|
Name |
Accession |
Description |
Interval |
E-value |
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-293 |
6.52e-161 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 449.56 E-value: 6.52e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFGYMPEER 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYLPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 GLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGL 160
Cdd:COG4152 81 GLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 161 DPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELR-SAGPCRHRIVVSSDAGWVRDLS 239
Cdd:COG4152 161 DPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRrQFGRNTLRLEADGDAGWLRALP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 240 GVHVVDVDGTAALVELADETAKQALLAEALSRGSLSEFTPVRPSLSEIYREVTA 293
Cdd:COG4152 241 GVTVVEEDGDGAELKLEDGADAQELLRALLARGPVREFEEVRPSLNEIFIEVVG 294
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-211 |
2.49e-102 |
|
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: 297.66 E-value: 2.49e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFGYMPEERG 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 82 LYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLD 161
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1450037824 162 PTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG 211
Cdd:cd03269 161 PVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-219 |
2.87e-84 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 252.68 E-value: 2.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPAT---VADRRTFGYMPE 78
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVArdpAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 79 ERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFS 158
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 159 GLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRSA 219
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-218 |
1.68e-71 |
|
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: 220.50 E-value: 1.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPAT---VADRRTFGYMP 77
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkepREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 78 EERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPF 157
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 158 SGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRS 218
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-207 |
2.47e-60 |
|
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: 189.53 E-value: 2.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG---RPATVADRRTFGYMPE 78
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdiKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 79 ERGLYvkqgvasqliylGQLagmsrpearrSVTELLErfgladrakdklesLSLGNQQRVQIAAAVMSRPQALILDEPFS 158
Cdd:cd03230 81 EPSLY------------ENL----------TVRENLK--------------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1450037824 159 GLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRV 207
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-211 |
2.69e-59 |
|
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: 188.19 E-value: 2.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPAT--VADRRTFGYMPEE 79
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQknIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 80 RGLYVKQGVASQLIYLGQLAGMSRpearRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSG 159
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 160 LDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG 211
Cdd:cd03268 157 LDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-292 |
7.46e-58 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 187.60 E-value: 7.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 9 RRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG-----RPATVadRRTFGYMPEERGLY 83
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvvrEPRKV--RRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 84 VKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPT 163
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 164 SVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRSAGPCRHRIVVSSDAGWVRDLSGVH- 242
Cdd:TIGR01188 159 TRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQSLKVEVSMLi 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 243 -------------VVDVDGTAALVELADETAKQALLAEALSRGSLSEFTPVRPSLSEIYREVT 292
Cdd:TIGR01188 239 aelgetglgllavTVDSDRIKILVPDGDETVPEIVEAAIRNGIRIRSISTERPSLDDVFLKLT 301
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-218 |
6.08e-55 |
|
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: 178.69 E-value: 6.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATvadrrtfGYMPEER 80
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT-------GLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 glyVKQGVA-----SQL---------IYLGQLAGM----------------SRPEARRSVTELLERFGLADRAKDKLESL 130
Cdd:COG0411 77 ---ARLGIArtfqnPRLfpeltvlenVLVAAHARLgrgllaallrlprarrEEREARERAEELLERVGLADRADEPAGNL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 131 SLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVA 209
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRlRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIA 233
|
....*....
