|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-364 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 537.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAM 80
Cdd:COG3839 1 MASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 161 PLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVGTPAM 240
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 241 NFADGTIARVGtnvlLDCNGARWPLASSrfARLQDGQQVKAAIRPNHLQLVAEGDPtpgtlTLTGMVELVELLGAEALVT 320
Cdd:COG3839 240 NLLPGTVEGGG----VRLGGVRLPLPAA--LAAAAGGEVTLGIRPEHLRLADEGDG-----GLEATVEVVEPLGSETLVH 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1142773718 321 LDWRGQPCAALVPAPMAPAPGAVVAFRFDEEALHLFDAGTERNV 364
Cdd:COG3839 309 VRLGGQELVARVPGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-362 |
6.31e-179 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 501.68 E-value: 6.31e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAM 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 161 PLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVGTPAM 240
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 241 NFADGTIARVGTNVLLDCnGARWPLAssRFARLQDGQQVKAAIRPNHLQLVAEGdptpGTLTLTgmVELVELLGAEALVT 320
Cdd:PRK11650 241 NLLDGRVSADGAAFELAG-GIALPLG--GGYRQYAGRKLTLGIRPEHIALSSAE----GGVPLT--VDTVELLGADNLAH 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1142773718 321 LDWRGQPCAALVPAPMAPAPGAVVAFRFDEEALHLFDAGTER 362
Cdd:PRK11650 312 GRWGGQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDADTGR 353
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-358 |
3.43e-149 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 426.05 E-value: 3.43e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAM 80
Cdd:COG3842 3 MPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 161 PLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVGTpaM 240
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGE--A 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 241 NFADGTIARVGTNVlLDCNGARWPLASSrfARLQDGQQVKAAIRPNHLQLVAEGDPTpgtlTLTGMVELVELLGAEALVT 320
Cdd:COG3842 240 NLLPGTVLGDEGGG-VRTGGRTLEVPAD--AGLAAGGPVTVAIRPEDIRLSPEGPEN----GLPGTVEDVVFLGSHVRYR 312
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1142773718 321 LDW-RGQP--CAALVPAPMAPAPGAVVAFRFDEEALHLFDA 358
Cdd:COG3842 313 VRLgDGQElvVRVPNRAALPLEPGDRVGLSWDPEDVVVLPA 353
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-322 |
5.23e-132 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 383.23 E-value: 5.23e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAM 80
Cdd:PRK11000 1 MASVTLRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 161 PLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVGTPAM 240
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 241 NFADGTIARVGTN---VLLDCNGARW-PLASSrfaRLQDGQQVKAAIRPNHLQLVAEGDptpgtLTLTGMVELVELLGAE 316
Cdd:PRK11000 240 NFLPVKVTATAIEqvqVELPNRQQVWlPVEGR---GVQVGANMSLGIRPEHLLPSDIAD-----VTLEGEVQVVEQLGNE 311
|
....*.
gi 1142773718 317 ALVTLD 322
Cdd:PRK11000 312 TQIHIQ 317
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-217 |
1.90e-124 |
|
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: 358.11 E-value: 1.90e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQ 83
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 84 NYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLS 163
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 164 NLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIG 217
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-327 |
4.77e-113 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 334.04 E-value: 4.77e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVN-DLPSRERNVAMVF 82
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 83 QNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPL 162
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 163 SNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVGtpAMNF 242
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG--CVNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 243 ADGTIArvGTNVLLDcngaRWPLASSRFArlqDGQQVKAAIRPNHLQLVAEGDptpGTLTLTGMVELVELLGAEALVTL- 321
Cdd:COG1118 240 LRGRVI--GGQLEAD----GLTLPVAEPL---PDGPAVAGVRPHDIEVSREPE---GENTFPATVARVSELGPEVRVELk 307
|
....*...
gi 1142773718 322 --DWRGQP 327
Cdd:COG1118 308 leDGEGQP 315
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-290 |
5.55e-112 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 332.30 E-value: 5.55e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPaVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQ 83
Cdd:PRK09452 15 VELRGISKSFDGKE-VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 84 NYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLS 163
Cdd:PRK09452 94 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 164 NLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVGTpaMNFA 243
Cdd:PRK09452 174 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGE--INIF 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1142773718 244 DGT-IARVG-TNVLLDCNGARWPLASSRfaRLQDGQQVKAAIRPNHLQL 290
Cdd:PRK09452 252 DATvIERLDeQRVRANVEGRECNIYVNF--AVEPGQKLHVLLRPEDLRV 298
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-236 |
1.81e-111 |
|
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: 325.73 E-value: 1.81e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAvLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQ 83
Cdd:cd03300 1 IELENVSKFYGGFVA-LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 84 NYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLS 163
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 164 NLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVG 236
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-217 |
4.99e-111 |
|
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: 324.09 E-value: 4.99e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 7 KALSKHYDGGPAVLhPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQNYA 86
Cdd:cd03259 4 KGLSKTYGSVRALD-DLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQDYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 87 LYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLD 166
Cdd:cd03259 83 LFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 167 AKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIG 217
Cdd:cd03259 163 AKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-323 |
1.20e-103 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 310.39 E-value: 1.20e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 2 AQITCKALSKHYDGGPAV---LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVND-----LPS 73
Cdd:NF040933 1 VTVRVENVTKIFKKGKKEvvaLDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 74 RERNVAMVFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTP 153
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 154 AVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAG 233
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 234 FVGTpaMNFADGTiarVGTNVLLDCNGARWPLAssrfARLQDGQQVKAAIRPNHLQL-VAEGDPTPGTLTL-TGMVELVE 311
Cdd:NF040933 241 LIGD--INLLEGK---VEEEGLVDGNDLKIPLP----NPKLEAGEVIIGIRPEDIDIsESDMRLPPGFVEVgKGRVKVSS 311
|
330
....*....|..
gi 1142773718 312 LLGAEALVTLDW 323
Cdd:NF040933 312 YAGGVFRVVVSP 323
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-327 |
5.63e-101 |
|
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: 303.50 E-value: 5.63e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAM 80
Cdd:TIGR03265 2 SPYLSIDNIRKRF-GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 161 PLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVGTpaM 240
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGE--V 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 241 NF-----ADGTIARVGTnVLLDCNGarwplassrfARLQDGQQVKAAIRPNHLQLVAeGDPTPGtlTLTGMVELVELLGA 315
Cdd:TIGR03265 239 NWlpgtrGGGSRARVGG-LTLACAP----------GLAQPGASVRLAVRPEDIRVSP-AGNAAN--LLLARVEDMEFLGA 304
|
330
....*....|..
gi 1142773718 316 EALVTLDWRGQP 327
Cdd:TIGR03265 305 FYRLRLRLEGLP 316
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-236 |
1.67e-96 |
|
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: 288.08 E-value: 1.67e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAvLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQ 83
Cdd:cd03296 3 IEVRNVSKRFGDFVA-LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 84 NYALYPHMTVYDNIAFGLR----RLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFD 159
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 160 EPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVG 236
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-326 |
3.93e-92 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 280.84 E-value: 3.93e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 7 KALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQNYA 86
Cdd:PRK11432 10 KNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 87 LYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLD 166
Cdd:PRK11432 89 LFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 167 AKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVGtpamnfaDGT 246
Cdd:PRK11432 169 ANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMG-------DAN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 247 I--ARVGTNVlLDCNGARWPLASSRFARLQDGqQVKAAIRPNHLQLVAEGDPTPGTltltgMVELVELLGAEALVTLDWR 324
Cdd:PRK11432 242 IfpATLSGDY-VDIYGYRLPRPAAFAFNLPDG-ECTVGVRPEAITLSEQGEESQRC-----TIKHVAYMGPQYEVTVDWH 314
|
..
gi 1142773718 325 GQ 326
Cdd:PRK11432 315 GQ 316
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-321 |
8.02e-89 |
|
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: 271.67 E-value: 8.02e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 35 LLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRR 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 115 VRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHD 194
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 195 QLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVGTPAMnFADGTIARVGTNVLLDcNGARWPLASSRFARLQ 274
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINV-FEATVIERKSEQVVLA-GVEGRRCDIYTDVPVE 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1142773718 275 DGQQVKAAIRPNHLQLVAEgDPTPGTLTLTGMVELVELLGAEALVTL 321
Cdd:TIGR01187 239 KDQPLHVVLRPEKIVIEEE-DEANSSNAIIGHVIDITYLGMTLEVHV 284
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
20-322 |
2.27e-88 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 271.18 E-value: 2.27e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQNYALYPHMTVYDNIAF 99
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 100 GLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKR 179
Cdd:NF040840 96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 180 LHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVGTPamNFADGTIARVGTNVLLDCN 259
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFE--NIIEGVAEKGGEGTILDTG 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 260 GARWPLASSRFARlqdgqqVKAAIRPNHLQLVAEGDPTPGTLTLTGMVELVELLGAEALVTLD 322
Cdd:NF040840 254 NIKIELPEEKKGK------VRIGIRPEDITISTEKVKTSARNEFKGKVEEIEDLGPLVKLTLD 310
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
8-237 |
1.56e-86 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 262.27 E-value: 1.56e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 8 ALSKhyDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQNYAL 87
Cdd:cd03299 5 NLSK--DWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 88 YPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDA 167
Cdd:cd03299 83 FPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 168 KLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVGT 237
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGF 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-216 |
5.48e-84 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 256.55 E-value: 5.48e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHY---DGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDlPSRERn 77
Cdd:COG1116 5 APALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-PGPDR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 78 vAMVFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFL 157
Cdd:COG1116 83 -GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 158 FDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLM--RGGHIEQI 216
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEE 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-266 |
6.77e-84 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 260.02 E-value: 6.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQ 83
Cdd:PRK10851 3 IEIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 84 NYALYPHMTVYDNIAFGL----RRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFD 159
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLtvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 160 EPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVGTpa 239
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE-- 239
|
250 260
....*....|....*....|....*..
gi 1142773718 240 MNFADGTIArvGTNVLLdcNGARWPLA 266
Cdd:PRK10851 240 VNRLQGTIR--GGQFHV--GAHRWPLG 262
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-216 |
6.09e-82 |
|
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: 250.08 E-value: 6.09e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPA---VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDlPSRERnvAM 80
Cdd:cd03293 1 LEVRNVSKTYGGGGGavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-PGPDR--GY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 161 PLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLM--RGGHIEQI 216
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
9-236 |
1.84e-81 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 249.72 E-value: 1.84e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQNYALY 88
Cdd:TIGR00968 6 ISKRF-GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 89 PHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAK 168
Cdd:TIGR00968 85 KHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 169 LRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVG 236
Cdd:TIGR00968 165 VRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-236 |
2.56e-78 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 243.84 E-value: 2.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMV 81
Cdd:COG1125 2 IEFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 82 FQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDA--LLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFD 159
Cdd:COG1125 82 IQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARALAADPPILLMD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 160 EPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVG 236
Cdd:COG1125 162 EPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVG 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-314 |
7.04e-77 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 242.43 E-value: 7.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYDGGPAVlHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQNYALY 88
Cdd:PRK11607 25 LTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 89 PHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAK 168
Cdd:PRK11607 104 PHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 169 LRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVGTpaMNFADGTI- 247
Cdd:PRK11607 184 LRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVFEGVLk 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 248 ARVGTNVLLDCNGARWPLASSRFARLQDGQQVKAAIRPNHLQLvAEGDPTPGTLTLTGMVELVELLG 314
Cdd:PRK11607 262 ERQEDGLVIDSPGLVHPLKVDADASVVDNVPVHVALRPEKIML-CEEPPADGCNFAVGEVIHIAYLG 327
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-236 |
5.64e-73 |
|
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: 227.95 E-value: 5.64e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMV 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 82 FQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLD--ALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFD 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 160 EPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVG 236
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-226 |
3.85e-71 |
|
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: 222.59 E-value: 3.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMV 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 82 FQNyalyP-----HMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVF 156
Cdd:COG1122 81 FQN----PddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 157 LFDEPLSNLDAKLRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-213 |
2.44e-70 |
|
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: 220.44 E-value: 2.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPA---VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRER---- 76
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 77 --NVAMVFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPA 154
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 155 VFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMtLADRVVLMRGGHI 213
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-214 |
4.36e-70 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 219.91 E-value: 4.36e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPA---VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRER---- 76
Cdd:COG1136 5 LELRNLTKSYGTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 77 --NVAMVFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPA 154
Cdd:COG1136 85 rrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 155 VFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDqLEAMTLADRVVLMRGGHIE 214
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-217 |
1.17e-69 |
|
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: 218.32 E-value: 1.17e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 23 IDLEIaDGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVND------LPSRERNVAMVFQNYALYPHMTVYDN 96
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 97 IAFGLRRLKVPADEIdrRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGD 176
Cdd:cd03297 96 LAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1142773718 177 IKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIG 217
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-212 |
3.33e-68 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 213.20 E-value: 3.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDL----PSRERNVA 79
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedelPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 80 MVFQNYALYPHMTVYDNIAFGLrrlkvpadeidrrvrdvarilsldalldrrpramSGGQQQRAAIARAMIKTPAVFLFD 159
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 160 EPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGH 212
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-212 |
2.52e-64 |
|
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: 204.62 E-value: 2.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 7 KALSKHYDGG-PAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMVFQ 83
Cdd:cd03225 3 KNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 84 NyalyP-HM----TVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLF 158
Cdd:cd03225 83 N----PdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 159 DEPLSNLDAKLRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGH 212
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-228 |
7.05e-64 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 204.46 E-value: 7.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDlPSRE-----RNV 78
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDinklrRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 79 AMVFQNYALYPHMTVYDNIAFGLRR-LKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFL 157
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1142773718 158 FDEPLSNLDAklrtQLRGD----IKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHT 228
Cdd:COG1126 160 FDEPTSALDP----ELVGEvldvMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
15-236 |
7.96e-64 |
|
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: 208.55 E-value: 7.96e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVNDLPS-----RERNVAMVFQNYALY 88
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIdGENIMKQSPVelrevRRKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 89 PHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAK 168
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 169 LRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVG 236
Cdd:TIGR01186 164 IRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-235 |
8.22e-63 |
|
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: 202.87 E-value: 8.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE------RNVAMVFQNYALYPHMTV 93
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 94 YDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQL 173
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 174 RGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFV 235
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-222 |
2.03e-62 |
|
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: 200.59 E-value: 2.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE-----RNV 78
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 79 AMVFQNYALYPHMTVYDNIAFGLRRL-KVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFL 157
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 158 FDEPLSNLD---AKLRTQLrgdIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:COG1127 165 YDEPTAGLDpitSAVIDEL---IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-226 |
2.16e-62 |
|
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: 204.56 E-value: 2.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 23 IDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVND------LPSRERNVAMVFQNYALYPHMTVYDN 96
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRRIGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 97 IAFGLRRLKVPADEIDrrVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGD 176
Cdd:COG4148 98 LLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPY 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1142773718 177 IKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:COG4148 176 LERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-213 |
1.46e-61 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 197.97 E-value: 1.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE-----RNV 78
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 79 AMVFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLF 158
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 159 DEPLSNLDAKLRTQLRGDIKRLHRqLKTTTLYVTHDQ--LEAMtlADRVVLMRGGHI 213
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLelVDRM--PKRVLELEDGRL 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-232 |
1.56e-61 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 198.06 E-value: 1.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPavLHpIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQ 83
Cdd:COG3840 2 LRLDDLTYRYGDFP--LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 84 NYALYPHMTVYDNIAFGLR-RLKVPADEIdRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPL 162
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGLRpGLKLTAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 163 SNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELY-GQPHTVFAA 232
Cdd:COG3840 158 SALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLdGEPPPALAA 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-213 |
1.86e-61 |
|
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: 197.37 E-value: 1.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDlPSRE-----RNV 78
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNinelrQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 79 AMVFQNYALYPHMTVYDNIAFGLRR-LKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFL 157
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 158 FDEPLSNLDAKLRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-222 |
3.22e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 197.21 E-value: 3.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAVlHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVNDLPSRERNVAMVF 82
Cdd:COG1131 1 IEVRGLTKRYGDKTAL-DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlGEDVARDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 83 QNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPL 162
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 163 SNLDAKLRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:COG1131 160 SGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-228 |
3.93e-61 |
|
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: 197.72 E-value: 3.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPA---VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNV 78
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 79 AMVFQNY--ALYPHMTVYDNIAFGLRRLKVPadEIDRRVRDVARILSLD-ALLDRRPRAMSGGQQQRAAIARAMIKTPAV 155
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 156 FLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDqLEAMT-LADRVVLMRGGHIEQIGTPAELYGQPHT 228
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHD-LAVVAhLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-226 |
2.25e-60 |
|
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: 203.60 E-value: 2.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPA----VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE---- 75
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 76 -RNVAMVFQN--YALYPHMTVYDNIAFGLRRLKV-PADEIDRRVRDVARILSLDA-LLDRRPRAMSGGQQQRAAIARAMI 150
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 151 KTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDqLEAM-TLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHD-LAVVrYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-222 |
1.42e-58 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 191.04 E-value: 1.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE-----RNV 78
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 79 AMVFQNYALYPHMTVYDNIAFG-------LRRL--KVPADEIDRrVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAM 149
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGrlgrtstWRSLlgLFPPEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 150 IKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHdQLE-AMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-222 |
3.91e-58 |
|
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: 189.25 E-value: 3.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE-----RNV 78
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 79 AMVFQNYALYPHMTVYDNIAFGLR-RLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFL 157
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1142773718 158 FDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-211 |
4.74e-56 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 185.07 E-value: 4.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHYDGGPA---VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDlPSRERN 77
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 78 VamVFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFL 157
Cdd:COG4525 80 V--VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 158 FDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGG 211
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-226 |
6.67e-56 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 183.76 E-value: 6.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 7 KALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNV----AMVF 82
Cdd:PRK09493 5 KNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 83 QNYALYPHMTVYDNIAFGLRRLK-VPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEP 161
Cdd:PRK09493 84 QQFYLFPHLTALENVMFGPLRVRgASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 162 LSNLDAklrtQLRGDIKRLHRQLKT---TTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK09493 164 TSALDP----ELRHEVLKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-238 |
1.77e-55 |
|
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: 183.32 E-value: 1.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPaVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMV 81
Cdd:COG1120 2 LEAENLSVGYGGRP-VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 82 FQNYALYPHMTVYDNIAFG----LRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFL 157
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 158 FDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAE---------LYGQPHT 228
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEvltpelleeVYGVEAR 240
|
250
....*....|
gi 1142773718 229 VFAAGFVGTP 238
Cdd:COG1120 241 VIEDPVTGRP 250
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-222 |
2.32e-55 |
|
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: 182.36 E-value: 2.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGE-LVIGDAVVNDLPSRERNVAMVF 82
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSiLIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 83 QNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPL 162
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 163 SNLDAKLRTQLRGDIKRLhRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:COG4555 161 NGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-217 |
2.57e-55 |
|
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: 181.94 E-value: 2.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPA---VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLP-----SRE 75
Cdd:cd03257 2 LEVKNLSVSFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 76 RNVAMVFQNY--ALYPHMTVYDNIAFGLRRLKVP--ADEIDRRVRDVARILSLDA-LLDRRPRAMSGGQQQRAAIARAMI 150
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 151 KTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDqLEAM-TLADRVVLMRGGHIEQIG 217
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHD-LGVVaKIADRVAVMYAGKIVEEG 228
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-243 |
3.83e-55 |
|
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: 183.04 E-value: 3.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYD-GGP---AVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVN-----DLPSR 74
Cdd:TIGR04521 1 IKLKNVSYIYQpGTPfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 75 ERNVAMVFQnyalYPHM-----TVYDNIAFGLRRLKVPADEIDRRVRDVARILSLD-ALLDRRPRAMSGGQQQRAAIARA 148
Cdd:TIGR04521 81 RKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 149 MIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHT 228
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDE 236
|
250
....*....|....*
gi 1142773718 229 VFAAGFVGTPAMNFA 243
Cdd:TIGR04521 237 LEKIGLDVPEITELA 251
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-225 |
5.94e-54 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 179.55 E-value: 5.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGG-PAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGE-LVIGDAVVND--LPSRERNVA 79
Cdd:TIGR04520 1 IEVENVSFSYPESeKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKvTVDGLDTLDEenLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 80 MVFQNyalyPH-----MTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPA 154
Cdd:TIGR04520 81 MVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 155 VFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDqLEAMTLADRVVLMRGGHIEQIGTPAELYGQ 225
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHD-MEEAVLADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-239 |
6.55e-54 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 186.26 E-value: 6.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGP-AVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGL---EAITGGELVIGDAVVNDLPSRER--N 77
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALRgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 78 VAMVFQN--YALYPhMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAV 155
Cdd:COG1123 85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 156 FLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFV 235
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVPRL 243
|
....
gi 1142773718 236 GTPA 239
Cdd:COG1123 244 GAAR 247
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-239 |
1.33e-53 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 181.04 E-value: 1.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPA---VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE----- 75
Cdd:COG1135 2 IELENLSKTFPTKGGpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 76 RNVAMVFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAV 155
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 156 FLFDEPLSNLDAKlrT-----QLrgdIKRLHRQLKTTTLYVTHDqleaM----TLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:COG1135 162 LLCDEATSALDPE--TtrsilDL---LKDINRELGLTIVLITHE----MdvvrRICDRVAVLENGRIVEQGPVLDVFANP 232
|
250
....*....|...
