdd:cd03297 20 DLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 100 LRMQKVNADdsHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQI 179
Cdd:cd03297 100 LKRKRNRED--RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 545130686 180 QRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03297 178 KKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-221 |
4.05e-74 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 228.02 E-value: 4.05e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ-KRHIGMVFQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 SYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545130686 163 ALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-285 |
5.61e-74 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 232.44 E-value: 5.61e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 11 KSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSP------QKRHIGMVFQSY 84
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 85 ALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSAL 164
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 165 DARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGNYNLLDADK 244
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 545130686 245 ATQLLQRPISSRIAIRP-----EAIELSRTGELDALV---RSHSLLGNV 285
Cdd:TIGR01186 241 AERIAQRMNTGPITKTAdkgprSALQLMRDERVDSLYvvdRQNKLVGVV 289
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-212 |
4.28e-73 |
|
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: 224.72 E-value: 4.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ----KRHIGM 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPNMTVEQNVAFGLR-MQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545130686 159 EPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKI 212
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-211 |
6.93e-73 |
|
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: 222.83 E-value: 6.93e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 6 VQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLS----PQKRHIGMVF 81
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 82 QSYALFPNMTVEQNVAFGLrmqkvnaddshkrvqevlqlvelkdlagryphqmSGGQCQRVALARSLVTRPRLLLLDEPL 161
Cdd:cd03229 83 QDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 545130686 162 SALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGK 211
Cdd:cd03229 129 SALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-229 |
9.64e-73 |
|
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: 225.31 E-value: 9.64e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGMVF 81
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 82 QSYALFPNMTVEQNVAFGL-----RMQKVNADDsHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLL 156
Cdd:COG1120 82 QEPPAPFGLTVRELVALGRyphlgLFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 157 LDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPV--DVF 229
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELleEVY 235
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-221 |
1.20e-72 |
|
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: 225.07 E-value: 1.20e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSY----AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVP--LSPQKRHI 77
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRrrRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 78 GMVFQSY--ALFPNMTVEQNVAFGLRMQKVnaDDSHKRVQEVLQLVEL-KDLAGRYPHQMSGGQCQRVALARSLVTRPRL 154
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 155 LLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-225 |
5.72e-72 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 226.11 E-value: 5.72e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAG----TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK----- 74
Cdd:COG1135 2 IELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 75 RHIGMVFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRL 154
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 155 LLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDqeealtMS------DRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE------MDvvrricDRVAVLENGRIVEQGPVLDVFANP 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-216 |
7.68e-71 |
|
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: 219.68 E-value: 7.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAG----TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKR---- 75
Cdd:cd03257 2 LEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 76 -HIGMVFQSY--ALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVEL---KDLAGRYPHQMSGGQCQRVALARSLV 149
Cdd:cd03257 82 kEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 150 TRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-214 |
1.83e-70 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 219.73 E-value: 1.83e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAG----TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKrh 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 77 iGMVFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLL 156
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 157 LDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLM--NQGKIVQ 214
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
9-235 |
2.00e-70 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 218.47 E-value: 2.00e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 9 LQKSYAGTPVfsDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMVFQSYALFP 88
Cdd:COG3840 7 LTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 89 NMTVEQNVAFGLRMQ-KVNADDsHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDAR 167
Cdd:COG3840 85 HLTVAQNIGLGLRPGlKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545130686 168 IRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIG 235
Cdd:COG3840 164 LRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-211 |
3.77e-69 |
|
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: 214.64 E-value: 3.77e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAG--TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGMV 80
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQsyalFP-----NMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLL 155
Cdd:cd03225 81 FQ----NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 156 LLDEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGK 211
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-216 |
8.45e-69 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 214.15 E-value: 8.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYA-GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK-----RHI 77
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 78 GMVFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLL 157
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545130686 158 DEPLSALD----ARIRKHLREqirqIQReLGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:COG2884 162 DEPTGNLDpetsWEIMELLEE----INR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-225 |
1.84e-67 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 211.29 E-value: 1.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGT----PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSP-----QK 74
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelrkAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 75 RHIGMVFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRL 154
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545130686 155 LLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-225 |
2.00e-67 |
|
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: 219.77 E-value: 2.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAG--TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGL---TSVDSGKILLDGQDIVPLSPQKR--H 76
Cdd:COG1123 5 LEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALRgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 77 IGMVFQS--YALFPnMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRL 154
Cdd:COG1123 85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545130686 155 LLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-297 |
1.23e-66 |
|
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: 213.04 E-value: 1.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDG---QD---IVPLSPQKRHIGMVFQSYALFPNMTVEQ 94
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDsarGIFLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 95 NVAFGLRmqKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLRE 174
Cdd:COG4148 97 NLLYGRK--RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 175 QIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGNYNLLDAdkatqllqrpis 254
Cdd:COG4148 175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEA------------ 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 545130686 255 sRIAIRPEAIELSR----TGELdaLVRSHSL-LGNVIRYRIEARGVEL 297
Cdd:COG4148 243 -TVAAHDPDYGLTRlalgGGRL--WVPRLDLpPGTRVRVRIRARDVSL 287
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-225 |
2.94e-66 |
|
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: 211.07 E-value: 2.94e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSY---AGT-PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGL---TSVDSGKILLDGQDIVPLSPQK-- 74
Cdd:COG0444 2 LEVRNLKVYFptrRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 75 ----RHIGMVFQ-SY-ALFPNMTVEQNVAFGLRM-QKVNADDSHKRVQEVLQLVEL---KDLAGRYPHQMSGGQCQRVAL 144
Cdd:COG0444 82 kirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 145 ARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTA 224
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFEN 241
|
.
gi 545130686 225 P 225
Cdd:COG0444 242 P 242
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-206 |
2.79e-65 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 204.64 E-value: 2.79e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVD---SGKILLDGQDIVPLSPQKRHIGMVF 81
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 82 QSYALFPNMTVEQNVAFGLRmQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPL 161
Cdd:COG4136 83 QDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 545130686 162 SALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFL 206
Cdd:COG4136 162 SKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-221 |
1.18e-64 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 204.52 E-value: 1.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYA-GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK-----RHI 77
Cdd:COG3638 3 LELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 78 GMVFQSYALFPNMTVEQNVAFGL--RM-------QKVNADDsHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSL 148
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGRlgRTstwrsllGLFPPED-RERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545130686 149 VTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-230 |
2.52e-64 |
|
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: 204.20 E-value: 2.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGT--PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDivPLSPQK-----RH 76
Cdd:TIGR04520 1 IEVENVSFSYPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENlweirKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 77 IGMVFQSyalfP-----NMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTR 151
Cdd:TIGR04520 79 VGMVFQN----PdnqfvGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545130686 152 PRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALtMSDRIFLMNQGKIVQSGdaetlytAPVDVFA 230
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEG-------TPREIFS 225
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-251 |
7.17e-64 |
|
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: 203.45 E-value: 7.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYA-GTP----VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVP-----LSPQ 73
Cdd:TIGR04521 1 IKLKNVSYIYQpGTPfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkkkLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 74 KRHIGMVFQ--SYALFPNmTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVEL-KDLAGRYPHQMSGGQCQRVALARSLVT 150
Cdd:TIGR04521 81 RKKVGLVFQfpEHQLFEE-TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 151 RPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGdaetlytAPVDVFA 230
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDG-------TPREVFS 232
|
250 260
....*....|....*....|..
gi 545130686 231 AG-FIGNYNlLDADKATQLLQR 251
Cdd:TIGR04521 233 DVdELEKIG-LDVPEITELARK 253
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-225 |
9.00e-64 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 201.86 E-value: 9.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHI----GM 79
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPNMTVEQNVAFG-LRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLD 158
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 159 EPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-225 |
1.30e-63 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 204.58 E-value: 1.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYA-GTPVFS----------DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSP 72
Cdd:COG4608 8 LEVRDLKKHFPvRGGLFGrtvgvvkavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 73 QK-----RHIGMVFQ-SYA-LFPNMTVEQNVAFGLRMQKVNADDSHK-RVQEVLQLVELK-DLAGRYPHQMSGGQCQRVA 143
Cdd:COG4608 88 RElrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGLASKAERReRVAELLELVGLRpEHADRYPHEFSGGQRQRIG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 144 LARSLVTRPRLLLLDEPLSALDARIRKhlreQI----RQIQRELGLTTIFVTHDqeeaLTM----SDRIFLMNQGKIVQS 215
Cdd:COG4608 168 IARALALNPKLIVCDEPVSALDVSIQA----QVlnllEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIVEI 239
|
250
....*....|
gi 545130686 216 GDAETLYTAP 225
Cdd:COG4608 240 APRDELYARP 249
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-287 |
2.08e-60 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 196.56 E-value: 2.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 7 QHLQKSYAG----TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ-----KRHI 77
Cdd:PRK11153 5 KNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrkaRRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 78 GMVFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLL 157
Cdd:PRK11153 85 GMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 158 DEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGny 237
Cdd:PRK11153 165 DEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQ-- 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 545130686 238 NLLDADKATQLLQRPISSRIAIRPEAIELSRTGE-LDAlvrshSLLGNVIR 287
Cdd:PRK11153 243 STLHLDLPEDYLARLQAEPTTGSGPLLRLEFTGEsVDA-----PLLSETAR 288
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-226 |
3.17e-60 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 193.00 E-value: 3.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQdivPLSPQKRHIGMV 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYAL---FPnMTVEQNVAFGLR-----MQKVNADDsHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRP 152
Cdd:COG1121 81 PQRAEVdwdFP-ITVRDVVLMGRYgrrglFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545130686 153 RLLLLDEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGkIVQSGDAETLYTAPV 226
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPEN 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-221 |
1.54e-59 |
|
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: 190.47 E-value: 1.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSV-----DSGKILLDGQDIVPLSPQ----K 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvlelR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 75 RHIGMVFQSYALFPnMTVEQNVAFGLRMQKV-NADDSHKRVQEVLQLVELKDLAGR--YPHQMSGGQCQRVALARSLVTR 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 152 PRLLLLDEPLSALDARIRKHLREQIRQIQRElgLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-212 |
3.08e-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: 187.99 E-value: 3.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ-KRHIGMVFQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 SYALFPNMTVEQNVafglrmqkvnaddshkrvqevlqlvelkdlagryphQMSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 545130686 163 ALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKI 212
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-221 |
3.28e-59 |
|
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: 190.45 E-value: 3.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 6 VQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ-KRHIGMVFQSY 84
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 85 ALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSAL 164
Cdd:COG4555 84 GLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 165 DARIRKHLREQIRQIqRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:COG4555 164 DVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-210 |
9.24e-59 |
|
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: 188.83 E-value: 9.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRhigMVFQSYALFPNMTVEQNVAFGL 100
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---VVFQNYSLLPWLTVRENIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 101 RMQKVNADDSHKR--VQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQ 178
Cdd:TIGR01184 80 DRVLPDLSKSERRaiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170 180 190
....*....|....*....|....*....|..
gi 545130686 179 IQRELGLTTIFVTHDQEEALTMSDRIFLMNQG 210
Cdd:TIGR01184 160 IWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-212 |
9.52e-59 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 188.10 E-value: 9.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGMVFQ 82
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 SYALFPNmTVEQNVAFGLRMQKVNADDshKRVQEVLQLVEL-KDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPL 161
Cdd:COG4619 82 EPALWGG-TVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 545130686 162 SALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKI 212
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-225 |
3.58e-58 |
|
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: 195.67 E-value: 3.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSvDSGKILLDGQDIVPLS-----PQKRHIGMVFQS-YA-LFPNMTVE 93
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrralrPLRRRMQVVFQDpFGsLSPRMTVG 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 94 QNVAFGLRMQKV--NADDSHKRVQEVLQLVELK-DLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRK 170
Cdd:COG4172 383 QIIAEGLRVHGPglSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQA 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 171 HLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:COG4172 463 QILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-216 |
1.20e-57 |
|
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: 184.18 E-value: 1.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGMVFQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 syalfpnmtveqnvafglrmqkvnaddshkrvqeVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545130686 163 ALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-219 |
8.23e-57 |
|
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: 183.79 E-value: 8.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGT----PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKR---- 75
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 76 --HIGMVFQSYALFPNMTVEQNVAfgLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPR 153
Cdd:COG4181 89 arHVGFVFQSFQLLPTLTALENVM--LPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 154 LLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALtMSDRIFLMNQGKIVQSGDAE 219
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLVEDTAAT 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-221 |
2.22e-56 |
|
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: 182.25 E-value: 2.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKR---HIGMVF 81
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 82 QSYALFPNMTVEQNVAFGLRMQKvnADDSHKRVQEVLQLV-ELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:cd03224 82 EGRRIFPELTVEENLLLGAYARR--RAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545130686 161 LSALDARIRKHLREQIRQIqRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:cd03224 160 SEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-227 |
3.87e-56 |
|
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: 182.38 E-value: 3.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 6 VQHLQKSYA-GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSP-----QKRHIGM 79
Cdd:cd03256 3 VENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPNMTVEQNVAFGL--RMQKVNA-----DDSHKRVQ-EVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTR 151
Cdd:cd03256 83 IFQQFNLIERLSVLENVLSGRlgRRSTWRSlfglfPKEEKQRAlAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 152 PRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVD 227
Cdd:cd03256 163 PKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLD 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-221 |
2.00e-55 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 191.59 E-value: 2.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAG--TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGM 79
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFpNMTVEQNVAFGlrmqkvNADDSHKRVQEVLQLVELKDLAGRYPHQM-----------SGGQCQRVALARSL 148
Cdd:COG2274 554 VLQDVFLF-SGTIRENITLG------DPDATDEEIIEAARLAGLHDFIEALPMGYdtvvgeggsnlSGGQRQRLAIARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545130686 149 VTRPRLLLLDEPLSALDARIRKHLREQIRQIQRelGLTTIFVTHDqEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-219 |
3.39e-55 |
|
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: 179.56 E-value: 3.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRH---IGMVF 81
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 82 QSYALFPNMTVEQNVAFGLRMQKVNA----------DDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTR 151
Cdd:cd03219 82 QIPRLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545130686 152 PRLLLLDEPLSALDARIRKHLREQIRQIqRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAE 219
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPD 228
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-225 |
3.55e-55 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 179.82 E-value: 3.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSfVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI---VPLSPQ---- 73
Cdd:COG4161 1 MS-IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKairl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 74 -KRHIGMVFQSYALFPNMTVEQN-VAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTR 151
Cdd:COG4161 80 lRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545130686 152 PRLLLLDEPLSALDARIRKHLREQIRQIQrELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAEtLYTAP 225
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQP 231
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-221 |
4.41e-55 |
|
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: 179.41 E-value: 4.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKR---HI 77
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 78 GMVFQSYALFPNMTVEQNVAFGLRMQKvNADDSHKRVQEVLQLV-ELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLL 156
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 157 LDEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:COG0410 160 LDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-214 |
1.92e-54 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 178.35 E-value: 1.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 6 VQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKrhiGMVFQSYA 85
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---GVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 86 LFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALD 165
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 545130686 166 ARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLM--NQGKIVQ 214
Cdd:PRK11248 161 AFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVE 211
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
4-213 |
2.29e-54 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 177.13 E-value: 2.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYaGT-----PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK---- 74
Cdd:TIGR02982 2 ISIRNLNHYY-GHgslrkQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQlvql 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 75 -RHIGMVFQSYALFPNMTVEQNVAFGLRMQ-KVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRP 152
Cdd:TIGR02982 81 rRRIGYIFQAHNLLGFLTARQNVQMALELQpNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545130686 153 RLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQeEALTMSDRIFLMNQGKIV 213
Cdd:TIGR02982 161 KLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDN-RILDVADRILQMEDGKLL 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-232 |
4.88e-54 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 178.29 E-value: 4.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 2 SFVSVQHLQKSY--AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQdivPLSPQ-----K 74
Cdd:PRK13635 4 EIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEEtvwdvR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 75 RHIGMVFQSY-ALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPR 153
Cdd:PRK13635 81 RQVGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545130686 154 LLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTmSDRIFLMNQGKIVQSGdaetlytAPVDVFAAG 232
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG-------TPEEIFKSG 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-225 |
5.52e-54 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 176.74 E-value: 5.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSfVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQ-----------DIVP 69
Cdd:PRK11124 1 MS-IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpsdkAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 70 LspqKRHIGMVFQSYALFPNMTVEQN-VAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSL 148
Cdd:PRK11124 80 L---RRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 149 VTRPRLLLLDEPLSALDARIRKhlreQIRQIQREL---GLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAeTLYTAP 225
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITA----QIVSIIRELaetGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQP 231
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-227 |
6.50e-54 |
|
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: 176.72 E-value: 6.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 6 VQHLQKSY-AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK-----RHIGM 79
Cdd:TIGR02315 4 VENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPNMTVEQNVAFGlRMQKVNA---------DDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVT 150
Cdd:TIGR02315 84 IFQHYNLIERLTVLENVLHG-RLGYKPTwrsllgrfsEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 151 RPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVD 227
Cdd:TIGR02315 163 QPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLR 239
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-212 |
1.40e-53 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 176.41 E-value: 1.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 6 VQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKiLLDGQdiVPLSPQKRHIGMVFQSYA 85
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGT--APLAEAREDTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 86 LFPNMTVEQNVAFGLRmqkvnaDDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALD 165
Cdd:PRK11247 92 LLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545130686 166 ARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKI 212
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-216 |
2.10e-53 |
|
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: 174.26 E-value: 2.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQdivPLSPQKRHIGMVFQSY 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 85 AL---FPnMTVEQNVAFGLR-----MQKVNADDShKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLL 156
Cdd:cd03235 78 SIdrdFP-ISVRDVVLMGLYghkglFRRLSKADK-AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 157 LDEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNqGKIVQSG 216
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-226 |
2.72e-53 |
|
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: 178.38 E-value: 2.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI------VPLSPQKRHIGMVFQSYALFPNMTVEQ 94
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkgIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 95 NVAFGlrMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLRE 174
Cdd:TIGR02142 95 NLRYG--MKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 545130686 175 QIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPV 226
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-197 |
3.33e-53 |
|
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: 173.43 E-value: 3.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ-KRHIGMVFQ 82
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 SYALFPNMTVEQNVAFGLRMQKVNADDShkRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|....*
gi 545130686 163 ALDARIRKHLREQIRQiQRELGLTTIFVTHDQEEA 197
Cdd:COG4133 161 ALDAAGVALLAELIAA-HLARGGAVLLTTHQPLEL 194
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-221 |
5.66e-53 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 174.00 E-value: 5.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 25 EVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMVFQSYALFPNMTVEQNVAFGLRMQ- 103
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNPGl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 104 KVNADdSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQREL 183
Cdd:PRK10771 101 KLNAA-QREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQER 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 545130686 184 GLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:PRK10771 180 QLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-227 |
1.51e-52 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 173.68 E-value: 1.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRC-------IAGLTSvdSGKILLDGQDIvpLSPQ--- 73
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGARV--EGEILLDGEDI--YDPDvdv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 74 ---KRHIGMVFQSYALFPnMTVEQNVAFGLRMQKV-NADDSHKRVQEVLQLV----ELKDLAGRYPHQMSGGQCQRVALA 145
Cdd:COG1117 88 velRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAalwdEVKDRLKKSALGLSGGQQQRLCIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 146 RSLVTRPRLLLLDEPLSALD----ARIrkhlREQIRQIQRElgLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDpistAKI----EELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
....*.