gi 1450037824 210 QGTAEELRS 218
Cdd:COG0411 234 EGTPAEVRA 242
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-215 |
6.75e-54 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 175.28 E-value: 6.75e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATvADRRTFGYMPEER 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-RARRRIGYVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 GLY------VKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILD 154
Cdd:COG1121 85 EVDwdfpitVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 155 EPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKgRVVAQGTAEE 215
Cdd:COG1121 165 EPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNR-GLVAHGPPEE 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-216 |
9.59e-53 |
|
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: 172.13 E-value: 9.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELT-RRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGYM 76
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNlrelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 ---PEerglyvkqgvaSQLIY----------LGQLaGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAA 143
Cdd:COG1122 81 fqnPD-----------DQLFAptveedvafgPENL-GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 144 VMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-218 |
2.52e-52 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 171.08 E-value: 2.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGR------PATVADR---RT 72
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglpPHEIARLgigRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 73 FGYMPEERGLYVKQGV------ASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMS 146
Cdd:cd03219 81 FQIPRLFPELTVLENVmvaaqaRTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 147 RPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRS 218
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-211 |
1.01e-50 |
|
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: 166.39 E-value: 1.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHT----AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG-----RPATVadRR 71
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAEA--RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 72 TFGYMPEERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQAL 151
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 152 ILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG 211
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-193 |
3.13e-49 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 162.26 E-value: 3.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD---RRTFGYMP 77
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARedyRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 78 EERGLYVKQGVASQLIYLGQLAGMSRPEARrsVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPF 157
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1450037824 158 SGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVD 193
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA 195
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-216 |
3.38e-49 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 163.30 E-value: 3.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRF-GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD-------RRT 72
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgralrrlRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 73 FGYMPEERGLYVKQGV-----ASQLIYLGQLAGMSR---PEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAV 144
Cdd:COG3638 82 IGMIFQQFNLVPRLSVltnvlAGRLGRTSTWRSLLGlfpPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 145 MSRPQALILDEPFSGLDP-TSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:COG3638 162 VQEPKLILADEPVASLDPkTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
1.38e-48 |
|
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: 168.93 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRF-----GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFGY 75
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEERGlYVKQGVASQL-----IY------LGQLAGMSRPEARRSVTELLERFGLADRAKDKL-ESLSLGNQQRVQIAAA 143
Cdd:COG1123 340 LRRRVQ-MVFQDPYSSLnprmtVGdiiaepLRLHGLLSRAERRERVAELLERVGLPPDLADRYpHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 144 VMSRPQALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-217 |
2.16e-48 |
|
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: 161.30 E-value: 2.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD-------RRTF 73
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekelyelRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 74 GYMPEERGLY----VKQGVAsqlIYLGQLAGMSRPEARRSVTELLERFGLADrAKDKLES-LSLGNQQRVQIAAAVMSRP 148
Cdd:COG1127 85 GMLFQGGALFdsltVFENVA---FPLREHTDLSEAEIRELVLEKLELVGLPG-AADKMPSeLSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 149 QALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELR 217
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-211 |
5.55e-48 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 159.24 E-value: 5.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 3 EVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATvADRRTFGYMPEERG- 81
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-KERKRIGYVPQRRSi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 82 -----LYVKQGVASQLI-YLGQLAGMSRpEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:cd03235 80 drdfpISVRDVVLMGLYgHKGLFRRLSK-ADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 156 PFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLsKGRVVAQG 211
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-217 |
2.20e-47 |
|
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: 158.05 E-value: 2.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGD--HTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG---RPATVADRRTFGYM 76
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysiRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEP 156
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 157 FSGLDPTSVDVMADLLREhTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELR 217
Cdd:cd03263 161 TSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-211 |
4.32e-47 |
|
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: 156.97 E-value: 4.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGqLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPAT---VADRRTFGYMPE 78
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLkqpQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 79 ERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFS 158
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 159 GLDPTSVDVMADLLREhTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG 211
Cdd:cd03264 160 GLDPEERIRFRNLLSE-LGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-211 |
4.62e-47 |
|
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: 156.91 E-value: 4.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPAT--VADRRTFGYMPEE 79
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTgvPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 80 RGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSG 159
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 160 LDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG 211