gi 1142773718 227 HTVFAAGFVGTPA 239
Cdd:COG1135 233 QSELTRRFLPTVL 245
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-222 |
7.95e-53 |
|
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: 175.83 E-value: 7.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE-----RNV 78
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 79 AMVFQNYALYPHMTVYDNIAFG-------LRRLKVPADEIDRrvRDVARILSLDALLD---RRPRAMSGGQQQRAAIARA 148
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrstWRSLFGLFPKEEK--QRALAALERVGLLDkayQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1142773718 149 MIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHdQLE-AMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLH-QVDlAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-226 |
4.31e-52 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 177.61 E-value: 4.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 23 IDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVND------LPSRERNVAMVFQNYALYPHMTVYDN 96
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 97 IAFGLRRLKVPadeiDRRVRD--VARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLR 174
Cdd:TIGR02142 96 LRYGMKRARPS----ERRISFerVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 175 GDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-228 |
3.35e-51 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 171.73 E-value: 3.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGD------AVVNDLPSRE-- 75
Cdd:COG4161 3 IQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 76 RNVAMVFQNYALYPHMTVYDN-IAFGLRRLKVPADE-IDRRVRDVARiLSLDALLDRRPRAMSGGQQQRAAIARAMIKTP 153
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQaREKAMKLLAR-LRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1142773718 154 AVFLFDEPLSNLDAKLRTQLRGDIKRLhRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTpAELYGQPHT 228
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQT 233
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
9-211 |
4.55e-51 |
|
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: 170.51 E-value: 4.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE-----RNVAMVFQ 83
Cdd:TIGR02673 7 VSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 84 NYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLS 163
Cdd:TIGR02673 87 DFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1142773718 164 NLDAKLRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGG 211
Cdd:TIGR02673 167 NLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-228 |
9.11e-51 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 170.58 E-value: 9.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGD------AVVNDLPSRE-- 75
Cdd:PRK11124 3 IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 76 RNVAMVFQNYALYPHMTVYDN-IAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPA 154
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 155 VFLFDEPLSNLDAKLRTQLRGDIKRLhRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTpAELYGQPHT 228
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQT 233
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-213 |
3.41e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 168.07 E-value: 3.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPaVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMV 81
Cdd:COG4619 1 LELEGLSFRVGGKP-ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 82 FQNYALYPhMTVYDNIAFGLRRLKVPADEidRRVRDVARILSLDA-LLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:COG4619 80 PQEPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 161 PLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-226 |
2.48e-49 |
|
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: 166.60 E-value: 2.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGP---AVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE----- 75
Cdd:cd03258 2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 76 RNVAMVFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAV 155
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 156 FLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHdQLEAM-TLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
12-222 |
4.58e-49 |
|
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: 165.82 E-value: 4.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 12 HYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAI-----TGGELVIGDAVVNDLP----SRERNVAMVF 82
Cdd:cd03260 8 VYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDvdvlELRRRVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 83 QNYALYPhMTVYDNIAFGLR-RLKVPADEIDRRVRDVARILSLDALLDRR--PRAMSGGQQQRAAIARAMIKTPAVFLFD 159
Cdd:cd03260 88 QKPNPFP-GSIYDNVAYGLRlHGIKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 160 EPLSNLDAKLRTQLRGDIKRLHRQlkTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:cd03260 167 EPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-213 |
1.19e-47 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 162.92 E-value: 1.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 7 KALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERnvaMVFQNYA 86
Cdd:PRK11247 16 NAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---LMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 87 LYPHMTVYDNIAFGLRRlkvpadeidrRVRDVARiLSLDA--LLDRR---PRAMSGGQQQRAAIARAMIKTPAVFLFDEP 161
Cdd:PRK11247 92 LLPWKKVIDNVGLGLKG----------QWRDAAL-QALAAvgLADRAnewPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 162 LSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-223 |
3.01e-46 |
|
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: 159.00 E-value: 3.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 3 QITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELV-----IGDAVVNDLPSRERN 77
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILlegtdITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 78 VAMVFQNYALYPHMTVYDNIAFG-----------LRRLKvPADEidRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIA 146
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGrlgykptwrslLGRFS-EEDK--ERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 147 RAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELY 223
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-217 |
3.31e-46 |
|
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: 158.40 E-value: 3.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDlPSRERNVamVFQNYALYPHMTVYDNIAF 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV--VFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 100 GLRRLKVPADEIDRR--VRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDI 177
Cdd:TIGR01184 78 AVDRVLPDLSKSERRaiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1142773718 178 KRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIG 217
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-217 |
6.44e-46 |
|
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: 156.95 E-value: 6.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 24 DLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQNYALYPHMTVYDNIAFGLR- 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 103 RLKVPADEiDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHR 182
Cdd:TIGR01277 98 GLKLNAEQ-QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCS 176
|
170 180 190
....*....|....*....|....*....|....*
gi 1142773718 183 QLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIG 217
Cdd:TIGR01277 177 ERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-226 |
7.64e-46 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 157.99 E-value: 7.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHYDGgPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVN-DLPSRER--- 76
Cdd:PRK11264 1 MSAIEVKNLVKKFHG-QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtARSLSQQkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 77 ------NVAMVFQNYALYPHMTVYDNIAFGLRRLK-VPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAM 149
Cdd:PRK11264 80 irqlrqHVGFVFQNFNLFPHRTVLENIIEGPVIVKgEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 150 IKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-225 |
1.17e-45 |
|
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: 164.93 E-value: 1.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 3 QITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAM 80
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALyPHMTVYDNIAFGlrrlKVPADeiDRRVRDVARILSLDALLDRRP-----------RAMSGGQQQRAAIARAM 149
Cdd:COG4988 416 VPQNPYL-FAGTIRENLRLG----RPDAS--DEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARAL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 150 IKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQlkTTTLYVTHDqLEAMTLADRVVLMRGGHIEQIGTPAELYGQ 225
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-222 |
1.67e-45 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 166.55 E-value: 1.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDG-GPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAM 80
Cdd:COG2274 474 IELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYpHMTVYDNIAFGlrrlkvpADEIDR-RVRDVARILSLDALLDRRP-----------RAMSGGQQQRAAIARA 148
Cdd:COG2274 554 VLQDVFLF-SGTIRENITLG-------DPDATDeEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 149 MIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRqlKTTTLYVTHDqLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-222 |
2.70e-45 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 155.90 E-value: 2.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 24 DLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQNYALYPHMTVYDNIAFGLR- 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 103 RLKVPADEiDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHR 182
Cdd:PRK10771 99 GLKLNAAQ-REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1142773718 183 QLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:PRK10771 178 ERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-213 |
2.77e-45 |
|
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: 155.34 E-value: 2.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 24 DLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQNYALYPHMTVYDNIAFGLR- 102
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 103 RLKVpaDEIDR-RVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLH 181
Cdd:cd03298 98 GLKL--TAEDRqAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|..
gi 1142773718 182 RQLKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-213 |
4.16e-45 |
|
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: 153.32 E-value: 4.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAvLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVNDLPSRERNVAMVF 82
Cdd:cd03230 1 IEVRNLSKRYGKKTA-LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDIKKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 83 QNYALYPHMTVYDNIAFglrrlkvpadeidrrvrdvarilsldalldrrpramSGGQQQRAAIARAMIKTPAVFLFDEPL 162
Cdd:cd03230 80 EEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 163 SNLDAKLRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:cd03230 124 SGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
19-213 |
6.93e-45 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 154.49 E-value: 6.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVNDLPS-----RERNVAMVFQNYALYPHMT 92
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLaGKEVTNLSYSqkiilRRELIGYIFQSFNLIPHLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 93 VYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQ 172
Cdd:NF038007 100 IFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNARA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1142773718 173 LRGDIKRLHRQlKTTTLYVTHDQlEAMTLADRVVLMRGGHI 213
Cdd:NF038007 180 VLQQLKYINQK-GTTIIMVTHSD-EASTYGNRIINMKDGKL 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-213 |
1.84e-44 |
|
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: 153.33 E-value: 1.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE-----RNV 78
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 79 AMVFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLF 158
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1142773718 159 DEPLSNLDAKLRTQLRGDIKRLHrQLKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-223 |
2.66e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 155.21 E-value: 2.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVND----LPSRERNVAMVFQ--NYALYPHmTV 93
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvkLSDIRKKVGLVFQypEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 94 YDNIAFGLRRLKVPADEIDRRVRDVARI--LSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRT 171
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 172 QLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELY 223
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
9-228 |
9.61e-44 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 152.65 E-value: 9.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI------------GDAVVNDLPSRER 76
Cdd:COG4598 14 LHKSF-GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVggeeirlkpdrdGELVPADRRQLQR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 77 ---NVAMVFQNYALYPHMTVYDNIAFG-LRRLKVPADEidrrVRDVARILsLD--ALLDRR---PRAMSGGQQQRAAIAR 147
Cdd:COG4598 93 irtRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAE----AIERAEAL-LAkvGLADKRdayPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 148 AMIKTPAVFLFDEPLSNLDAklrtQLRGDIKRLHRQLKT---TTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYG 224
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDP----ELVGEVLKVMRDLAEegrTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFG 243
|
....
gi 1142773718 225 QPHT 228
Cdd:COG4598 244 NPKS 247
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-233 |
5.84e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 150.24 E-value: 5.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHYDGGPaVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRernVAM 80
Cdd:COG1121 4 MPAIELENLTVSYGGRP-VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR---IGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPH--MTVYDNIAFGLRR----LKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPA 154
Cdd:COG1121 80 VPQRAEVDWDfpITVRDVVLMGRYGrrglFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 155 VFLFDEPLSNLDAKLRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQiGTPAE---------LYGQ 225
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEvltpenlsrAYGG 237
|
....*...
gi 1142773718 226 PHTVFAAG 233
Cdd:COG1121 238 PVALLAHG 245
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-212 |
1.68e-42 |
|
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: 146.76 E-value: 1.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPA-VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAM 80
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYpHMTVYDNIafglrrlkvpadeidrrvrdvarilsldalldrrpraMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 161 PLSNLDAKLRTQLRGDIKRLHRqlKTTTLYVTHDqLEAMTLADRVVLMRGGH 212
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-222 |
3.47e-42 |
|
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: 147.27 E-value: 3.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYDGG--PAVLHpIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDA-VVNDLPSRERNVAMVFQNY 85
Cdd:cd03263 6 LTKTYKKGtkPAVDD-LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsIRTDRKAARQSLGYCPQFD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 86 ALYPHMTVYDNIAFgLRRLK-VPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSN 164
Cdd:cd03263 85 ALFDELTVREHLRF-YARLKgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 165 LDAKLRTQLRGDIKRLhrQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:cd03263 164 LDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-226 |
4.83e-42 |
|
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: 149.82 E-value: 4.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYDGGPAVLHPID---LEIADGEFIVLLGPSGCGKSTMLRMIAGLE---AITGGELVIGDAVVNDLPSRE------R 76
Cdd:COG0444 7 LKVYFPTRRGVVKAVDgvsFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKElrkirgR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 77 NVAMVFQN-Y-ALYPHMTVYDNIAFGLRR-LKVPADEIDRRVRDVARILSLD---ALLDRRPRAMSGGQQQRAAIARAMI 150
Cdd:COG0444 87 EIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQRVMIARALA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 151 KTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDqLEAM-TLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:COG0444 167 LEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHD-LGVVaEIADRVAVMYAGRIVEEGPVEELFENP 242
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-221 |
4.87e-42 |
|
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: 147.58 E-value: 4.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPA---VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRER---- 76
Cdd:COG4181 9 IELRGLTKTVGTGAGeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 77 --NVAMVFQNYALYPHMTVYDNIAfglrrlkVPAdEI--DRRVRDVARIL----SLDALLDRRPRAMSGGQQQRAAIARA 148
Cdd:COG4181 89 arHVGFVFQSFQLLPTLTALENVM-------LPL-ELagRRDARARARALlervGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 149 MIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQleamTLA---DRVVLMRGGHIEQIGTPAE 221
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDP----ALAarcDRVLRLRAGRLVEDTAATA 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-222 |
6.16e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 154.94 E-value: 6.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 12 HYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMVFQNYALYp 89
Cdd:COG1132 348 SYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 90 HMTVYDNIAFGlrRLKVPADEidrrVRDVARILSLDALLDRRP-----------RAMSGGQQQRAAIARAMIKTPAVFLF 158
Cdd:COG1132 427 SGTIRENIRYG--RPDATDEE----VEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 159 DEPLSNLDAKLRTQLRGDIKRLHRQlkTTTLYVTHdQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:COG1132 501 DEATSALDTETEALIQEALERLMKG--RTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-236 |
9.09e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 149.95 E-value: 9.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPA---VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE----- 75
Cdd:PRK11153 2 IELKNISKVFPQGGRtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 76 RNVAMVFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAV 155
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 156 FLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFV 235
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFI 241
|
.
gi 1142773718 236 G 236
Cdd:PRK11153 242 Q 242
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-234 |
1.67e-41 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 150.57 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 25 LEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGD---AVVNDLPSRE---RNVAMVFQNYALYPHMTVYDNIA 98
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREvrrKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 99 FGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIK 178
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 179 RLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGF 234
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-222 |
1.97e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 147.06 E-value: 1.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMVFQNyalyPH-----M 91
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKIGIIFQN----PDnqfigA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 92 TVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRT 171
Cdd:PRK13632 100 TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKR 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 172 QLRGDIKRLHRQLKTTTLYVTHDQLEAmTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:PRK13632 180 EIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-213 |
5.13e-41 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 145.99 E-value: 5.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHYDGG--------PAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLP 72
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 73 SRE-----RNVAMVFQNY--ALYPHMTVYDNIAFGLRRLkVPADEIDR--RVRDVARILSLDA-LLDRRPRAMSGGQQQR 142
Cdd:PRK10419 81 RAQrkafrRDIQMVFQDSisAVNPRKTVREIIREPLRHL-LSLDKAERlaRASEMLRAVDLDDsVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 143 AAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-163 |
1.05e-40 |
|
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: 141.25 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVN--DLPSRERNVAMVFQNYALYPHMTVYDNI 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTddERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 98 AFGLRRLKVPADEIDRRVRDVARILSLDALLDRR----PRAMSGGQQQRAAIARAMIKTPAVFLFDEPLS 163
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-226 |
1.09e-40 |
|
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: 144.59 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVND-------LPSRE 75
Cdd:TIGR03005 1 VRFSDVTKRF-GILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVeGEQLYHMpgrngplVPADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 76 RNVA-------MVFQNYALYPHMTVYDNIAFG-LRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIAR 147
Cdd:TIGR03005 80 KHLRqmrnkigMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 148 AMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:TIGR03005 160 ALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQP 238
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-222 |
1.46e-40 |
|
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: 143.28 E-value: 1.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAVlHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVNDLPSRERNVAMVF 82
Cdd:cd03265 1 IEVENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaGHDVVREPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 83 QNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPL 162
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 163 SNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-226 |
1.64e-40 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 143.97 E-value: 1.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVV---------NDLPSR 74
Cdd:TIGR00972 2 IEIENLNLFY-GEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFdgqdiydkkIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 75 ERNVAMVFQNYALYPhMTVYDNIAFGLRRLKV-PADEIDRRVRDVARILSL-DALLDR---RPRAMSGGQQQRAAIARAM 149
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALwDEVKDRlhdSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 150 IKTPAVFLFDEPLSNLDAKlrtqLRGDIKRLHRQLKT--TTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPI----ATGKIEELIQELKKkyTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNP 234
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
9-226 |
1.98e-40 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 146.03 E-value: 1.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYD-------GGPAVLHPID---LEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--- 75
Cdd:COG4608 13 LKKHFPvrgglfgRTVGVVKAVDgvsFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 76 --RNVAMVFQN-YA-LYPHMTVYDNIAFGLRRLKV-PADEIDRRVRDVARILSLDA-LLDRRPRAMSGGQQQRAAIARAM 149
Cdd:COG4608 93 lrRRMQMVFQDpYAsLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 150 IKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDqleamtL------ADRVVLMRGGHIEQIGTPAELY 223
Cdd:COG4608 173 ALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD------LsvvrhiSDRVAVMYLGKIVEIAPRDELY 246
|
...
gi 1142773718 224 GQP 226
Cdd:COG4608 247 ARP 249
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-222 |
3.70e-40 |
|
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: 142.19 E-value: 3.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPaVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERN---VAM 80
Cdd:cd03224 1 LEVENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHMTVYDNIAFGLRRLKvpadeIDRRVRDVARILS----LDALLDRRPRAMSGGQQQRAAIARAMIKTPAVF 156
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARR-----RAKRKARLERVYElfprLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 157 LFDEPLSNLDAKLRTQLRGDIKRLhRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-206 |
4.58e-40 |
|
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: 141.46 E-value: 4.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 2 AQITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVNDLPSRERNVAM 80
Cdd:COG4133 1 MMLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWnGEPIRDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHMTVYDNIAFGLRRLKVPADeiDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1142773718 161 PLSNLDAKLRTQLRGDIKRlHRQLKTTTLYVTHDQLEAmtLADRVV 206
Cdd:COG4133 158 PFTALDAAGVALLAELIAA-HLARGGAVLLTTHQPLEL--AAARVL 200
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-212 |
9.39e-40 |
|
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: 138.92 E-value: 9.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYDGGPaVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMVFQnya 86
Cdd:cd00267 5 LSFRYGGRT-ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 87 lyphmtvydniafglrrlkvpadeidrrvrdvarilsldalldrrpraMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLD 166
Cdd:cd00267 81 ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1142773718 167 AKLRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGH 212
Cdd:cd00267 113 PASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-211 |
3.09e-39 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 140.61 E-value: 3.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITckALSKHYDGGPAvLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDlPSRERNVam 80
Cdd:PRK11248 1 MLQIS--HLYADYGGKPA-LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 161 PLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGG 211
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-226 |
4.56e-39 |
|
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: 146.83 E-value: 4.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 2 AQITCKALSKHYDGGPA-VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNV 78
Cdd:COG4987 332 PSLELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 79 AMVFQNYALYpHMTVYDNIAFGlrrlkvpADEI-DRRVRDVARILSLDALLDRRP-----------RAMSGGQQQRAAIA 146
Cdd:COG4987 412 AVVPQRPHLF-DTTLRENLRLA-------RPDAtDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 147 RAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQlkTTTLYVTHDqLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG--RTVLLITHR-LAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-213 |
6.70e-39 |
|
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: 138.65 E-value: 6.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYD---GGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGL-EAITGGELVIGDAVVNDLPSRERNVA 79
Cdd:cd03266 2 ITADALTKRFRdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLlEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 80 MVFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFD 159
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 160 EPLSNLDAKLRTQLRGDIKRLhRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-217 |
9.40e-39 |
|
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: 137.18 E-value: 9.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 5 TCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMVF 82
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 83 QnyalyphmtvydniafglrrlkvpadeidrrvrdVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPL 162
Cdd:cd03214 80 Q----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1142773718 163 SNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIG 217
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
15-194 |
2.25e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 137.23 E-value: 2.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGL---EAITGGELVIGDAVVNDLPSRERNVAMVFQNYALYPHM 91
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlspAFSASGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 92 TVYDNIAFGLRRlKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRT 171
Cdd:COG4136 92 SVGENLAFALPP-TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180
....*....|....*....|...