gi 545130686 222 YTAPVD 227
Cdd:COG1117 241 FTNPKD 246
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-229 |
1.92e-52 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 174.47 E-value: 1.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSfVSVQHLQKSY-AGTP----VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI----VPLS 71
Cdd:PRK13637 1 MS-IKIENLTHIYmEGTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkkVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 72 PQKRHIGMVFQ--SYALFPNmTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELK--DLAGRYPHQMSGGQCQRVALARS 147
Cdd:PRK13637 80 DIRKKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 148 LVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGdaetlytAPVD 227
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG-------TPRE 231
|
..
gi 545130686 228 VF 229
Cdd:PRK13637 232 VF 233
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
8-211 |
5.27e-52 |
|
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: 170.89 E-value: 5.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 8 HLQKSY-AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLS----PQ-KRHIGMVF 81
Cdd:TIGR02673 6 NVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRgrqlPLlRRRIGVVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 82 QSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPL 161
Cdd:TIGR02673 86 QDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545130686 162 SALDArirkHLREQIRQIQREL---GLTTIFVTHDQEEALTMSDRIFLMNQGK 211
Cdd:TIGR02673 166 GNLDP----DLSERILDLLKRLnkrGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
12-216 |
5.61e-52 |
|
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: 170.75 E-value: 5.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 12 SYAGTPVfsDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMVFQSYALFPNMT 91
Cdd:cd03298 9 SYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 92 VEQNVAFGLRMQ-KVNADDsHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRK 170
Cdd:cd03298 87 VEQNVGLGLSPGlKLTAED-RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 545130686 171 HLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03298 166 EMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-213 |
6.20e-52 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 172.19 E-value: 6.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKS-YAGTP----VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKR--H 76
Cdd:COG1101 2 LELKNLSKTfNPGTVnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 77 IGMVFQSYAL--FPNMTVEQNVA--------FGLRMQKVNADdsHKRVQEVLQLVE------LKDLAGryphQMSGGQCQ 140
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGLTKKR--RELFRELLATLGlglenrLDTKVG----LLSGGQRQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545130686 141 RVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIV 213
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-221 |
1.34e-51 |
|
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: 169.86 E-value: 1.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ-KRHIGMVFQ 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 SYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545130686 163 ALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-225 |
1.41e-51 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 171.09 E-value: 1.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI---VPLSPQKR-- 75
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQKGli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 76 -----HIGMVFQSYALFPNMTVEQNVAFG-LRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLV 149
Cdd:PRK11264 81 rqlrqHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 150 TRPRLLLLDEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-204 |
4.19e-51 |
|
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: 168.18 E-value: 4.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 6 VQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRH------IGM 79
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASkfrrekLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDE 159
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 545130686 160 PLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEAlTMSDRI 204
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVA-KQADRV 203
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-226 |
1.08e-50 |
|
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: 168.11 E-value: 1.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKR-HIGMVF- 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRaRLGIGYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 82 -QSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:cd03218 81 pQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545130686 161 LSALDARIRKHLREQIRQI-QRELGlttIFVT-HDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPV 226
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILkDRGIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-216 |
2.65e-50 |
|
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: 166.24 E-value: 2.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMVFQS 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 YALFPNMTVEQNVAFGLRMQKVnaddSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545130686 164 LDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03268 157 LDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-162 |
3.90e-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: 163.97 E-value: 3.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 19 FSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGMVFQSYALFPNMTVEQNV 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKslRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 97 AFGLRMQKVNADDSHKRVQEVLQLVELKDLA----GRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-222 |
8.65e-50 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 165.97 E-value: 8.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRH---I 77
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRArlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 78 GMVFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLL 157
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545130686 158 DEPLSALD----ARIRK---HLREqirqiqRELGlttIFVT-HDQEEALTMSDRIFLMNQGKIVQSGDAETLY 222
Cdd:COG1137 161 DEPFAGVDpiavADIQKiirHLKE------RGIG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEIL 224
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-225 |
3.76e-49 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 164.62 E-value: 3.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIV-------PLSPQ--- 73
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYhmpgrngPLVPAdek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 74 -----KRHIGMVFQSYALFPNMTVEQNVAFG-LRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARS 147
Cdd:TIGR03005 81 hlrqmRNKIGMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545130686 148 LVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQP 238
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-222 |
7.69e-49 |
|
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: 171.48 E-value: 7.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYA-GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGMV 80
Cdd:COG4988 337 IELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPnMTVEQNVAFGlrmqKVNADDShkRVQEVLQLVELKDLAGRYPHQM-----------SGGQCQRVALARSLV 149
Cdd:COG4988 417 PQNPYLFA-GTIRENLRLG----RPDASDE--ELEAALEAAGLDEFVAALPDGLdtplgeggrglSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545130686 150 TRPRLLLLDEPLSALDARIRKHLREQIRQIQRelGLTTIFVTHDqEEALTMSDRIFLMNQGKIVQSGDAETLY 222
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-216 |
1.86e-48 |
|
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: 161.59 E-value: 1.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVtLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDiVPLSPQK--RHIGMVF 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD-VLKQPQKlrRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 82 QSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPL 161
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545130686 162 SALD--ARIRkhlreqIRQIQRELGLTTIFV--THDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03264 159 AGLDpeERIR------FRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-225 |
2.16e-48 |
|
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: 169.87 E-value: 2.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAG----TPVFSDINCEVAKGEFVTLLGPSGCGKS----TLLRCIAGLTSVDSGKILLDGQDIVPLSP 72
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 73 QK------RHIGMVFQ--SYALFPNMTVEQNVAFGLRM-QKVNADDSHKRVQEVLQLVELKDLAGR---YPHQMSGGQCQ 140
Cdd:COG4172 84 RElrrirgNRIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 141 RVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDqeeaLT----MSDRIFLMNQGKIVQSG 216
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQG 239
|
....*....
gi 545130686 217 DAETLYTAP 225
Cdd:COG4172 240 PTAELFAAP 248
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-224 |
3.24e-48 |
|
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: 162.18 E-value: 3.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGL---TSVDSGKIL---LDGQDIVPLspqK 74
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlppTYGNDVRLFgerRGGEDVWEL---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 75 RHIGMVfqSYALF----PNMTVEQNVAFGL-----RMQKVNADDsHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALA 145
Cdd:COG1119 78 KRIGLV--SPALQlrfpRDETVLDVVLSGFfdsigLYREPTDEQ-RERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545130686 146 RSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTA 224
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTS 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
11-212 |
3.92e-48 |
|
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: 161.04 E-value: 3.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 11 KSY-AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK-----RHIGMVFQSY 84
Cdd:cd03292 8 KTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKIGVVFQDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 85 ALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSAL 164
Cdd:cd03292 88 RLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545130686 165 DARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKI 212
Cdd:cd03292 168 DPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-216 |
4.61e-48 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 160.75 E-value: 4.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAG--TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ-KRHIGMV 80
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAaRQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 161 LSALDARIRKHLREQIRQIQRelGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-211 |
5.67e-48 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 158.56 E-value: 5.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI--VPLSPQKRHIGMVFQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIakLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 syalfpnmtveqnvafglrmqkvnaddshkrvqevlqlvelkdlagryphqMSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 545130686 163 ALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGK 211
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-222 |
6.84e-48 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 162.21 E-value: 6.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 17 PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVP--LSPQKRHIGMVFQSY-ALFPNMTVE 93
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenVWDIRHKIGMVFQNPdNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 94 QNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLR 173
Cdd:PRK13650 101 DDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 545130686 174 EQIRQIQRELGLTTIFVTHDQEEaLTMSDRIFLMNQGKIVQSGDAETLY 222
Cdd:PRK13650 181 KTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-231 |
1.36e-47 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 160.71 E-value: 1.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGMVFQ 82
Cdd:PRK13548 4 EARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 SYAL-FPnMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLV------TRPRLL 155
Cdd:PRK13548 84 HSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 156 LLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG------DAETL---YTAPV 226
Cdd:PRK13548 163 LLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGtpaevlTPETLrrvYGADV 242
|
....*
gi 545130686 227 DVFAA 231
Cdd:PRK13548 243 LVQPH 247
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-225 |
1.43e-47 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 162.95 E-value: 1.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRH-----IGMVFQS--YALFPNMTVE 93
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavrsdIQMIFQDplASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 94 QNVAFGLRM--QKVNADDSHKRVQEVLQLVEL-KDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRK 170
Cdd:PRK15079 119 EIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 171 HLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK15079 199 QVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-217 |
1.70e-47 |
|
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: 159.26 E-value: 1.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 23 NCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMVFQSYALFPNMTVEQNVAFGLRM 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 103 Q-KVNADDSHKrVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQR 181
Cdd:TIGR01277 98 GlKLNAEQQEK-VVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCS 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 545130686 182 ELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGD 217
Cdd:TIGR01277 177 ERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-226 |
7.74e-47 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 158.74 E-value: 7.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGMVFQ 82
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 SYAL-FPnMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLV-------TRPRL 154
Cdd:COG4559 83 HSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 155 LLLDEPLSALDarirkhLREQIR--QIQREL---GLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPV 226
Cdd:COG4559 162 LFLDEPTSALD------LAHQHAvlRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDEL 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-216 |
8.21e-47 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 166.49 E-value: 8.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 12 SY-AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGMVFQSYALFp 88
Cdd:COG1132 348 SYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 89 NMTVEQNVAFGlrmqKVNADDshKRVQEVLQLVELKDLAGRYPHQM-----------SGGQCQRVALARSLVTRPRLLLL 157
Cdd:COG1132 427 SGTIRENIRYG----RPDATD--EEVEEAAKAAQAHEFIEALPDGYdtvvgergvnlSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545130686 158 DEPLSALDARIRKHLREQIRQIQRelGLTTIFVTHdQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:COG1132 501 DEATSALDTETEALIQEALERLMK--GRTTIVIAH-RLSTIRNADRILVLDDGRIVEQG 556
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-211 |
1.09e-46 |
|
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: 155.62 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGT--PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGM 79
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFpNMTVEQNVafglrmqkvnaddshkrvqevlqlvelkdlagryphqMSGGQCQRVALARSLVTRPRLLLLDE 159
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 545130686 160 PLSALDARIRKHLREQIRQIQRelGLTTIFVTHDqEEALTMSDRIFLMNQGK 211
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-221 |
8.44e-46 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 162.11 E-value: 8.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 3 FVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSP---QKRHIGM 79
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPNMTVEQNVAFG---LRMQKVNADDSHKRVQEVLQLVEL----KDLAGRYphqmSGGQCQRVALARSLVTRP 152
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGrepRRGGLIDWRAMRRRARELLARLGLdidpDTPVGDL----SVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545130686 153 RLLLLDEPLSALDARIRKHLREQIRQIqRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-225 |
1.26e-45 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 155.73 E-value: 1.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI----------VPLSPQ 73
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgelVPADRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 74 K-----RHIGMVFQSYALFPNMTVEQNVAFG-LRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARS 147
Cdd:COG4598 89 QlqrirTRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545130686 148 LVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:COG4598 169 LAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-229 |
4.27e-45 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 154.09 E-value: 4.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGMVF 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 82 QSYALFPNMTVEQNVAFGlRMQ----KVNADDsHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLL 157
Cdd:COG4604 82 QENHINSRLTVRELVAFG-RFPyskgRLTAED-REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 158 DEPLSALDArirKHLRE---QIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPV--DVF 229
Cdd:COG4604 160 DEPLNNLDM---KHSVQmmkLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVlsDIY 233
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
9-213 |
5.00e-45 |
|
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: 152.89 E-value: 5.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 9 LQKSYA----GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKR------HIG 78
Cdd:TIGR02211 7 LGKRYQegklDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkKLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 79 MVFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLD 158
Cdd:TIGR02211 87 FIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 159 EPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMsDRIFLMNQGKIV 213
Cdd:TIGR02211 167 EPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLF 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-216 |
5.27e-45 |
|
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: 152.91 E-value: 5.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSY----AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPlSPQ--KRHI 77
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAeaRRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 78 GMVFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLL 157
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545130686 158 DEPLSALDARIRKHLREQIRQiQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-221 |
8.51e-45 |
|
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: 152.68 E-value: 8.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKR---HIGMVF 81
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 82 QSYALFPNMTVEQNVAFGLRMQKvnaDDSHKRVQEVLQLVE-LKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALP---RRSRKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545130686 161 LSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-261 |
5.64e-44 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 155.19 E-value: 5.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSP------QKRHIGMVFQSYALFPNMTVEQ 94
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevRRKKIAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 95 NVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLRE 174
Cdd:PRK10070 126 NTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 175 QIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIGNYNLLDADKATQLLQRPIS 254
Cdd:PRK10070 206 ELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARRTPN 285
|
....*..