Cdd:cd03259 161 LDAKLREELREELKElQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-216 |
6.86e-47 |
|
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: 157.51 E-value: 6.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRP------ATVAdrRTFG 74
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslsrRELA--RRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 75 YMPEER----GLYVKQGVA-SQLIYLGQLAGMSrPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQ 149
Cdd:COG1120 79 YVPQEPpapfGLTVRELVAlGRYPHLGLFGRPS-AEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450037824 150 ALILDEPFSGLDPTS-VDVMaDLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:COG1120 158 LLLLDEPTSHLDLAHqLEVL-ELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-217 |
1.20e-46 |
|
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: 155.99 E-value: 1.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG-----RPATVadRRTFGYM 76
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvrEPREV--RRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADrAKDKL-ESLSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLE-AADRLvKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 156 PFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELR 217
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-216 |
4.13e-46 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 158.34 E-value: 4.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPAT--VADRRTFGYMPE 78
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglPPEKRNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 79 ERGLY----VKQGVASQLiylgQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILD 154
Cdd:COG3842 85 DYALFphltVAENVAFGL----RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 155 EPFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHqlDLVD--RLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:COG3842 161 EPLSALDAKLREEMREELRRlQRELGITFIYVTH--DQEEalALADRIAVMNDGRIEQVGTPEEI 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-216 |
2.05e-45 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 156.46 E-value: 2.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPAT----VADRRTfGYMP 77
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtnlpPRERRV-GFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 78 EERGLY----VKQGVAsqliylgqlAGM-----SRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRP 148
Cdd:COG1118 82 QHYALFphmtVAENIA---------FGLrvrppSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 149 QALILDEPFSGLDptsVDVMADL---LRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:COG1118 153 EVLLLDEPFGALD---AKVRKELrrwLRRlHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-206 |
2.15e-45 |
|
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: 152.62 E-value: 2.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 3 EVQELTRRFGDHT--AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGYm 76
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlkelRRKVGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 peerglyVKQGVASQLIY----------LGQLaGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMS 146
Cdd:cd03225 80 -------VFQNPDDQFFGptveeevafgLENL-GLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 147 RPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGR 206
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-218 |
4.26e-45 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 152.20 E-value: 4.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD-----RRTFGYM 76
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpheraRAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEERGLYVKQGVASQLIyLGQLAGmSRPEARRSVTELLERF-GLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:cd03224 81 PEGRRIFPELTVEENLL-LGAYAR-RRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 156 PFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRS 218
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-218 |
3.49e-44 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 150.13 E-value: 3.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGR------PATVAdRRTFG 74
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpPHRIA-RLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 75 YMPEERGLYVKQGVASQLIyLGQLAGMSRPEARRSVTELLERF-GLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALIL 153
Cdd:COG0410 82 YVPEGRRIFPSLTVEENLL-LGAYARRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 154 DEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRS 218
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-219 |
4.24e-44 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 159.90 E-value: 4.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 3 EVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD---RRTFGYMPEE 79
Cdd:NF033858 268 EARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDiatRRRVGYMSQA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 80 RGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSG 159
Cdd:NF033858 348 FSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSG 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 160 LDPTSVD----VMADLLRehtREGVPVLFSSHQLD---LVDRLSdglvVLSKGRVVAQGTAEELRSA 219
Cdd:NF033858 428 VDPVARDmfwrLLIELSR---EDGVTIFISTHFMNeaeRCDRIS----LMHAGRVLASDTPAALVAA 487
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-209 |
1.35e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 149.47 E-value: 1.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRF----GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTfGYM 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR-GVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEERGLY----VKQGVAsqliyLG-QLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQAL 151
Cdd:COG1116 86 FQEPALLpwltVLDNVA-----LGlELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 152 ILDEPFSGLDP-TSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSK--GRVVA 209
Cdd:COG1116 161 LMDEPFGALDAlTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-211 |
3.58e-43 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 147.16 E-value: 3.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFGYMPEERG 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHKIGSLIESPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 82 LYVKQGVASQLIYLGQLAGMsrPEARrsVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLD 161
Cdd:TIGR03740 81 LYENLTARENLKVHTTLLGL--PDSR--IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1450037824 162 PTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG 211
Cdd:TIGR03740 157 PIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQG 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-237 |
3.68e-43 |
|
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: 147.65 E-value: 3.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATV-------ADRRTFG 74
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaelyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 75 YMPEERGLY----VKQGVASQLIYLGQLagmSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQA 150
Cdd:cd03261 81 MLFQSGALFdsltVFENVAFPLREHTRL---SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 151 LILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRsagpcrhrivvS 229
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR-----------A 226
|
....*...