gi 1142773718 172 QLRGDIKRLHRQLKTTTLYVTHD 194
Cdd:COG4136 171 QFREFVFEQIRQRGIPALLVTHD 193
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-223 |
3.64e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 138.61 E-value: 3.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMVFQNyalyPH-----MT 92
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGMVFQN----PDnqfvgAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 93 VYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQ 172
Cdd:PRK13635 99 VQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRRE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 173 LRGDIKRLHRQLKTTTLYVTHDQLEAMTlADRVVLMRGGHIEQIGTPAELY 223
Cdd:PRK13635 179 VLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-221 |
5.27e-38 |
|
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: 136.80 E-value: 5.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERN---VAMVFQNY 85
Cdd:cd03219 6 LTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRTFQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 86 ALYPHMTVYDNI----------AFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAV 155
Cdd:cd03219 85 RLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 156 FLFDEPLSNLDAKLRTQLRGDIKRLhRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAE 221
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
15-229 |
7.30e-38 |
|
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: 136.75 E-value: 7.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAIT-GGELVI-----GDAVVNDLPSRERNVAMVFQNYaLY 88
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLfgerrGGEDVWELRKRIGLVSPALQLR-FP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 89 PHMTVYDNIAFGL----RRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSN 164
Cdd:COG1119 93 RDETVLDVVLSGFfdsiGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAG 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 165 LDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHI------EQIGTPA---ELYGQPHTV 229
Cdd:COG1119 173 LDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVvaagpkEEVLTSEnlsEAFGLPVEV 246
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-221 |
1.54e-37 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 136.32 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERN---VAMVFQNY 85
Cdd:COG0411 10 LTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgIARTFQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 86 ALYPHMTVYDNIA---------------FGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMI 150
Cdd:COG0411 89 RLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 151 KTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDqLEA-MTLADRVVLMRGGhiEQI--GTPAE 221
Cdd:COG0411 169 TEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHD-MDLvMGLADRIVVLDFG--RVIaeGTPAE 239
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-225 |
2.21e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 136.40 E-value: 2.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPA--VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGL-EAITGGELVIGDAVVND-LPSRERNVA 79
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLlEAESGQIIIDGDLLTEEnVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 80 MVFQNyalyPH-----MTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPA 154
Cdd:PRK13650 85 MVFQN----PDnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 155 VFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDqLEAMTLADRVVLMRGGHIEQIGTPAELYGQ 225
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-222 |
1.71e-36 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 133.28 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMV 81
Cdd:COG4604 2 IEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 82 FQNYALYPHMTVYDNIAFGlR------RLKvpadEIDRRVRDVA-RILSLDALLDRRPRAMSGGQQQRAAIAraMI---K 151
Cdd:COG4604 81 RQENHINSRLTVRELVAFG-RfpyskgRLT----AEDREIIDEAiAYLDLEDLADRYLDELSGGQRQRAFIA--MVlaqD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 152 TPAVFLfDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:COG4604 154 TDYVLL-DEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-206 |
1.96e-36 |
|
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: 131.97 E-value: 1.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 7 KALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE-----RN-VAM 80
Cdd:TIGR03608 2 KNISKKF-GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrREkLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1142773718 161 PLSNLDAKLRTQlrgdIKRLHRQLK---TTTLYVTHDQlEAMTLADRVV 206
Cdd:TIGR03608 161 PTGSLDPKNRDE----VLDLLLELNdegKTIIIVTHDP-EVAKQADRVI 204
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-213 |
2.01e-36 |
|
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: 131.61 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDavvNDLPSRER--NVAMVFQN-- 84
Cdd:cd03226 5 ISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERrkSIGYVMQDvd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 85 YALYPHmTVYDNIAFGLRrlkvPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSN 164
Cdd:cd03226 82 YQLFTD-SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1142773718 165 LDAKLRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:cd03226 157 LDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-229 |
6.45e-36 |
|
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: 132.24 E-value: 6.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 18 AVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE-----RNVAMVFQNY--ALYPH 90
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQDSpsAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 91 MTVYDNIAFGLRRL-KVPADEIDRRVRDVARILSLDA-LLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAK 168
Cdd:TIGR02769 105 MTVRQIIGEPLRHLtSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 169 LRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHI-EQIGTpAELYGQPHTV 229
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIvEECDV-AQLLSFKHPA 245
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-226 |
3.25e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 130.91 E-value: 3.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVN------DLPSRERNVAMVFQnyalYP-HM- 91
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQ----FPeHQl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 92 ---TVYDNIAFGLRRLKVPADEIDRRVRDVARILSLD-ALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDA 167
Cdd:PRK13634 99 feeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 168 KLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-226 |
4.36e-35 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 132.31 E-value: 4.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 23 IDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVND------LPSRERNVAMVFQNYALYPHMTVYDN 96
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEKRRIGYVFQDARLFPHYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 97 IAFGLRrlKVPADEIDrrvrDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGD 176
Cdd:PRK11144 97 LRYGMA--KSMVAQFD----KIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1142773718 177 IKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK11144 171 LERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-227 |
2.16e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 127.85 E-value: 2.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAvLHPIDLEIADGEFIVLLGPSGCGKSTMLR-------MIAGLEaITG-----GELVIGDAV-VND 70
Cdd:COG1117 12 IEVRNLNVYYGDKQA-LKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR-VEGeilldGEDIYDPDVdVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 71 LpsReRNVAMVFQNYALYPhMTVYDNIAFGLRRLKV-PADEIDRRVRDvarilSLD--AL-------LDRRPRAMSGGQQ 140
Cdd:COG1117 90 L--R-RRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEE-----SLRkaALwdevkdrLKKSALGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 141 QRAAIARAMIKTPAVFLFDEPLSNLD----AKlrtqlrgdIKRLHRQLKT--TTLYVTHDQLEAMTLADRVVLMRGGHIE 214
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDpistAK--------IEELILELKKdyTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
250
....*....|...
gi 1142773718 215 QIGTPAELYGQPH 227
Cdd:COG1117 233 EFGPTEQIFTNPK 245
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-213 |
2.28e-34 |
|
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: 126.70 E-value: 2.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHY-DGGPA--VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRER---- 76
Cdd:TIGR02211 2 LKCENLGKRYqEGKLDtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 77 --NVAMVFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPA 154
Cdd:TIGR02211 82 nkKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 155 VFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDqleaMTLA---DRVVLMRGGHI 213
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHD----LELAkklDRVLEMKDGQL 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-228 |
6.47e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 126.62 E-value: 6.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVV---------------NDLPS 73
Cdd:PRK10619 11 LHKRY-GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvadkNQLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 74 RERNVAMVFQNYALYPHMTVYDNI------AFGLRRlkvpADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIAR 147
Cdd:PRK10619 90 LRTRLTMVFQHFNLWSHMTVLENVmeapiqVLGLSK----QEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 148 AMIKTPAVFLFDEPLSNLDAklrtQLRGDIKRLHRQLK---TTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYG 224
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
....
gi 1142773718 225 QPHT 228
Cdd:PRK10619 242 NPQS 245
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-225 |
7.67e-34 |
|
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: 125.81 E-value: 7.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 12 HYDG-GPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVND--LPSRERNVAMVFQNYALY 88
Cdd:cd03251 9 RYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDytLASLRRQIGLVSQDVFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 89 pHMTVYDNIAFGLRrlkvpaDEIDRRVRDVARILSLDALLDRRPRA-----------MSGGQQQRAAIARAMIKTPAVFL 157
Cdd:cd03251 89 -NDTVAENIAYGRP------GATREEVEEAARAANAHEFIMELPEGydtvigergvkLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 158 FDEPLSNLDAKLRTQLRGDIKRL--HRqlktTTLYVTHdQLEAMTLADRVVLMRGGHIEQIGTPAELYGQ 225
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLmkNR----TTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-215 |
7.92e-34 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 125.70 E-value: 7.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 6 CKALSKHYDGGPA---VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPS------RER 76
Cdd:PRK11629 8 CDNLCKRYQEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 77 NVAMVFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVF 156
Cdd:PRK11629 88 KLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 157 LFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDqleaMTLADRV---VLMRGGHIEQ 215
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHD----LQLAKRMsrqLEMRDGRLTA 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-222 |
2.30e-33 |
|
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: 124.71 E-value: 2.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHYDGGPaVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERN--- 77
Cdd:COG0410 1 MPMLEVENLHAGYGGIH-VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 78 VAMVFQNYALYPHMTVYDNIAFGLRRLKvpadEIDRRVRDVARILS----LDALLDRRPRAMSGGQQQRAAIARAMIKTP 153
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGAYARR----DRAEVRADLERVYElfprLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 154 AVFLFDEPLSNLDAKLRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-208 |
3.53e-33 |
|
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: 123.41 E-value: 3.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 6 CKALSKHYDGGPaVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRernVAMVFQNY 85
Cdd:cd03235 2 VEDLTVSYGGHP-VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR---IGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 86 AL---YPhMTVYDNIAFGLRRLKVPADEIDRRVRDVAR----ILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLF 158
Cdd:cd03235 78 SIdrdFP-ISVRDVVLMGLYGHKGLFRRLSKADKAKVDealeRVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1142773718 159 DEPLSNLDAKLRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLM 208
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
23-226 |
6.15e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 125.97 E-value: 6.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 23 IDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELV-IGDAVV--NDLPSRE--RNVAMVFQN--YALYPHMTVYD 95
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLgmKDDEWRAvrSDIQMIFQDplASLNPRMTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 96 NIAFGLR--RLKVPADEIDRRVRDV-ARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQ 172
Cdd:PRK15079 120 IIAEPLRtyHPKLSRQEVKDRVKAMmLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 173 LRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK15079 200 VVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-218 |
1.43e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 127.83 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVV---NDLPSRERNVAM 80
Cdd:COG1129 5 LEMRGISKSF-GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrSPRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHMTVYDNIAFG---LRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFL 157
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGrepRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 158 FDEPLSNLDAKlrtqlrgDIKRLH---RQLK---TTTLYVTHDQLEAMTLADRVVLMRGGHIeqIGT 218
Cdd:COG1129 164 LDEPTASLTER-------EVERLFriiRRLKaqgVAIIYISHRLDEVFEIADRVTVLRDGRL--VGT 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-226 |
1.94e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 122.64 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 13 YDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGL-----EAITGGELVI-GDAV----VNDLPSReRNVAMVF 82
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLfGRNIyspdVDPIEVR-REVGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 83 QNYALYPHMTVYDNIAFGLR--RLKVPADEIDRRVRDVARILSL-DALLDR---RPRAMSGGQQQRAAIARAMIKTPAVF 156
Cdd:PRK14267 92 QYPNPFPHLTIYDNVAIGVKlnGLVKSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 157 LFDEPLSNLDAKLRTQlrgdIKRLHRQLKT--TTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK14267 172 LMDEPTANIDPVGTAK----IEELLFELKKeyTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-228 |
3.08e-32 |
|
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: 127.49 E-value: 3.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 18 AVlHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAiTGGELVIGDAVVNDLPSRE-----RNVAMVFQN-YA-LYPH 90
Cdd:COG4172 301 AV-DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 91 MTVYDNIAFGLRRLKVPADEIDRRVRdVARILS---LD-ALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLD 166
Cdd:COG4172 379 MTVGQIIAEGLRVHGPGLSAAERRAR-VAEALEevgLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 167 AKLRTQLRGDIKRLHRQLKTTTLYVTHDqLEAM-TLADRVVLMRGGHI-EQiGTPAELYGQPHT 228
Cdd:COG4172 458 VSVQAQILDLLRDLQREHGLAYLFISHD-LAVVrALAHRVMVMKDGKVvEQ-GPTEQVFDAPQH 519
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-225 |
4.36e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 122.50 E-value: 4.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGG-----PAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPS--RER 76
Cdd:PRK13633 5 IKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 77 NVA-MVFQNyalyPH-----MTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMI 150
Cdd:PRK13633 85 NKAgMVFQN----PDnqivaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1142773718 151 KTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTlADRVVLMRGGHIEQIGTPAELYGQ 225
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
12-213 |
4.91e-32 |
|
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: 120.39 E-value: 4.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 12 HYDGGP-AVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMVFQNYALY 88
Cdd:cd03245 11 SYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGYVPQDVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 89 pHMTVYDNIAFGlrrlKVPADeiDRRVRDVARILSLDALLDRRPRAM-----------SGGQQQRAAIARAMIKTPAVFL 157
Cdd:cd03245 91 -YGTLRDNITLG----APLAD--DERILRAAELAGVTDFVNKHPNGLdlqigergrglSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 158 FDEPLSNLDAKLRTQLrgdIKRLHRQLKTTTLYV-THdQLEAMTLADRVVLMRGGHI 213
Cdd:cd03245 164 LDEPTSAMDMNSEERL---KERLRQLLGDKTLIIiTH-RPSLLDLVDRIIVMDSGRI 216
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-213 |
2.24e-31 |
|
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: 126.13 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDG-GPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAM 80
Cdd:TIGR03375 464 IEFRNVSFAYPGqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYpHMTVYDNIAFGlrrlkVPADEiDRRVRDVARILSLDALLDRRP-----------RAMSGGQQQRAAIARAM 149
Cdd:TIGR03375 544 VPQDPRLF-YGTLRDNIALG-----APYAD-DEEILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARAL 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1142773718 150 IKTPAVFLFDEPLSNLDAKLRTQLrgdIKRLHRQL-KTTTLYVTHdQLEAMTLADRVVLMRGGHI 213
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMDNRSEERF---KDRLKRWLaGKTLVLVTH-RTSLLDLVDRIIVMDNGRI 677
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-208 |
2.65e-31 |
|
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: 124.71 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 3 QITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLP--SRERNVAM 80
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADadSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHmTVYDNIAFGlrRLKVPADEIDRRVRDV-------ARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTP 153
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLA--RPDASDAEIREALERAgldefvaALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1142773718 154 AVFLFDEPLSNLDAKLRTQLRGDIKRLHRqlKTTTLYVTHDqLEAMTLADRVVLM 208
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-225 |
3.89e-31 |
|
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: 124.14 E-value: 3.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHY---DGG--PAVlHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGEL--VIGDAVVN------D 70
Cdd:TIGR03269 280 IKVRNVSKRYisvDRGvvKAV-DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvRVGDEWVDmtkpgpD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 71 LPSR-ERNVAMVFQNYALYPHMTVYDNI--AFGLrrlKVPADEIDRRVRDVARILSLD-----ALLDRRPRAMSGGQQQR 142
Cdd:TIGR03269 359 GRGRaKRYIGILHQEYDLYPHRTVLDNLteAIGL---ELPDELARMKAVITLKMVGFDeekaeEILDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 143 AAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
...
gi 1142773718 223 YGQ 225
Cdd:TIGR03269 516 VEE 518
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-194 |
4.25e-31 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 118.05 E-value: 4.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE-----RNV 78
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 79 AMVFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVrdvARILSLDALLDRR---PRAMSGGQQQRAAIARAMIKTPAV 155
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRV---SAALDKVGLLDKAknfPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1142773718 156 FLFDEPLSNLDAKLRTqlrgDIKRLHRQLK---TTTLYVTHD 194
Cdd:PRK10908 159 LLADEPTGNLDDALSE----GILRLFEEFNrvgVTVLMATHD 196
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-232 |
7.69e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.03 E-value: 7.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVND---LPSRERNVA 79
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIKYDkksLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 80 MVFQN-----YAlyPhmTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPA 154
Cdd:PRK13639 82 IVFQNpddqlFA--P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 155 VFLFDEPLSNLDAKLRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAA 232
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKA 234
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-223 |
1.08e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 118.32 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPA-VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAM 80
Cdd:PRK13648 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNyalyPH-----MTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAV 155
Cdd:PRK13648 88 VFQN----PDnqfvgSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 156 FLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTlADRVVLMRGGHIEQIGTPAELY 223
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-222 |
1.13e-30 |
|
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: 117.33 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 13 YDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLP--SRERNVAMVFQNYALYPH 90
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkSLRSMIGVVLQDTFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 91 mTVYDNIAFGlrRLKVPADEIDRrvrdVARILSLDALLDRRPRA-----------MSGGQQQRAAIARAMIKTPAVFLFD 159
Cdd:cd03254 92 -TIMENIRLG--RPNATDEEVIE----AAKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 160 EPLSNLDAKLRTQLRGDIKRLhrQLKTTTLYVTHdQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKL--MKGRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-213 |
1.25e-30 |
|
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: 116.55 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQ 83
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 84 NYALYPHMTVYDNIAFGLRRLKVPADEIDRrvrdVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLS 163
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1142773718 164 NLDAKLRTQLRgDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:cd03268 156 GLDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-223 |
1.32e-30 |
|
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: 116.87 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRER---NVAM 80
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 161 PLSNLDAKlrtqLRGDIKRLHRQLKTTTLYV---THDQLEAMTLADRVVLMRGGHIEQIGTPAELY 223
Cdd:cd03218 160 PFAGVDPI----AVQDIQKIIKILKDRGIGVlitDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-226 |
1.91e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 117.78 E-value: 1.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 14 DGGPAvLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVND---LPSRERNVAMVFQN-YALYP 89
Cdd:PRK13644 13 DGTPA-LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfskLQGIRKLVGIVFQNpETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 90 HMTVYDNIAFGLRRLKVPADEIDRRV-RDVARIlSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAK 168
Cdd:PRK13644 92 GRTVEEDLAFGPENLCLPPIEIRKRVdRALAEI-GLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 169 LRTQLRGDIKRLHRQLKtTTLYVTHDqLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK13644 171 SGIAVLERIKKLHEKGK-TIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-222 |
2.22e-30 |
|
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: 116.56 E-value: 2.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 13 YDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVN--DLPSRERNVAMVFQNYALYpH 90
Cdd:cd03253 10 YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRevTLDSLRRAIGVVPQDTVLF-N 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 91 MTVYDNIAFGlrRLKVPADEIdRRVRDVA----RILSL----DALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPL 162
Cdd:cd03253 89 DTIGYNIRYG--RPDATDEEV-IEAAKAAqihdKIMRFpdgyDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 163 SNLDAKLRTQLRGDIKRLHRqlKTTTLYVTHdQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:cd03253 166 SALDTHTEREIQAALRDVSK--GRTTIVIAH-RLSTIVNADKIIVLKDGRIVERGTHEEL 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-225 |
2.86e-30 |
|
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: 116.48 E-value: 2.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMVFQNYALYPhMTVYDN 96
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 97 IAFGLRrlkvpaDEIDRRVRDVAR-------ILSL----DALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNL 165
Cdd:cd03249 97 IRYGKP------DATDEEVEEAAKkanihdfIMSLpdgyDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 166 DAKLRTQLRGDIKRLHRqlKTTTLYVTHdQLEAMTLADRVVLMRGGHIEQIGTPAELYGQ 225
Cdd:cd03249 171 DAESEKLVQEALDRAMK--GRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-226 |
3.25e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.55 E-value: 3.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGL-----EAITGGELVIG--DAVVNDLPS 73
Cdd:PRK14247 1 MNKIEIRDLKVSF-GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDgqDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 74 RERNVAMVFQNYALYPHMTVYDNIAFGLR--RLKVPADEIDRRVRDVARILSL-DALLDR--RPRA-MSGGQQQRAAIAR 147
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFENVALGLKlnRLVKSKKELQERVRWALEKAQLwDEVKDRldAPAGkLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 148 AMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLktTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-206 |
9.44e-30 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 114.43 E-value: 9.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMVFQNYALYPHmT 92
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 93 VYDNIAFGLR-RLKVPadEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRT 171
Cdd:PRK10247 97 VYDNLIFPWQiRNQQP--DPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180 190
....*....|....*....|....*....|....*
gi 1142773718 172 QLRGDIKRLHRQLKTTTLYVTHDQLEaMTLADRVV 206
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVI 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-213 |
1.23e-29 |
|
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: 112.14 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAvLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVNDLP--SRERNVAM 80
Cdd:cd03216 1 LELRGITKRFGGVKA-LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVdGKEVSFASPrdARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQnyalyphmtvydniafglrrlkvpadeidrrvrdvarilsldalldrrpraMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:cd03216 80 VYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 161 PLSNLDAKLRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-233 |
2.22e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.83 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE-RN-VAMV 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSkVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 82 FQNyalyPH-----MTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVF 156
Cdd:PRK13647 85 FQD----PDdqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 157 LFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLyVTHDQLEAMTLADRVVLMRGGHIEQIGTPaELYGQPHTVFAAG 233
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIV-ATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDIVEQAG 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-208 |
2.27e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 112.71 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 13 YDGGPaVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAvvndlpsreRNVAMVFQNYALYPHM- 91
Cdd:NF040873 2 YGGRP-VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------ARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 92 -TVYDNIAFGL---RRLKVPADEIDRRVRDVA-RILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLD 166
Cdd:NF040873 72 lTVRDLVAMGRwarRGLWRRLTRDDRAAVDDAlERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1142773718 167 AKLRTQLRGDIKRLHRQlKTTTLYVTHDqLEAMTLADRVVLM 208
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHD-LELVRRADPCVLL 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-217 |
2.44e-29 |
|
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: 113.06 E-value: 2.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAvLHPIDLEIADGeFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVNDLPSRERNVAMVF 82
Cdd:cd03264 1 LQLENLTKRYGKKRA-LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 83 QNYALYPHMTVYDNIAFgLRRLK-VPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEP 161
Cdd:cd03264 79 QEFGVYPNFTVREFLDY-IAWLKgIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 162 LSNLDAKLRTQLRGDIKRLHRQlkTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIG 217
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-226 |
2.45e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 113.97 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHYdGGPAVLHPIDLEIADGEfIV-LLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRER--- 76
Cdd:COG1137 1 MMTLEAENLVKSY-GKRTVVKDVSLEVNQGE-IVgLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 77 ------NVAMVFQNyalyphMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMI 150
Cdd:COG1137 79 gigylpQEASIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 151 KTPAVFLFDEPLSNLD--AKlrtqlrGDIKRLHRQLKTTTLYV--T-HDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQ 225
Cdd:COG1137 153 TNPKFILLDEPFAGVDpiAV------ADIQKIIRHLKERGIGVliTdHNVRETLGICDRAYIISEGKVLAEGTPEEILNN 226
|
.
gi 1142773718 226 P 226
Cdd:COG1137 227 P 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
9-241 |
3.68e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 115.45 E-value: 3.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYD------GGPAVLHPID---LEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIG--DAVVND---LPSR 74
Cdd:PRK11308 11 LKKHYPvkrglfKPERLVKALDgvsFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQgqDLLKADpeaQKLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 75 ERNVAMVFQN-YA-LYPHMTVYDNIAFGLR-RLKVPADEIDRRVRDVARILSLDA-LLDRRPRAMSGGQQQRAAIARAMI 150
Cdd:PRK11308 91 RQKIQIVFQNpYGsLNPRKKVGQILEEPLLiNTSLSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 151 KTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP-HTV 229
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPrHPY 250
|
250
....*....|..