gi 545130686 255 SRIAIRP 261
Cdd:PRK10070 286 GLIRKTP 292
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-221 |
6.02e-44 |
|
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: 158.39 E-value: 6.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSY--AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGM 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFpNMTVEQNvafgLRMQKVNADDShkRVQEVLQLVELKDLAGRYPH-----------QMSGGQCQRVALARSL 148
Cdd:COG4987 414 VPQRPHLF-DTTLREN----LRLARPDATDE--ELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545130686 149 VTRPRLLLLDEPLSALDARIRKHLREQIRQIQRelGLTTIFVTHDQEEALTMsDRIFLMNQGKIVQSGDAETL 221
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEEL 556
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-216 |
1.96e-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: 148.58 E-value: 1.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQdivPLSPQKRH-IGMVFQ 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK---PLDIAARNrIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 SYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545130686 163 ALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03269 158 GLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-229 |
1.99e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 150.53 E-value: 1.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAG--TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVP--LSPQKRHIGM 79
Cdd:PRK13632 8 IKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSY-ALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLD 158
Cdd:PRK13632 88 IFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545130686 159 EPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALtMSDRIFLMNQGKIVQSGDaetlytaPVDVF 229
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGK-------PKEIL 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-251 |
2.11e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 150.94 E-value: 2.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSY-AGTP----VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVP------LSP 72
Cdd:PRK13634 3 ITFQKVEHRYqYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknkkLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 73 QKRHIGMVFQsyalFPNM-----TVEQNVAFGLRMQKVNADDSHKRVQEVLQLVEL-KDLAGRYPHQMSGGQCQRVALAR 146
Cdd:PRK13634 83 LRKKVGIVFQ----FPEHqlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 147 SLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPV 226
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
250 260
....*....|....*....|....*
gi 545130686 227 DVFAAGfignynlLDADKATQLLQR 251
Cdd:PRK13634 239 ELEAIG-------LDLPETVKFKRA 256
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-223 |
7.70e-43 |
|
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: 148.80 E-value: 7.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 2 SFVSVQHLQKSYAGT---------PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSP 72
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGglfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 73 Q-----KRHIGMVFQ-SYALF-PNMTVEQNVAFGLR-MQKVNADDSHKRVQEVLQLVELK-DLAGRYPHQMSGGQCQRVA 143
Cdd:TIGR02769 81 KqrrafRRDVQLVFQdSPSAVnPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 144 LARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYT 223
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-213 |
1.90e-42 |
|
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: 144.49 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSP---QKRHIGMV 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPrdaRRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 fqsyalfpnmtveqnvafglrmqkvnaddshkrvqevlqlvelkdlagrypHQMSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:cd03216 81 ---------------------------------------------------YQLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545130686 161 LSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIV 213
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-222 |
4.70e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 146.82 E-value: 4.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVP--LSPQKRHIGMVFQS-YALFPNMTVEQNVA 97
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdnFEKLRKHIGIVFQNpDNQFVGSIVKYDVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 98 FGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIR 177
Cdd:PRK13648 107 FGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVR 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 545130686 178 QIQRELGLTTIFVTHDQEEALTmSDRIFLMNQGKIVQSGDAETLY 222
Cdd:PRK13648 187 KVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-221 |
4.98e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 147.56 E-value: 4.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQdivPLSPQKRH-IGmvfq 82
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE---PLDPEDRRrIG---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 sY-----ALFPNMTV-EQNVAFGlRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLL 156
Cdd:COG4152 75 -YlpeerGLYPKMKVgEQLVYLA-RLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 157 LDEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-213 |
7.39e-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: 144.32 E-value: 7.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSY-AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRhIGMVFQS 83
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKS-IGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 --YALFPNmTVEQNVAFGLRmqkvNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPL 161
Cdd:cd03226 80 vdYQLFTD-SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 545130686 162 SALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIV 213
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-219 |
1.34e-41 |
|
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: 151.82 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 14 AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGMVFQSYALFPNmT 91
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 92 VEQNVAfglRMQKVNADDshkrVQEVLQLVELKDLAGRYP-----------HQMSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:COG4618 422 IAENIA---RFGDADPEK----VVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545130686 161 LSALDARIRKHLREQIRQIqRELGLTTIFVTHDQeEALTMSDRIFLMNQGKIVQSGDAE 219
Cdd:COG4618 495 NSNLDDEGEAALAAAIRAL-KARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRD 551
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-225 |
1.43e-41 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 145.37 E-value: 1.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYA-GTPVFS--------DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLS 71
Cdd:COG4167 2 SALLEVRNLSKTFKyRTGLFRrqqfeavkPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 72 PQKR--HIGMVFQ--SYALFPNMTVEQNVAFGLRMQ-KVNADDSHKRVQEVLQLVEL-KDLAGRYPHQMSGGQCQRVALA 145
Cdd:COG4167 82 YKYRckHIRMIFQdpNTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 146 RSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-221 |
3.05e-41 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 144.52 E-value: 3.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK-----R 75
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlytvrK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 76 HIGMVFQSYALFPNMTVEQNVAFGLRMQ-KVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRL 154
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 155 LLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-214 |
5.27e-41 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 144.06 E-value: 5.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTP---------VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLS 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGlsgkhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 72 PQ-----KRHIGMVFQSY--ALFPNMTVEQNVAFGLR-MQKVNADDSHKRVQEVLQLVELKD-LAGRYPHQMSGGQCQRV 142
Cdd:PRK10419 81 RAqrkafRRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545130686 143 ALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQ 214
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-216 |
2.89e-40 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 140.42 E-value: 2.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 16 TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGMVFQSYALFpNMTVE 93
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYVPQDVTLF-YGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 94 QNVAFGlrmqKVNADDShkRVQEVLQLVELKDLAGRYPH-----------QMSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:cd03245 96 DNITLG----APLADDE--RILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545130686 163 ALDARIRKHLREQIRQIQRelGLTTIFVTHDQeEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03245 170 AMDMNSEERLKERLRQLLG--DKTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-226 |
3.17e-40 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 144.25 E-value: 3.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 34 LLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQ---DI---VPLSPQKRHIGMVFQSYALFPNMTVEQNVAFGLRmqkvna 107
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAekgICLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 108 ddsHKRVQEVLQLVEL---KDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELG 184
Cdd:PRK11144 103 ---KSMVAQFDKIVALlgiEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREIN 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 545130686 185 LTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPV 226
Cdd:PRK11144 180 IPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-221 |
3.38e-40 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 140.83 E-value: 3.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 15 GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI--VPLSPQKRHIGMVFQSYALFpNMTV 92
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIreVTLDSLRRAIGVVPQDTVLF-NDTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 93 EQNVAFGlrmqKVNADDshKRVQEVLQLVELKDLAGRYPHQ-----------MSGGQCQRVALARSLVTRPRLLLLDEPL 161
Cdd:cd03253 92 GYNIRYG----RPDATD--EEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 162 SALDARIRKHLREQIRQIQRelGLTTIFVTHDQEEALTmSDRIFLMNQGKIVQSGDAETL 221
Cdd:cd03253 166 SALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
15-230 |
4.09e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 141.75 E-value: 4.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 15 GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI----VPLSPQKRHIGMVFQSY--ALFP 88
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkKSLLEVRKTVGIVFQNPddQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 89 NmTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARI 168
Cdd:PRK13639 94 P-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545130686 169 RKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGdaetlytAPVDVFA 230
Cdd:PRK13639 173 ASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEG-------TPKEVFS 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-222 |
6.31e-40 |
|
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: 140.06 E-value: 6.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGT--PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI--VPLSPQKRHIGM 79
Cdd:cd03251 1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFpNMTVEQNVAFGLRmqkvnaDDSHKRVQEVLQLVELKDLAGRYPH-----------QMSGGQCQRVALARSL 148
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGRP------GATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545130686 149 VTRPRLLLLDEPLSALDARIRKHLREQIRQIQRelGLTTIFVTHdQEEALTMSDRIFLMNQGKIVQSGDAETLY 222
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-220 |
1.58e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 145.55 E-value: 1.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ---KRHIGMV 80
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdaiALGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPNMTVEQNVAFGL---RMQKVNADDSHKRVQEVLQLVELK-DLAgRYPHQMSGGQCQRVALARSLVTRPRLLL 156
Cdd:COG3845 86 HQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDvDPD-AKVEDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 157 LDEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGD-AET 220
Cdd:COG3845 165 LDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDtAET 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-229 |
8.07e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 138.78 E-value: 8.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 2 SFVSVQHLQKSYAGT--PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDS---GKILLDGqdiVPLSPQ--- 73
Cdd:PRK13640 4 NIVEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDG---ITLTAKtvw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 74 --KRHIGMVFQSY-ALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVT 150
Cdd:PRK13640 81 diREKVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545130686 151 RPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEAlTMSDRIFLMNQGKIVQSGdaetlytAPVDVF 229
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQG-------SPVEIF 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-222 |
9.66e-39 |
|
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: 137.29 E-value: 9.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 17 PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGMVFQSYALFpNMTVEQ 94
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwlRSQIGLVSQEPVLF-DGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 95 NVAFGlrmqKVNADDSHkrVQEVLQLVELKD-----------LAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:cd03249 96 NIRYG----KPDATDEE--VEEAAKKANIHDfimslpdgydtLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545130686 164 LDARIRKHLREQIRQIQRelGLTTIFVTHdQEEALTMSDRIFLMNQGKIVQSGDAETLY 222
Cdd:cd03249 170 LDAESEKLVQEALDRAMK--GRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-216 |
1.57e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 137.91 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 16 TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ---KRHIGMVFQSyalfPN--- 89
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwdiRNKAGMVFQN----PDnqi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 90 --MTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDAR 167
Cdd:PRK13633 99 vaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 545130686 168 IRKHLREQIRQIQRELGLTTIFVTHDQEEALTmSDRIFLMNQGKIVQSG 216
Cdd:PRK13633 179 GRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-212 |
3.65e-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: 133.50 E-value: 3.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGT--PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGMV 80
Cdd:cd03246 2 EVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNelGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPNmTVEQNVafglrmqkvnaddshkrvqevlqlvelkdlagryphqMSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:cd03246 82 PQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 545130686 161 LSALDARIRKHLREQIRQIqRELGLTTIFVTHdQEEALTMSDRIFLMNQGKI 212
Cdd:cd03246 124 NSHLDVEGERALNQAIAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-210 |
8.33e-38 |
|
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: 134.48 E-value: 8.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 6 VQHLQKSYA-----GT--PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQ----DIVPLSPQ- 73
Cdd:COG4778 7 VENLSKTFTlhlqgGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPRe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 74 -----KRHIGMVFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKD-LAGRYPHQMSGGQCQRVALARS 147
Cdd:COG4778 87 ilalrRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPErLWDLPPATFSGGEQQRVNIARG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545130686 148 LVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQG 210
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
20-225 |
1.00e-37 |
|
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: 134.42 E-value: 1.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 20 SDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGL----TSVDSGKILLDGQDIVPLSPQKRHIGMVFQS--YALFPNMTVE 93
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLTCLAILGLlppgLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 94 QNVAFGLRMQKVNADDSHKRVQEVLQLVELKD---LAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRK 170
Cdd:TIGR02770 83 NHAIETLRSLGKLSKQARALILEALEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 171 HLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:TIGR02770 163 RVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNP 217
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
25-225 |
1.04e-37 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 137.02 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 25 EVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRH-----IGMVFQS-YA-LFPNMTVEQNVA 97
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllrqkIQIVFQNpYGsLNPRKKVGQILE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 98 FGLrmqKVNADDSHK----RVQEVLQLVELK-DLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHL 172
Cdd:PRK11308 117 EPL---LINTSLSAAerreKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQV 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545130686 173 REQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK11308 194 LNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-225 |
3.01e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 133.88 E-value: 3.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVD-----SGKILLDGQDI--VPLSPQ 73
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIfkMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 74 KRHIGMVFQSYALFPNMTVEQNVAFGLRMQKV--NADDSHKRVQEVLQLVEL----KDLAGRYPHQMSGGQCQRVALARS 147
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545130686 148 LVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRElgLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
7-196 |
3.99e-36 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 129.83 E-value: 3.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 7 QHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGMVFQSY 84
Cdd:PRK10247 11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyRQQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 85 ALFPNmTVEQNVAFGLRMQKVNADDshKRVQEVLQLVELKD-LAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:PRK10247 91 TLFGD-TVYDNLIFPWQIRNQQPDP--AIFLDDLERFALPDtILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190
....*....|....*....|....*....|...
gi 545130686 164 LDARIRKHLREQIRQIQRELGLTTIFVTHDQEE 196
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
4.63e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 131.46 E-value: 4.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGT-PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVP--LSPQKRHI 77
Cdd:PRK13652 1 MHLIETRDLCYSYSGSkEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 78 GMVFQSY--ALFpNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLL 155
Cdd:PRK13652 81 GLVFQNPddQIF-SPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 156 LLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-233 |
4.77e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 131.37 E-value: 4.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 22 INCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVP--LSPQKRHIGMVFQSY-ALFPNMTVEQNVAF 98
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAenVWNLRRKIGMVFQNPdNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 99 GLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQ 178
Cdd:PRK13642 106 GMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 179 IQRELGLTTIFVTHDQEEALTmSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGF 233
Cdd:PRK13642 186 IKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGL 239
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
14-224 |
5.61e-36 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 137.30 E-value: 5.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 14 AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGMVFQSYALFpNMT 91
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGYVPQDPRLF-YGT 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 92 VEQNVAFGLRmqkvNADDShkRVQEVLQLVELKDLAGRYPH-----------QMSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:TIGR03375 555 LRDNIALGAP----YADDE--EILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDEP 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545130686 161 LSALDARIRKHLREQIRQIQRelGLTTIFVTHDQeEALTMSDRIFLMNQGKIVQSGDAETLYTA 224
Cdd:TIGR03375 629 TSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPKDQVLEA 689
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-230 |
5.81e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 131.12 E-value: 5.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYA-GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI----VPLSPQKRHIG 78
Cdd:PRK13636 6 LKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 79 MVFQS--YALFpNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLL 156
Cdd:PRK13636 86 MVFQDpdNQLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545130686 157 LDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDaetlytaPVDVFA 230
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN-------PKEVFA 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
5-231 |
8.81e-36 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 130.11 E-value: 8.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHiGMV-- 80
Cdd:PRK11300 7 SVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiaRM-GVVrt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPNMTVEQN--VAfglRMQKVNA----------------DDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRV 142
Cdd:PRK11300 86 FQHVRLFREMTVIENllVA---QHQQLKTglfsgllktpafrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 143 ALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLY 222
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
....*....
gi 545130686 223 TAPvDVFAA 231
Cdd:PRK11300 243 NNP-DVIKA 250
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-225 |
2.46e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 128.81 E-value: 2.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVD-----SGKILLDGQDIvpLSPQ----- 73
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNI--YSPDvdpie 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 74 -KRHIGMVFQSYALFPNMTVEQNVAFGLRMQKV--NADDSHKRVQEVLQLV----ELKDLAGRYPHQMSGGQCQRVALAR 146
Cdd:PRK14267 83 vRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAalwdEVKDRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545130686 147 SLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRElgLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-256 |
2.79e-35 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 128.59 E-value: 2.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 6 VQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGMVFQS 83
Cdd:PRK11231 5 TENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 YALFPNMTVEQNVAFGlRMQKVN-----ADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLD 158
Cdd:PRK11231 85 HLTPEGITVRELVAYG-RSPWLSlwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 159 EPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGdaetlytAPVDVFAAGFIGNYN 238
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG-------TPEEVMTPGLLRTVF 235
|
250
....*....|....*...
gi 545130686 239 LLDAdkatQLLQRPISSR 256
Cdd:PRK11231 236 DVEA----EIHPEPVSGT 249
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
15-225 |
3.27e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 128.95 E-value: 3.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 15 GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKIL---LDGQDIVPLSPQKRHIGMVFQS-YALFPNM 90
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRKLVGIVFQNpETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 91 TVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRK 170
Cdd:PRK13644 94 TVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 171 HLREQIRQIQRElGLTTIFVTHDQEEaLTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK13644 174 AVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
17-221 |
6.65e-35 |
|
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: 134.48 E-value: 6.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 17 PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGMVFQSYALFpNMTVEQ 94
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLF-SRSIRD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 95 NVAFGlrmqKVNADDSHkrVQEVLQLVELKDLAGRYPH-----------QMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:TIGR01846 550 NIALC----NPGAPFEH--VIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFDEATSA 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 545130686 164 LDARIRKHLREQIRQIQRelGLTTIFVTHdQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:TIGR01846 624 LDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
8-229 |
1.31e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 127.55 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 8 HLQK-SY---AGTP----VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK----- 74
Cdd:PRK13649 4 NLQNvSYtyqAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 75 -RHIGMVFQsyalFPNM-----TVEQNVAFGLRMQKVNADDSHKRVQEVLQLVEL-KDLAGRYPHQMSGGQCQRVALARS 147
Cdd:PRK13649 84 rKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 148 LVTRPRLLLLDEPLSALDARIRKHLREQIRQIQrELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGdaetlytAPVD 227
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG-------KPKD 231
|
..
gi 545130686 228 VF 229
Cdd:PRK13649 232 IF 233
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-219 |
1.59e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 125.76 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSY-AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ-----KRHI 77
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpflRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 78 GMVFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLL 157
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545130686 158 DEPLSALDARIRKHLREQIRQIQReLGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAE 219
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-225 |
2.62e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 126.24 E-value: 2.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIV--------------- 68
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 69 PLSPQKRHIGMVFQSYALFPNMTVEQNVAFG-LRMQKVNADDSHKRVQEVLQLVELKDLA-GRYPHQMSGGQCQRVALAR 146
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 147 SLVTRPRLLLLDEPLSALDARIrkhLREQIRQIQR--ELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTA 224
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPEL---VGEVLRIMQQlaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
.
gi 545130686 225 P 225
Cdd:PRK10619 243 P 243
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-216 |
4.49e-34 |
|
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: 123.43 E-value: 4.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 12 SYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSV--DSGKILLDGQDIVPLSPqKRHIGMVFQSYALFPN 89
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSF-RKIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 90 MTVEQNVAFGLRMQKVnaddshkrvqevlqlvelkdlagryphqmSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIR 169
Cdd:cd03213 97 LTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545130686 170 KHLREQIRQIqRELGLTTIFVTHD-QEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03213 148 LQVMSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-206 |
4.93e-34 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 123.50 E-value: 4.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 12 SYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGmvfqsyALFPnMT 91
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVP------DSLP-LT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 92 VEQNVAFGL-----RMQKVNADDsHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDA 166
Cdd:NF040873 74 VRDLVAMGRwarrgLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 545130686 167 RIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFL 206
Cdd:NF040873 153 ESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
15-221 |
4.97e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 126.00 E-value: 4.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 15 GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGMVFQSY--ALFpNM 90
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvRSKVGLVFQDPddQVF-SS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 91 TVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRK 170
Cdd:PRK13647 96 TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 545130686 171 HLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:PRK13647 176 TLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-225 |
5.56e-34 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 130.60 E-value: 5.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 18 VFSDINCEVAKGEFVTLLGPSGCGKST----LLRCIAGltsvdSGKILLDGQDIVPLS-----PQKRHIGMVFQ--SYAL 86
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNrrqllPVRHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 87 FPNMTVEQNVAFGLRMQK--VNADDSHKRVQEVLQLVELK-DLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545130686 164 LDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAP 517
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-211 |
6.71e-34 |
|
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: 123.35 E-value: 6.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGqdivplspqkrHIGMVFQS 83
Cdd:cd03250 6 ASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 yALFPNMTVEQNVAFGLRMqkvnaddSHKRVQEVLQLVEL-KDLAgRYPHQ-----------MSGGQCQRVALARSLVTR 151
Cdd:cd03250 75 -PWIQNGTIRENILFGKPF-------DEERYEKVIKACALePDLE-ILPDGdlteigekginLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545130686 152 PRLLLLDEPLSALDARIRKHLREQIrqIQREL--GLTTIFVTHdQEEALTMSDRIFLMNQGK 211
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFENC--ILGLLlnNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-214 |
1.03e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 123.77 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 16 TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSP------QKRHIGMVFQSYALFPN 89
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 90 MTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIR 169
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 545130686 170 KHLREQIRQIQRELGLTTIFVTHDQEEALTMSdRIFLMNQGKIVQ 214
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTA 225
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-216 |
1.13e-33 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 124.17 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLS------PQKRHI 77
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELElyqlseAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 78 -----GMVFQSYALFPNMTVEQNVAFGLRMQKVNA---DDSHKRVQEVLQLVELKdlAGRY---PHQMSGGQCQRVALAR 146
Cdd:TIGR02323 84 mrtewGFVHQNPRDGLRMRVSAGANIGERLMAIGArhyGNIRATAQDWLEEVEID--PTRIddlPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 147 SLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-234 |
1.51e-33 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 123.80 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 22 INCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSvDSGKILLDGQDIVPLSPQK--RHIGMVFQSYALFPNMTVEQNVAFG 99
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 100 LRmQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVT-------RPRLLLLDEPLSALDARIRKHL 172
Cdd:COG4138 94 QP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545130686 173 REQIRQIqRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPV--DVFAAGFI 234
Cdd:COG4138 173 DRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENlsEVFGVKFR 235
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-221 |
1.90e-33 |
|
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: 123.10 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 12 SYA-GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI--VPLSPQKRHIGMVFQSYALFP 88
Cdd:cd03254 11 SYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIrdISRKSLRSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 89 NmTVEQNVAFGlrmqKVNADDshKRVQEVLQLVELKDLAGRYP-----------HQMSGGQCQRVALARSLVTRPRLLLL 157
Cdd:cd03254 91 G-TIMENIRLG----RPNATD--EEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545130686 158 DEPLSALDARIRKHLREQIRQIQRelGLTTIFVTHdQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-216 |
2.68e-33 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 123.50 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLS------PQKRHIG 78
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalseAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 79 MVFQSYalfpnmtVEQNVAFGLRMQkVNADDShkrVQEVLQLV------ELKDLAGRY--------------PHQMSGGQ 138
Cdd:PRK11701 88 RTEWGF-------VHQHPRDGLRMQ-VSAGGN---IGERLMAVgarhygDIRATAGDWlerveidaariddlPTTFSGGM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545130686 139 CQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
12-207 |
3.49e-33 |
|
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: 128.17 E-value: 3.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 12 SYAGT-PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGMVFQSYALFP 88
Cdd:TIGR02857 330 AYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAWVPQHPFLFA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 89 NmTVEQNVAFGLRmqkvnaDDSHKRVQEVLQLVELKDL-----------AGRYPHQMSGGQCQRVALARSLVTRPRLLLL 157
Cdd:TIGR02857 410 G-TIAENIRLARP------DASDAEIREALERAGLDEFvaalpqgldtpIGEGGAGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 545130686 158 DEPLSALDARIRKHLREQIRQIQRelGLTTIFVTHDQEEALTMsDRIFLM 207
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-219 |
5.11e-33 |
|
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: 127.61 E-value: 5.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 22 INCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKI-LLDGQDIVPLSPQ--------KRHIGMVFQSYALFPNMTV 92
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDMTKPgpdgrgraKRYIGILHQEYDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 93 EQNV--AFGLRMQkvnadDSHKRVQEVLQLV-------ELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:TIGR03269 383 LDNLteAIGLELP-----DELARMKAVITLKmvgfdeeKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 164 LDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAE 219
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-221 |
6.60e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 128.02 E-value: 6.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSY--AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGM 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAalRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFpNMTVEQNvafgLRMQKVNADDShkRVQEVLQLVELKDLA-------------GRyphQMSGGQCQRVALAR 146
Cdd:PRK11160 419 VSQRVHLF-SATLRDN----LLLAAPNASDE--ALIEVLQQVGLEKLLeddkglnawlgegGR---QLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 147 SLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRelGLTTIFVTHdQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-226 |
6.86e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 122.19 E-value: 6.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVD-----SGKILLDGQDIvpLSPQ----- 73
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNI--YSPRtdtvd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 74 -KRHIGMVFQSYALFPnMTVEQNVAFGLRMQKVNadDSH---KRVQEVLQLV----ELKDLAGRYPHQMSGGQCQRVALA 145
Cdd:PRK14239 84 lRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIK--DKQvldEAVEKSLKGAsiwdEVKDRLHDSALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 146 RSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRElgLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
.