gi 1450037824 230 SDAGWVRD 237
Cdd:cd03261 227 SDDPLVRQ 234
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-210 |
3.23e-42 |
|
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: 144.54 E-value: 3.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGD----HTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTfGYMP 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR-GYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 78 EERGLY----VKQGVAsqliyLG-QLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALI 152
Cdd:cd03293 80 QQDALLpwltVLDNVA-----LGlELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 153 LDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSK--GRVVAQ 210
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-291 |
7.26e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 146.77 E-value: 7.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 7 LTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVlwqgrpatvadrRTFGYMP-EERGLYVK 85
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV------------RVLGYVPfKRRKEFAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 86 Q-GVA----SQLIY----------LGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQA 150
Cdd:COG4586 96 RiGVVfgqrSQLWWdlpaidsfrlLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 151 LILDEPFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRSA-GPCRhRIVV 228
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEyNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERfGPYK-TIVL 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 229 SSDAGWVR-DLS-GVHVVDVDGTAALVELADETAKQALLAEALSRGSLSEFTPVRPSLSEIYREV 291
Cdd:COG4586 255 ELAEPVPPlELPrGGEVIEREGNRVRLEVDPRESLAEVLARLLARYPVRDLTIEEPPIEEVIRRI 319
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
1.27e-41 |
|
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: 150.05 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRF--GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHG---GQVLWQGRPATVADRRTFGy 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 mpeERGLYVKQGVASQLIYL---GQLA------GMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMS 146
Cdd:COG1123 83 ---RRIGMVFQDPMTQLNPVtvgDQIAealenlGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 147 RPQALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-216 |
4.04e-41 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 142.48 E-value: 4.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD-----RRTFGY 75
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhkraRLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEE----RGLYVKQGVASQLiylgQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQAL 151
Cdd:COG1137 83 LPQEasifRKLTVEDNILAVL----ELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450037824 152 ILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQ----LDLVDRLSdglvVLSKGRVVAQGTAEEL 216
Cdd:COG1137 159 LLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNvretLGICDRAY----IISEGKVLAEGTPEEI 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-216 |
4.38e-41 |
|
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: 141.95 E-value: 4.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDH----TAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPAT-------VAD 69
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgkelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 70 RRTFGYMPEERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQ 149
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1450037824 150 ALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-219 |
9.47e-41 |
|
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: 141.48 E-value: 9.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFG----DHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFgym 76
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 peerglyvkqgvASQLIYLGQ-------------------LAGMSRPEARRSVTELLERFGLADRAKDKL-ESLSLGNQQ 136
Cdd:COG1124 78 ------------RRRVQMVFQdpyaslhprhtvdrilaepLRIHGLPDREERIAELLEQVGLPPSFLDRYpHQLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 137 RVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEE 215
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
....
gi 1450037824 216 LRSA 219
Cdd:COG1124 226 LLAG 229
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-211 |
2.05e-40 |
|
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: 138.72 E-value: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 3 EVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFgympeergl 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 83 yvkqgvASQLIYLGQlagmsrpearrsvteLLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDP 162
Cdd:cd03214 72 ------ARKIAYVPQ---------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 163 T-SVDVMaDLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG 211
Cdd:cd03214 131 AhQIELL-ELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-216 |
3.02e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 143.29 E-value: 3.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPatVADRRtfgymPEER 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD--VTDLP-----PKDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 G---------LY----VKQGVASQLiylgQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSR 147
Cdd:COG3839 76 NiamvfqsyaLYphmtVYENIAFPL----KLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 148 PQALILDEPFSGLDPTS-VDVMADLLREHTREGVPVLFSSHqlDLVD--RLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:COG3839 152 PKVFLLDEPLSNLDAKLrVEMRAEIKRLHRRLGTTTIYVTH--DQVEamTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-206 |
5.40e-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: 136.61 E-value: 5.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 3 EVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTfgympeergl 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 83 yvkqgVASQLIYLGQLAGmsrpearrsvtellerfgladrakdkleslslGNQQRVQIAAAVMSRPQALILDEPFSGLDP 162
Cdd:cd00267 71 -----LRRRIGYVPQLSG--------------------------------GQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1450037824 163 TSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGR 206
Cdd:cd00267 114 ASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-216 |
5.49e-40 |
|
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: 139.36 E-value: 5.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGD-HTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGYM 76
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDpvelRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGL-----ADRAKDKlesLSLGNQQRVQIAAAVMSRPQAL 151