gi 1142773718 230 FAAGFVGTPAMN 241
Cdd:PRK11308 251 TQALLSATPRLN 262
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-223 |
4.00e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 114.46 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGP----AVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVN------DLPS 73
Cdd:PRK13649 3 INLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 74 RERNVAMVFQnyalYPHM-----TVYDNIAFGLRRLKVPADEIDRRVRDVARILSLD-ALLDRRPRAMSGGQQQRAAIAR 147
Cdd:PRK13649 83 IRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 148 AMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHrQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELY 223
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-244 |
8.06e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 113.68 E-value: 8.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE------RNVAMVFQnyalYPHM-- 91
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvrKKVGVVFQ----FPESql 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 92 ---TVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDA-LLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDA 167
Cdd:PRK13643 98 feeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 168 KLRTQLRGDIKRLHRQLKTTTLyVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYgQPHTVFAAGFVGTP-AMNFAD 244
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVL-VTHLMDDVADYADYVYLLEKGHIISCGTPSDVF-QEVDFLKAHELGVPkATHFAD 253
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-234 |
3.35e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 111.72 E-value: 3.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGL-EAITG-----GELVIGDAVVNdlpsRERNVAMVFQNY-ALYPHMT 92
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLfEEFEGkvkidGELLTAENVWN----LRRKIGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 93 VYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQ 172
Cdd:PRK13642 99 VEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 173 LRGDIKRLHRQLKTTTLYVTHDQLEAMTlADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGF 234
Cdd:PRK13642 179 IMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGL 239
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-221 |
3.41e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 111.36 E-value: 3.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMV 81
Cdd:COG4559 2 LEAENLSVRL-GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 82 FQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMI-------KTPA 154
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 155 VFLFDEPLSNLDakLRTQLRgdIKRLHRQL---KTTTLYVTHD-QLEAMtLADRVVLMRGGHIEQIGTPAE 221
Cdd:COG4559 161 WLFLDEPTSALD--LAHQHA--VLRLARQLarrGGGVVAVLHDlNLAAQ-YADRILLLHQGRLVAQGTPEE 226
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-222 |
6.77e-28 |
|
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: 109.54 E-value: 6.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 7 KALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRER---NVAMVFQ 83
Cdd:TIGR03410 4 SNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 84 NYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILslDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLS 163
Cdd:TIGR03410 83 GREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVL--KEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 164 NLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-233 |
1.47e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 110.27 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHY-DGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGL--------EAITGGELVIGDAVVNDLpsR 74
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDGITLTAKTVWDI--R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 75 ERnVAMVFQNyalyPH-----MTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAM 149
Cdd:PRK13640 84 EK-VGIVFQN----PDnqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 150 IKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAmTLADRVVLMRGGHIEQIGTPAELYGQPHTV 229
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEML 237
|
....
gi 1142773718 230 FAAG 233
Cdd:PRK13640 238 KEIG 241
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-213 |
1.62e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 108.96 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 23 IDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVvndlPSRERN-----VAMVF-QNYALYPHMTVYDN 96
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV----PWKRRKkflrrIGVVFgQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 97 IAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGD 176
Cdd:cd03267 116 FYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNF 195
|
170 180 190
....*....|....*....|....*....|....*..
gi 1142773718 177 IKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:cd03267 196 LKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-225 |
2.07e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.94 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIG----DAVVNDLPSRERNVA 79
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkpiDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 80 MVFQ--NYALYPhMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFL 157
Cdd:PRK13636 86 MVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 158 FDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQ 225
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-213 |
3.77e-27 |
|
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: 106.15 E-value: 3.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGG-PAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAM 80
Cdd:cd03246 1 LEVENVSFRYPGAePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHmTVYDNIafglrrlkvpadeidrrvrdvarilsldalldrrpraMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 161 PLSNLDAKLRTQLRGDIKRLhRQLKTTTLYVTHdQLEAMTLADRVVLMRGGHI 213
Cdd:cd03246 123 PNSHLDVEGERALNQAIAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
15-221 |
8.74e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.55 E-value: 8.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMVFQNYALYPHMT 92
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSLSFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 93 VYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMI------KTPAVFLFDEPLSNLD 166
Cdd:PRK13548 93 VEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 167 akLRTQLRgdIKRLHRQL----KTTTLYVTHD-QLEAMtLADRVVLMRGGHIEQIGTPAE 221
Cdd:PRK13548 173 --LAHQHH--VLRLARQLaherGLAVIVVLHDlNLAAR-YADRIVLLHQGRLVADGTPAE 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-211 |
2.77e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.12 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 23 IDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVnDLPS----RERNVAMVFQNYALYPHMTVYDNIA 98
Cdd:COG3845 24 VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSprdaIALGIGMVHQHFMLVPNLTVAENIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 99 FGL---RRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRG 175
Cdd:COG3845 103 LGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFE 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 1142773718 176 DIKRLhRQLKTTTLYVTHDQLEAMTLADRVVLMRGG 211
Cdd:COG3845 183 ILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-227 |
3.45e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 105.89 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGgPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIG----------DAVVNdLPS 73
Cdd:PRK14258 8 IKVNNLSFYYDT-QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGrveffnqniyERRVN-LNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 74 RERNVAMVFQNYALYPhMTVYDNIAFGLR----RLKVPADEI-DRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARA 148
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKivgwRPKLEIDDIvESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 149 MIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRG-----GHIEQIGTPAELY 223
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIF 244
|
....
gi 1142773718 224 GQPH 227
Cdd:PRK14258 245 NSPH 248
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-221 |
4.07e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.48 E-value: 4.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 3 QITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAM 80
Cdd:PRK11231 2 TLRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHMTVYDNIAFGlR--------RLkvpADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKT 152
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYG-RspwlslwgRL---SAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 153 PAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKtTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAE 221
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-222 |
7.42e-26 |
|
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: 109.42 E-value: 7.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 7 KALSKHYDG-GPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVND--LPSRERNVAMVFQ 83
Cdd:TIGR02203 334 RNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADytLASLRRQVALVSQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 84 NYALYPHmTVYDNIAFGLRRlkvpadEIDR-RVRDVARILSLDALLDRRPRA-----------MSGGQQQRAAIARAMIK 151
Cdd:TIGR02203 414 DVVLFND-TIANNIAYGRTE------QADRaEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 152 TPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQlkTTTLYVTHdQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERLMQG--RTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-235 |
7.89e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 104.74 E-value: 7.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 13 YDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVN--------DLPSRERNVAMVFQN 84
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqiDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 85 YALYPHMTVYDNIAFGLRRLKVPAD-EIDRRVRDVARILSL-DALLDR--RPRA-MSGGQQQRAAIARAMIKTPAVFLFD 159
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwKEVYDRlnSPASqLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 160 EPLSNLDAkLRTQlrgDIKRLHRQLKT--TTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFV 235
Cdd:PRK14246 179 EPTSMIDI-VNSQ---AIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-225 |
1.11e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 105.25 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVND-------LPSRERnVAMVFQnyalYPHMT 92
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyiRPVRKR-IGMVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 93 VYDN-----IAFGLRRLKVPADEidrrVRDVARILSLDA-----LLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPL 162
Cdd:PRK13646 98 LFEDtvereIIFGPKNFKMNLDE----VKNYAHRLLMDLgfsrdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 163 SNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQ 225
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-222 |
1.14e-25 |
|
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: 103.72 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 16 GPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIG--DAVVNDLPSRERNVAMVFQNYALYpHMTV 93
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDghDLALADPAWLRRQVGVVLQENVLF-NRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 94 YDNIAfglrrLKVPADEIdRRVRDVAR-------ILSL----DALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPL 162
Cdd:cd03252 93 RDNIA-----LADPGMSM-ERVIEAAKlagahdfISELpegyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 163 SNLDAKLRtqlRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:cd03252 167 SALDYESE---HAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
1.93e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.11 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNV 78
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 79 AMVFQN---YALYPhmTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAV 155
Cdd:PRK13652 81 GLVFQNpddQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 156 FLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-223 |
2.29e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 104.32 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVV-------NDLPSRERNVAMVFQ--NYALYPH 90
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkkiKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 91 mTVYDNIAFGLRRLKVPADEIDRRVRDVARILSL-DALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKL 169
Cdd:PRK13645 107 -TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 170 RTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELY 223
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-208 |
2.76e-25 |
|
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: 101.47 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 3 QITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLeaiTGGELVIGDAVVNDLPSRERN----V 78
Cdd:cd03213 8 NLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGR---RTGLGVSGEVLINGRPLDKRSfrkiI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 79 AMVFQNYALYPHMTVYDNIAFglrrlkvpadeidrrvrdVARIlsldalldrrpRAMSGGQQQRAAIARAMIKTPAVFLF 158
Cdd:cd03213 85 GYVPQDDILHPTLTVRETLMF------------------AAKL-----------RGLSGGERKRVSIALELVSNPSLLFL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 159 DEPLSNLDAKLRTQLRGDIKRLhRQLKTTTLYVTHdQL--EAMTLADRVVLM 208
Cdd:cd03213 136 DEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIH-QPssEIFELFDKLLLL 185
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-213 |
3.36e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 103.24 E-value: 3.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLP--SRERNVAMVFQNYAL--YPHMTVY 94
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPeyKRAKYIGRVFQDPMMgtAPSMTIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 95 DNIA--------FGLRRlkvpadEIDRRVRDVARI------LSLDALLDRRPRAMSGGQQQraAIARAM--IKTPAVFLF 158
Cdd:COG1101 101 ENLAlayrrgkrRGLRR------GLTKKRRELFREllatlgLGLENRLDTKVGLLSGGQRQ--ALSLLMatLTKPKLLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 159 DEPLSNLD---AKLRTQLrgdIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:COG1101 173 DEHTAALDpktAALVLEL---TEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-221 |
4.10e-25 |
|
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: 107.14 E-value: 4.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 18 AVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMVFQNYALYPHmTVYD 95
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TIAE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 96 NIAfglrRLkvpADEIDRRVRDVAR-------ILSL----DALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSN 164
Cdd:COG4618 425 NIA----RF---GDADPEKVVAAAKlagvhemILRLpdgyDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 165 LDAKLRTQLRGDIKRLhRQLKTTTLYVTHDQlEAMTLADRVVLMRGGHIEQIGTPAE 221
Cdd:COG4618 498 LDDEGEAALAAAIRAL-KARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-226 |
4.95e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.55 E-value: 4.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAvLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVN---------DLPSR 74
Cdd:PRK14239 6 LQVSDLSVYYNKKKA-LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNghniysprtDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 75 ERNVAMVFQNYALYPhMTVYDNIAFGLRRlkvpADEIDRRVRDVARILSL------DALLDR---RPRAMSGGQQQRAAI 145
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGLRL----KGIKDKQVLDEAVEKSLkgasiwDEVKDRlhdSALGLSGGQQQRVCI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 146 ARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLktTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQ 225
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMN 237
|
.
gi 1142773718 226 P 226
Cdd:PRK14239 238 P 238
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-213 |
5.01e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 104.01 E-value: 5.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 23 IDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGElvigdAVVNDL-PSRER-----NVAMVF-QNYALYPHMTVYD 95
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGE-----VRVLGYvPFKRRkefarRIGVVFgQRSQLWWDLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 96 NIAFgLRRL-KVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLR 174
Cdd:COG4586 116 SFRL-LKAIyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIR 194
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1142773718 175 GDIKRLHRQLKTTTLYVTHD--QLEAmtLADRVVLMRGGHI 213
Cdd:COG4586 195 EFLKEYNRERGTTILLTSHDmdDIEA--LCDRVIVIDHGRI 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-213 |
9.53e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 102.01 E-value: 9.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAvLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLeaITGGEL------VIGDAV------VNDL 71
Cdd:PRK09984 5 IRVEKLAKTFNQHQA-LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--ITGDKSagshieLLGRTVqregrlARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 72 PSRERNVAMVFQNYALYPHMTVYDNIAFGLR----------RLKVPADEiDRRVRDVARIlSLDALLDRRPRAMSGGQQQ 141
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcfSWFTREQK-QRALQALTRV-GMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 142 RAAIARAMIKTPAVFLFDEPLSNLDAKlRTQLRGDIKRLHRQLKTTTLYVTHDQLE-AMTLADRVVLMRGGHI 213
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPE-SARIVMDTLRDINQNDGITVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-222 |
1.34e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 101.77 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 23 IDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLpSRER------NVAMVFQNYALYPHMTVYDN 96
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAM-SRSRlytvrkRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 97 IAFGLRR-LKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRG 175
Cdd:PRK11831 105 VAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1142773718 176 DIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:PRK11831 185 LISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-211 |
1.70e-24 |
|
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: 100.05 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 7 KALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSR-------ERnva 79
Cdd:cd03269 4 ENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNrigylpeER--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 80 mvfqnyALYPHMTVYDNIAFgLRRLK-VPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLF 158
Cdd:cd03269 80 ------GLYPKMKVIDQLVY-LAQLKgLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 159 DEPLSNLDAkLRTQLrgdIKRLHRQLK---TTTLYVTHDQLEAMTLADRVVLMRGG 211
Cdd:cd03269 153 DEPFSGLDP-VNVEL---LKDVIRELAragKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-222 |
1.93e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 101.72 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSR-------ER 76
Cdd:COG4152 2 LELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigylpeER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 77 nvamvfqnyALYPHMTVYDNIAFgLRRLK-VPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAV 155
Cdd:COG4152 81 ---------GLYPKMKVGEQLVY-LARLKgLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 156 FLFDEPLSNLDAKLRTQLRGDIKRLHRQlKTTTLYVTHdQLE-AMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSH-QMElVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-217 |
3.42e-24 |
|
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: 99.53 E-value: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIgdavvndlpsRERNVAMVFQNYALYPHMTVYDNIA 98
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV----------RGRVSSLLGLGGGFNPELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 99 FGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIK 178
Cdd:cd03220 107 LNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLR 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 1142773718 179 RLHRQLKtTTLYVTHDQLEAMTLADRVVLMRGGHIEQIG 217
Cdd:cd03220 187 ELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-211 |
5.82e-24 |
|
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: 99.05 E-value: 5.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI--GDAVVnDLPS---------RERNVAMVFQNYAL 87
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWV-DLAQaspreilalRRRTIGYVSQFLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 88 YPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLD-ALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLD 166
Cdd:COG4778 105 IPRVSALDVVAEPLLERGVDREEARARARELLARLNLPeRLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1142773718 167 AKLRTQLRGDIKRLHRQlKTTTLYVTHDqLEAM-TLADRVVLMRGG 211
Cdd:COG4778 185 AANRAVVVELIEEAKAR-GTAIIGIFHD-EEVReAVADRVVDVTPF 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
9-198 |
6.75e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 98.70 E-value: 6.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYDGGP---AVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPS------RERNVA 79
Cdd:PRK10584 12 LKKSVGQGEhelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearaklRAKHVG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 80 MVFQNYALYPHMTVYDNIafglrrlKVPA---DEIDRRVRDVARIL----SLDALLDRRPRAMSGGQQQRAAIARAMIKT 152
Cdd:PRK10584 92 FVFQSFMLIPTLNALENV-------ELPAllrGESSRQSRNGAKALleqlGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1142773718 153 PAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHD-QLEA 198
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDlQLAA 211
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-226 |
7.10e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.39 E-value: 7.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 16 GPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVN-DLPSRERNVAMVFQNYALyPHMTVY 94
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRElDPESWRKHLSWVGQNPQL-PHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 95 DNIAFGlrRLKVPADEIDRRVR--DVARILS-----LDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDA 167
Cdd:PRK11174 441 DNVLLG--NPDASDEQLQQALEnaWVSEFLPllpqgLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 168 KLRTQLRGDIKRLHRQlkTTTLYVTHdQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK11174 519 HSEQLVMQALNAASRR--QTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-210 |
7.67e-24 |
|
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: 99.02 E-value: 7.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 26 EIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIgdavvnDLPSrernVAMVFQNYALYPHMTVYDniafgLRRLK 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI------ELDT----VSYKPQYIKADYEGTVRD-----LLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 106 VPADEIDRRVR-DVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQL 184
Cdd:cd03237 86 TKDFYTHPYFKtEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENN 165
|
170 180
....*....|....*....|....*.
gi 1142773718 185 KTTTLYVTHDQLEAMTLADRVVLMRG 210
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-203 |
1.21e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.09 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 7 KALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLR-------MIAGLEA---ITGGELVIGDAVVNDLPSRER 76
Cdd:PRK14243 14 ENLNVYY-GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRVegkVTFHGKNLYAPDVDPVEVRRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 77 nVAMVFQNYALYPHmTVYDNIAFGLRRL--KVPADE-IDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTP 153
Cdd:PRK14243 93 -IGMVFQKPNPFPK-SIYDNIAYGARINgyKGDMDElVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 154 AVFLFDEPLSNLD--AKLRtqlrgdIKRLHRQLKT--TTLYVTHDQLEAMTLAD 203
Cdd:PRK14243 171 EVILMDEPCSALDpiSTLR------IEELMHELKEqyTIIIVTHNMQQAARVSD 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-222 |
1.52e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 98.04 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHYDGgPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRER---N 77
Cdd:PRK10895 1 MATLTAKNLAKAYKG-RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarrG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 78 VAMVFQNYALYPHMTVYDNIAFGLR-RLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVF 156
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 157 LFDEPLSNLDAKLRTqlrgDIKRLHRQLKTTTLYV---THDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:PRK10895 160 LLDEPFAGVDPISVI----DIKRIIEHLRDSGLGVlitDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-234 |
1.93e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 98.54 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVN----DLPSRERNVAMVFQNyalyPHMTVY 94
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQD----PEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 95 -----DNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKL 169
Cdd:PRK13638 92 ytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1142773718 170 RTQLRGDIKRLHRQLKTTTLyVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGF 234
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGL 235
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-211 |
1.97e-23 |
|
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: 96.77 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 16 GPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGdavvndlpsreRNVAMVFQNyALYPHMTVYD 95
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP-----------GSIAYVSQE-PWIQNGTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 96 NIAFGLrrlkvPADEidRRVRDVARILSLDALLDRRPR-----------AMSGGQQQRAAIARAMIKTPAVFLFDEPLSN 164
Cdd:cd03250 85 NILFGK-----PFDE--ERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1142773718 165 LDAKLRTQLRGDIKRLHRQLKTTTLYVTHdQLEAMTLADRVVLMRGG 211
Cdd:cd03250 158 VDAHVGRHIFENCILGLLLNNKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
14-222 |
2.80e-23 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 101.96 E-value: 2.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 14 DGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEA-ITGGELVIGDAVVN-DLPSRERNVAMVFQNYALYPHm 91
Cdd:TIGR03797 463 PDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETpESGSVFYDGQDLAGlDVQAVRRQLGVVLQNGRLMSG- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 92 TVYDNIAFGLRrlkVPADEidrrVRDVARILSLDALLDRRPRAM-----------SGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:TIGR03797 542 SIFENIAGGAP---LTLDE----AWEAARMAGLAEDIRAMPMGMhtvisegggtlSGGQRQRLLIARALVRKPRILLFDE 614
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 161 PLSNLDAklRTQlRGDIKRLHRqLKTTTLYVTHdQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:TIGR03797 615 ATSALDN--RTQ-AIVSESLER-LKVTRIVIAH-RLSTIRNADRIYVLDAGRVVQQGTYDEL 671
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3-213 |
2.95e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 98.62 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 3 QITCKALSKHYDGGPA----VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGG------------------E 60
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 61 LVIGDAVVNDLPSRE--------RNVAMVFQ--NYALYpHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLD-ALLD 129
Cdd:PRK13651 82 KVLEKLVIQKTRFKKikkikeirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 130 RRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLyVTHDQLEAMTLADRVVLMR 209
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIIL-VTHDLDNVLEWTKRTIFFK 239
|
....