gi 545130686 226 V 226
Cdd:PRK14239 239 K 239
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-221 |
1.10e-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: 127.14 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGT--PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGM 79
Cdd:TIGR02203 331 VEFRNVTFRYPGRdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAslRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFpNMTVEQNVAFGLRMQKVNAddshkRVQEVLQLVELKDLAGRYP---HQ--------MSGGQCQRVALARSL 148
Cdd:TIGR02203 411 VSQDVVLF-NDTIANNIAYGRTEQADRA-----EIERALAAAYAQDFVDKLPlglDTpigengvlLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545130686 149 VTRPRLLLLDEPLSALDArirkhlrEQIRQIQREL-----GLTTIFVTHdQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:TIGR02203 485 LKDAPILILDEATSALDN-------ESERLVQAALerlmqGRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-227 |
1.59e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 121.68 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDS-----GKILLDGQDI----VPLSPQK 74
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 75 RHIGMVFQSYALFPnMTVEQNVAFGLRM----QKVNADDShkrVQEVLQLVELKDLAGRYPHQ----MSGGQCQRVALAR 146
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIvgwrPKLEIDDI---VESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 147 SLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSD--RIFLMNQ---GKIVQSGDAETL 221
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDftAFFKGNEnriGQLVEFGLTKKI 243
|
....*.
gi 545130686 222 YTAPVD 227
Cdd:PRK14258 244 FNSPHD 249
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-212 |
1.67e-32 |
|
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: 119.07 E-value: 1.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQksyaGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRH-IGMVF- 81
Cdd:cd03215 5 LEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIrAGIAYv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 82 ----QSYALFPNMTVEQNVAFglrmqkvnaddshkrvqevlqlvelkdlagryPHQMSGGQCQRVALARSLVTRPRLLLL 157
Cdd:cd03215 81 pedrKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 158 DEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKI 212
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-222 |
4.42e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 121.04 E-value: 4.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYA---GTP----VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVP------L 70
Cdd:PRK13646 1 MTIRFDNVSYTyqkGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 71 SPQKRHIGMVFQ--SYALFPNmTVEQNVAFGLRMQKVNADDSHKRVQEVL-QLVELKDLAGRYPHQMSGGQCQRVALARS 147
Cdd:PRK13646 81 RPVRKRIGMVFQfpESQLFED-TVEREIIFGPKNFKMNLDEVKNYAHRLLmDLGFSRDVMSQSPFQMSGGQMRKIAIVSI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 148 LVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLY 222
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-216 |
4.89e-32 |
|
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: 119.17 E-value: 4.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 18 VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSpqkrhIGMVFQsyalfPNMTVEQNVA 97
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG-----LGGGFN-----PELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 98 FGLRMQKVNADDSHKRVQEVLQLVELKDLA----GRYphqmSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLR 173
Cdd:cd03220 107 LNGRLLGLSRKEIDEKIDEIIEFSELGDFIdlpvKTY----SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 545130686 174 EQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03220 183 RRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-221 |
4.97e-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: 119.51 E-value: 4.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 18 VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGMVFQSYALFpNMTVEQN 95
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 96 VAFGlrmqkvNADDSHKRVQEVLQLVELKDLAGRYPH-----------QMSGGQCQRVALARSLVTRPRLLLLDEPLSAL 164
Cdd:cd03252 96 IALA------DPGMSMERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 165 DARIRKHLREQIRQIQRelGLTTIFVTHdQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:cd03252 170 DYESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-225 |
9.32e-32 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 124.97 E-value: 9.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 29 GEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK-----RHIGMVFQS-YA-LFPNMTVEQNVAFGLR 101
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 102 MQKV-NADDSHKRVQEVLQLVELK-DLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQI 179
Cdd:PRK10261 430 VHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 545130686 180 QRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK10261 510 QRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-216 |
1.04e-31 |
|
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: 118.53 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 18 VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGL---TSVDSGKILLDGQdivPLSPQ--KRHIGMVFQSYALFPNMTV 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQ---PRKPDqfQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 93 EQNVAFG--LRMQKVNADDSHKRVQEVLQL--VELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARI 168
Cdd:cd03234 99 RETLTYTaiLRLPRKSSDAIRKKRVEDVLLrdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 545130686 169 RKHLREQIRQIQRE--LGLTTIfvtHD-QEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03234 179 ALNLVSTLSQLARRnrIVILTI---HQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-208 |
1.49e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 117.96 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 2 SFVSVQHLQKSYAG----TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKR-- 75
Cdd:PRK10584 5 NIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARak 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 76 ----HIGMVFQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTR 151
Cdd:PRK10584 85 lrakHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 152 PRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMN 208
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVN 221
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-221 |
1.57e-31 |
|
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: 124.16 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 17 PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI--VPLSPQKRHIGMVFQSYALFpNMTVEQ 94
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIrdVTQASLRAAIGIVPQDTVLF-NDTIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 95 NVAFGlrmqkvNADDSHKRVQEVLQLVELKDLAGRYPHQM-----------SGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:COG5265 451 NIAYG------RPDASEEEVEAAARAAQIHDFIESLPDGYdtrvgerglklSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545130686 164 LDARIRKHLREQIRQIQRelGLTTIFVTH------DqeealtmSDRIFLMNQGKIVQSGDAETL 221
Cdd:COG5265 525 LDSRTERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAEL 579
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-219 |
2.72e-31 |
|
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: 123.23 E-value: 2.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 16 TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGMVFQSYALFPNmTVE 93
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 94 QNVAfglRMQKvNADDshKRVQEVLQLVELKDLAGRYPH-----------QMSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:TIGR01842 410 ENIA---RFGE-NADP--EKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 163 ALDARIRKHLREQIRQIQRElGLTTIFVTHdQEEALTMSDRIFLMNQGKIVQSGDAE 219
Cdd:TIGR01842 484 NLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERD 538
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-231 |
3.59e-31 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 122.47 E-value: 3.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRH---IGMV 80
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHqlgIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPNMTVEQNVAFGLrmqkVNADDSHKRVQEVLQL--VELK--------DLAGRyphqmsggqcQRVALARSLVT 150
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFGL----PKRQASMQKMKQLLAAlgCQLDldssagslEVADR----------QIVEILRGLMR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 151 RPRLLLLDEPLSALDARIRKHLREQIRQIQrELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTApvDVFA 230
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIRELL-AQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD--DIIQ 234
|
.
gi 545130686 231 A 231
Cdd:PRK15439 235 A 235
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-221 |
6.04e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 116.92 E-value: 6.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI--VPLSPQ-KRHI 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIslLPLHARaRRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 78 GMVFQSYALFPNMTVEQNVAFGLRMQK-VNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLL 156
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545130686 157 LDEPLSALD-------ARIRKHLREQirqiqrelGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:PRK10895 161 LDEPFAGVDpisvidiKRIIEHLRDS--------GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-225 |
8.15e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 122.26 E-value: 8.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 12 SYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVdSGKILLDGQDIVPLSPQ--KRHIGMVFQSYALFPN 89
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPEswRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 90 mTVEQNVAFGlrmqKVNADDShkRVQEVLQLVELKDLAGRYPH-----------QMSGGQCQRVALARSLVTRPRLLLLD 158
Cdd:PRK11174 438 -TLRDNVLLG----NPDASDE--QLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 159 EPLSALDARIRKHLREQIRQIQRelGLTTIFVTHdQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNAASR--RQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-230 |
1.00e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 117.24 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 15 GTPV----FSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVP------LSPQKRHIGMVFQ-- 82
Cdd:PRK13641 15 GTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnknLKKLRKKVSLVFQfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 SYALFPNmTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELK-DLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPL 161
Cdd:PRK13641 95 EAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545130686 162 SALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQsgdaetlYTAPVDVFA 230
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIK-------HASPKEIFS 234
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-221 |
1.22e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 118.39 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 11 KSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGqdiVPLSPQKR----HIGMVFQSYAL 86
Cdd:PRK13536 49 KSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG---VPVPARARlaraRIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 87 FPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDA 166
Cdd:PRK13536 126 DLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 167 RIRKHLREQIRQIQrELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:PRK13536 206 HARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-225 |
1.74e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 119.18 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIG 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 79 MVFQSYALFPNMTVEQNVAFGL---RMQKVNADDSHKR-VQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRL 154
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRtphRSRFDTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 155 LLLDEPLSALDarirkhLREQIRQIQ--REL---GLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK09536 161 LLLDEPTASLD------INHQVRTLElvRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-233 |
1.78e-30 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 115.80 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 25 EVAKGEFVTLLGPSGCGKSTLLRCIAGLTSvDSGKILLDGQDI--VPLSPQKRHIGMVFQSYALFPNMTVEQNVAFGLRm 102
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLeaWSAAELARHRAYLSQQQTPPFAMPVFQYLTLHQP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 103 QKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALA-------RSLVTRPRLLLLDEPLSALDARIRKHLREQ 175
Cdd:PRK03695 96 DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQAALDRL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 176 IRQIQReLGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPV--DVFAAGF 233
Cdd:PRK03695 176 LSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENlaQVFGVNF 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-235 |
1.86e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 116.35 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 8 HLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSV-----DSGKILLDGQDIV---PLSPQKRHIGM 79
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFnyrDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPnMTVEQNVAFGLRMQKVNADD-----SHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRL 154
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRAHKLVPRKefrgvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 155 LLLDEPLSALDARIRKHLREQIRQIQRElgLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFI 234
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
|
.
gi 545130686 235 G 235
Cdd:PRK14271 263 A 263
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-225 |
1.91e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 115.91 E-value: 1.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 18 VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSV-DS-----GKILLDGQDIVPLSPQK--RHIGMVFQSYALFPN 89
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSkikvdGKVLYFGKDIFQIDAIKlrKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 90 MTVEQNVAFGLRMQKVNADDSHKR-VQEVLQLV----ELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSAL 164
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKiVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545130686 165 DARIRKHLREQIRQIQRElgLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK14246 185 DIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-219 |
2.02e-30 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 115.55 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTS--VDSGKILLDGQDIVPLSPQKRH---IGM 79
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERAragIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPNMTVEQ--NVAFG-LRMQKVNADDSHKRVQEVLQLVEL-KDLAGRYPHQ-MSGGQCQRVALARSLVTRPRL 154
Cdd:COG0396 82 AFQYPVEIPGVSVSNflRTALNaRRGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 155 LLLDEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHdQEEALTM--SDRIFLMNQGKIVQSGDAE 219
Cdd:COG0396 162 AILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITH-YQRILDYikPDFVHVLVDGRIVKSGGKE 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-230 |
2.80e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 116.26 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLdGQDIVPLSPQK--------R 75
Cdd:PRK13645 12 VSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDYAIPANLKKikevkrlrK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 76 HIGMVFQ--SYALFPNmTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVEL-KDLAGRYPHQMSGGQCQRVALARSLVTRP 152
Cdd:PRK13645 91 EIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545130686 153 RLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGdaetlytAPVDVFA 230
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG-------SPFEIFS 240
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-220 |
3.55e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 114.79 E-value: 3.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 18 VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSpqkrhIGMVFQsyalfPNMTVEQNVA 97
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLE-----LGAGFH-----PELTGRENIY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 98 FGLRMQKVNADDSHKRVQEVLQLVELKDLA----GRYphqmSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLR 173
Cdd:COG1134 111 LNGRLLGLSRKEIDEKFDEIVEFAELGDFIdqpvKTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545130686 174 EQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAET 220
Cdd:COG1134 187 ARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-225 |
3.77e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 120.60 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 17 PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGMVFQSYALFpNMTVEQ 94
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLF-SGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 95 NVAFGLRmqkvnaDDSHKRVQEVLQLVELKDLAGRYPH-----------QMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:TIGR00958 574 NIAYGLT------DTPDEEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545130686 164 LDARIrkhlrEQIRQIQREL-GLTTIFVTHdQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:TIGR00958 648 LDAEC-----EQLLQESRSRaSRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-229 |
8.09e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 115.22 E-value: 8.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 13 YAGTPVFsDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDgqDIVPLS--------PQKRHIGMVFQsy 84
Cdd:PRK13643 17 FASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIVVSStskqkeikPVRKKVGVVFQ-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 85 alFPNM-----TVEQNVAFGLRMQKVNADDSHKRVQEVLQLVEL-KDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLD 158
Cdd:PRK13643 92 --FPESqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545130686 159 EPLSALDARIRKHLREQIRQIQrELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGdaetlytAPVDVF 229
Cdd:PRK13643 170 EPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG-------TPSDVF 232
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-225 |
8.36e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 115.99 E-value: 8.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 22 INCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTS----VDSGKILLDGQDIVPLSPQKRH------IGMVFQS--YALFPN 89
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRnlvgaeVAMIFQDpmTSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 90 MTVEQNVAFGLRM-QKVNADDSHKRVQEVLQLVELKDLAGR---YPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALD 165
Cdd:PRK11022 106 YTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 166 ARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK11022 186 VTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-219 |
9.25e-30 |
|
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: 9.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTS--VDSGKILLDGQDIVPLSPQKRH---IGM 79
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERArlgIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPNMTVEQ-----NVAFglrmqkvnaddshkrvqevlqlvelkdlagryphqmSGGQCQRVALARSLVTRPRL 154
Cdd:cd03217 82 AFQYPPEIPGVKNADflryvNEGF------------------------------------SGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 155 LLLDEPLSALDARIRKHLREQIRQIqRELGLTTIFVTHDQEEALTM-SDRIFLMNQGKIVQSGDAE 219
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-226 |
1.09e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 114.90 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKR-HIGMVFQ 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARqRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 SYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545130686 163 ALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPV 226
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-217 |
3.80e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 113.64 E-value: 3.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSY-AGTP----VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK---- 74
Cdd:PRK13651 3 IKVKNIVKIFnKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 75 ----------------------RHIGMVFQ--SYALFPNmTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVEL-KDLAGR 129
Cdd:PRK13651 83 vleklviqktrfkkikkikeirRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 130 YPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDA-------RIRKHLREQirqiqrelGLTTIFVTHDQEEALTMSD 202
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPqgvkeilEIFDNLNKQ--------GKTIILVTHDLDNVLEWTK 233
|
250
....*....|....*
gi 545130686 203 RIFLMNQGKIVQSGD 217
Cdd:PRK13651 234 RTIFFKDGKIIKDGD 248
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-213 |
7.14e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.89 E-value: 7.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLqksyAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ---KRHIGMV- 80
Cdd:COG1129 258 EVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdaiRAGIAYVp 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 --FQSYALFPNMTVEQNVAFGL-----RMQKVNADDSHKRVQEVLQLVELK-----DLAGryphQMSGGQCQRVALARSL 148
Cdd:COG1129 334 edRKGEGLVLDLSIRENITLASldrlsRGGLLDRRRERALAEEYIKRLRIKtpspeQPVG----NLSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 149 VTRPRLLLLDEPLSALD--ArirkhlREQIRQIQREL---GLTTIFVTHDQEEALTMSDRIFLMNQGKIV 213
Cdd:COG1129 410 ATDPKVLILDEPTRGIDvgA------KAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-213 |
7.89e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 116.75 E-value: 7.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 18 VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSP------QKRHIGMVFQSYALFPNMT 91
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalaqlRREHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 92 VEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKH 171
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 545130686 172 LREQIRQIqRELGLTTIFVTHDQEEAlTMSDRIFLMNQGKIV 213
Cdd:PRK10535 183 VMAILHQL-RDRGHTVIIVTHDPQVA-AQAERVIEIRDGEIV 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
34-225 |
1.10e-28 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 111.42 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 34 LLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQdivPL-----SPQKRHIGMVFQ--SYALFPNMTVEQNVAFGLRMQ-KV 105
Cdd:PRK15112 44 IIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLhfgdySYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNtDL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 106 NADDSHKRVQEVLQLVELK-DLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELG 184
Cdd:PRK15112 121 EPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQG 200
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 545130686 185 LTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK15112 201 ISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
21-225 |
1.28e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 111.03 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSV-----DSGKILLDGQDI----VPLSPQKRHIGMVFQSYALFPNmT 91
Cdd:PRK14243 28 NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyapdVDPVEVRRRIGMVFQKPNPFPK-S 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 92 VEQNVAFGLRMQ--KVNADDSHKRV--QEVLqLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDAR 167
Cdd:PRK14243 107 IYDNIAYGARINgyKGDMDELVERSlrQAAL-WDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPI 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 168 IRKHLREQIRQIQRElgLTTIFVTHDQEEALTMSDRIFLMN---------QGKIVQSGDAETLYTAP 225
Cdd:PRK14243 186 STLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSP 250
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-192 |
1.32e-28 |
|
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: 109.37 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ-KRHIGMVFQS 83
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 YALFPNMTVEQNVAFGLRMqkvnADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:TIGR01189 82 PGLKPELSALENLHFWAAI----HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190
....*....|....*....|....*....|
gi 545130686 164 LDARIRKHLREQIRQ-IQRelGLTTIFVTH 192
Cdd:TIGR01189 158 LDKAGVALLAGLLRAhLAR--GGIVLLTTH 185
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-225 |
1.35e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 116.11 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 8 HLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKS----TLLRCI-AGLTSVDSGKILLD--GQDIVPLSPQK----RH 76
Cdd:PRK10261 21 AFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeQAGGLVQCDKMLLRrrSRQVIELSEQSaaqmRH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 77 -----IGMVFQS--YALFPNMTVEQNVAFGLRM-QKVNADDS---HKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALA 145
Cdd:PRK10261 101 vrgadMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAmveAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 146 RSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-225 |
1.73e-28 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 110.56 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 13 YAGTPVFSDINCEVAKGEFVTLLGPSGCGKStlLRCIAGL------TSVDSGKILLDGQDIVPLSPQKRHIGMVFQS--Y 84
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALgilpagVRQTAGRVLLDGKPVAPCALRGRKIATIMQNprS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 85 ALFPNMTVEQNVAFGLRMQKVNADDShkRVQEVLQLVELKD---LAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPL 161
Cdd:PRK10418 91 AFNPLHTMHTHARETCLALGKPADDA--TLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545130686 162 SALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-224 |
2.99e-28 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 110.46 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 7 QHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHIGMVFQSY 84
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 85 ALFPNMTVEQNVAFG--------LRMQKVNADdshkRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLL 156
Cdd:PRK10253 91 TTPGDITVQELVARGryphqplfTRWRKEDEE----AVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545130686 157 LDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTA 224
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-192 |
5.89e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 113.75 E-value: 5.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQ-KSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILL-DGQDIVPLsPQKrhigmvf 81
Cdd:COG4178 363 LALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFL-PQR------- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 82 qSYalFPNMTveqnvafgLRMQ----KVNADDSHKRVQEVLQLVELKDLAGRY------PHQMSGGQCQRVALARSLVTR 151
Cdd:COG4178 435 -PY--LPLGT--------LREAllypATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHK 503
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 545130686 152 PRLLLLDEPLSALDARIRKHLREQIRqiQRELGLTTIFVTH 192
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLR--EELPGTTVISVGH 542
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-218 |
7.94e-28 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 108.43 E-value: 7.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK---RHI 77
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 78 GMVFQSYALFPNMTVEQNVAFGLRMqkVNADDSHKRVQEVLQLV-ELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLL 156
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFF--AERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545130686 157 LDEPLSALDARIRKHLREQIRQIqRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIV--QSGDA 218
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVleDTGDA 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-219 |
8.75e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 108.95 E-value: 8.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 2 SFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSG----------KILLDGQDIVPLS 71
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREGRLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 72 PQKRHIGMVFQSYALFPNMTVEQNVAFGL---------------RMQKvnaddshKRVQEVLQLVELKDLAGRYPHQMSG 136
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwrtcfswftREQK-------QRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 137 GQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
...