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpaefADRYPHE---LSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 152 ILDEPFSGLDPTSVDVMAD-LLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEeFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-216 |
6.81e-40 |
|
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: 139.24 E-value: 6.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGD-HTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG-------RPATVADRRTF 73
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 74 GYMPEERGLYVKQGVAsQLIYLGQLAGMS---------RPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAV 144
Cdd:cd03256 81 GMIFQQFNLIERLSVL-ENVLSGRLGRRStwrslfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 145 MSRPQALILDEPFSGLDP-TSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:cd03256 160 MQQPKLILADEPVASLDPaSSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-216 |
1.94e-39 |
|
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: 137.67 E-value: 1.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD-----RRTFGYM 76
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmhkraRLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEP 156
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 157 FSGLDPTSVDVMADLLREHTREGVPVLFSSHQ----LDLVDRlsdgLVVLSKGRVVAQGTAEEL 216
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNvretLSITDR----AYIIYEGKVLAEGTPEEI 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-206 |
3.54e-39 |
|
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: 135.39 E-value: 3.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRtfgympeerg 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 82 lyvkqgvasqliylgqlagmsRPEARRSVTELLERFGLADR--AKDKL-ESLSLGNQQRVQIAAAVMSRPQALILDEPFS 158
Cdd:cd03229 71 ---------------------LPPLRRRIGMVFQDFALFPHltVLENIaLGLSGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1450037824 159 GLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGR 206
Cdd:cd03229 130 ALDPITRREVRALLKSlQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-211 |
5.30e-39 |
|
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: 136.48 E-value: 5.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRF----GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRtfgyM 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRR----L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEERGL---YVKQG----------VASQL--IYLGQLAGMSRPEARRSVTELLERFGLADRAKDKL-ESLSLGNQQRVQI 140
Cdd:cd03257 77 RKIRRKeiqMVFQDpmsslnprmtIGEQIaePLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYpHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 141 AAAVMSRPQALILDEPFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG 211
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKlQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-208 |
6.20e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 135.95 E-value: 6.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRF-GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPatVAD---------R 70
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD--LSRlkrreipylR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 71 RTFGYMPEERGLY----VKQGVASQLiylgQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMS 146
Cdd:COG2884 79 RRIGVVFQDFRLLpdrtVYENVALPL----RVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 147 RPQALILDEPFSGLDP-TSVDVMaDLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVV 208
Cdd:COG2884 155 RPELLLADEPTGNLDPeTSWEIM-ELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-216 |
4.09e-38 |
|
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: 134.73 E-value: 4.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFG-DHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD-------RRT 72
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkklrklRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 73 FGYMPEERGL----YVKQGVAS-QLIYLGQLAGMSR---PEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAV 144
Cdd:TIGR02315 81 IGMIFQHYNLierlTVLENVLHgRLGYKPTWRSLLGrfsEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 145 MSRPQALILDEPFSGLDP-TSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPkTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-216 |
1.48e-37 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 133.17 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD-----RRTFGYM 76
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPmheraRLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTE-LLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEaLLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 156 PFSGLDPTSVDVMADLLREHTREGVPVLFSSHQ----LDLVDRlsdgLVVLSKGRVVAQGTAEEL 216
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNvretLDICDR----AYIISDGKVLAEGTPAEI 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-210 |
1.53e-37 |
|
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: 130.63 E-value: 1.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRtfgympEERg 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR------DAR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 82 lyvKQGVAsqLIYlgQLagmsrpearrsvtellerfgladrakdkleslSLGNQQRVQIAAAVMSRPQALILDEPFSGLD 161
Cdd:cd03216 74 ---RAGIA--MVY--QL--------------------------------SVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1450037824 162 PTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQ 210
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-216 |
5.24e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 137.46 E-value: 5.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTfgymPEER 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD----AQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 GLY-VKQ--GVASQL-----IYLGQLAG----MSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRP 148
Cdd:COG1129 80 GIAiIHQelNLVPNLsvaenIFLGREPRrgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1450037824 149 QALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-207 |
1.45e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.55 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGYMP 77
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppewRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 78 EERGLYvKQGVASQLIYLGQLAGMSRPEARrsVTELLERFGLADRAKDK-LESLSLGNQQRVQIAAAVMSRPQALILDEP 156
Cdd:COG4619 81 QEPALW-GGTVRDNLPFPFQLRERKFDRER--ALELLERLGLPPDILDKpVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 157 FSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRV 207
Cdd:COG4619 158 TSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-216 |
1.90e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 132.24 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRP----ATVADRRTfGYMP 77