gi 1142773718 210 GGHI 213
Cdd:PRK13651 240 DGKI 243
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-221 |
6.40e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 96.30 E-value: 6.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIgdavvndlpsRERNVAMV-----FQnyalyPHMTV 93
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV----------NGRVSALLelgagFH-----PELTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 94 YDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQL 173
Cdd:COG1134 106 RENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKC 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1142773718 174 RGDIKRLHRQlKTTTLYVTHDqLEAM-TLADRVVLMRGGHIEQIGTPAE 221
Cdd:COG1134 186 LARIRELRES-GRTVIFVSHS-MGAVrRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
15-226 |
9.70e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.21 E-value: 9.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE---RNVAMVFQNYALYPHM 91
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarMGVVRTFQHVRLFREM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 92 TVYDNIAFGLRR----------LKVPA------DEIDRRVRDVARIlSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAV 155
Cdd:PRK11300 96 TVIENLLVAQHQqlktglfsglLKTPAfrraesEALDRAATWLERV-GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 156 FLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-226 |
1.03e-22 |
|
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: 99.76 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKS----TMLRMIAGLEAITGGELVIGDAVVNDLPSRE------RNVAMVFQN--YA 86
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQEpmTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 87 LYPHMTVYDNIAFGLRR-LKVPADEIDRRVRDV---ARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPL 162
Cdd:COG4172 105 LNPLHTIGKQIAEVLRLhRGLSGAAARARALELlerVGIPDPERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPT 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 163 SNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDqleaMTL----ADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:COG4172 185 TALDVTVQAQILDLLKDLQRELGMALLLITHD----LGVvrrfADRVAVMRQGEIVEQGPTAELFAAP 248
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-213 |
1.04e-22 |
|
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: 95.42 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 25 LEIADGEFIVLLGPSGCGKSTMLRMIAGLeaITGGELVIGDAVVNDLPSR----ERNVAMVFQNYALYPHMTVYDNIAFG 100
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGR--VEGGGTTSGQILFNGQPRKpdqfQKCVAYVRQDDILLPGLTVRETLTYT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 101 LR-RLKVPADEIDRRVRDVARILSLDALL---DRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGD 176
Cdd:cd03234 106 AIlRLPRKSSDAIRKKRVEDVLLRDLALTrigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVST 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 1142773718 177 IKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:cd03234 186 LSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-227 |
1.54e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.21 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVndlPSRER----NVAMVFQN 84
Cdd:PRK13536 47 VSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV---PARARlaraRIGVVPQF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 85 YALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSN 164
Cdd:PRK13536 123 DNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 165 LDAKLRTQLRGDIKRLHRQLKTTTLyVTHDQLEAMTLADRVVLMRGGHI-----------EQIGTPA-ELY-GQPH 227
Cdd:PRK13536 203 LDPHARHLIWERLRSLLARGKTILL-TTHFMEEAERLCDRLCVLEAGRKiaegrphalidEHIGCQViEIYgGDPH 277
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
14-213 |
1.96e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 99.41 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 14 DGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPS------RERNVAMVFQNYAL 87
Cdd:PRK10535 18 EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalaqlRREHFGFIFQRYHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 88 YPHMTVYDNIafglrrlKVPA-----DEIDRRVRDVARI--LSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:PRK10535 98 LSHLTAAQNV-------EVPAvyaglERKQRLLRAQELLqrLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 161 PLSNLDAKLRTQLRGDIKRLhRQLKTTTLYVTHDQLEAMTlADRVVLMRGGHI 213
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
15-222 |
2.63e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.60 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMVFQNYALYPHMT 92
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVPQDTSLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 93 VYDNIAFG----LRRLKvPADEIDRR-VRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDA 167
Cdd:PRK09536 94 VRQVVEMGrtphRSRFD-TWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1142773718 168 KLRTQLRGDIKRLHRQLKtTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:PRK09536 173 NHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-194 |
3.11e-22 |
|
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: 98.20 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 2 AQITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVA 79
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 80 MVFQNYALYpHMTVYDNIAFGlrrlkvPADEIDRRVRDVARILSLDALLDRRP-----------RAMSGGQQQRAAIARA 148
Cdd:TIGR02868 413 VCAQDAHLF-DTTVRENLRLA------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1142773718 149 MIKTPAVFLFDEPLSNLDAKLRTQLRGDIkrLHRQLKTTTLYVTHD 194
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-226 |
4.44e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 98.26 E-value: 4.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIgDAVvnDLPSRE-----RNVAMVFQNYALYPHmTV 93
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL-DGV--PLVQYDhhylhRQVALVGQEPVLFSG-SV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 94 YDNIAFGLRRlkVPADEIdrrvRDVARILSLDALLDRRPRA-----------MSGGQQQRAAIARAMIKTPAVFLFDEPL 162
Cdd:TIGR00958 572 RENIAYGLTD--TPDEEI----MAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 163 SNLDAKLRTQLRGDIKRLHRqlktTTLYVTHdQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:TIGR00958 646 SALDAECEQLLQESRSRASR----TVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-232 |
4.80e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.85 E-value: 4.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKST----MLRMIAgleaiTGGELVIGDAVVND------LPSRERnVAMVFQ--NYA 86
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNlnrrqlLPVRHR-IQVVFQdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 87 LYPHMTVYDNIAFGLR--RLKVPADEIDRRVRDVARILSLDALLDRR-PRAMSGGQQQRAAIARAMIKTPAVFLFDEPLS 163
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 164 NLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGH-IEQigtpaelyGQPHTVFAA 232
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEvVEQ--------GDCERVFAA 516
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-194 |
6.24e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 6.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIgdavvndlPSRERnVAMVFQNYALY 88
Cdd:COG0488 4 LSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--------PKGLR-IGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 89 PHMTVYDNIAFGLRRLK--------------VPADEIDRRVR---------------DVARILS----LDALLDRRPRAM 135
Cdd:COG0488 74 DDLTVLDTVLDGDAELRaleaeleeleaklaEPDEDLERLAElqeefealggweaeaRAEEILSglgfPEEDLDRPVSEL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 136 SGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAK----LRTQLrgdikrlhRQLKTTTLYVTHD 194
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDLEsiewLEEFL--------KNYPGTVLVVSHD 208
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-249 |
7.68e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 94.92 E-value: 7.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERN------------------VAM 80
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELitnpyskkiknfkelrrrVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQ--NYALYPHmTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLD-ALLDRRPRAMSGGQQQRAAIARAMIKTPAVFL 157
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 158 FDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLyVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVGT 237
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILDAKANNKTVFV-ITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHIINSTSIQVP 278
|
250
....*....|..
gi 1142773718 238 PAMNFADGTIAR 249
Cdd:PRK13631 279 RVIQVINDLIKK 290
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-229 |
1.26e-21 |
|
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: 92.43 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 21 HPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGL----EAITGGELVIGDAVVNDLPSRERNVAMVFQN--YALYPHMTVY 94
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLTCLAILGLlppgLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 95 DNIAFGLRRLKVPADEIDRRVRDVARILSLDA---LLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRT 171
Cdd:TIGR02770 83 NHAIETLRSLGKLSKQARALILEALEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 172 QLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP-HTV 229
Cdd:TIGR02770 163 RVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPkHET 221
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-222 |
1.28e-21 |
|
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: 96.81 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 12 HYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLP--SRERNVAMVFQNYALYp 89
Cdd:COG5265 366 GYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTqaSLRAAIGIVPQDTVLF- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 90 HMTVYDNIAFGlrRLKVPADEidrrVRDVARILSLDALLDRRPRAM-----------SGGQQQRAAIARAMIKTPAVFLF 158
Cdd:COG5265 445 NDTIAYNIAYG--RPDASEEE----VEAAARAAQIHDFIESLPDGYdtrvgerglklSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1142773718 159 DEPLSNLDAKLRTQLRGDIKRLHRQlkTTTLYVTHdQLEAMTLADRVVLMRGGHI-EQiGTPAEL 222
Cdd:COG5265 519 DEATSALDSRTERAIQAALREVARG--RTTLVIAH-RLSTIVDADEILVLEAGRIvER-GTHAEL 579
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-236 |
1.50e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 93.24 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVN--------DLPSRERNVAMVFQNYA 86
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGgrsifnyrDVLEFRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 87 LYPhMTVYDNIAFGLRRLK-VPADEIdrRVRDVARILSL---DALLDR---RPRAMSGGQQQRAAIARAMIKTPAVFLFD 159
Cdd:PRK14271 112 PFP-MSIMDNVLAGVRAHKlVPRKEF--RGVAQARLTEVglwDAVKDRlsdSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 160 EPLSNLDAKLRTQLRGDIKRLHRQLktTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVG 236
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVA 263
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-213 |
1.53e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 92.63 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPS----REr 76
Cdd:PRK11614 3 KVMLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakimRE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 77 NVAMVFQNYALYPHMTVYDNIAFGlrrlKVPADEIDRRVRdVARILSL-DALLDRRPR---AMSGGQQQRAAIARAMIKT 152
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMG----GFFAERDQFQER-IKWVYELfPRLHERRIQragTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 153 PAVFLFDEPLSNLDAKLRTQLRGDIKRLhRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-222 |
1.65e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.44 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEA--ITGGELVIGDAVVNDLPSRER---NVAMVFQNYALYPHMTV 93
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERaraGIFLAFQYPVEIPGVSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 94 YD--NIAFGLRRLK-VPADEIDRRVRDVARILSLDALLDRRP--RAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDA- 167
Cdd:COG0396 95 SNflRTALNARRGEeLSAREFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDId 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 168 KLRTQLRGdIKRLHRQlKTTTLYVTHDQ--LEAMTlADRVVLMRGGHIEQIGTPaEL 222
Cdd:COG0396 175 ALRIVAEG-VNKLRSP-DRGILIITHYQriLDYIK-PDFVHVLVDGRIVKSGGK-EL 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-222 |
1.85e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.93 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 16 GPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSR--ERNVAMVFQNYALYPHMTV 93
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 94 YDNIAFG-------LRRLKVpadEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLD 166
Cdd:PRK10575 103 RELVAIGrypwhgaLGRFGA---ADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 167 AKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-222 |
2.06e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.72 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 2 AQITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVNDLPSRERNVAM 80
Cdd:PRK13537 6 APIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 161 PLSNLDAKLRTQLRGDIKRLHRQLKtTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-238 |
4.07e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.97 E-value: 4.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMVFQNYALYPHMT 92
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 93 VYDNIAFG--------LRRLKVPADEIDRRVRDVArilsLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSN 164
Cdd:PRK10253 98 VQELVARGryphqplfTRWRKEDEEAVTKAMQATG----ITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 165 LDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAE---------LYGQPHTVFAAGFV 235
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEivtaelierIYGLRCMIIDDPVA 253
|
...
gi 1142773718 236 GTP 238
Cdd:PRK10253 254 GTP 256
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
17-222 |
6.49e-21 |
|
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: 94.81 E-value: 6.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 17 PAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIG--DAVVNDLPSRERNVAMVFQNYALYPHmTVY 94
Cdd:TIGR01846 470 PEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDgvDLAIADPAWLRRQMGVVLQENVLFSR-SIR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 95 DNIAFGlrRLKVPadeiDRRVRDVARILSLDALLDRRPR-----------AMSGGQQQRAAIARAMIKTPAVFLFDEPLS 163
Cdd:TIGR01846 549 DNIALC--NPGAP----FEHVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFDEATS 622
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 164 NLDAKLRTQLrgdIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:TIGR01846 623 ALDYESEALI---MRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-226 |
1.13e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 91.04 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVN------DLPSRERNVAMVFQnyalYPHM-- 91
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQ----FPEAql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 92 ---TVYDNIAFGLRRLKVPADEIDRRVRDVARILSL-DALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDA 167
Cdd:PRK13641 99 fenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 168 KLRTQLRGDIKRLHRQLKTTTLyVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGHTVIL-VTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-222 |
1.57e-20 |
|
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: 93.33 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGgPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAI--TGGELVIGDAVVN-----DLPSR-- 74
Cdd:TIGR03269 1 IEVKNLTKKFDG-KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHVALCEkcgyvERPSKvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 75 ----------------------------ERNVAMVFQ-NYALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLD 125
Cdd:TIGR03269 80 epcpvcggtlepeevdfwnlsdklrrriRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 126 ALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRV 205
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*..
gi 1142773718 206 VLMRGGHIEQIGTPAEL 222
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEV 256
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-217 |
2.11e-20 |
|
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: 87.75 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLP-SRERNVAMVFQNYALYpHMTVYDNI 97
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEkALSSLISVLNQRPYLF-DTTLRNNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 98 afGLRrlkvpadeidrrvrdvarilsldalldrrpraMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLrgdI 177
Cdd:cd03247 96 --GRR--------------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL---L 138
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1142773718 178 KRLHRQLK-TTTLYVTHdQLEAMTLADRVVLMRGGHIEQIG 217
Cdd:cd03247 139 SLIFEVLKdKTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-226 |
4.39e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 92.23 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 23 IDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE-----RNVAMVFQN-YA-LYPHMTVYD 95
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 96 NIAFGLRRLKV-PADEIDRRVrdvARILSLDALLD----RRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLR 170
Cdd:PRK10261 423 SIMEPLRVHGLlPGKAAAARV---AWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 171 TQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK10261 500 GQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-234 |
4.78e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 88.36 E-value: 4.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAiTGGELVIGDAVVNDLPSRE--RNVAMVFQNYALYPHMTVYDNI 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 98 AFGLRRlKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIK-------TPAVFLFDEPLSNLDAKLR 170
Cdd:COG4138 91 ALHQPA-GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 171 TQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYgQPH---TVFAAGF 234
Cdd:COG4138 170 AALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPEnlsEVFGVKF 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-226 |
8.25e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 88.31 E-value: 8.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 22 PIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVN--DLPSRERNVAMVFQN--YALYPHMTVYDNI 97
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDpsTSLNPRQRISQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 98 AFGLRrLKVPADEIDRRVRDVARILSLDALLDRR---PRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLR 174
Cdd:PRK15112 111 DFPLR-LNTDLEPEQREKQIIETLRQVGLLPDHAsyyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLI 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 175 GDIKRLHRQLKTTTLYVTHdQLEAMT-LADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK15112 190 NLMLELQEKQGISYIYVTQ-HLGMMKhISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-213 |
8.83e-20 |
|
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: 87.14 E-value: 8.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSR--ERNVAMVFQNYALYPHmTVYDN 96
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 97 IAFGLRrlKVPADEI---------DRRVRDVARILSLDAllDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDA 167
Cdd:cd03248 108 IAYGLQ--SCSFECVkeaaqkahaHSFISELASGYDTEV--GEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1142773718 168 KLRTQLRGDIKRLHRqlKTTTLYVTHdQLEAMTLADRVVLMRGGHI 213
Cdd:cd03248 184 ESEQQVQQALYDWPE--RRTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
9-222 |
1.12e-19 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 90.95 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLpsrERNVAMVFQNY-AL 87
Cdd:TIGR01193 479 VSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQFINYlPQ 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 88 YPHM---TVYDNIAFGLRRlKVPADEIDRRVrDVARI--------LSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVF 156
Cdd:TIGR01193 556 EPYIfsgSILENLLLGAKE-NVSQDEIWAAC-EIAEIkddienmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 157 LFDEPLSNLDAKLRTQLrgdIKRLHRQLKTTTLYVTHdQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:TIGR01193 634 ILDESTSNLDTITEKKI---VNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-214 |
1.16e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVvndlpsrerNVAMVFQ 83
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV---------KIGYFDQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 84 NYA-LYPHMTVYDNIafglRRLKVPADEIDrrVRDVarilsLDALL------DRRPRAMSGGQQQRAAIARAMIKTPAVF 156
Cdd:COG0488 386 HQEeLDPDKTVLDEL----RDGAPGGTEQE--VRGY-----LGRFLfsgddaFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 157 LFDEPLSNLDAKLRTQL-------RGdikrlhrqlktTTLYVTHDQ--LEamTLADRVVLMRGGHIE 214
Cdd:COG0488 455 LLDEPTNHLDIETLEALeealddfPG-----------TVLLVSHDRyfLD--RVATRILEFEDGGVR 508
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-196 |
1.88e-19 |
|
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: 85.49 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDL-PSRERNVAMVFQNYALYPHMTV 93
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQrDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 94 YDNIAFgLRRLKVPADeidRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQL 173
Cdd:TIGR01189 91 LENLHF-WAAIHGGAQ---RTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170 180
....*....|....*....|...
gi 1142773718 174 RGdIKRLHRQLKTTTLYVTHDQL 196
Cdd:TIGR01189 167 AG-LLRAHLARGGIVLLTTHQDL 188
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-222 |
2.40e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 90.18 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 18 AVLHpIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGE-LVIGDAVV-NDLPSRERnVAMVFQNYALYPHMTVYD 95
Cdd:NF033858 281 AVDH-VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEaWLFGQPVDaGDIATRRR-VGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 96 NIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRG 175
Cdd:NF033858 359 NLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1142773718 176 DIKRLHRQLKTTTLYVTHDQLEAMtLADRVVLMRGGHIEQIGTPAEL 222
Cdd:NF033858 439 LLIELSREDGVTIFISTHFMNEAE-RCDRISLMHAGRVLASDTPAAL 484
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-213 |
3.40e-19 |
|
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: 84.41 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 16 GPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVF------QNYALYP 89
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvpedrKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 90 HMTVYDNIAFGlrrlkvpadeidrrvrdvarilsldALLdrrpramSGGQQQRAAIARAMIKTPAVFLFDEPLSNLD--A 167
Cdd:cd03215 92 DLSVAENIALS-------------------------SLL-------SGGNQQKVVLARWLARDPRVLILDEPTRGVDvgA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1142773718 168 KLrtqlrgDIKRLHRQLK---TTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:cd03215 140 KA------EIYRLIRELAdagKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-222 |
3.76e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 89.11 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGP-AVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAM 80
Cdd:PRK11160 339 LTLNNVSFTYPDQPqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHmTVYDNIAFGLrrlkvpADEIDRRVRDVARILSLDALLDRRP----------RAMSGGQQQRAAIARAMI 150
Cdd:PRK11160 419 VSQRVHLFSA-TLRDNLLLAA------PNASDEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 151 KTPAVFLFDEPLSNLDAKLRTQlrgdIKRLHRQLKT--TTLYVTHdQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQ----ILELLAEHAQnkTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
9-213 |
4.79e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 85.75 E-value: 4.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYDGGPAvLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELV--IGDAVVNDL---PSRERNVAM--- 80
Cdd:PRK11701 12 LTKLYGPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrMRDGQLRDLyalSEAERRRLLrte 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 ---VFQNYA--LYPHMTVYDNI-----AFGLR---RLKVPADEIDRRVR-DVARIlsldallDRRPRAMSGGQQQRAAIA 146
Cdd:PRK11701 91 wgfVHQHPRdgLRMQVSAGGNIgerlmAVGARhygDIRATAGDWLERVEiDAARI-------DDLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 147 RAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-167 |
7.89e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.16 E-value: 7.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVFQNyALYPHMTVY 94
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRN-AMKPALTVA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 95 DNIAFgLRRLKvpaDEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDA 167
Cdd:PRK13539 92 ENLEF-WAAFL---GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-218 |
1.14e-18 |
|
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: 87.79 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVN--DLPSRERNVAMVFQNYALYPHmTVYDN 96
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqwDRETFGKHIGYLPQDVELFPG-TVAEN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 97 IAfglrRLKVPADeiDRRVRDVAR-------ILSL----DALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNL 165
Cdd:TIGR01842 412 IA----RFGENAD--PEKIIEAAKlagvhelILRLpdgyDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 166 DAKLRTQLRGDIKRLHRQlKTTTLYVTHdQLEAMTLADRVVLMRGGHIEQIGT 218
Cdd:TIGR01842 486 DEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGE 536
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-195 |
1.28e-18 |
|
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: 81.73 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPaVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVvndlpsrernvamvfq 83
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 84 NYALYPHmtvydniafglrrlkvpadeidrrvrdvarilsldalldrrpraMSGGQQQRAAIARAMIKTPAVFLFDEPLS 163
Cdd:cd03221 64 KIGYFEQ--------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190
....*....|....*....|....*....|..
gi 1142773718 164 NLDAKLRTQLRGDIKRLHRqlktTTLYVTHDQ 195
Cdd:cd03221 100 HLDLESIEALEEALKEYPG----TVILVSHDR 127
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-193 |
1.97e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.17 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 14 DGGPaVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELvigdavvnDLPSRERnvaMVF---QNY----- 85
Cdd:COG4178 374 DGRP-LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGAR---VLFlpqRPYlplgt 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 86 ---AL-YPHmtvydniafglrrlkvPADEI-DRRVRDVARILSLDALLDR------RPRAMSGGQQQRAAIARAMIKTPA 154
Cdd:COG4178 442 lreALlYPA----------------TAEAFsDAELREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPD 505
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1142773718 155 VFLFDEPLSNLDAKLRTQLrgdIKRLHRQLKTTTL-YVTH 193
Cdd:COG4178 506 WLFLDEATSALDEENEAAL---YQLLREELPGTTViSVGH 542
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-218 |
2.31e-18 |
|
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: 86.80 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAvLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGL--------EAITGGELVIGDAVVNdlpSRE 75
Cdd:TIGR02633 2 LEMKGIVKTFGGVKA-LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwdgEIYWSGSPLKASNIRD---TER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 76 RNVAMVFQNYALYPHMTVYDNIAFG----LRRLKVPADEIDRRVRDVARILSLDALLDRRPRA-MSGGQQQRAAIARAMI 150
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 151 KTPAVFLFDEPLSNLDAKlRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGhiEQIGT 218
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG--QHVAT 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-222 |
2.54e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.64 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPaVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDL-PSRERNVA--M 80
Cdd:PRK15439 12 LCARSISKQYSGVE-VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtPAKAHQLGiyL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHMTVYDNIAFGLRRLKVPAdeidRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPKRQASM----QKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 161 PLSNLDAKLRTQLRGDIKRLhRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:PRK15439 167 PTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-227 |
8.35e-18 |
|
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: 82.19 E-value: 8.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAVlHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-----GDAVVNDLPSRERNV 78
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGC-RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 79 AM------VFQNYALYPHMTVY--DNI-----AFGLR---RLKVPADEIDRRVR-DVARIlsldallDRRPRAMSGGQQQ 141
Cdd:TIGR02323 83 LMrtewgfVHQNPRDGLRMRVSagANIgerlmAIGARhygNIRATAQDWLEEVEiDPTRI-------DDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 142 RAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAE 221
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQ 235
|
....*.