gi 545130686 217 DAE 219
Cdd:PRK09984 236 SSQ 238
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-221 |
1.99e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.66 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQ-KSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSP-QKRHIGMVF- 81
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPrERRRLGVAYi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 82 ----QSYALFPNMTVEQNVAFGLRMQKVNAD----DSHKRVQEVLQLVELKDLAGRYPHQ----MSGGQCQRVALARSLV 149
Cdd:COG3845 339 pedrLGRGLVPDMSVAENLILGRYRRPPFSRggflDRKAIRAFAEELIEEFDVRTPGPDTparsLSGGNQQKVILARELS 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 150 TRPRLLLLDEPLSALD----ARIRKHLREqirqiQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:COG3845 419 RDPKLLIAAQPTRGLDvgaiEFIHQRLLE-----LRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-221 |
5.20e-27 |
|
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: 111.37 E-value: 5.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYA-GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGMV 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHtlRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPNmTVEQNVAFGLRmQKVNADDshkrVQEVLQLVELKDLAGRYPH-----------QMSGGQCQRVALARSLV 149
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAK-ENVSQDE----IWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545130686 150 TRPRLLLLDEPLSALDARIRKHLREQIRQIQRElglTTIFVTHDQEEAlTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-243 |
5.37e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 108.27 E-value: 5.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYaGTP-----VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVD---SGKILLDGQDIVPLsP 72
Cdd:PRK09473 10 DALLDVKDLRVTF-STPdgdvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNL-P 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 73 QKR-------HIGMVFQS--YALFPNMTVEQNVAFGL----RMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQC 139
Cdd:PRK09473 88 EKElnklraeQISMIFQDpmTSLNPYMRVGEQLMEVLmlhkGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 140 QRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAE 219
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNAR 247
|
250 260
....*....|....*....|....
gi 545130686 220 TLYTAPVDVFAAGFIGNYNLLDAD 243
Cdd:PRK09473 248 DVFYQPSHPYSIGLLNAVPRLDAE 271
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-216 |
5.55e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 105.88 E-value: 5.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQK-SYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGqdIVPLSPQKRH---IGMV 80
Cdd:cd03267 22 SLKSLFKrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRKKFlrrIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 F-QSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDE 159
Cdd:cd03267 100 FgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 160 PLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-232 |
5.56e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 107.02 E-value: 5.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 13 YAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQdivPLSPQKR-------HIGMVFQSya 85
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDYSKRgllalrqQVATVFQD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 86 lfPNMTV-----EQNVAFGLRMQKVNADDSHKRVQEVLQLVElkdlAGRYPHQ----MSGGQCQRVALARSLVTRPRLLL 156
Cdd:PRK13638 86 --PEQQIfytdiDSDIAFSLRNLGVPEAEITRRVDEALTLVD----AQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 157 LDEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDaetlytaPVDVFAAG 232
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA-------PGEVFACT 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-193 |
6.14e-27 |
|
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: 110.53 E-value: 6.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 6 VQHLQKSYAGTP-VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI--VPLSPQKRHIGMVFQ 82
Cdd:TIGR02868 337 LRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVssLDQDEVRRRVSVCAQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 SYALFpNMTVEQNVAFGlrmqkvNADDSHKRVQEVLQLVELKDLAGRYPHQM-----------SGGQCQRVALARSLVTR 151
Cdd:TIGR02868 417 DAHLF-DTTVRENLRLA------RPDATDEELWAALERVGLADWLRALPDGLdtvlgeggarlSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 545130686 152 PRLLLLDEPLSALDARIRKHLREQIRQIQRelGLTTIFVTHD 193
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-225 |
1.18e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.79 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 17 PVFSDINCEVAKGEFVTLLGPSGCGKS-TLLRCIAGLTS----VDSGKILLDGQDIVPLSPQK-RH-----IGMVFQS-- 83
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvYPSGDIRFHGESLLHASEQTlRGvrgnkIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 YALFPNMTVEQNVAFGLRMQK-VNADDSHKRVQEVLQLVELKDLAGR---YPHQMSGGQCQRVALARSLVTRPRLLLLDE 159
Cdd:PRK15134 103 VSLNPLHTLEKQLYEVLSLHRgMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 160 PLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK15134 183 PTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAP 248
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
17-192 |
1.21e-26 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 104.12 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 17 PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIvplspqkRHIGMVFQSYALF--------P 88
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-------RRQRDEYHQDLLYlghqpgikT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 89 NMTVEQNVAFGLRMQKVNADDshkRVQEVLQLVelkDLAGR--YP-HQMSGGQCQRVALARSLVTRPRLLLLDEPLSALD 165
Cdd:PRK13538 88 ELTALENLRFYQRLHGPGDDE---ALWEALAQV---GLAGFedVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190
....*....|....*....|....*....|.
gi 545130686 166 ----ARIRKHLREQIRQiqrelGLTTIFVTH 192
Cdd:PRK13538 162 kqgvARLEALLAQHAEQ-----GGMVILTTH 187
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-225 |
1.47e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.86 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHL-----QKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSG-----------KILLDGQDI 67
Cdd:PRK13631 22 LRVKNLycvfdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 68 VPLSPQ-------KRHIGMVFQ--SYALFPNmTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKD-LAGRYPHQMSGG 137
Cdd:PRK13631 102 NPYSKKiknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 138 QCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGD 217
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
....*...
gi 545130686 218 AETLYTAP 225
Cdd:PRK13631 260 PYEIFTDQ 267
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-216 |
2.95e-26 |
|
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: 102.39 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAG--TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRH-IGMV 80
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFpNMTVEQNVafglrmqkvnaddshkrvqevlqlvelkdlaGRyphQMSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:cd03247 81 NQRPYLF-DTTLRNNL-------------------------------GR---RFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 161 LSALDARIRKHLREQIRQIQRElgLTTIFVTHdQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKD--KTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-225 |
3.90e-26 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 104.04 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGmv 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 fqsyALFPnMTVEQNVAFGLRMQKVNADDSHKRVQEVlQLVElkdlagrYPHQ-MSGGQCQRVALARSLVTRPRLLLLDE 159
Cdd:PRK09544 80 ----TTLP-LTVNRFLRLRPGTKKEDILPALKRVQAG-HLID-------APMQkLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 160 PLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQgKIVQSGDAETLYTAP 225
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHP 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-221 |
5.80e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 105.17 E-value: 5.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGqdivpLSPQK------RHIGMVF-QSYALFPNMTVE 93
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-----YVPFKrrkefaRRIGVVFgQRSQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 94 QNvaFGL--RMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKH 171
Cdd:COG4586 115 DS--FRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545130686 172 LREQIRQIQRELGlTTIFVT-HDQE--EALtmSDRIFLMNQGKIVQSGDAETL 221
Cdd:COG4586 193 IREFLKEYNRERG-TTILLTsHDMDdiEAL--CDRVIVIDHGRIIYDGSLEEL 242
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-173 |
8.01e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 102.26 E-value: 8.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 15 GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSP--QKRHIGmvfQSYALFPNMTV 92
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeACHYLG---HRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 93 EQNVAFGLRMQkvNADDSHkrVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDAR----- 167
Cdd:PRK13539 91 AENLEFWAAFL--GGEELD--IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAavalf 166
|
....*....
gi 545130686 168 ---IRKHLR 173
Cdd:PRK13539 167 aelIRAHLA 175
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-216 |
3.46e-25 |
|
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: 100.65 E-value: 3.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGT--PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI--VPLSPQKRHIGM 79
Cdd:cd03244 3 IEFKNVSLRYRPNlpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIskIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPNmTVEQNVA-FGLrmqkvnADDShkRVQEVLQLVELKDLAGRYPHQM-----------SGGQCQRVALARS 147
Cdd:cd03244 83 IPQDPVLFSG-TIRSNLDpFGE------YSDE--ELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545130686 148 LVTRPRLLLLDEPLSALD----ARIRKHLREQIRQIqrelglTTIFVTHdQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03244 154 LLRKSKILVLDEATASVDpetdALIQKTIREAFKDC------TVLTIAH-RLDTIIDSDRILVLDKGRVVEFD 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-193 |
3.61e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.53 E-value: 3.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 6 VQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILldgqdivpLSPQKRhIGMVFQSYA 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS--------IPKGLR-IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 86 LFPNMTVEQNVAFGL--------RMQKVNA-----DDSHKRVQEVLQLVELKD----------------LAGRYPHQ--- 133
Cdd:COG0488 72 LDDDLTVLDTVLDGDaelraleaELEELEAklaepDEDLERLAELQEEFEALGgweaearaeeilsglgFPEEDLDRpvs 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545130686 134 -MSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRelglTTIFVTHD 193
Cdd:COG0488 152 eLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG----TVLVVSHD 208
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-216 |
4.26e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 105.43 E-value: 4.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGT-PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI--VPLSPQKRHIGMV 80
Cdd:PRK13657 335 VEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIrtVTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFpNMTVEQNvafgLRMQKVNADDSH-----KRVQeVLQLVELKD-----LAGRYPHQMSGGQCQRVALARSLVT 150
Cdd:PRK13657 415 FQDAGLF-NRSIEDN----IRVGRPDATDEEmraaaERAQ-AHDFIERKPdgydtVVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 151 RPRLLLLDEPLSALDARIRKHLREQIRQIQRelGLTTIFVTHdQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRVVESG 551
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
29-225 |
9.49e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 102.29 E-value: 9.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 29 GEFVTLLGPSGCGKSTLLRCIAGLTS----VDSGKILLDGQDIVPLSPQKRH------IGMVFQ--SYALFPNMTVEQNV 96
Cdd:COG4170 33 GEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERRkiigreIAMIFQepSSCLDPSAKIGDQL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 97 AF--------GLRMQKVNAddSHKRVQEVLQLVELKD---LAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALD 165
Cdd:COG4170 113 IEaipswtfkGKWWQRFKW--RKKRAIELLHRVGIKDhkdIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAME 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545130686 166 ----ARIRKhLREQIRQIQrelGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:COG4170 191 sttqAQIFR-LLARLNQLQ---GTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-217 |
1.45e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 103.54 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKR-HIGMVFQSY-----ALFPNMTVEQ 94
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVYISEdrkrdGLVLGMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 95 NVA------FGLRMQKVNADDSHKRVQEVLQLVELKDlagryPHQ------MSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:PRK10762 350 NMSltalryFSRAGGSLKHADEQQAVSDFIRLFNIKT-----PSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 163 ALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIvqSGD 217
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI--SGE 476
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-233 |
3.79e-24 |
|
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: 102.57 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSV--DSGKIL----------------LDGQ 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 66 --------------DIVPLSPQ-----KRHIGMVFQ-SYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKD 125
Cdd:TIGR03269 81 pcpvcggtlepeevDFWNLSDKlrrriRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 126 LAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIF 205
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260
....*....|....*....|....*...
gi 545130686 206 LMNQGKIVQSGDAETLytapVDVFAAGF 233
Cdd:TIGR03269 241 WLENGEIKEEGTPDEV----VAVFMEGV 264
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
29-226 |
4.20e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 99.09 E-value: 4.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 29 GEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGMVFQSYALFPNMTVEQNVAFGL-----R 101
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQQLPAAEGMTVRELVAIGRypwhgA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 102 MQKVNADDsHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQR 181
Cdd:PRK10575 117 LGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQ 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 545130686 182 ELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPV 226
Cdd:PRK10575 196 ERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-221 |
1.29e-23 |
|
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: 101.05 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDS--GKILLDGQDIVPLS---PQKRHIG 78
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNirdTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 79 MVFQSYALFPNMTVEQNVAFG----LRMQKVNADDSHKRVQEVLQLVELKDL-AGRYPHQMSGGQCQRVALARSLVTRPR 153
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545130686 154 LLLLDEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-224 |
4.43e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 99.79 E-value: 4.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSY-AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGMV 80
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPNmTVEQNVAFGlrmqkvnADDSHKRVQEVLQLVELKDLAGRYP-----------HQMSGGQCQRVALARSLV 149
Cdd:PRK10790 421 QQDPVVLAD-TFLANVTLG-------RDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLV 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 150 TRPRLLLLDEPLSALDARIRKHLREQIRQIQRElglTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTA 224
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-211 |
9.07e-23 |
|
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: 92.13 E-value: 9.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDgqdivplspqkrhigmvfqs 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 yalfpnmtveQNVAFGlrmqkvnaddshkrvqevlqlvelkdlagrYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:cd03221 61 ----------STVKIG------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545130686 164 LDARIRKHLREQIRQIQRELglttIFVTHDQEEALTMSDRIFLMNQGK 211
Cdd:cd03221 101 LDLESIEALEEALKEYPGTV----ILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-225 |
1.43e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 98.25 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 17 PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI--VPLSPQKRHIGMVFQSYALFPNmTVEQ 94
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtkLQLDSWRSRLAVVSQTPFLFSD-TVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 95 NVAFGlrmqkvNADDSHKRVQEVLQLVELKDLAGRYPH-----------QMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:PRK10789 408 NIALG------RPDATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545130686 164 LDARIRKHLREQIRQIQRElglTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK10789 482 VDGRTEHQILHNLRQWGEG---RTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-216 |
1.50e-22 |
|
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: 93.10 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 10 QKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVD---SGKILLDGQDIVP-LSPQKRHIGMVFQSYA 85
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEfAEKYPGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 86 LFPNMTVEQNVAFGLRMQkvnaddshkrvqevlqlvelkdlAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALD 165
Cdd:cd03233 94 HFPTLTVRETLDFALRCK-----------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 545130686 166 ARIRKHLREQIRQIQRELGLTTIF-VTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03233 151 SSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-192 |
2.20e-22 |
|
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: 92.94 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 18 VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ-KRHIGMVFQSYALFPNMTVEQNV 96
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 97 AFglrmqkVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQI 176
Cdd:cd03231 95 RF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
170
....*....|....*.