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPvpsrARHARQRV-GVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 78 EERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPF 157
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1450037824 158 SGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-210 |
5.83e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 128.62 E-value: 5.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGD----HTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD------- 69
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerelarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 70 -RRTFGY-------MPEergLYVKQGVASQLIYlgqlAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIA 141
Cdd:COG1136 84 rRRHIGFvfqffnlLPE---LTALENVALPLLL----AGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 142 AAVMSRPQALILDEPFSGLDP-TSVDVMaDLLREHTRE-GVPVLFSSHQLDLVDRlSDGLVVLSKGRVVAQ 210
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSkTGEEVL-ELLRELNRElGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
9-211 |
2.13e-35 |
|
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: 127.45 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 9 RRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVlwqgrpatvadrRTFGYMP-EERGLYVKQ- 86
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV------------RVAGLVPwKRRKKFLRRi 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 87 ----GVASQLIY----------LGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALI 152
Cdd:cd03267 97 gvvfGQKTQLWWdlpvidsfylLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 153 LDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG 211
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-211 |
4.26e-35 |
|
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: 125.87 E-value: 4.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQeLTRRFGDHTAvdQVSFTVPdGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRP--------ATVADRRT 72
Cdd:cd03297 1 MLCVD-IEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkiNLPPQQRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 73 FGYMPEERGLYVKQGVASQLIYlgQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALI 152
Cdd:cd03297 77 IGLVFQQYALFPHLNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 153 LDEPFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG 211
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELKQiKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-216 |
4.46e-35 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 128.28 E-value: 4.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGD-HTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGY 75
Cdd:COG1125 1 MIEFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDpvelRRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEERGLY----VKQGVASqliyLGQLAGMSRPEARRSVTELLERFGL-ADRAKDKLES-LSLGNQQRVQIAAAVMSRPQ 149
Cdd:COG1125 81 VIQQIGLFphmtVAENIAT----VPRLLGWDKERIRARVDELLELVGLdPEEYRDRYPHeLSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1450037824 150 ALILDEPFSGLDP-TSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:COG1125 157 ILLMDEPFGALDPiTREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEI 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-208 |
4.88e-35 |
|
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: 125.45 E-value: 4.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 3 EVQELTRRFGDHT-AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFGYmpeerg 81
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIG------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 82 lYVKQGVASQL----IYLGQLAGMSRPEARRSVTE-LLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEP 156
Cdd:cd03226 75 -YVMQDVDYQLftdsVREELLLGLKELDAGNEQAEtVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 157 FSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVV 208
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-218 |
2.21e-34 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 125.10 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPA--------------- 65
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 66 TVADRRTFGYMPEERGLYVKQgvaSQLIYLGQLAGMSR-PEARRSVTE-------LLERFGLADRAKDKLESLSLGNQQR 137
Cdd:PRK11300 85 TFQHVRLFREMTVIENLLVAQ---HQQLKTGLFSGLLKtPAFRRAESEaldraatWLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 138 VQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
..
gi 1450037824 217 RS 218
Cdd:PRK11300 242 RN 243
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-271 |
3.19e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 126.73 E-value: 3.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRF----GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD------- 69
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSerelraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 70 ---------------RRTfgympeerglyVKQGVASQLiylgQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGN 134
Cdd:COG1135 81 rrkigmifqhfnllsSRT-----------VAENVALPL----EIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 135 QQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTA 213
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPV 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 214 EELRSAgPcRHRI------VVSSDAGWVRDLSGVHVVDVDGTAALVELADETAKQALLAEALSR 271
Cdd:COG1135 226 LDVFAN-P-QSELtrrflpTVLNDELPEELLARLREAAGGGRLVRLTFVGESADEPLLSELARR 287
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-216 |
7.16e-34 |
|
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: 123.12 E-value: 7.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPAT--VADRRTFGYMPEE 79
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITnlPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 80 RGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSG 159
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1450037824 160 LD-PTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:cd03300 161 LDlKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-216 |
1.38e-33 |
|
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: 124.78 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRF----GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQ---IHGGQVLWQGRPATVADRRTf 73
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 74 gyMPEERG-----------------LYVKQGVASQLIYLGqlaGMSRPEARRSVTELLERFGLADrAKDKLES----LSL 132
Cdd:COG0444 80 --LRKIRGreiqmifqdpmtslnpvMTVGDQIAEPLRIHG---GLSKAEARERAIELLERVGLPD-PERRLDRypheLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 133 GNQQRVQIAAAVMSRPQALILDEPFSGLDPTS----VDVMADLLREHtreGVPVLFSSHQLDLVDRLSDGLVVLSKGRVV 208
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIqaqiLNLLKDLQREL---GLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
....*...