gi 1142773718 222 LYGQPH 227
Cdd:TIGR02323 236 VLDDPQ 241
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-222 |
2.46e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.86 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 13 YDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVND--LPSRERNVAMVFQNYALYpH 90
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvtRASLRRNIAVVFQDAGLF-N 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 91 MTVYDNIAFGlrrlkvPADEIDRRVRDVA-----------RILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFD 159
Cdd:PRK13657 423 RSIEDNIRVG------RPDATDEEMRAAAeraqahdfierKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 160 EPLSNLDAKLRTQLRGDIKRLHRQlkTTTLYVTHdQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:PRK13657 497 EATSALDVETEAKVKAALDELMKG--RTTFIIAH-RLSTVRNADRILVFDNGRVVESGSFDEL 556
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-211 |
3.37e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 10 SKHYDGGPAvLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVV--NDLPSRERNVAMVFQNYA 86
Cdd:PRK11288 11 GKTFPGVKA-LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEMRfaSTTAALAAGVAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 87 LYPHMTVYDNIAFGlrRLKVPADEIDRR--VRDVARILS---LDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEP 161
Cdd:PRK11288 90 LVPEMTVAENLYLG--QLPHKGGIVNRRllNYEAREQLEhlgVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1142773718 162 LSNLDAKLRTQLRGDIKRLhRQLKTTTLYVTHDQLEAMTLADRVVLMRGG 211
Cdd:PRK11288 168 TSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-222 |
4.66e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.79 E-value: 4.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLeaITGGELVIGDAVVN----DLPSRERNVAMVFQNYALYPHMTVYD 95
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFR--SPKGVKGSGSVLLNgmpiDAKEMRAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 96 NIAFGLR-RLK--VPADEIDRRVRDVARILSLDALLD------RRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLD 166
Cdd:TIGR00955 119 HLMFQAHlRMPrrVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 167 AKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-226 |
5.80e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.60 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 17 PAVLHpIDLEIADGEFIVLLGPSGCGKS-TMLRMIAGLEAiTGGELVIGDAVvndLPSRERNV----------------- 78
Cdd:PRK10261 30 AAVRN-LSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKML---LRRRSRQVielseqsaaqmrhvrga 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 79 --AMVFQN--YALYPHMTVYDNIAFGLRRLKVPADEID----RRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMI 150
Cdd:PRK10261 105 dmAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAmveaKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 151 KTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-237 |
6.77e-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: 6.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYDG--GPAVlHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGE-LVIGDAVVNdlpsrerNVAMVFQNY 85
Cdd:TIGR01257 1943 LTKVYSGtsSPAV-DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDaTVAGKSILT-------NISDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 86 ALYPHMTVYDNIAFGLRRL-------KVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLF 158
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHLylyarlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 159 DEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLyVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQphtvFAAGFVGT 237
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIIREGRAVVL-TSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSK----FGDGYIVT 2168
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-213 |
1.26e-16 |
|
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: 77.69 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGleAITGGELVIGDAVVNDLPSRE------RNVAMVFQNYALYPHMTV 93
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN--RTEGNVSVEGDIHYNGIPYKEfaekypGEIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 94 YDNIAFglrRLKVPADEIDRRVrdvarilsldalldrrpramSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQL 173
Cdd:cd03233 101 RETLDF---ALRCKGNEFVRGI--------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1142773718 174 RGDIKRLHRQLKTTTLyVTHDQ--LEAMTLADRVVLMRGGHI 213
Cdd:cd03233 158 LKCIRTMADVLKTTTF-VSLYQasDEIYDLFDKVLVLYEGRQ 198
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
15-213 |
1.45e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.22 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVLHPIDLEIADGEfIV-LLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVndlpsRERNVA------MVF----- 82
Cdd:COG1129 263 SVGGVVRDVSFSVRAGE-ILgIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-----RIRSPRdairagIAYvpedr 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 83 QNYALYPHMTVYDNIAFG-LRRLK----VPADEIDRRVRDVARILSLDAL-LDRRPRAMSGGQQQRAAIARAMIKTPAVF 156
Cdd:COG1129 337 KGEGLVLDLSIRENITLAsLDRLSrgglLDRRRERALAEEYIKRLRIKTPsPEQPVGNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 157 LFDEPlsnldaklrTqlRG-------DIKRLHRQLK---TTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:COG1129 417 ILDEP---------T--RGidvgakaEIYRLIRELAaegKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-226 |
1.81e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 80.91 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVND--LPSRERNVAMVFQNYALYPHmTVYDN 96
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqLDSWRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 97 IAFGlrRLKVPADEIDRrvrdVARILSLDALLDRRPRA-----------MSGGQQQRAAIARAMIKTPAVFLFDEPLSNL 165
Cdd:PRK10789 409 IALG--RPDATQQEIEH----VARLASVHDDILRLPQGydtevgergvmLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 166 DAKLRTQLrgdIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK10789 483 DGRTEHQI---LHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-222 |
2.55e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 81.32 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLR-MIAGLEAITGGELVIgdavvndlpsrERNVAMVFQNYALYpHMTVYDNIA 98
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI-----------RGTVAYVPQVSWIF-NATVRDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 99 FGLrrlKVPADEIDRRVRDVARILSLDAL-------LDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRT 171
Cdd:PLN03130 701 FGS---PFDPERYERAIDVTALQHDLDLLpggdlteIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGR 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 172 QLRGdiKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:PLN03130 778 QVFD--KCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-225 |
2.68e-16 |
|
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: 76.80 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEA--ITGGELVIGDAVVNDLPSRER---NVAMVFQNYALYP 89
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERarlGIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 90 HMTVYDniaFgLRRLKVpadeidrrvrdvarilsldalldrrprAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDA-K 168
Cdd:cd03217 91 GVKNAD---F-LRYVNE---------------------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIdA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 169 LRTQLRGdIKRLHRQlKTTTLYVTHDQ--LEAMTlADRVVLMRGGHIEQIGtPAELYGQ 225
Cdd:cd03217 140 LRLVAEV-INKLREE-GKSVLIITHYQrlLDYIK-PDRVHVLYDGRIVKSG-DKELALE 194
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-210 |
5.09e-16 |
|
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: 75.30 E-value: 5.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 26 EIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGgelvigdavvndlpsrernvamvfqnyalyphmtvyDNIAFGLRRLK 105
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNG------------------------------------DNDEWDGITPV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 106 VPADEIDrrvrdvarilsldalldrrpraMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLK 185
Cdd:cd03222 65 YKPQYID----------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|....*
gi 1142773718 186 TTTLYVTHDQLEAMTLADRVVLMRG 210
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-226 |
5.35e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.05 E-value: 5.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 17 PAVLHPIDLEIADGEFIVLLGPSGCGKS----TMLRMI-AGLEAITGGELVIGDAVV-NDLpsRERNVAMVFQN--YALY 88
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQTAGRVLLDGKPVApCAL--RGRKIATIMQNprSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 89 PHMTVYDNIAFGLRRLKVPADeiDRRVRDVARILSLD---ALLDRRPRAMSGGQQQRAAIARAMIkTPAVFLF-DEPLSN 164
Cdd:PRK10418 94 PLHTMHTHARETCLALGKPAD--DATLTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIALALL-CEAPFIIaDEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 165 LDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-227 |
5.92e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.68 E-value: 5.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 13 YDG--GPAvLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVND--LPSRERNVAMVFQNYALY 88
Cdd:PRK11176 351 YPGkeVPA-LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLASLRNQVALVSQNVHLF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 89 pHMTVYDNIAFGlRRLKVPADEIDRRVRdVARILS--------LDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:PRK11176 430 -NDTIANNIAYA-RTEQYSREQIEEAAR-MAYAMDfinkmdngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDE 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 161 PLSNLDAKLRTQLRGDIKRLhrQLKTTTLYVTHdQLEAMTLADRVVLMRGGHIEQIGTPAEL------YGQPH 227
Cdd:PRK11176 507 ATSALDTESERAIQAALDEL--QKNRTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAELlaqngvYAQLH 576
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-234 |
8.71e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.79 E-value: 8.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGpAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAG---LEAITGGELVIGDAVVNDLPSRERNVAM 80
Cdd:PRK13547 2 LTADHLHVARRHR-AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltGGGAPRGARVTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPH-------MTVYDNIAFGLRRLKVPADEIDRRVRDVA-RILSL---DALLDRRPRAMSGGQQQRAAIARAM 149
Cdd:PRK13547 81 LARLRAVLPQaaqpafaFSAREIVLLGRYPHARRAGALTHRDGEIAwQALALagaTALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 150 ---------IKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPA 220
Cdd:PRK13547 161 aqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250
....*....|....
gi 1142773718 221 ELYGQPHTVFAAGF 234
Cdd:PRK13547 241 DVLTPAHIARCYGF 254
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-211 |
1.21e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 75.45 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 16 GPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAG-LEAITG----GELVIGDAVVNDLPSRER-NVAMVFQNYALYp 89
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGkvhwSNKNESEPSFEATRSRNRySVAYAAQKPWLL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 90 HMTVYDNIAFGlrrlkVPADEidRRVRDVARILSLDALLDRRPRA-----------MSGGQQQRAAIARAMIKTPAVFLF 158
Cdd:cd03290 92 NATVEENITFG-----SPFNK--QRYKAVTDACSLQPDIDLLPFGdqteigerginLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 159 DEPLSNLDAKLRTQL-RGDIKRLHRQLKTTTLYVTHdQLEAMTLADRVVLMRGG 211
Cdd:cd03290 165 DDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-225 |
1.38e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.22 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 3 QITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSR--ERNVAM 80
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHmTVYDNIAFG--LRRLKVPADEIDRRVRDVARILS--LDALLDRRPRAMSGGQQQRAAIARAMIKTPAVF 156
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTLGrdISEEQVWQALETVQLAELARSLPdgLYTPLGEQGNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 157 LFDEPLSNLDAKLRTQLRGDIKRLHRQlktTTLYVTHDQLEAMTLADRV-VLMRGGHIEQiGTPAELYGQ 225
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTIlVLHRGQAVEQ-GTHQQLLAA 564
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-226 |
1.45e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.07 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 14 DGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEA----ITGGELVIGDAVVNdLPSRERN------VAMVFQ 83
Cdd:PRK09473 26 DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangrIGGSATFNGREILN-LPEKELNklraeqISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 84 N--YALYPHMTVYDNIAFGL----RRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFL 157
Cdd:PRK09473 105 DpmTSLNPYMRVGEQLMEVLmlhkGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 158 FDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-221 |
1.90e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 78.67 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIgdavvndlpsrERNVAMVFQNyALYPHMTVYDNIA 98
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-----------ERSIAYVPQQ-AWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 99 FglrrlkvpADEID-RRVRDVARILSLDALLDRRPRAM-----------SGGQQQRAAIARAMIKTPAVFLFDEPLSNLD 166
Cdd:PTZ00243 743 F--------FDEEDaARLADAVRVSQLEADLAQLGGGLeteigekgvnlSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1142773718 167 AKLRTQLRGDIKRLHRQLKTTTLyVTHdQLEAMTLADRVVLMRGGHIEQIGTPAE 221
Cdd:PTZ00243 815 AHVGERVVEECFLGALAGKTRVL-ATH-QVHVVPRADYVVALGDGRVEFSGSSAD 867
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-179 |
2.69e-15 |
|
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: 74.07 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVNDLPSRERNVAMVFQNYALYPHMTV 93
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 94 YDNIAFglrrlkVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLD----AKL 169
Cdd:cd03231 91 LENLRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagvARF 164
|
170
....*....|
gi 1142773718 170 RTQLRGDIKR 179
Cdd:cd03231 165 AEAMAGHCAR 174
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-222 |
3.71e-15 |
|
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: 77.68 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLR-MIAGLEAITGGELVIGdavvndlpsrerNVAMVFQNyALYPHMTV 93
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHVHMKG------------SVAYVPQQ-AWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 94 YDNIAFGlRRLKVPadeidrRVRDVARILSLDALLDRRPRA-----------MSGGQQQRAAIARAMIKTPAVFLFDEPL 162
Cdd:TIGR00957 716 RENILFG-KALNEK------YYQQVLEACALLPDLEILPSGdrteigekgvnLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 163 SNLDAKLRTQLRGDIKRLHRQLKTTT-LYVTHDqLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:TIGR00957 789 SAVDAHVGKHIFEHVIGPEGVLKNKTrILVTHG-ISYLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-210 |
3.98e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.77 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 26 EIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELvigdavvndlpSRERNVAMVFQNYALYPHMTVYDNiafgLRRLK 105
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-----------DPELKISYKPQYIKPDYDGTVEDL----LRSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 106 VPAD------EIDRRvrdvariLSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKR 179
Cdd:PRK13409 426 DDLGssyyksEIIKP-------LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 498
|
170 180 190
....*....|....*....|....*....|.
gi 1142773718 180 LHRQLKTTTLYVTHDQLEAMTLADRVVLMRG 210
Cdd:PRK13409 499 IAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
16-213 |
1.38e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.95 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 16 GPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVNDLPSRERNVAMVF-----QNYALYP 89
Cdd:PRK11288 265 GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdGKPIDIRSPRDAIRAGIMLcpedrKAEGIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 90 HMTVYDNIAFGLRRLKVPADEI--DRRVRDVARiLSLDALLDRRP------RAMSGGQQQRAAIARAMIKTPAVFLFDEP 161
Cdd:PRK11288 345 VHSVADNINISARRHHLRAGCLinNRWEAENAD-RFIRSLNIKTPsreqliMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 162 LSNLDAKLRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-210 |
2.12e-14 |
|
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: 74.82 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 8 ALSKHYDG-----GPAVLHPidleiadGEFIVLLGPSGCGKSTMLRMIAGLEAITGGElVIGDAVVNDLPSRernvamVF 82
Cdd:COG1245 346 DLTKSYGGfslevEGGEIRE-------GEVLGIVGPNGIGKTTFAKILAGVLKPDEGE-VDEDLKISYKPQY------IS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 83 QNYalypHMTVYDNiafgLRrlKVPADEIDRRV--RDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:COG1245 412 PDY----DGTVEEF----LR--SANTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 161 PLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHD-QLEAMtLADRVVLMRG 210
Cdd:COG1245 482 PSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDiYLIDY-ISDRLMVFEG 531
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-223 |
2.22e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.01 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLrmiagleaitggelvigDAVVNDLPSRERNVAMVFQNYALYPHM------TV 93
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLI-----------------SAMLGELSHAETSSVVIRGSVAYVPQVswifnaTV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 94 YDNIAFGLrrlKVPADEIDRRVRDVARILSLDALLDR-------RPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLD 166
Cdd:PLN03232 696 RENILFGS---DFESERYWRAIDVTALQHDLDLLPGRdlteigeRGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 167 AKLRTQLRGDIKRLHRQLKTTTLyVThDQLEAMTLADRVVLMRGGHIEQIGTPAELY 223
Cdd:PLN03232 773 AHVAHQVFDSCMKDELKGKTRVL-VT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-211 |
5.80e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.28 E-value: 5.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLP---SRERNVAM 80
Cdd:PRK09700 6 ISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 81 VFQNYALYPHMTVYDNIAFG--LRRLKVPADEID-RRVRDVARILSLDALLDRRPRA----MSGGQQQRAAIARAMIKTP 153
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGrhLTKKVCGVNIIDwREMRVRAAMMLLRVGLKVDLDEkvanLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 154 AVFLFDEPLSNLDAKLRTQLRGDIKRLhRQLKTTTLYVTHDQLEAMTLADRVVLMRGG 211
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-195 |
5.88e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.37 E-value: 5.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAitgGELVIGDAVVNDLPsrernvamvfqnyaLYPHMTVYDNIA 98
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK---GTPVAGCVDVPDNQ--------------FGREASLIDAIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 99 fglrrlkvpadeIDRRVRDVARILSL----DA-LLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQL 173
Cdd:COG2401 108 ------------RKGDFKDAVELLNAvglsDAvLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180
....*....|....*....|..
gi 1142773718 174 RGDIKRLHRQLKTTTLYVTHDQ 195
Cdd:COG2401 176 ARNLQKLARRAGITLVVATHHY 197
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-244 |
6.74e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.38 E-value: 6.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGleAITGGELViGDAVVND-LPSRE--RNVAMVFQNYALYPHMTVYD 95
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG--RIQGNNFT-GTILANNrKPTKQilKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 96 NIAF-GLRRL--KVPADEIDRRVRDVARILSLDA-----LLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDA 167
Cdd:PLN03211 160 TLVFcSLLRLpkSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 168 KLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVfaaGFVGTPAMNFAD 244
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESV---GFSPSFPMNPAD 313
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
17-213 |
7.27e-14 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 73.07 E-value: 7.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 17 PAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVNDLPSRERNV-AMVFQNYALYPHMT-- 92
Cdd:TIGR01194 355 GFALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLdGAAVSADSRDDYRDLfSAIFADFHLFDDLIgp 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 93 ------VYDNIAFGLRRLkvpadEIDRRVrdvarilSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLD 166
Cdd:TIGR01194 435 degehaSLDNAQQYLQRL-----EIADKV-------KIEDGGFSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQD 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 167 AKLR----TQLRGDIKRLHRqlktTTLYVTHDQlEAMTLADRVVLMRGGHI 213
Cdd:TIGR01194 503 PAFKrffyEELLPDLKRQGK----TIIIISHDD-QYFELADQIIKLAAGCI 548
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-226 |
9.68e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.43 E-value: 9.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKS----TMLRMIAGLEAI-TGGE-LVIGDAVVNDLPSRERNV-----AMVFQN--Y 85
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDiRFHGESLLHASEQTLRGVrgnkiAMIFQEpmV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 86 ALYPHMTV----YDNIAF--GLRRLKVPADEID--RRV--RDVARILSldalldRRPRAMSGGQQQRAAIARAMIKTPAV 155
Cdd:PRK15134 104 SLNPLHTLekqlYEVLSLhrGMRREAARGEILNclDRVgiRQAAKRLT------DYPHQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 156 FLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQP 226
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAP 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-213 |
1.07e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 14 DGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERNVAMVF------QNYAL 87
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedrLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 88 YPHMTVYDNIAFGL-------RRLKVPADEIDRRVRDVA-----RILSLDAlldrRPRAMSGGQQQRAAIARAMIKTPAV 155
Cdd:COG3845 348 VPDMSVAENLILGRyrrppfsRGGFLDRKAIRAFAEELIeefdvRTPGPDT----PARSLSGGNQQKVILARELSRDPKL 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 156 FLFDEPLSNLDAklrtqlrGDIKRLHRQLK------TTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:COG3845 424 LIAAQPTRGLDV-------GAIEFIHQRLLelrdagAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-234 |
1.40e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 72.74 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVlHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDA-VVNDLPSRERNVAMVFQNYALYPHMTV 93
Cdd:TIGR01257 942 GRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdIETNLDAVRQSLGMCPQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 94 YDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQL 173
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 174 rGDIKRLHRQLKTTTLyVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELygqpHTVFAAGF 234
Cdd:TIGR01257 1101 -WDLLLKYRSGRTIIM-STHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTGF 1155
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-210 |
1.83e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.91 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 24 DLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVN----DLPsreRNVAMvfqnyalyphmTVYDNIA 98
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDLIVArlqqDPP---RNVEG-----------TVYDFVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 99 FGLRRL------------KVPADEIDR----------------------RVRDVARILSLDAllDRRPRAMSGGQQQRAA 144
Cdd:PRK11147 89 EGIEEQaeylkryhdishLVETDPSEKnlnelaklqeqldhhnlwqlenRINEVLAQLGLDP--DAALSSLSGGWLRKAA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 145 IARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKrlhrQLKTTTLYVTHDQLEAMTLADRVV-LMRG 210
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK----TFQGSIIFISHDRSFIRNMATRIVdLDRG 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-221 |
2.64e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.11 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITckalsKHYDGGPAvLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGL--EAITGGELVIGDAVV---NDLPSRE 75
Cdd:PRK13549 8 MKNIT-----KTFGGVKA-LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELqasNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 76 RNVAMVFQNYALYPHMTVYDNIAFG---LRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKT 152
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENIFLGneiTPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 153 PAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGhiEQIGT-PAE 221
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG--RHIGTrPAA 228
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-196 |
3.29e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.05 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVNDLPSRERNVAMVFQNYALYPHMTVYDNI 97
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 98 AFGLRrLKVPADEIDrrvrDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDI 177
Cdd:PRK13540 96 LYDIH-FSPGAVGIT----ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI 170
|
170
....*....|....*....
gi 1142773718 178 KRlHRQLKTTTLYVTHDQL 196
Cdd:PRK13540 171 QE-HRAKGGAVLLTSHQDL 188
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-194 |
3.37e-13 |
|
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: 71.12 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 2 AQI--TCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVigdavvndlPSRERNVA 79
Cdd:TIGR03719 1 AQYiyTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR---------PQPGIKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 80 MVFQNYALYPHMTVYDNIAFGLRRLKV--------------PADEIDRRVRDVARILS-LDAL----LDRR-PRAM---- 135
Cdd:TIGR03719 72 YLPQEPQLDPTKTVRENVEEGVAEIKDaldrfneisakyaePDADFDKLAAEQAELQEiIDAAdawdLDSQlEIAMdalr 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 136 -----------SGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLrgdiKRLHRQLKTTTLYVTHD 194
Cdd:TIGR03719 152 cppwdadvtklSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWL----ERHLQEYPGTVVAVTHD 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-221 |
6.76e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.04 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLeaITG-GELVIGDAVVNDLPSRE--RNVAMVFQNYALYPHMTVYDN 96
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL--LPGsGSIQFAGQPLEAWSAAElaRHRAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 97 IAFGLRRlKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIAramiktpAVFL--------------FDEPL 162
Cdd:PRK03695 90 LTLHQPD-KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLA-------AVVLqvwpdinpagqlllLDEPM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 163 SNLDAKLRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAE 221
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-226 |
7.11e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.00 E-value: 7.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHYDGGPAVLHPID---LEIADGEFIVLLGPSGCGKSTMLRMIAGL----EAITGGELVIGDAVVNDLPS 73
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 74 RER------NVAMVFQN--YALYPHMTVYDNIafgLRRLKVP--ADEIDRRVRDVaRILSLDAL------LDRRPRAMSG 137
Cdd:PRK11022 81 KERrnlvgaEVAMIFQDpmTSLNPCYTVGFQI---MEAIKVHqgGNKKTRRQRAI-DLLNQVGIpdpasrLDVYPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 138 GQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIG 217
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
....*....