gi 545130686 177 RQiQRELGLTTIFVTH 192
Cdd:cd03231 169 AG-HCARGGMVVLTTH 183
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-213 |
2.70e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLdGQDIvplspqkrHIGMVFQS 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV--------KIGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 YALF-PNMTVEQNV---AFGLRMQKVNA---------DDSHKRVqevlqlvelKDLagryphqmSGGQCQRVALARSLVT 150
Cdd:COG0488 387 QEELdPDKTVLDELrdgAPGGTEQEVRGylgrflfsgDDAFKPV---------GVL--------SGGEKARLALAKLLLS 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 151 RPRLLLLDEPLSALDArirkHLREQIrqiqrELGL-----TTIFVTHDQE--EALTmsDRIFLMNQGKIV 213
Cdd:COG0488 450 PPNVLLLDEPTNHLDI----ETLEAL-----EEALddfpgTVLLVSHDRYflDRVA--TRILEFEDGGVR 508
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
8-216 |
1.10e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.50 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 8 HLQKSYAGtpvfsdinceVAK-GEFVTLLGPSGCGKSTLLRCIAGLTSVD---SGKILLDGQDIvPLSPQKRHIGMVFQS 83
Cdd:TIGR00955 39 HLLKNVSG----------VAKpGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI-DAKEMRAISAYVQQD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 YALFPNMTVEQNVAFG--LRMQK-VNADDSHKRVQEVLQLVELKDLA-------GRYpHQMSGGQCQRVALARSLVTRPR 153
Cdd:TIGR00955 108 DLFIPTLTVREHLMFQahLRMPRrVTKKEKRERVDEVLQALGLRKCAntrigvpGRV-KGLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 154 LLLLDEPLSALDArirkHLREQIRQIQREL---GLTTIFVTHD-QEEALTMSDRIFLMNQGKIVQSG 216
Cdd:TIGR00955 187 LLFCDEPTSGLDS----FMAYSVVQVLKGLaqkGKTIICTIHQpSSELFELFDKIILMAEGRVAYLG 249
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-217 |
1.14e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 95.24 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 3 FVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ---KRHIGM 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPNMTVEQNVAFGLRMQK----VNADDSHK---RVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRP 152
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKkvcgVNIIDWREmrvRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 153 RLLLLDEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGD 217
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGM 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-221 |
1.26e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 95.00 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 7 QHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDS--GKILLDGQDIVPLS---PQKRHIGMVF 81
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNirdTERAGIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 82 QSYALFPNMTVEQNVAFG---LRMQKVNADDSHKRVQEVLQLVELK-DLAGRYPHqMSGGQCQRVALARSLVTRPRLLLL 157
Cdd:PRK13549 89 QELALVKELSVLENIFLGneiTPGGIMDYDAMYLRAQKLLAQLKLDiNPATPVGN-LGLGQQQLVEIAKALNKQARLLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545130686 158 DEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:PRK13549 168 DEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-216 |
4.57e-21 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 94.31 E-value: 4.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSY--AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI-VPLSPQKRHIGMV 80
Cdd:TIGR01257 929 VCVKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 161 LSALDARIRKHLREQIrqIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-221 |
5.39e-21 |
|
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: 93.86 E-value: 5.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 17 PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQdiVPLSPQKrhigmvfqsyALFPNMTVEQNV 96
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQ----------AWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 97 AFGLRMQKvnaddshKRVQEVLQ----LVELKDLA-------GRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALD 165
Cdd:TIGR00957 720 LFGKALNE-------KYYQQVLEacalLPDLEILPsgdrteiGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 166 ARIRKHLREQIRQIQREL-GLTTIFVTHDQeEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:TIGR00957 793 AHVGKHIFEHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-221 |
5.52e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.54 E-value: 5.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAG--TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI--VPLSPQKRHIGM 79
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFpNMTVEQNVAFGlrmqkvnADDSHKR--VQEVLQLVELKDLAGRYPH-----------QMSGGQCQRVALAR 146
Cdd:PRK11176 422 VSQNVHLF-NDTIANNIAYA-------RTEQYSReqIEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 147 SLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRElglTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELQKN---RTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-212 |
5.71e-21 |
|
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: 89.45 E-value: 5.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 16 TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIvplsPQKRH------IGMVFQSYALFPN 89
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI----SQYEHkylhskVSLVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 90 mTVEQNVAFGLR---MQKVNADDSHKRVQEVLQLVEL--KDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSAL 164
Cdd:cd03248 103 -SLQDNIAYGLQscsFECVKEAAQKAHAHSFISELASgyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545130686 165 DARIRKHLREQIRQIQRElglTTIFVTHDQEEALTMSDRIFLMNQGKI 212
Cdd:cd03248 182 DAESEQQVQQALYDWPER---RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-221 |
7.31e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 93.27 E-value: 7.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVP--LSPQKRhIGMVFQSYALFPNMTVEQNVAF 98
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAgdIATRRR-VGYMSQAFSLYGELTVRQNLEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 99 GLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQ 178
Cdd:NF033858 363 HARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIE 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545130686 179 IQRELGLtTIFV-THDQEEALTmSDRIFLMNQGK---------IVQSGDAETL 221
Cdd:NF033858 443 LSREDGV-TIFIsTHFMNEAER-CDRISLMHAGRvlasdtpaaLVAARGAATL 493
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
22-225 |
1.48e-20 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 90.63 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 22 INCEVAKGEFVTLLGPSGCGKSTLLRCIAGLT----SVDSGKILLDGQDIVPLSPQKRH------IGMVFQ--SYALFPN 89
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRERRklvghnVSMIFQepQSCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 90 MTVEQNVA--------FGLRMQKVNAddSHKRVQEVLQLVELKD---LAGRYPHQMSGGQCQRVALARSLVTRPRLLLLD 158
Cdd:PRK15093 106 ERVGRQLMqnipgwtyKGRWWQRFGW--RKRRAIELLHRVGIKDhkdAMRSFPYELTEGECQKVMIAIALANQPRLLIAD 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 159 EPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PRK15093 184 EPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-210 |
2.48e-20 |
|
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: 87.77 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 14 AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKI-----LLDGQDIVPLSPQKRH-IGMVFQSYALF 87
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRYsVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 88 pNMTVEQNVAFG--LRMQKVNADDSHKRVQEVLQLVELKDLA--GRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:cd03290 92 -NATVEENITFGspFNKQRYKAVTDACSLQPDIDLLPFGDQTeiGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545130686 164 LDARIRKHL-REQIRQIQRELGLTTIFVTHdQEEALTMSDRIFLMNQG 210
Cdd:cd03290 171 LDIHLSDHLmQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-215 |
5.15e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.50 E-value: 5.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 19 FSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKR-HIGMVF-----QSYALFPNMTV 92
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 93 EQNV--------AFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRyphqMSGGQCQRVALARSLVTRPRLLLLDEPLSAL 164
Cdd:PRK15439 359 AWNVcalthnrrGFWIKPARENAVLERYRRALNIKFNHAEQAART----LSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 545130686 165 DARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQS 215
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGA 484
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-216 |
5.94e-20 |
|
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: 86.31 E-value: 5.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAG--TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI--VPLSPQKRHIGM 79
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIstIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPNmTVEQNVafglrmqKVNADDSHKRVQEVLQLVELKDlagryphQMSGGQCQRVALARSLVTRPRLLLLDE 159
Cdd:cd03369 87 IPQDPTLFSG-TIRSNL-------DPFDEYSDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545130686 160 PLSAL----DARIRKHLREqirqiqrELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSG 216
Cdd:cd03369 152 ATASIdyatDALIQKTIRE-------EFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-234 |
3.49e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 85.65 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAG-LTSVD-------SGKILLDGQDIVPLSPQK- 74
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGaprgarvTGDVTLNGEPLAAIDAPRl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 75 --RHIGMVFQSYALFPnMTVEQNVAFGLRMQKVNADDSHKRVQEV----LQLVELKDLAGRYPHQMSGGQCQRVALARSL 148
Cdd:PRK13547 82 arLRAVLPQAAQPAFA-FSAREIVLLGRYPHARRAGALTHRDGEIawqaLALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 149 ---------VTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGdae 219
Cdd:PRK13547 161 aqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG--- 237
|
250
....*....|....*
gi 545130686 220 tlytAPVDVFAAGFI 234
Cdd:PRK13547 238 ----APADVLTPAHI 248
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-214 |
8.32e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.76 E-value: 8.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ---KRHIGMVFQSY---ALFPNMTVEQ 94
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdavKKGMAYITESRrdnGFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 95 NVA---------FGLRMQKVNADDSHKRVQEVLQLVELK-DLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSAL 164
Cdd:PRK09700 361 NMAisrslkdggYKGAMGLFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGI 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 545130686 165 DARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQ 214
Cdd:PRK09700 441 DVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-221 |
1.05e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 87.10 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 12 SYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAG-LTSVDSGKILLDGQdiVPLSPQkrhIGMVFqsyalfpNM 90
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT--VAYVPQ---VSWIF-------NA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 91 TVEQNVAFGLRMQKvnadDSHKRVQEV------LQLVELKDLA--GRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:PLN03130 694 TVRDNILFGSPFDP----ERYERAIDVtalqhdLDLLPGGDLTeiGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545130686 163 ALDArirkHLREQI--RQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:PLN03130 770 ALDA----HVGRQVfdKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-202 |
1.69e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 82.31 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVP-LSPQKRHIGMVFQ 82
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 SYALFPNMTVEQNVAFGLRMQKVNADdshkrVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:PRK13540 82 RSGINPYLTLRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 545130686 163 ALDARIRKHLREQIRQIQRELGltTIFVTHDQEEALTMSD 202
Cdd:PRK13540 157 ALDELSLLTIITKIQEHRAKGG--AVLLTSHQDLPLNKAD 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-218 |
2.02e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.73 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQdivplsPQK------ 74
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ------EMRfastta 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 75 ---RHIGMVFQSYALFPNMTVEQNVAFGL---RMQKVNADDSHKRVQEVLQ--------LVELKDLagryphqmSGGQCQ 140
Cdd:PRK11288 76 alaAGVAIIYQELHLVPEMTVAENLYLGQlphKGGIVNRRLLNYEAREQLEhlgvdidpDTPLKYL--------SIGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545130686 141 RVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDA 218
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVATFDD 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-192 |
2.16e-18 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 81.05 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 14 AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLdgqdivplsPQKRHIGMVFQ-SYalFPNMTv 92
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQrPY--LPLGT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 93 eqnvafgLRmqkvnaddshkrvqEVLqlvelkdlagRYP--HQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRK 170
Cdd:cd03223 80 -------LR--------------EQL----------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|..
gi 545130686 171 HLREQIrqiqRELGLTTIFVTH 192
Cdd:cd03223 129 RLYQLL----KELGITVISVGH 146
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-213 |
4.58e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 85.00 E-value: 4.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 1 MSFVSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDgQDIVPLSPQK---RHI 77
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVARLQQdppRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 78 -GMVF---------------QSYALFPNMTVEQNVAFGLRMQKVNADDSH-------KRVQEVLQLVEL---KDLAgryp 131
Cdd:PRK11147 80 eGTVYdfvaegieeqaeylkRYHDISHLVETDPSEKNLNELAKLQEQLDHhnlwqleNRINEVLAQLGLdpdAALS---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 132 hQMSGGQCQRVALARSLVTRPRLLLLDEPLSALD-ARIrkhlrEQIRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQG 210
Cdd:PRK11147 156 -SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDiETI-----EWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRG 229
|
...
gi 545130686 211 KIV 213
Cdd:PRK11147 230 KLV 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-208 |
2.35e-17 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 82.68 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGT-PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLdgqdivplSPQKRhIGMVFQS 83
Cdd:TIGR03719 6 TMNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--------QPGIK-VGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 YALFPNMTVEQNVAFGL--------RMQKVNA------DDSHK------RVQEVLQLVELKDL---------AGRYP--- 131
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGVaeikdaldRFNEISAkyaepdADFDKlaaeqaELQEIIDAADAWDLdsqleiamdALRCPpwd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 132 ---HQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDArirkhlrEQIRQIQREL----GlTTIFVTHdqeealtmsDRI 204
Cdd:TIGR03719 157 advTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA-------ESVAWLERHLqeypG-TVVAVTH---------DRY 219
|
....
gi 545130686 205 FLMN 208
Cdd:TIGR03719 220 FLDN 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-234 |
2.54e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 83.14 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 6 VQHLQKSYAGT--PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVP-LSPQKRHIGMVFQ 82
Cdd:TIGR01257 1940 LNELTKVYSGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTnISDVHQNMGYCPQ 2019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 SYALFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:TIGR01257 2020 FDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545130686 163 ALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTApvdvFAAGFI 234
Cdd:TIGR01257 2100 GMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSK----FGDGYI 2166
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-224 |
2.59e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.31 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 15 GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDiVPLSPQKRHIGMVFQSYAL---FPnMT 91
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-TRQALQKNLVAYVPQSEEVdwsFP-VL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 92 VEQNVAFG----LRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALD-- 165
Cdd:PRK15056 97 VEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDvk 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545130686 166 --ARIRKHLREqirqiQRELGLTTIFVTHDQEEALTMSDRIfLMNQGKIVQSGDAETLYTA 224
Cdd:PRK15056 177 teARIISLLRE-----LRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFTA 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-222 |
3.26e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 82.72 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 17 PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAG-LTSVDSGKILLDGQdiVPLSPQkrhIGMVFqsyalfpNMTVEQN 95
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS--VAYVPQ---VSWIF-------NATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 96 VAFGLRMQKV---NADDShKRVQEVLQLVELKDLA--GRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDArirk 170
Cdd:PLN03232 699 ILFGSDFESErywRAIDV-TALQHDLDLLPGRDLTeiGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA---- 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545130686 171 HLREQIRQ--IQREL-GLTTIFVThDQEEALTMSDRIFLMNQGKIVQSGDAETLY 222
Cdd:PLN03232 774 HVAHQVFDscMKDELkGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-195 |
4.60e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.85 E-value: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 16 TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIvplspqkrHIGmvfqsyalfPNMTVEQN 95
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN--------QFG---------REASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 96 VAfglrmqkvnADDSHKRVQEVLQLVELKD--LAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLR 173
Cdd:COG2401 106 IG---------RKGDFKDAVELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170 180
....*....|....*....|..
gi 545130686 174 EQIRQIQRELGLTTIFVTHDQE 195
Cdd:COG2401 177 RNLQKLARRAGITLVVATHHYD 198
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-211 |
6.65e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.46 E-value: 6.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 18 VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDS--GKILLDGQDivPLSPQKRHIGMVFQSYALFPNMTVEQN 95
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRK--PTKQILKRTGFVTQDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 96 VAFG--LRMQKVNADDSHKRVQEV------LQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDAR 167
Cdd:PLN03211 161 LVFCslLRLPKSLTKQEKILVAESviselgLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 545130686 168 IRKHLREQIRQIQRElGLTTIFVTHD-QEEALTMSDRIFLMNQGK 211
Cdd:PLN03211 241 AAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-229 |
8.79e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 81.23 E-value: 8.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 56 DSGKILLDGQDIVP--LSPQKRHIGMVFQSYALFpNMTVEQNVAFGlrmqkvNADDSHKRVQEVLQLVELKDL------- 126
Cdd:PTZ00265 1275 NSGKILLDGVDICDynLKDLRNLFSIVSQEPMLF-NMSIYENIKFG------KEDATREDVKRACKFAAIDEFieslpnk 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 127 ----AGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHdQEEALTMSD 202
Cdd:PTZ00265 1348 ydtnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSD 1426
|
170 180 190
....*....|....*....|....*....|..
gi 545130686 203 RIFLMNQ----GKIVQS-GDAETLYTAPVDVF 229
Cdd:PTZ00265 1427 KIVVFNNpdrtGSFVQAhGTHEELLSVQDGVY 1458
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-212 |
1.47e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 80.40 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 22 INCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGMVFQSYALFPNMtveqnvafg 99
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAVFTDFHLFDQL--------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 100 LRMQKVNADDshKRVQ---EVLQL---VELKDlaGRYPH-QMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHL 172
Cdd:PRK10522 413 LGPEGKPANP--ALVEkwlERLKMahkLELED--GRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREF 488
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 545130686 173 REQIRQIQRELGLTTIFVTHDqEEALTMSDRIFLMNQGKI 212
Cdd:PRK10522 489 YQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-212 |
1.57e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.87 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGL-TSVDSGKILLDGQDIVPLSPQK--RH-IGMVFQS---YALFPNMTVE 93
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQaiRAgIAMVPEDrkrHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 94 QNV------AFGLRMQkVNADDSHKRVQEVLQLVELKDLAGRYP-HQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDA 166
Cdd:TIGR02633 358 KNItlsvlkSFCFKMR-IDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 545130686 167 RIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKI 212
Cdd:TIGR02633 437 GAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-204 |
2.31e-16 |
|
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: 77.06 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 25 EVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDiVPLSPQKrhIGMVFQsyalfpnMTVEQnvafgLRMQK 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-VSYKPQY--IKADYE-------GTVRD-----LLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 105 VNADDSHKRVQ-EVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQREL 183
Cdd:cd03237 86 TKDFYTHPYFKtEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENN 165
|
170 180
....*....|....*....|.
gi 545130686 184 GLTTIFVTHDQEEALTMSDRI 204
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRL 186
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-165 |
3.04e-16 |
|
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: 79.21 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDgqDIVplspqkrHIGMVFQS 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETV-------KLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 Y-ALFPNMTVEQNVAFGLRMQKVN----------------ADDSHKRVQevlqlvelkdlagryphQMSGGQCQRVALAR 146
Cdd:TIGR03719 394 RdALDPNKTVWEEISGGLDIIKLGkreipsrayvgrfnfkGSDQQKKVG-----------------QLSGGERNRVHLAK 456
|
170
....*....|....*....
gi 545130686 147 SLVTRPRLLLLDEPLSALD 165
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLD 475
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
101-223 |
3.48e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 78.24 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 101 RMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQ 180
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV 191
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 545130686 181 RElGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYT 223
Cdd:NF000106 192 RD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
6-219 |
3.91e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 76.60 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 6 VQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTS--VDSGKILLDGQDIVPLSPQKR-HIG--MV 80
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESILDLEPEERaHLGifLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSYALFPNMTVEQ--NVAFGLRMQKVNADDSH-----KRVQEVLQLVELKD-LAGRYPHQ-MSGGQCQRVALARSLVTR 151
Cdd:CHL00131 90 FQYPIEIPGVSNADflRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMALLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545130686 152 PRLLLLDEPLSALDARIRKHLREQIRQIqRELGLTTIFVTHDQEeaL---TMSDRIFLMNQGKIVQSGDAE 219
Cdd:CHL00131 170 SELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYQR--LldyIKPDYVHVMQNGKIIKTGDAE 237
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-197 |
5.09e-16 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 78.52 E-value: 5.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 12 SYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGltsvD-----SGKILLDGQ---------DIvplspqKRHI 77
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DhpqgySNDLTLFGRrrgsgetiwDI------KKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 78 GMVfqSYALFPNMTVEQNV----------AFGLrMQKVnADDSHKRVQEVLQLVELKDLAGRYP-HQMSGGQcQRVAL-A 145
Cdd:PRK10938 339 GYV--SSSLHLDYRVSTSVrnvilsgffdSIGI-YQAV-SDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQ-QRLALiV 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 545130686 146 RSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTHDQEEA 197
Cdd:PRK10938 414 RALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-175 |
1.19e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.50 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 16 TPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDiVPLSPQKRHIGMVFQSYALFPNMTVEQN 95
Cdd:PRK13543 24 EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-ATRGDRSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 96 VAF-----GLRMQKVNADdshkrvqeVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDAR--- 167
Cdd:PRK13543 103 LHFlcglhGRRAKQMPGS--------ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEgit 174
|
170
....*....|...