gi 1142773718 218 TPAELYGQP 226
Cdd:PRK11022 237 KAHDIFRAP 245
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-257 |
8.11e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.84 E-value: 8.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 29 DGEFIVLLGPSGCGKSTMLRMIAGleaitggELV--IGDavVNDLPSRErNVAMVFQNYALYPHMT-VYDN--------- 96
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSG-------ELIpnLGD--YEEEPSWD-EVLKRFRGTELQNYFKkLYNGeikvvhkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 97 -IAFGLRRLKVPADEIDRRV------RDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKL 169
Cdd:PRK13409 168 yVDLIPKVFKGKVRELLKKVdergklDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 170 RTQLRGDIKRLHRqlKTTTLYVTHDQLEAMTLADRVvlmrggHIeqigtpaeLYGQPHtvfAAGFVGTPAmnfadGTiaR 249
Cdd:PRK13409 248 RLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNV------HI--------AYGEPG---AYGVVSKPK-----GV--R 301
|
....*...
gi 1142773718 250 VGTNVLLD 257
Cdd:PRK13409 302 VGINEYLK 309
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-213 |
8.38e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.14 E-value: 8.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 18 AVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLeaiTGGELVIGDAVV-------NDLPSRER-NVAMVFQNYALYP 89
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASN---TDGFHIGVEGVItydgitpEEIKKHYRgDVVYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 90 HMTVYDNIAFGLrRLKVPADEID--------RRVRDV-ARILSLDALLDRRP-----RAMSGGQQQRAAIARAMIKTPAV 155
Cdd:TIGR00956 152 HLTVGETLDFAA-RCKTPQNRPDgvsreeyaKHIADVyMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 156 FLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLyVTHDQL--EAMTLADRVVLMRGGHI 213
Cdd:TIGR00956 231 QCWDNATRGLDSATALEFIRALKTSANILDTTPL-VAIYQCsqDAYELFDKVIVLYEGYQ 289
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-219 |
1.04e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.45 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVvndlpsrerNVAMVFQNYALYPHM--T 92
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL---------RIGYVPQKLYLDTTLplT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 93 VYdniAFGLRRLKVPADEIDRRVRDVarilSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQ 172
Cdd:PRK09544 86 VN---RFLRLRPGTKKEDILPALKRV----QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1142773718 173 LRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRvVLMRGGHIEQIGTP 219
Cdd:PRK09544 159 LYDLIDQLRRELDCAVLMVSHDLHLVMAKTDE-VLCLNHHICCSGTP 204
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-210 |
1.36e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.41 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 18 AVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIgDAVVNDLPSRERNVAMVFQNYALYPHMTVYDNI 97
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATRGDRSRFMAYLGHLPGLKADLSTLENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 98 AF-----GLRRLKVPADEIdrrvrdvaRILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTq 172
Cdd:PRK13543 104 HFlcglhGRRAKQMPGSAL--------AIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGIT- 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1142773718 173 LRGDIKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRG 210
Cdd:PRK13543 175 LVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLEA 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-210 |
1.70e-12 |
|
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: 68.66 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 30 GEFIVLLGPSGCGKSTMLRMIAGleaitggELV--IGDavVNDLPSRERnVAMVFQNYALYPHMT-VYDN---------- 96
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSG-------ELKpnLGD--YDEEPSWDE-VLKRFRGTELQDYFKkLANGeikvahkpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 97 IAFGLRRLKVPADEI----DRR--VRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLR 170
Cdd:COG1245 169 VDLIPKVFKGTVRELlekvDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQR 248
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1142773718 171 TQLRGDIKRLHRQLKtTTLYVTHDqLEAM-TLADRVVLMRG 210
Cdd:COG1245 249 LNVARLIRELAEEGK-YVLVVEHD-LAILdYLADYVHILYG 287
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-193 |
1.88e-12 |
|
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: 64.87 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIgdavvndlPSRErNVAMVFQ 83
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--------PEGE-DLLFLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 84 NyalyPHMTVydniafG-LRrlkvpadeidrrvrdvarilslDALLdrRP--RAMSGGQQQRAAIARAMIKTPAVFLFDE 160
Cdd:cd03223 72 R----PYLPL------GtLR----------------------EQLI--YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|...
gi 1142773718 161 PLSNLDAKLRTQLRgdikRLHRQLKTTTLYVTH 193
Cdd:cd03223 118 ATSALDEESEDRLY----QLLKELGITVISVGH 146
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-257 |
3.39e-12 |
|
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: 65.85 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 28 ADGEFIVLLGPSGCGKSTMLRMIAG------------------LEAITGGELVIgdaVVNDLPSRERNVAMVFQNYALYP 89
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdwdeiLDEFRGSELQN---YFTKLLEGDVKVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 90 HmTVYDNIAFGLRRlkvpADEIDRrVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKL 169
Cdd:cd03236 101 K-AVKGKVGELLKK----KDERGK-LDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 170 RTQLRGDIKRLHRQLKtTTLYVTHDQLEAMTLADRVvlmrggHIeqigtpaeLYGQPHtvfAAGFVGTPAmnfadGTiaR 249
Cdd:cd03236 175 RLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYI------HC--------LYGEPG---AYGVVTLPK-----SV--R 229
|
....*...
gi 1142773718 250 VGTNVLLD 257
Cdd:cd03236 230 EGINEFLD 237
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
59-222 |
1.01e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 59 GELVIGDAVVNDLPSRE-RNVAMVFQNYALYPHMTVYDNIAFGlrrlkvPADEIDRRVRDVARILSLDALLDRRP----- 132
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLPnkydt 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 133 ------RAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHdQLEAMTLADRVV 206
Cdd:PTZ00265 1351 nvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIV 1429
|
170 180
....*....|....*....|.
gi 1142773718 207 LMR-----GGHIEQIGTPAEL 222
Cdd:PTZ00265 1430 VFNnpdrtGSFVQAHGTHEEL 1450
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-211 |
1.88e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 9 LSKHYDGGPAvLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE---RNVAMVFQNY 85
Cdd:PRK10982 4 ISKSFPGVKA-LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaleNGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 86 ALYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILS-LDALLDRRPRA--MSGGQQQRAAIARAMIKTPAVFLFDEPL 162
Cdd:PRK10982 83 NLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDeLDIDIDPRAKVatLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1142773718 163 SNLDAKLRTQLRGDIKRLhRQLKTTTLYVTHDQLEAMTLADRVVLMRGG 211
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-225 |
2.81e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 65.32 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 16 GPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGleaitggELVIGDAVVNdlpsRERNVAMVFQNYALYPHmTVYD 95
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG-------ELEPSEGKIK----HSGRISFSPQTSWIMPG-TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 96 NIAFGLRRlkvpaDEIdrRVRDVARILSLDALLDRRPR-----------AMSGGQQQRAAIARAMIKTPAVFLFDEPLSN 164
Cdd:TIGR01271 506 NIIFGLSY-----DEY--RYTSVIKACQLEEDIALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 165 LDAKLRTQLRGDIkrLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQ 225
Cdd:TIGR01271 579 LDVVTEKEIFESC--LCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-211 |
3.02e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.52 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 30 GEFIVLLGPSGCGKSTMLRMIAglEAITGGELVIGDAVVNDLP---SRERNVAMVFQNYALYPHMTVYDNIAFG--LRRL 104
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGRPldsSFQRSIGYVQQQDLHLPTSTVRESLRFSayLRQP 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 105 K-VPADEIDRRVRDVARILSL----DALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLF-DEPLSNLDAklrtQLRGDIK 178
Cdd:TIGR00956 867 KsVSKSEKMEYVEEVIKLLEMesyaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDS----QTAWSIC 942
|
170 180 190
....*....|....*....|....*....|....*...
gi 1142773718 179 RLHRQLKTT--TLYVTHDQLEAMTLA--DRVVLM-RGG 211
Cdd:TIGR00956 943 KLMRKLADHgqAILCTIHQPSAILFEefDRLLLLqKGG 980
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
11-219 |
4.37e-11 |
|
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: 62.13 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 11 KHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTM----LRMIagleAITGGELVIGDAVVNDLPSRE--RNVAMVFQN 84
Cdd:cd03244 11 RYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHDlrSRISIIPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 85 YALYPHmTVYDNIA-FGlrrlKVPADEIDRRVRDV-------ARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVF 156
Cdd:cd03244 87 PVLFSG-TIRSNLDpFG----EYSDEELWQALERVglkefveSLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 157 LFDEPLSNLD--------AKLRTQLRGdikrlhrqlkTTTLYVTHdQLEAMTLADRVVLMRGGHIEQIGTP 219
Cdd:cd03244 162 VLDEATASVDpetdaliqKTIREAFKD----------CTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-222 |
5.66e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.38 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYdGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGEL-VIGDAVVNdlpSRERN----- 77
Cdd:NF033858 2 ARLEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGDMAD---ARHRRavcpr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 78 VAMVFQ----NyaLYPHMTVYDNIAFGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTP 153
Cdd:NF033858 78 IAYMPQglgkN--LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 154 AVFLFDEPLSNLDAKLRTQ---LRGDIKRLHRQLktTTLYVTHDQLEAMTLaDRVVLMRGGHIEQIGTPAEL 222
Cdd:NF033858 156 DLLILDEPTTGVDPLSRRQfweLIDRIRAERPGM--SVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-173 |
7.42e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 61.04 E-value: 7.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 37 GPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPsrERNVAMVFQNYALYPHMTVYDNIAFGlrrlkvpaDEIDRRVR 116
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--KPYCTYIGHNLGLKLEMTVFENLKFW--------SEIYNSAE 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 117 DV-ARI--LSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQL 173
Cdd:PRK13541 103 TLyAAIhyFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-230 |
8.43e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.84 E-value: 8.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 15 GGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVND--LPSRERNVAMVFQNYALYPHMT 92
Cdd:PLN03232 1247 GLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFSGTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 93 VYDNIAFGLRRLKVPADEIDR-RVRDVAR--ILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKL 169
Cdd:PLN03232 1327 RFNIDPFSEHNDADLWEALERaHIKDVIDrnPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 170 RTQLRGDIKrlhRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVF 230
Cdd:PLN03232 1407 DSLIQRTIR---EEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
33-166 |
1.79e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.65 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 33 IV-LLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVndlpsrernVAMVFQNY-ALYPHMTVYDNIAFGLRRLKVPADE 110
Cdd:TIGR03719 350 IVgVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK---------LAYVDQSRdALDPNKTVWEEISGGLDIIKLGKRE 420
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 111 IDRRVRdVARILSLDALLDRRPRAMSGGQQQRAAIARaMIKTPA-VFLFDEPLSNLD 166
Cdd:TIGR03719 421 IPSRAY-VGRFNFKGSDQQKKVGQLSGGERNRVHLAK-TLKSGGnVLLLDEPTNDLD 475
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
23-227 |
2.46e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.36 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 23 IDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEA----ITGGELVIGDAVVNDLPSRER------NVAMVFQ--NYALYPH 90
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERrklvghNVSMIFQepQSCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 91 MTVYDNIA---------------FGLRRLKvpADEIDRRVRdvarILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAV 155
Cdd:PRK15093 106 ERVGRQLMqnipgwtykgrwwqrFGWRKRR--AIELLHRVG----IKDHKDAMRSFPYELTEGECQKVMIAIALANQPRL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 156 FLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDqLEAMT-LADRVVLMRGGHIEQIGTPAELYGQPH 227
Cdd:PRK15093 180 LIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHD-LQMLSqWADKINVLYCGQTVETAPSKELVTTPH 251
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-210 |
3.34e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.28 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 2 AQITCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDlPSRERNVAMV 81
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 82 FQNYAL---YPhMTVYDNIAFG-------LRRLKvpadEIDRRVRDVAriLSLDALLDRRPRA---MSGGQQQRAAIARA 148
Cdd:PRK15056 84 PQSEEVdwsFP-VLVEDVVMMGryghmgwLRRAK----KRDRQIVTAA--LARVDMVEFRHRQigeLSGGQKKRVFLARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1142773718 149 MIKTPAVFLFDEPLSNLDAKlrTQLRgdIKRLHRQLK---TTTLYVTHDQLEAMTLADRVVLMRG 210
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVK--TEAR--IISLLRELRdegKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-219 |
4.12e-10 |
|
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: 58.96 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 17 PAVLHPIDLEIADGEFIVLLGPSGCGKSTM-LRMIAGLEAITGGELVIG-DAVVNDLPSRERNVAMVFQNYALYPHmTVY 94
Cdd:cd03369 21 PPVLKNVSFKVKAGEKIGIVGRTGAGKSTLiLALFRFLEAEEGKIEIDGiDISTIPLEDLRSSLTIIPQDPTLFSG-TIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 95 DNIAfglrrlkvPADEI-DRRVRDVARILSLDALLdrrpramSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQL 173
Cdd:cd03369 100 SNLD--------PFDEYsDEEIYGALRVSEGGLNL-------SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1142773718 174 RGDIkrlHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTP 219
Cdd:cd03369 165 QKTI---REEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-213 |
4.13e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 23 IDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRER-NVAMVF-----QNYALYPHMT---- 92
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPlawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 93 ----VYDNIAFGLRRLKVPAdeIDRRVRDVARILSLDAllDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAK 168
Cdd:PRK15439 362 vcalTHNRRGFWIKPARENA--VLERYRRALNIKFNHA--EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1142773718 169 LRTQLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:PRK15439 438 ARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-193 |
5.04e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.58 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQITCKALSKHYDGGPAVLHPIDLE--IADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDA-VVNDLPSR--E 75
Cdd:PTZ00265 380 IKKIQFKNVRFHYDTRKDVEIYKDLNftLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKwwR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 76 RNVAMVFQNYALYPHmTVYDNIAFGLRRLK----------------------------------------VPADEI---- 111
Cdd:PTZ00265 460 SKIGVVSQDPLLFSN-SIKNNIKYSLYSLKdlealsnyynedgndsqenknkrnscrakcagdlndmsntTDSNELiemr 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 112 -------DRRVRDVAR-------ILSL----DALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQL 173
Cdd:PTZ00265 539 knyqtikDSEVVDVSKkvlihdfVSALpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260
....*....|....*....|
gi 1142773718 174 RGDIKRLHRQLKTTTLYVTH 193
Cdd:PTZ00265 619 QKTINNLKGNENRITIIIAH 638
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-222 |
8.50e-10 |
|
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: 60.20 E-value: 8.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHY----DGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLpSRER--- 76
Cdd:COG4615 328 LELRGVTYRYpgedGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD-NREAyrq 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 77 NVAMVFQNYALYPHMTVYDNIAFG------LRRLkvpadEIDRRVRDVARILSldalldrrPRAMSGGQQQRAAIARAMI 150
Cdd:COG4615 407 LFSAVFSDFHLFDRLLGLDGEADPararelLERL-----ELDHKVSVEDGRFS--------TTDLSQGQRKRLALLVALL 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 151 KTPAVFLFDEPLSNLDAKLR----TQLRGDIKRLHRqlktTTLYVTHDQlEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:COG4615 474 EDRPILVFDEWAADQDPEFRrvfyTELLPELKARGK----TVIAISHDD-RYFDLADRVLKMDYGKLVELTGPAAL 544
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-225 |
1.10e-09 |
|
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: 58.71 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 16 GPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGleaitggELVIGDAVVNdlpsRERNVAMVFQNYALYPHmTVYD 95
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILG-------ELEPSEGKIK----HSGRISFSSQFSWIMPG-TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 96 NIAFGlrrlkVPADEIdrRVRDVARILSLDALLDRRPR-----------AMSGGQQQRAAIARAMIKTPAVFLFDEPLSN 164
Cdd:cd03291 117 NIIFG-----VSYDEY--RYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 165 LDAKLRTQLRGdiKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQ 225
Cdd:cd03291 190 LDVFTEKEIFE--SCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-222 |
1.10e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.50 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEA--ITGGELVIGDAVVNDLPSRERN---VAMVFQNYALYPHMTV 93
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESILDLEPEERAhlgIFLAFQYPIEIPGVSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 94 YD--NIAFGLRRLKVPADEID-----RRVRDVARILSLDA-LLDRR-PRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSN 164
Cdd:CHL00131 102 ADflRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPsFLSRNvNEGFSGGEKKRNEILQMALLDSELAILDETDSG 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 165 LDAK-LRTQLRGdIKRLHRQLKTTTLyVTHDQ-LEAMTLADRVVLMRGGHIEQIGTpAEL 222
Cdd:CHL00131 182 LDIDaLKIIAEG-INKLMTSENSIIL-ITHYQrLLDYIKPDYVHVMQNGKIIKTGD-AEL 238
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-168 |
1.40e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.51 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 23 IDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDL-PSRERNVAMVFQNYALYPHMTVYDNIAFgL 101
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrDEYHQDLLYLGHQPGIKTELTALENLRF-Y 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 102 RRLKVPADEiDRRVRDVARIlSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAK 168
Cdd:PRK13538 99 QRLHGPGDD-EALWEALAQV-GLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-213 |
1.64e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 56.56 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 23 IDLEIADGEFIVLLGPSGCGKSTMLRmiagleaiTGGELVIGDAVVNDLPSRERN-VAMVFQNYALyphmtvydnIAFGL 101
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTLVN--------EGLYASGKARLISFLPKFSRNkLIFIDQLQFL---------IDVGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 102 RRLKvpadeidrrvrdvarilsldalLDRRPRAMSGGQQQRAAIARAMIKTP--AVFLFDEPLSNLDAKLRTQLRGDIKR 179
Cdd:cd03238 77 GYLT----------------------LGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1142773718 180 LhRQLKTTTLYVTHDqLEAMTLADRVVLM------RGGHI 213
Cdd:cd03238 135 L-IDLGNTVILIEHN-LDVLSSADWIIDFgpgsgkSGGKV 172
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
19-198 |
1.81e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.26 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIagleaiTG-------------------GELV------IG--------D 65
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI------TGdhpqgysndltlfgrrrgsGETIwdikkhIGyvssslhlD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 66 AVVNdlpSRERNVAM--VFQNYALYphMTVYDniafglrRLKVPADE-IDrrvrdvarILSLDALLDRRP-RAMSGGQQQ 141
Cdd:PRK10938 349 YRVS---TSVRNVILsgFFDSIGIY--QAVSD-------RQQKLAQQwLD--------ILGIDKRTADAPfHSLSWGQQR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 142 RAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLEA 198
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
23-227 |
2.25e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 58.38 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 23 IDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEA----ITGGELVIGDAVVNDLPSRER------NVAMVFQN--YALYPH 90
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQEpsSCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 91 MTVYDNIAFGLrrlkvPADEIDRRV--RDVARILSLDALLDR------------RPRAMSGGQQQRAAIARAMIKTPAVF 156
Cdd:COG4170 106 AKIGDQLIEAI-----PSWTFKGKWwqRFKWRKKRAIELLHRvgikdhkdimnsYPHELTEGECQKVMIAMAIANQPRLL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 157 LFDEPLSNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDqLEAMT-LADRVVLMRGGHIEQIGTPAELYGQPH 227
Cdd:COG4170 181 IADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHD-LESISqWADTITVLYCGQTVESGPTEQILKSPH 251
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-194 |
3.13e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 1 MAQI--TCKALSKHYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVigdavvndlPSRERNV 78
Cdd:PRK11819 2 MAQYiyTMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR---------PAPGIKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 79 AMVFQNYALYPHMTVYDNIAFGLRRLKV--------------PADEIDRRVRDVARILS-LDAL----LDRR-PRAM--- 135
Cdd:PRK11819 73 GYLPQEPQLDPEKTVRENVEEGVAEVKAaldrfneiyaayaePDADFDALAAEQGELQEiIDAAdawdLDSQlEIAMdal 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773718 136 ------------SGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKlrtqlrgDIKRLHRQLKT---TTLYVTHD 194
Cdd:PRK11819 153 rcppwdakvtklSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE-------SVAWLEQFLHDypgTVVAVTHD 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-216 |
5.15e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 23 IDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVV---NDLPSRERNVAMVFQNY---ALYPHMTVYDN 96
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprSPLDAVKKGMAYITESRrdnGFFPNFSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 97 IAFgLRRLKV-----------PADEidRRVRDVAR-ILSLD-ALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLS 163
Cdd:PRK09700 362 MAI-SRSLKDggykgamglfhEVDE--QRTAENQReLLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 164 NLDAKLRTQlrgdIKRLHRQLK---TTTLYVTHDQLEAMTLADRVVLMRGGHIEQI 216
Cdd:PRK09700 439 GIDVGAKAE----IYKVMRQLAddgKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-211 |
6.18e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 25 LEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELV-IGDAVVNDLP--SRERNVAMVFQNYALYPHMTVYDNIAFGl 101
Cdd:PRK10762 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGPksSQEAGIGIIHQELNLIPQLTIAENIFLG- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 102 RRLKVPADEID-RRVRDVArilslDALLDR-----RPRAMSG----GQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRT 171
Cdd:PRK10762 104 REFVNRFGRIDwKKMYAEA-----DKLLARlnlrfSSDKLVGelsiGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1142773718 172 QLRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGG 211
Cdd:PRK10762 179 SLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
30-213 |
1.40e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.16 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 30 GEFIVLLGPSGCGKSTMLRMIAGLEaiTGGeLVIGDAVVNDLPSRERNVAMVF----QNYALYPHMTVYDNIAFG--LRR 103
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRK--TGG-YIEGDIRISGFPKKQETFARISgyceQNDIHSPQVTVRESLIYSafLRL 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 104 LK-VPADEIDRRVRDVARILSLDALLDR---RP--RAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAK-----LRTq 172
Cdd:PLN03140 983 PKeVSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARaaaivMRT- 1061
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1142773718 173 LRGDIKRlHRQLKTTTLYVTHDQLEAMtlaDRVVLM-RGGHI 213
Cdd:PLN03140 1062 VRNTVDT-GRTVVCTIHQPSIDIFEAF---DELLLMkRGGQV 1099
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
33-166 |
1.93e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 33 IV-LLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVvndlpsrerNVAMVFQNY-ALYPHMTVYDNIAFGLRRLKVPADE 110
Cdd:PRK11819 352 IVgIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV---------KLAYVDQSRdALDPNKTVWEEISGGLDIIKVGNRE 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 111 IDRRvrdvarilsldALLDR----------RPRAMSGGQQQRAAIARaMIKTPA-VFLFDEPLSNLD 166
Cdd:PRK11819 423 IPSR-----------AYVGRfnfkggdqqkKVGVLSGGERNRLHLAK-TLKQGGnVLLLDEPTNDLD 477
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
16-213 |
2.43e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 16 GPAVlHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVNDLPSRERNVAMVF-----QNYALYP 89
Cdd:PRK10762 265 GPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdGHEVVTRSPQDGLANGIVYisedrKRDGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 90 HMTVYDNIAF-GLRRLKVPADEIDRR-----VRDVARILSLDA-LLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPL 162
Cdd:PRK10762 344 GMSVKENMSLtALRYFSRAGGSLKHAdeqqaVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773718 163 SNLD--AKlrtqlrGDIKRLHRQLKTTTL---YVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:PRK10762 424 RGVDvgAK------KEIYQLINQFKAEGLsiiLVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-166 |
2.98e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 30 GEFIVLLGPSGCGKSTMLR-MIAGLEAiTGGELVIGDAVvndlpsrerNVAMvFQNY--ALYPHMTVYDNIAFGLRRLKV 106
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKlMLGQLQA-DSGRIHCGTKL---------EVAY-FDQHraELDPEKTVMDNLAEGKQEVMV 413
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 107 paDEIDRRVrdvarilsLDALLD--------RRP-RAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLD 166
Cdd:PRK11147 414 --NGRPRHV--------LGYLQDflfhpkraMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-215 |
5.55e-08 |
|
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: 53.70 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 3 QITCKALSKHY-DGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLeAITGGELVIGDAVVNDLPSRERNVAmv 81
Cdd:cd03289 2 QMTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRKA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 82 fqnYALYPHMTVydnIAFGLRRLKVPADEI--DRRVRDVARILSLDALLDRRPR-----------AMSGGQQQRAAIARA 148
Cdd:cd03289 79 ---FGVIPQKVF---IFSGTFRKNLDPYGKwsDEEIWKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 149 MIKTPAVFLFDEPLSNLDAKLRTQLRgdiKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQ 215
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPITYQVIR---KTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-213 |
8.75e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 52.65 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTM----------LRMIAGL----------------EAITGgelvIGDAVVNDLPS 73
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLsayarqflgqmdkpdvDSIEG----LSPAIAIDQKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 74 RERNvamvfqnyalyPHMTV------YDNIafglrRLKVPADEIDRRVRDVARIlSLDAL-LDRRPRAMSGGQQQRAAIA 146
Cdd:cd03270 87 TSRN-----------PRSTVgtvteiYDYL-----RLLFARVGIRERLGFLVDV-GLGYLtLSRSAPTLSGGEAQRIRLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1142773718 147 R--AMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLhRQLKTTTLYVTHDQlEAMTLADRVVLM------RGGHI 213
Cdd:cd03270 150 TqiGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE-DTIRAADHVIDIgpgagvHGGEI 222
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
12-225 |
1.16e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.82 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 12 HYDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGL-EAITGGELVIGDAVVNDLPSRERN-VAMVFQNYALYP 89
Cdd:PRK10522 331 AYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLyQPQSGEILLDGKPVTAEQPEDYRKlFSAVFTDFHLFD 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 90 HMTVYDN-------IAFGLRRLKVpADEIdrRVRDvARILSLDalldrrpraMSGGQQQRAAIARAMIKTPAVFLFDEPL 162
Cdd:PRK10522 411 QLLGPEGkpanpalVEKWLERLKM-AHKL--ELED-GRISNLK---------LSKGQKKRLALLLALAEERDILLLDEWA 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773718 163 SNLDAKLRTQLRGDIKRLHRQLKTTTLYVTHDQLeAMTLADRVVLMRGGHIeqigtpAELYGQ 225
Cdd:PRK10522 478 ADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDH-YFIHADRLLEMRNGQL------SELTGE 533
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-193 |
1.45e-07 |
|
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: 53.60 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 16 GPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVNDLPSRERNVAMVFQNYALYPhMTVY 94
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpAKGKLFYVPQRPYMTLGTLRDQIIYP-DSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 95 DNIAFGLRrlkvpadeiDRRVRDVARILSLDALLDRR---------PRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSnl 165
Cdd:TIGR00954 543 DMKRRGLS---------DKDLEQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTS-- 611
|
170 180
....*....|....*....|....*...
gi 1142773718 166 daKLRTQLRGDIKRLHRQLKTTTLYVTH 193
Cdd:TIGR00954 612 --AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-213 |
2.14e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 4 ITCKALSKHYDGGPaVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGD-AVVNDLPsreRNVAMVF 82
Cdd:PRK15064 320 LEVENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEnANIGYYA---QDHAYDF 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 83 QNyalypHMTVYDNIAfglrRLKVPADEiDRRVRDV-ARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEP 161
Cdd:PRK15064 396 EN-----DLTLFDWMS----QWRQEGDD-EQAVRGTlGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1142773718 162 LSNLDAKlrtqlrgDIKRLHRQLKT---TTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:PRK15064 466 TNHMDME-------SIESLNMALEKyegTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-272 |
3.01e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 17 PAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRE--RNVAMVFQNYALYPhmtvy 94
Cdd:PLN03130 1252 PPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLGIIPQAPVLFS----- 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 95 DNIAFGLRRLKVPAD-----EIDR-RVRDVAR--ILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLD 166
Cdd:PLN03130 1327 GTVRFNLDPFNEHNDadlweSLERaHLKDVIRrnSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 167 aklrtqLRGDI---KRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVFAAGFVGTPAMN-- 241
Cdd:PLN03130 1407 ------VRTDAliqKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQSTGAANaq 1480
|
250 260 270
....*....|....*....|....*....|....*.
gi 1142773718 242 FADGTIARVGTNVLLD-----CNGARWPLASSRFAR 272
Cdd:PLN03130 1481 YLRSLVFGGDEDRLAReeskaLDGQRKWLASSRWAA 1516
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
108-232 |
5.21e-07 |
|
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: 51.94 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 108 ADEIDRRVRDVARIL---SLDAL-LDRRPRAMSGGQQQRAAIARAMIK--TPAVFLFDEPLSNLDAKLRTQLRGDIKRLh 181
Cdd:TIGR00630 458 AEEVLKEIRERLGFLidvGLDYLsLSRAAGTLSGGEAQRIRLATQIGSglTGVLYVLDEPSIGLHQRDNRRLINTLKRL- 536
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 182 RQLKTTTLYVTHDQlEAMTLADRVVLM------RGGHIEQIGTPAELYGQPHTVFAA 232
Cdd:TIGR00630 537 RDLGNTLIVVEHDE-DTIRAADYVIDIgpgageHGGEVVASGTPEEILANPDSLTGQ 592
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-230 |
6.60e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.70 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 14 DGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTML----RMIagleAITGGELVIGDAVVNDLPSRE--RNVAMVFQNYAL 87
Cdd:PTZ00243 1320 EGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLltfmRMV----EVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVL 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 88 YPHmTVYDNI----------------AFGLR-RLKVPADEIDRRVRDVARILSLdalldrrpramsgGQQQRAAIARAMI 150
Cdd:PTZ00243 1396 FDG-TVRQNVdpfleassaevwaaleLVGLReRVASESEGIDSRVLEGGSNYSV-------------GQRQLMCMARALL 1461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 151 KTPAVF-LFDEPLSNLDAKLRTQLRGDIKRLHRQLktTTLYVTHdQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTV 229
Cdd:PTZ00243 1462 KKGSGFiLMDEATANIDPALDRQIQATVMSAFSAY--TVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSI 1538
|
.
gi 1142773718 230 F 230
Cdd:PTZ00243 1539 F 1539
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-204 |
7.15e-07 |
|
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: 48.52 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 30 GEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAvvndlpsrernvamvfqnyalyphmtvydniafglrrlkvpad 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 110 eidRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDI-----KRLHRQL 184
Cdd:smart00382 39 ---EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSEK 115
|
170 180
....*....|....*....|
gi 1142773718 185 KTTTLYVTHDQLEAMTLADR 204
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLR 135
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
30-167 |
8.93e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 48.78 E-value: 8.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 30 GEFIVLLGPSGCGKSTMLRMIAGLEaiTGGeLVIGDAVVNDLPSRE---RNVAMVFQNYALYPHMTVYDNIAFglrrlkv 106
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRK--TAG-VITGEILINGRPLDKnfqRSTGYVEQQDVHSPNLTVREALRF------- 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 107 padeidrrvrdvarilslDALLdrrpRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDA 167
Cdd:cd03232 103 ------------------SALL----RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
16-195 |
1.24e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.40 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 16 GPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLE--AITGGELVIGDAVVNDLPSRER---NVAMVFQNYALYPH 90
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 91 MT--VYDNIAFGLRRLKVPADEIDR-----RVRDVARILSLDA-LLDRRPR-AMSGGQQQRAAIARAMIKTPAVFLFDEP 161
Cdd:PRK09580 93 VSnqFFLQTALNAVRSYRGQEPLDRfdfqdLMEEKIALLKMPEdLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDES 172
|
170 180 190
....*....|....*....|....*....|....
gi 1142773718 162 LSNLDAKLRTQLRGDIKRLhRQLKTTTLYVTHDQ 195
Cdd:PRK09580 173 DSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQ 205
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
102-222 |
1.51e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.73 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 102 RRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKRLH 181
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV 191
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1142773718 182 RQlKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL 222
Cdd:NF000106 192 RD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
236-288 |
4.65e-06 |
|
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK transport protein.
Pssm-ID: 465563 [Multi-domain] Cd Length: 53 Bit Score: 43.34 E-value: 4.65e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1142773718 236 GTPAMNFADGTIARVGTNVLLDcnGARWPLASSRFARLQ--DGQQVKAAIRPNHL 288
Cdd:pfam17912 1 GSPPMNFLPATVVEDGLLVLGG--GVTLPLPEGQVLALKlyVGKEVILGIRPEHI 53
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
22-209 |
6.62e-06 |
|
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: 45.81 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 22 PIDLEIADGEFIVLLGPSGCGKSTMLRMIAgleaitggelvigdavvndlpsrernvamvfqnYALYPHMTVYDNIAFGL 101
Cdd:cd03227 13 PNDVTFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LALGGAQSATRRRSGVK 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 102 RRLKVPADEIDRrvrdvarILSLDALldrrpramSGGQQQRAAIARAMI---KTPAVF-LFDEPLSNLDAKLRTQLRGDI 177
Cdd:cd03227 60 AGCIVAAVSAEL-------IFTRLQL--------SGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAI 124
|
170 180 190
....*....|....*....|....*....|..
gi 1142773718 178 KRlHRQLKTTTLYVTHDqLEAMTLADRVVLMR 209
Cdd:cd03227 125 LE-HLVKGAQVIVITHL-PELAELADKLIHIK 154
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-215 |
8.23e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.98 E-value: 8.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 3 QITCKALSKHY-DGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLeAITGGELVIGDAVVNDLPSRERNVAmv 81
Cdd:TIGR01271 1217 QMDVQGLTAKYtEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRKA-- 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 82 fqnYALYPHMTVydnIAFGLRRLKVPADE--IDRRVRDVARILSLDALLDRRPR-----------AMSGGQQQRAAIARA 148
Cdd:TIGR01271 1294 ---FGVIPQKVF---IFSGTFRKNLDPYEqwSDEEIWKVAEEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARS 1367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 149 MIKTPAVFLFDEPLSNLDAKLRTQLRgdiKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQ 215
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIR---KTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-217 |
1.34e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.35 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELvigdavvndlpSRERNVAMVFQNYALYPHMTVYDNIAF 99
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAISAGLSGQLTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 100 GLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGDIKR 179
Cdd:PRK13546 109 KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYE 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 1142773718 180 LHRQLKtTTLYVTHDQLEAMTLADRVVLMRGGHIEQIG 217
Cdd:PRK13546 189 FKEQNK-TIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-183 |
2.03e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 20 LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLpSRERNVAMVFQNYALYPH-MTVYDNIA 98
Cdd:PRK10938 19 LQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRL-SFEQLQKLVSDEWQRNNTdMLSPGEDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 99 FGLRRLKVPADEIDRRVR--DVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGD 176
Cdd:PRK10938 98 TGRTTAEIIQDEVKDPARceQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAEL 177
|
....*..
gi 1142773718 177 IKRLHRQ 183
Cdd:PRK10938 178 LASLHQS 184
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-166 |
2.05e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 13 YDGGPAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAG-LEAITGGELvigdavvndlpsRERNVAM-VFQNYalypH 90
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGeLQPSSGTVF------------RSAKVRMaVFSQH----H 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 91 MTVYDNIAFGLRRLK-----VPadeiDRRVRDVARILSLDALLDRRPR-AMSGGQQQRAAIARAMIKTPAVFLFDEPLSN 164
Cdd:PLN03073 582 VDGLDLSSNPLLYMMrcfpgVP----EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNH 657
|
..
gi 1142773718 165 LD 166
Cdd:PLN03073 658 LD 659
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-232 |
2.53e-05 |
|
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: 45.28 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 3 QITCKALSKHYDGG-PAVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPS---RERnV 78
Cdd:cd03288 19 EIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLhtlRSR-L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 79 AMVFQNYALYPhmtvyDNIAFGLRRLKVPADEIDRRVRDVARILS--------LDALLDRRPRAMSGGQQQRAAIARAMI 150
Cdd:cd03288 98 SIILQDPILFS-----GSIRFNLDPECKCTDDRLWEALEIAQLKNmvkslpggLDAVVTEGGENFSVGQRQLFCLARAFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 151 KTPAVFLFDEPLSNLDAKLRTQLRgdiKRLHRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQPHTVF 230
Cdd:cd03288 173 RKSSILIMDEATASIDMATENILQ---KVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
..
gi 1142773718 231 AA 232
Cdd:cd03288 250 AS 251
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-214 |
9.73e-05 |
|
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: 44.43 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 30 GEFIVLLGPSGCGKSTMLRMIAGL-EAITGGELVIGD---AVVNDLPSRERNVAMVFQN---YALYPHMTVYDNIAF--- 99
Cdd:TIGR02633 286 GEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGkpvDIRNPAQAIRAGIAMVPEDrkrHGIVPILGVGKNITLsvl 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 100 ----GLRRLKVPADE--IDRRVRDVA-RILSLDALLDRrpraMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQ 172
Cdd:TIGR02633 366 ksfcFKMRIDAAAELqiIGSAIQRLKvKTASPFLPIGR----LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYE 441
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1142773718 173 LRGDIKRLHRQlKTTTLYVTHDQLEAMTLADRVVLMRGGHIE 214
Cdd:TIGR02633 442 IYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
128-231 |
3.17e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 128 LDRRPRAMSGGQQQRAAIARAMIK--TPAVFLFDEPLSNLDAKLRTQLRGDIKRLHRQlKTTTLYVTHDQlEAMTLADRV 205
Cdd:PRK00635 470 PERALATLSGGEQERTALAKHLGAelIGITYILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDE-QMISLADRI 547
|
90 100 110
....*....|....*....|....*....|..
gi 1142773718 206 VLMR------GGHIEQIGTPAELYGQPHTVFA 231
Cdd:PRK00635 548 IDIGpgagifGGEVLFNGSPREFLAKSDSLTA 579
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-225 |
4.02e-04 |
|
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: 42.63 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-----GDAVVNDLPSR-----------ERNVAMVF 82
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdglniAKIGLHDLRFKitiipqdpvlfSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 83 QNYALYPHMTVYdnIAFGLRRLK--VPA--DEIDRRVRDVARILSLdalldrrpramsgGQQQRAAIARAMIKTPAVFLF 158
Cdd:TIGR00957 1381 DPFSQYSDEEVW--WALELAHLKtfVSAlpDKLDHECAEGGENLSV-------------GQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773718 159 DEPLSNLDAKLRTQLRGDIKrlhRQLKTTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQ 225
Cdd:TIGR00957 1446 DEATAAVDLETDNLIQSTIR---TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-206 |
5.94e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 40.67 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 34 VLLGPSGCGKSTMLRMIagLEAITG-----GELVIGDAVVNDLPSRERNVAMVFQN-----YALYPHMTVYDNIAFglrr 103
Cdd:cd03240 26 LIVGQNGAGKTTIIEAL--KYALTGelppnSKGGAHDPKLIREGEVRAQVKLAFENangkkYTITRSLAILENVIF---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 104 lkVPADEIdrrvrdvarilslDALLDRRPRAMSGGQQQ------RAAIARAM-IKTPAVFLfDEPLSNLDA-KLRTQLRg 175
Cdd:cd03240 100 --CHQGES-------------NWPLLDMRGRCSGGEKVlasliiRLALAETFgSNCGILAL-DEPTTNLDEeNIEESLA- 162
|
170 180 190
....*....|....*....|....*....|..
gi 1142773718 176 DIKRLHRQLKTTTLYV-THDQlEAMTLADRVV 206
Cdd:cd03240 163 EIIEERKSQKNFQLIViTHDE-ELVDAADHIY 193
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
281-356 |
7.29e-04 |
|
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: 37.98 E-value: 7.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773718 281 AAIRPNHLQLVAEGDptpgtlTLTGMVELVELLGAEALVTLDWRGQPCAALVPAPMAPAPGAV---VAFRFDEEALHLF 356
Cdd:pfam08402 1 LAIRPEKIRLAAAAN------GLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHARPPAPgdrVGLGWDPEDAHVL 73
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
22-51 |
3.40e-03 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 38.38 E-value: 3.40e-03
10 20 30
....*....|....*....|....*....|
gi 1142773718 22 PIDLEIADGEFIVLLGPSGCGKSTMLRMIA 51
Cdd:cd03243 21 PNDINLGSGRLLLITGPNMGGKSTYLRSIG 50
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
12-225 |
6.24e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 38.72 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 12 HYdggpaVLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVI-GDAVVNDLPSRERNVAMVFQNYALYPH 90
Cdd:PRK13545 37 HY-----ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGSAALIAISSGLNGQLTGIENIELKGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 91 MtvydniaFGLRRLKVpaDEIDRRVRDVARIlslDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLR 170
Cdd:PRK13545 112 M-------MGLTKEKI--KEIIPEIIEFADI---GKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773718 171 TQLRGDIKRLHRQLKtTTLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAEL---YGQ 225
Cdd:PRK13545 180 KKCLDKMNEFKEQGK-TIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVvdhYDE 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
77-213 |
6.38e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 38.76 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 77 NVAMVFQN---YALYPHMTVYDNIA------FGLRRLKVPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIAR 147
Cdd:PRK13549 339 GIAMVPEDrkrDGIVPVMGVGKNITlaaldrFTGGSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAK 418
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773718 148 AMIKTPAVFLFDEPLSNLD--AKLrtqlrgDIKRLHRQLK---TTTLYVTHDQLEAMTLADRVVLMRGGHI 213
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDvgAKY------EIYKLINQLVqqgVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
130-166 |
8.08e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.30 E-value: 8.08e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1142773718 130 RRPRAMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLD 166
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-211 |
9.32e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.23 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 17 PAV--LHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGL--------EAITGGELV----IGDavvndlpSRERNVAMVF 82
Cdd:NF040905 12 PGVkaLDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyegEILFDGEVCrfkdIRD-------SEALGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 83 QNYALYPHMTVYDNIAFGLRRLK---VPADEIDRRVRDVARILSLDALLDRRPRAMSGGQQQRAAIARAMIKTPAVFLFD 159
Cdd:NF040905 85 QELALIPYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1142773718 160 EPLSNLDAKLRTQLRGDIKRLHRQLKTTTLyVTHDQLEAMTLADRVVLMRGG 211
Cdd:NF040905 165 EPTAALNEEDSAALLDLLLELKAQGITSII-ISHKLNEIRRVADSITVLRDG 215
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-225 |
9.58e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 38.23 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 19 VLHPIDLEIADGEFIVLLGPSGCGKSTMLRMIAGLEAITGGELVIGDAVVNDLPSRERnVAMVFQNYALYPHMTvydnia 98
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQ-LEFLRADESPLQHLA------ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773718 99 fglrrlKVPADEIDRRVRDVARILSL--DALLDRRPRaMSGGQQQRAAIARAMIKTPAVFLFDEPLSNLDAKLRTQLRGD 176
Cdd:PRK10636 400 ------RLAPQELEQKLRDYLGGFGFqgDKVTEETRR-FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1142773718 177 IKRLHRQLktttLYVTHDQLEAMTLADRVVLMRGGHIEQIGTPAELYGQ 225
Cdd:PRK10636 473 LIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQ 517
|
|
| |