gi 545130686 168 -----IRKHLREQ 175
Cdd:PRK13543 175 lvnrmISAHLRGG 187
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
15-213 |
1.43e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.26 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 15 GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK--RHiGMVF-----QSYALF 87
Cdd:PRK11288 265 GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaiRA-GIMLcpedrKAEGII 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 88 PNMTVEQNVAFGLRMQKVNADDSHKRVQEvlqlvelKDLAGRY----------PHQ----MSGGQCQRVALARSLVTRPR 153
Cdd:PRK11288 344 PVHSVADNINISARRHHLRAGCLINNRWE-------AENADRFirslniktpsREQlimnLSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545130686 154 LLLLDEPLSALDArirkHLREQIRQIQREL---GLTTIFVTHDQEEALTMSDRIFLMNQGKIV 213
Cdd:PRK11288 417 VILLDEPTRGIDV----GAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-210 |
1.46e-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: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 15 GTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQdiVPLSPQKRHIgmvfqsyalFPNmTVEQ 94
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFSSQFSWI---------MPG-TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 95 NVAFGLRMQKVnaddshkRVQEVLQLVELKDLAGRYPHQ-----------MSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:cd03291 117 NIIFGVSYDEY-------RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545130686 164 LDARIRKHLREQIrQIQRELGLTTIFVTHDQEEaLTMSDRIFLMNQG 210
Cdd:cd03291 190 LDVFTEKEIFESC-VCKLMANKTRILVTSKMEH-LKKADKILILHEG 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
11-221 |
1.72e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 77.08 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 11 KSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQK---RHIGMVFQSYALF 87
Cdd:PRK10982 6 KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaleNGISMVHQELNLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 88 PNMTVEQNVAFGLRMQK---VNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSAL 164
Cdd:PRK10982 86 LQRSVMDNMWLGRYPTKgmfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 165 DARIRKHLREQIRQIqRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:PRK10982 166 TEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-219 |
2.80e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 76.74 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILldgqdivplspQKRHIGMVFQSyALFPNMTVEQNVAFgl 100
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILF-- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 101 rMQKVNADDSHKRVQeVLQL-VELKDLAGRYPHQ-------MSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHL 172
Cdd:PTZ00243 744 -FDEEDAARLADAVR-VSQLeADLAQLGGGLETEigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV 821
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545130686 173 REQIRqIQRELGLTTIFVTHdQEEALTMSDRIFLMNQGKIVQSGDAE 219
Cdd:PTZ00243 822 VEECF-LGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSA 866
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-229 |
3.62e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.55 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 17 PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVP--LSPQKRHIGMVFQSYALFPNmTVEQ 94
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFSG-TVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 95 NV-AFGlrmQKVNADdshkrVQEVLQLVELKDLAGRYP-----------HQMSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:PLN03232 1329 NIdPFS---EHNDAD-----LWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 163 ALDARIRKHLREQIRQiqrELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVF 229
Cdd:PLN03232 1401 SVDVRTDSLIQRTIRE---EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-204 |
3.93e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.00 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 25 EVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDgqdiVPLS--PQKrhigmVFQSYalfpNMTVEQNvafgLRM 102
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----LKISykPQY-----IKPDY----DGTVEDL----LRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 103 QKVNADDSHKRVqEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRE 182
Cdd:PRK13409 424 ITDDLGSSYYKS-EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEE 502
|
170 180
....*....|....*....|....*.
gi 545130686 183 LGLTTIFVTHDqeeaLTM----SDRI 204
Cdd:PRK13409 503 REATALVVDHD----IYMidyiSDRL 524
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-217 |
4.65e-15 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 73.67 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLT--SVDSGKILLDGQDIVPLSPQKRH---IG 78
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAgegIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 79 MVFQ--------SYALFPNMTVeqNVAFGLRMQK-VNADDSHKRVQEVLQLVEL-KDLAGRYPHQ-MSGGQCQRVALARS 147
Cdd:PRK09580 82 MAFQypveipgvSNQFFLQTAL--NAVRSYRGQEpLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545130686 148 LVTRPRLLLLDEPLSALDARIRKHLREQIRQIqRELGLTTIFVTHDQE-EALTMSDRIFLMNQGKIVQSGD 217
Cdd:PRK09580 160 AVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRiLDYIKPDYVHVLYQGRIVKSGD 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
11-220 |
5.06e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.60 E-value: 5.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 11 KSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDS--GKILLDGQ-----DIVplSPQKRHIGMVFQS 83
Cdd:NF040905 9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcrfkDIR--DSEALGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 YALFPNMTVEQNVAFGLRMQK---VNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:NF040905 87 LALIPYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 161 LSALDARIRKHLREQIRQIqRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAET 220
Cdd:NF040905 167 TAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRA 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-212 |
5.32e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.35 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGL-TSVDSGKILLDGQDIVPLSPQ---KRHIGMVFQS---YALFPNMTVE 93
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQqaiAQGIAMVPEDrkrDGIVPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 94 QNVAFGL--RMQKVNADDSHKRVQEVLQlvELKDLAGRYPH------QMSGGQCQRVALARSLVTRPRLLLLDEPLSALD 165
Cdd:PRK13549 360 KNITLAAldRFTGGSRIDDAAELKTILE--SIQRLKVKTASpelaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545130686 166 ARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKI 212
Cdd:PRK13549 438 VGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-210 |
5.51e-15 |
|
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: 76.10 E-value: 5.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 12 SYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQdiVPLSPQKRHIgmvfqsyalFPNmT 91
Cdd:TIGR01271 435 SLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--ISFSPQTSWI---------MPG-T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 92 VEQNVAFGLRMQKVnaddshkRVQEVLQLVELKDLAGRYPHQ-----------MSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:TIGR01271 503 IKDNIIFGLSYDEY-------RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 545130686 161 LSALDARIRKHLREqiRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQG 210
Cdd:TIGR01271 576 FTHLDVVTEKEIFE--SCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-210 |
8.18e-15 |
|
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: 71.89 E-value: 8.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAG--LTSVDSGKILLDGQDIVPLSPqkRHIGMVFQSYALFPNMTVEqnvaf 98
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQ--RSTGYVEQQDVHSPNLTVR----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 99 glrmqkvnaddshkrvqEVLQL-VELKDLagryphqmSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIR 177
Cdd:cd03232 98 -----------------EALRFsALLRGL--------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
170 180 190
....*....|....*....|....*....|....*
gi 545130686 178 QIQRElGLtTIFVTHDQEEALTMS--DRIFLMNQG 210
Cdd:cd03232 153 KLADS-GQ-AILCTIHQPSASIFEkfDRLLLLKRG 185
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-213 |
1.26e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 74.54 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDgqdivplspQKRHIGMVFQ- 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS---------ENANIGYYAQd 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 SYALFPN-MTV-------------EQNVAFGL-RMQkVNADDSHKRVQeVLqlvelkdlagryphqmSGGQCQRVALARS 147
Cdd:PRK15064 391 HAYDFENdLTLfdwmsqwrqegddEQAVRGTLgRLL-FSQDDIKKSVK-VL----------------SGGEKGRMLFGKL 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545130686 148 LVTRPRLLLLDEPLSALDArirkhlrEQIRQIQRELGL---TTIFVTHDQEEALTMSDRIFLMNQGKIV 213
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDM-------ESIESLNMALEKyegTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-221 |
3.94e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.24 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVplspQKRHIGMVFQS 83
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA----DARHRRAVCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 YA---------LFPNMTVEQNVAFGLRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRL 154
Cdd:NF033858 78 IAympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545130686 155 LLLDEPLSALDARIRKHLREQIRQIQREL-GLTTIFVTHDQEEALTMsDRIFLMNQGKIVQSGDAETL 221
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-204 |
1.23e-13 |
|
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: 71.35 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 25 EVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKIllDGQDIVPLSPQKrhigmVFQSYalfpNMTVEQNvafgLRMQK 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQY-----ISPDY----DGTVEEF----LRSAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 105 VNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELG 184
Cdd:COG1245 427 TDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRG 506
|
170 180
....*....|....*....|....
gi 545130686 185 LTTIFVTHDqeeaLTM----SDRI 204
Cdd:COG1245 507 KTAMVVDHD----IYLidyiSDRL 526
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-221 |
1.31e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 71.69 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 17 PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI--VPLSPQKRHIGMVFQSYALFPNmTVEQ 94
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIskFGLMDLRKVLGIIPQAPVLFSG-TVRF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 95 NV-AFGlrmQKVNADdshkrVQEVLQLVELKDLAGRYP-----------HQMSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:PLN03130 1332 NLdPFN---EHNDAD-----LWESLERAHLKDVIRRNSlgldaevseagENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545130686 163 ALDAR----IRKHLREQIRQIqrelglTTIFVTHdQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:PLN03130 1404 AVDVRtdalIQKTIREEFKSC------TMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-217 |
1.34e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.68 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 26 VAKGEFVTLLGPSGCGKSTLLRCIAGLTS---VDSGKILLDGQdivPL-SPQKRHIGMVFQSYALFPNMTVEQNVAFGLR 101
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGR---PLdSSFQRSIGYVQQQDLHLPTSTVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 102 M---QKVNADDSHKRVQEVLQLVELKDLA----GRYPHQMSGGQCQRVALARSLVTRPRLLL-LDEPLSALDAR----IR 169
Cdd:TIGR00956 863 LrqpKSVSKSEKMEYVEEVIKLLEMESYAdavvGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQtawsIC 942
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 545130686 170 KHLREQIRQIQrelgltTIFVTHDQEEALTMS--DRIFLMNQG-KIVQSGD 217
Cdd:TIGR00956 943 KLMRKLADHGQ------AILCTIHQPSAILFEefDRLLLLQKGgQTVYFGD 987
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-214 |
1.36e-13 |
|
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: 69.88 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSY--AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDsGKILLDG--QDIVPLSPQKRHIGM 79
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGvsWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPNmTVEQNVafglrmqKVNADDSHKRVQEVLQLVELKDLAGRYPHQM-----------SGGQCQRVALARSL 148
Cdd:cd03289 82 IPQKVFIFSG-TFRKNL-------DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 149 VTRPRLLLLDEPLSALDARIRKHLREQIRQiqrELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQ 214
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQ---AFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-218 |
2.13e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 71.09 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSY--AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDsGKILLDG--QDIVPLSPQKRHIGM 79
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvsWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 80 VFQSYALFPNmTVEQNVafglrmqKVNADDSHKRVQEVLQLVELKDLAGRYPHQM-----------SGGQCQRVALARSL 148
Cdd:TIGR01271 1297 IPQKVFIFSG-TFRKNL-------DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSI 1368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 149 VTRPRLLLLDEPLSALDARIRKHLREQIRQIQRElgLTTIFVTHDQEEALTMSDriFLMNQGKIVQSGDA 218
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN--CTVILSEHRVEALLECQQ--FLVIEGSSVKQYDS 1434
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-208 |
2.48e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 34 LLGPSGCGKSTLLRCIAGLTSVDSGKILLdgqdivplSPQKRhIGMVFQSYALFPNMTVEQNVAFGL--------RMQKV 105
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARP--------APGIK-VGYLPQEPQLDPEKTVRENVEEGVaevkaaldRFNEI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 106 NA------DDSHK------RVQEVLQLVELKDL---------AGRYPH------QMSGGQCQRVALARSLVTRPRLLLLD 158
Cdd:PRK11819 109 YAayaepdADFDAlaaeqgELQEIIDAADAWDLdsqleiamdALRCPPwdakvtKLSGGERRRVALCRLLLEKPDMLLLD 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545130686 159 EPLSALDAR----IRKHLreqirqiQRELGlTTIFVTHdqeealtmsDRIFLMN 208
Cdd:PRK11819 189 EPTNHLDAEsvawLEQFL-------HDYPG-TVVAVTH---------DRYFLDN 225
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-192 |
6.85e-13 |
|
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: 69.39 E-value: 6.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 14 AGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGM-VFQSYALFPnMTV 92
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLgTLRDQIIYP-DSS 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 93 EQnvafglrMQKvnADDSHKRVQEVLQLVELKDLAGR---------YPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:TIGR00954 542 ED-------MKR--RGLSDKDLEQILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSA 612
|
170 180
....*....|....*....|....*....
gi 545130686 164 ldarIRKHLREQIRQIQRELGLTTIFVTH 192
Cdd:TIGR00954 613 ----VSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-211 |
1.22e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIV---PLSPQKRHIGMVF 81
Cdd:PRK10762 6 QLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngPKSSQEAGIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 82 QSYALFPNMTVEQNVAFGL----RMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLL 157
Cdd:PRK10762 86 QELNLIPQLTIAENIFLGRefvnRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545130686 158 DEPLSALDARIRKHLREQIRQIqRELGLTTIFVTHDQEEALTMSDRIFLMNQGK 211
Cdd:PRK10762 166 DEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-213 |
4.40e-12 |
|
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: 66.75 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 22 INCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQ--KRHIGMVFQSYALFPnmtveqnvafg 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREayRQLFSAVFSDFHLFD----------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 100 lRMQKVNADDSHKRVQEVLQLVELKDL----AGRY-PHQMSGGQCQRVALarsLVT----RPrLLLLDEPLSALDARIRK 170
Cdd:COG4615 420 -RLLGLDGEADPARARELLERLELDHKvsveDGRFsTTDLSQGQRKRLAL---LVAlledRP-ILVFDEWAADQDPEFRR 494
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 545130686 171 HLREQIRQIQRELGLTTIFVTHDqEEALTMSDRIFLMNQGKIV 213
Cdd:COG4615 495 VFYTELLPELKARGKTVIAISHD-DRYFDLADRVLKMDYGKLV 536
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-219 |
6.99e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.67 E-value: 6.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 29 GEFVTLLGPSGCGKSTLLRCIAGLTS----VDSGKILLDGQDIVPLSPQKRhiGMVFQSYAL---FPNMTVEQNVAFGLR 101
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKKHYR--GDVVYNAETdvhFPHLTVGETLDFAAR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 102 MQKVNaddshKRVQEVLQLVELKDLAGRY------PHQ------------MSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:TIGR00956 165 CKTPQ-----NRPDGVSREEYAKHIADVYmatyglSHTrntkvgndfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRG 239
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545130686 164 LDA----RIRKHLREQIRQIQrelglTTIFVTHDQ--EEALTMSDRIFLMNQGKIVQSGDAE 219
Cdd:TIGR00956 240 LDSatalEFIRALKTSANILD-----TTPLVAIYQcsQDAYELFDKVIVLYEGYQIYFGPAD 296
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-225 |
7.55e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.59 E-value: 7.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 18 VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILL-DGQDI--VPLSPQKRHIGMVFQSYALFPNmTVEQ 94
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLkdINLKWWRSKIGVVSQDPLLFSN-SIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 95 NVAFGLRMQK--------------VNADDSHKR-------------------------------------VQEVLQLVEL 123
Cdd:PTZ00265 479 NIKYSLYSLKdlealsnyynedgnDSQENKNKRnscrakcagdlndmsnttdsneliemrknyqtikdseVVDVSKKVLI 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 124 KD-----------LAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELGLTTIFVTH 192
Cdd:PTZ00265 559 HDfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
250 260 270
....*....|....*....|....*....|...
gi 545130686 193 dQEEALTMSDRIFLMNQGKIVQSGDAETLYTAP 225
Cdd:PTZ00265 639 -RLSTIRYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
17-231 |
1.07e-11 |
|
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: 64.16 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 17 PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI--VPLSPQKRHIGMVFQSYALFPNmtveq 94
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIskLPLHTLRSRLSIILQDPILFSG----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 95 NVAFGLRMQKVNADDshkRVQEVLQLVELKDLAGRYP-----------HQMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:cd03288 110 SIRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLARAFVRKSSILIMDEATAS 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545130686 164 LDARIRKHLREQIRQIQRELGLTTIfvTHDQEEALTmSDRIFLMNQGKIVQSGDAETLYTAPVDVFAA 231
Cdd:cd03288 187 IDMATENILQKVVMTAFADRTVVTI--AHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFAS 251
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-206 |
1.12e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 62.01 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 28 KGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLdgqdivplspqkrhigmvfqsyalfpnmtveqnvafglrmqkVNA 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY------------------------------------------IDG 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 108 DDSHKRVQEVLQLVelkdLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIR-----QIQRE 182
Cdd:smart00382 39 EDILEEVLDQLLLI----IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSE 114
|
170 180
....*....|....*....|....
gi 545130686 183 LGLTTIFVTHDQEEALTMSDRIFL 206
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-195 |
1.36e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 6 VQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKIlldgqdivplspqkrHIGM-----V 80
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI---------------HCGTklevaY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 FQSY--ALFPNMTVEQNVAFGLRMQKVNADDSHkrVQEVLQLVELKDLAGRYP-HQMSGGQCQRVALARSLVTRPRLLLL 157
Cdd:PRK11147 387 FDQHraELDPEKTVMDNLAEGKQEVMVNGRPRH--VLGYLQDFLFHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLIL 464
|
170 180 190
....*....|....*....|....*....|....*...
gi 545130686 158 DEPLSALDARIRKHLREQIRQIQRelglTTIFVTHDQE 195
Cdd:PRK11147 465 DEPTNDLDVETLELLEELLDSYQG----TVLLVSHDRQ 498
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-231 |
1.70e-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: 65.35 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 18 VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDI--VPLSPQKRHIGMVFQSYALFPNmtveqn 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIakIGLHDLRFKITIIPQDPVLFSG------ 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 96 vafGLRMqkvNADD----SHKRVQEVLQLVELKDLAGRYP----HQ-------MSGGQCQRVALARSLVTRPRLLLLDEP 160
Cdd:TIGR00957 1375 ---SLRM---NLDPfsqySDEEVWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545130686 161 LSALDARIRKHLREQIRQiQRElGLTTIFVTHDQEEALTMSdRIFLMNQGKIVQsgdaetlYTAPVDVFAA 231
Cdd:TIGR00957 1449 TAAVDLETDNLIQSTIRT-QFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAE-------FGAPSNLLQQ 1509
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-165 |
1.91e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLdGQDIvplspqkrHIGMVFQS 83
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--------KLAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 Y-ALFPNMTVEQNVAFGLRMQKVN----------------ADDSHKRVQevlqlvelkdlagryphQMSGGQCQRVALAR 146
Cdd:PRK11819 396 RdALDPNKTVWEEISGGLDIIKVGnreipsrayvgrfnfkGGDQQKKVG-----------------VLSGGERNRLHLAK 458
|
170
....*....|....*....
gi 545130686 147 SLVTRPRLLLLDEPLSALD 165
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLD 477
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-254 |
4.15e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 63.76 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 20 SDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKIlldgqDIvplspqKRHIGMVFQSYALFPNMTVEQNVAF- 98
Cdd:PRK13545 41 NNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DI------KGSAALIAISSGLNGQLTGIENIELk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 99 GLRMQKvnaddSHKRVQEVL-QLVELKDLaGRYPHQ----MSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLR 173
Cdd:PRK13545 110 GLMMGL-----TKEKIKEIIpEIIEFADI-GKFIYQpvktYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 174 EQIRQIqRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLytapVDVFAAgFIGNYNLLDADKATQLLQRPI 253
Cdd:PRK13545 184 DKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV----VDHYDE-FLKKYNQMSVEERKDFREEQI 257
|
.
gi 545130686 254 S 254
Cdd:PRK13545 258 S 258
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-204 |
4.68e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 60.66 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 25 EVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVpLSPQKRhigmvfqsyalfpnmtveqnvafglrmqk 104
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-YKPQYI----------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 105 vnaddshkrvqevlqlvelkdlagryphQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRELG 184
Cdd:cd03222 71 ----------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|
gi 545130686 185 LTTIFVTHDQEEALTMSDRI 204
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRI 142
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
4-176 |
1.16e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 59.89 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFsDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLspQKRHIGMVFQS 83
Cdd:PRK13541 2 LSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI--AKPYCTYIGHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 YALFPNMTVEQNVAFGLRMQkvnadDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:PRK13541 79 LGLKLEMTVFENLKFWSEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETN 153
|
170
....*....|...
gi 545130686 164 LDARIRKHLREQI 176
Cdd:PRK13541 154 LSKENRDLLNNLI 166
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-216 |
1.95e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.09 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 29 GEFVTLLGPSGCGKSTLLRCIAGLTSvdSGKIllDGQDIVPLSPQK-----RHIGMVFQSYALFPNMTVEQNVAFG--LR 101
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKT--GGYI--EGDIRISGFPKKqetfaRISGYCEQNDIHSPQVTVRESLIYSafLR 981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 102 MQK-VNADDSHKRVQEVLQLVE---LKDLAGRYP--HQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQ 175
Cdd:PLN03140 982 LPKeVSKEEKMMFVDEVMELVEldnLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRT 1061
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 545130686 176 IRQIQrELGLTTIFVTH----DQEEALtmsDRIFLMNQ-GKIVQSG 216
Cdd:PLN03140 1062 VRNTV-DTGRTVVCTIHqpsiDIFEAF---DELLLMKRgGQVIYSG 1103
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-193 |
2.51e-09 |
|
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: 56.99 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 29 GEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKI------------------------LLDGQDIVPLSPQkrhigmvfqsY 84
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildefrgselqnyftkLLEGDVKVIVKPQ----------Y 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 85 A-LFPNmTVEQNVafGLRMQKVnaDDSHKrVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSA 163
Cdd:cd03236 96 VdLIPK-AVKGKV--GELLKKK--DERGK-LDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190
....*....|....*....|....*....|
gi 545130686 164 LDARIRKHLREQIRQIQRElGLTTIFVTHD 193
Cdd:cd03236 170 LDIKQRLNAARLIRELAED-DNYVLVVEHD 198
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-221 |
1.87e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.44 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQdivplspqkrhIGMVFQSYALFPNMTVEQNVAFGL 100
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAGLSGQLTGIENIEFKM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 101 RMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIq 180
Cdd:PRK13546 111 LCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF- 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 545130686 181 RELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETL 221
Cdd:PRK13546 190 KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-216 |
1.20e-07 |
|
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: 50.78 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 21 DINCEVAKGEFVTLLGPSGCGKSTLLrciagltsvdsgkilldgQDIVPLSPQKRHIGmvfqSYALFPNmtveqnvafgl 100
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLV------------------NEGLYASGKARLIS----FLPKFSR----------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 101 rmQKVNADDSHKRVQEV-LQLVELkdlaGRYPHQMSGGQCQRVALARSLVTRPR--LLLLDEPLSALDARIRKHLREQIR 177
Cdd:cd03238 60 --NKLIFIDQLQFLIDVgLGYLTL----GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIK 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 545130686 178 QIqRELGLTTIFVTHDqEEALTMSDRIFLM------NQGKIVQSG 216
Cdd:cd03238 134 GL-IDLGNTVILIEHN-LDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
32-205 |
1.69e-07 |
|
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: 51.07 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 32 VTLL-GPSGCGKSTLLRCIagltsvdsgKILLDGQdivpLSPQKRhigmvfqSYALFPNMTVEQNVAFGLRMQ-KVNADD 109
Cdd:cd03240 24 LTLIvGQNGAGKTTIIEAL---------KYALTGE----LPPNSK-------GGAHDPKLIREGEVRAQVKLAfENANGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 110 SHKRVQEVLQLV--------ELKDLAGRYPHQMSGGQ------CQRVALARSLVTRPRLLLLDEPLSALDA-RIRKHLRE 174
Cdd:cd03240 84 KYTITRSLAILEnvifchqgESNWPLLDMRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEeNIEESLAE 163
|
170 180 190
....*....|....*....|....*....|.
gi 545130686 175 QIRQIQRELGLTTIFVTHDqEEALTMSDRIF 205
Cdd:cd03240 164 IIEERKSQKNFQLIVITHD-EELVDAADHIY 193
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-212 |
1.84e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.55 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 13 YAGTPV-FSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRHIGMVFQSYALFPNMT 91
Cdd:PLN03073 518 YPGGPLlFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 92 VEQnvafGLRMQKVNADDSHKRVQEVLQLVELkdlagrypHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKH 171
Cdd:PLN03073 598 CFP----GVPEQKLRAHLGSFGVTGNLALQPM--------YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEA 665
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 545130686 172 LREQIRQIQRELglttIFVTHDQEEALTMSDRIFLMNQGKI 212
Cdd:PLN03073 666 LIQGLVLFQGGV----LMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-190 |
2.08e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 25 EVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLS--PQKRHIGMVFQSyaLFPNMTVEQNVAFGLRM 102
Cdd:PRK10938 25 TLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSfeQLQKLVSDEWQR--NNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 103 QKVNADDSHK--RVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQ 180
Cdd:PRK10938 103 AEIIQDEVKDpaRCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLH 182
|
170
....*....|
gi 545130686 181 RElGLTTIFV 190
Cdd:PRK10938 183 QS-GITLVLV 191
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-223 |
2.93e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 17 PVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVPLSPQKRhIGMVF-------QSYALFPN 89
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEA-INHGFalvteerRSTGIYAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 90 MTVEQNV----------AFGLRMQKVNADDShkrvQEVLQLVELKDlAGRYPH--QMSGGQCQRVALARSLVTRPRLLLL 157
Cdd:PRK10982 341 LDIGFNSlisnirnyknKVGLLDNSRMKSDT----QWVIDSMRVKT-PGHRTQigSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545130686 158 DEPLSALDARIRKHLREQIRQIQRElGLTTIFVTHDQEEALTMSDRIFLMNQGKIvqSGDAETLYT 223
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV--AGIVDTKTT 478
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-219 |
3.26e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 4 VSVQHLQKSYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGltsvdsgkilldgqdivPLSPQKRHIGMVfqs 83
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG-----------------ELAPVSGEIGLA--- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 84 yalfpnmtveQNVAFGLRMQK----VNADDShkRVQEVLQLV------ELKDLAGRYPHQ----------MSGGQCQRVA 143
Cdd:PRK10636 373 ----------KGIKLGYFAQHqlefLRADES--PLQHLARLApqeleqKLRDYLGGFGFQgdkvteetrrFSGGEKARLV 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 144 LARSLVTRPRLLLLDEPLSALDARIRKHLREQIrqIQRELGLttIFVTHDQEEALTMSDRIFLMNQGKIVQ-SGDAE 219
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL--IDFEGAL--VVVSHDRHLLRSTTDDLYLVHDGKVEPfDGDLE 513
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
257-325 |
4.48e-07 |
|
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: 46.84 E-value: 4.48e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 257 IAIRPEAIELSRTGE-LDALVRSHSLLGNVIRYRIEARGVELVVDVLNRSADDLHPDGQRLALSIDPSAL 325
Cdd:pfam08402 1 LAIRPEKIRLAAAANgLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHARPPAPGDRVGLGWDPEDA 70
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-213 |
5.58e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 5 SVQHLQksYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLT--SVDSGKILLDGQDIVpLSPQKRHI--GMV 80
Cdd:NF040905 264 TVYHPL--HPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVD-VSTVSDAIdaGLA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 81 F-----QSYALFPNMTVEQNVAFGlRMQKVnaddSHKRVqeVLQLVELKdLAGRYPHQM--------------SGGQCQR 141
Cdd:NF040905 341 YvtedrKGYGLNLIDDIKRNITLA-NLGKV----SRRGV--IDENEEIK-VAEEYRKKMniktpsvfqkvgnlSGGNQQK 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545130686 142 VALARSLVTRPRLLLLDEPLSALD--ARIrkhlreQIRQIQREL---GLTTIFVTHDQEEALTMSDRIFLMNQGKIV 213
Cdd:NF040905 413 VVLSKWLFTDPDVLILDEPTRGIDvgAKY------EIYTIINELaaeGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-220 |
4.24e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 12 SYAGTPVFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAgLTSVD----SGKIL-----LDGQDIVPL-----SPQKRHI 77
Cdd:PLN03073 186 SVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA-MHAIDgipkNCQILhveqeVVGDDTTALqcvlnTDIERTQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 78 GMVFQSYALFPNMTVEQNVAFGLRMQKVNADDSH----KRVQEVLQLVELKD-----------LAG---------RYPHQ 133
Cdd:PLN03073 265 LLEEEAQLVAQQRELEFETETGKGKGANKDGVDKdavsQRLEEIYKRLELIDaytaearaasiLAGlsftpemqvKATKT 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 134 MSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRQIQRelglTTIFVTHDQEEALT-MSDRIFLMNQGKI 212
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSHAREFLNTvVTDILHLHGQKLV 420
|
....*...
gi 545130686 213 VQSGDAET 220
Cdd:PLN03073 421 TYKGDYDT 428
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-193 |
5.71e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.86 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 28 KGEFVTLLGPSGCGKSTLLRCIAG-----LTSVDSGkilLDGQDIVplspqKRHIGMVFQSYalFpNMTVEQNVAFGLRM 102
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGelkpnLGDYDEE---PSWDEVL-----KRFRGTELQDY--F-KKLANGEIKVAHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 103 QKV----------------NADDsHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLSALDA 166
Cdd:COG1245 167 QYVdlipkvfkgtvrelleKVDE-RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180
....*....|....*....|....*..
gi 545130686 167 RIRKHLREQIRQIQRElGLTTIFVTHD 193
Cdd:COG1245 246 YQRLNVARLIRELAEE-GKYVLVVEHD 271
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
15-229 |
1.41e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 15 GTP-VFSDINCEVAKGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLDGQDIVP--LSPQKRHIGMVFQSYALFpNMT 91
Cdd:PTZ00243 1321 GLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVLF-DGT 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 92 VEQNVAFGLRMQKvnaddshkrvQEVLQLVELKDLAGRYPHQMSG--------------GQCQRVALARSLVTRPR-LLL 156
Cdd:PTZ00243 1400 VRQNVDPFLEASS----------AEVWAALELVGLRERVASESEGidsrvleggsnysvGQRQLMCMARALLKKGSgFIL 1469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545130686 157 LDEPLSALDARIRkhlreqiRQIQREL-----GLTTIFVTHdQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVF 229
Cdd:PTZ00243 1470 MDEATANIDPALD-------RQIQATVmsafsAYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
27-205 |
3.31e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.50 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 27 AKGEFVTLLGPSGCGKSTLLRCIAgltsvdsgkilldgqdivplspqkrhigmvfqsyalfpnmtveqnVAFGLRMQKVN 106
Cdd:cd03227 19 GEGSLTIITGPNGSGKSTILDAIG---------------------------------------------LALGGAQSATR 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 107 A-DDSHKRVQEVLQLVELKDLAgrypHQMSGGQCQRVALA-----RSLVTRPrLLLLDEPLSALDARIRKHLREQIRQiQ 180
Cdd:cd03227 54 RrSGVKAGCIVAAVSAELIFTR----LQLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILE-H 127
|
170 180
....*....|....*....|....*
gi 545130686 181 RELGLTTIFVTHDQEEALtMSDRIF 205
Cdd:cd03227 128 LVKGAQVIVITHLPELAE-LADKLI 151
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-193 |
5.59e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 28 KGEFVTLLGPSGCGKSTLLRCIAG-----LTSVDSG-------------------KILLDGQDIVPLSPQKRH-IGMVFQ 82
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGelipnLGDYEEEpswdevlkrfrgtelqnyfKKLYNGEIKVVHKPQYVDlIPKVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 83 SyalfpnmTVEQNVAfglrmqKVnadDSHKRVQEVLQLVELKDLAGRYPHQMSGGQCQRVALARSLVTRPRLLLLDEPLS 162
Cdd:PRK13409 178 G-------KVRELLK------KV---DERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190
....*....|....*....|....*....|....*
gi 545130686 163 ALDarirkhLREQIR--QIQREL--GLTTIFVTHD 193
Cdd:PRK13409 242 YLD------IRQRLNvaRLIRELaeGKYVLVVEHD 270
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
110-268 |
9.44e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 110 SHKRVQEVLQ-----LVELKDLAGRY--PHQ----MSGGQCQRVALARSL------VTrprlLLLDEPLSALDARIRKHL 172
Cdd:PRK00635 442 KSLSIEEVLQglksrLSILIDLGLPYltPERalatLSGGEQERTALAKHLgaeligIT----YILDEPSIGLHPQDTHKL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 173 REQIRQIqRELGLTTIFVTHDqEEALTMSDRIFLMNQGKIVQSGdaETLYT-APVDvfaagFIGNYNLLDADKATQLLQR 251
Cdd:PRK00635 518 INVIKKL-RDQGNTVLLVEHD-EQMISLADRIIDIGPGAGIFGG--EVLFNgSPRE-----FLAKSDSLTAKYLRQELTI 588
|
170
....*....|....*..
gi 545130686 252 PISSRIAIRPEAIELSR 268
Cdd:PRK00635 589 PIPEKRTNSLGTLTLSK 605
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
134-216 |
3.59e-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: 41.09 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 134 MSGGQCQRVALARSLVTRPR--LLLLDEPLSALDARIRKHLREQIRQIqRELGLTTIFVTHDqEEALTMSDRIFLM---- 207
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHD-EDTIRAADHVIDIgpga 215
|
90
....*....|.
gi 545130686 208 --NQGKIVQSG 216
Cdd:cd03270 216 gvHGGEIVAQG 226
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
29-251 |
8.72e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 29 GEFVTLLGPSGCGKSTLLRCIAGLTSVDSGKILLdgqdivplsPQKRHIGMVFQSYALFPNMTVEQNV-------AFGLR 101
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF---------PGNWQLAWVNQETPALPQPALEYVIdgdreyrQLEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 102 MQKVNA-DDSHKRVQ-----EVLQLVELKDLAGRYPHQM--------------SGGQCQRVALARSLVTRPRLLLLDEPL 161
Cdd:PRK10636 98 LHDANErNDGHAIATihgklDAIDAWTIRSRAASLLHGLgfsneqlerpvsdfSGGWRMRLNLAQALICRSDLLLLDEPT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 162 SALDARIRKHLREQIRQIQRelglTTIFVTHDQEEALTMSDRIFLMNQGKIVQsgdaetlYTapvdvfaagfiGNYNLLD 241
Cdd:PRK10636 178 NHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPIVDKIIHIEQQSLFE-------YT-----------GNYSSFE 235
|
250
....*....|
gi 545130686 242 ADKATQLLQR 251
Cdd:PRK10636 236 VQRATRLAQQ 245
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
70-204 |
2.14e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 70 LSPQKRHIGMVFQSYALFPNMTVEQNVAFglrMQKVNADDSHKRV-QEVLQ-----LVELKDLA------GRYPHQMSGG 137
Cdd:TIGR00630 416 LKPEALAVTVGGKSIADVSELSIREAHEF---FNQLTLTPEEKKIaEEVLKeirerLGFLIDVGldylslSRAAGTLSGG 492
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545130686 138 QCQRVALARSLVTRPR--LLLLDEPLSALDARIRKHLREQIRQIqRELGLTTIFVTHDqEEALTMSDRI 204
Cdd:TIGR00630 493 EAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD-EDTIRAADYV 559
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
19-189 |
2.62e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.25 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 19 FSDINCEVAKGefVTLL-GPSGCGKSTLLRCIA--------GLTSVDSGKILLDGQDIVPLSPQKRHIGMVFQSYALFPN 89
Cdd:pfam13476 9 FRDQTIDFSKG--LTLItGPNGSGKTTILDAIKlalygktsRLKRKSGGGFVKGDIRIGLEGKGKAYVEITFENNDGRYT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 90 MTVEqnvafglRMQKVNADDSHKRVQEVLQLVELKDLAGRYPHQmsggqcqrvaLARSLVTRPRLLLLDEplSALDARIR 169
Cdd:pfam13476 87 YAIE-------RSRELSKKKGKTKKKEILEILEIDELQQFISEL----------LKSDKIILPLLVFLGQ--EREEEFER 147
|
170 180
....*....|....*....|
gi 545130686 170 KHLREQIRQIQRELGLTTIF 189
Cdd:pfam13476 148 KEKKERLEELEKALEEKEDE 167
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
26-192 |
7.69e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 36.98 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 26 VAKGEFVTLLGPSGCGKSTLLRCIAglTSVDSGKILLDGQDIVplspqkRHIGMVFQSyalfpnmTVEQNVAFGLRMQKV 105
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDLA--AAVATGKPWLGGPRVP------EQGKVLYVS-------AEGPADELRRRLRAA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545130686 106 NADDSHKRVQEVLQLVELKDLagryPHQMSGGQC---QRVALARSL--VTRPRLLLLDePLSAL------DARIRKHLRE 174
Cdd:pfam13481 95 GADLDLPARLLFLSLVESLPL----FFLDRGGPLldaDVDALEAALeeVEDPDLVVID-PLARAlggdenSNSDVGRLVK 169
|
170
....*....|....*...
gi 545130686 175 QIRQIQRELGLTTIFVTH 192
Cdd:pfam13481 170 ALDRLARRTGATVLLVHH 187
|
|
|