gi 1450037824 209 AQGTAEEL 216
Cdd:COG0444 231 EEGPVEEL 238
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-216 |
1.41e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 127.84 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADrrtfgymPEEr 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRS-------PRD- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 glyvkqgvASQL--------------------IYLGQ----LAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQ 136
Cdd:COG3845 77 --------AIALgigmvhqhfmlvpnltvaenIVLGLeptkGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 137 RVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG----- 211
Cdd:COG3845 149 RVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVdtaet 228
|
....*
gi 1450037824 212 TAEEL 216
Cdd:COG3845 229 SEEEL 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-207 |
2.95e-33 |
|
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: 121.06 E-value: 2.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGD----HTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD-------- 69
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 70 RRTFGYMPEE----RGLYVKQGVASQLIylgqLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVM 145
Cdd:cd03255 81 RRHIGFVFQSfnllPDLTALENVELPLL----LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 146 SRPQALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRlSDGLVVLSKGRV 207
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-212 |
6.16e-33 |
|
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: 128.21 E-value: 6.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 16 AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATV---ADRRTFGYMPEERGLYVKQGVASQL 92
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETnldAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 93 IYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLL 172
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1450037824 173 REHtREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGT 212
Cdd:TIGR01257 1105 LKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-215 |
7.10e-33 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 123.37 E-value: 7.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRF----GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD------- 69
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 70 RRTFGYMPEERGLY----VKQGVASQLiylgQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVM 145
Cdd:PRK11153 81 RRQIGMIFQHFNLLssrtVFDNVALPL----ELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 146 SRPQALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEE 215
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-216 |
9.80e-33 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 120.48 E-value: 9.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD------RRTFG 74
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKkdinklRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 75 YMPEERGLY----VKQGVASQLIylgQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQA 150
Cdd:COG1126 81 MVFQQFNLFphltVLENVTLAPI---KVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 151 LILDEPFSGLDPTSV----DVMADLlrehTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:COG1126 158 MLFDEPTSALDPELVgevlDVMRDL----AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
1.17e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 121.34 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHT-AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRP------ATVADRRTF 73
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikydkkSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 74 GYM---PEERgLY---VKQGVAsqliyLGQL-AGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMS 146
Cdd:PRK13639 81 GIVfqnPDDQ-LFaptVEEDVA-----FGPLnLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 147 RPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRS 218
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-158 |
1.22e-32 |
|
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: 117.36 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 17 VDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGYMPEERGLYVKQGVASQL 92
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDErkslRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 93 IYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLE----SLSLGNQQRVQIAAAVMSRPQALILDEPFS 158
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-216 |
1.87e-32 |
|
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: 119.75 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD--RRTFGYMPEE 79
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPvqERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 80 RGLY----VKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:cd03296 83 YALFrhmtVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 156 PFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRlHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
2.08e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 120.68 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRF-GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGY 75
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENirevRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEERGLYVKQGVASQLIYLGQL-AGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILD 154
Cdd:PRK13652 83 VFQNPDDQIFSPTVEQDIAFGPInLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 155 EPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-207 |
2.41e-32 |
|
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: 118.66 E-value: 2.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRF-GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRP-------ATVADRRTF 73
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 74 GYMPEERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALIL 153
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 154 DEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRV 207
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-216 |
3.20e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 118.70 E-value: 3.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAvdQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATvadrrtfGYMPEER 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT-------ALPPAER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 G-------------LYVKQGVAsqliyLGQLAGMS-RPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAA-VM 145
Cdd:COG3840 72 PvsmlfqennlfphLTVAQNIG-----LGLRPGLKlTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARClVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 146 SRPqALILDEPFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:COG3840 147 KRP-ILLLDEPFSALDPALRQEMLDLVDElCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-216 |
4.35e-32 |
|
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: 119.86 E-value: 4.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 14 HTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD-------RRTFGY---MPEergly 83
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKkkklkdlRKKVGLvfqFPE----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 84 vkqgvaSQL--------IYLGQLA-GMSRPEARRSVTELLERFGLADRAKDKleS---LSLGNQQRVQIAAAVMSRPQAL 151
Cdd:TIGR04521 93 ------HQLfeetvykdIAFGPKNlGLSEEEAEERVKEALELVGLDEEYLER--SpfeLSGGQMRRVAIAGVLAMEPEVL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 152 ILDEPFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:TIGR04521 165 ILDEPTAGLDPKGRKEILDLFKRlHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-216 |
4.74e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 121.09 E-value: 4.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATV---ADRRTFGYMPE 78
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPArarLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 79 ERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFS 158
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1450037824 159 GLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-216 |
5.28e-32 |
|
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: 118.05 E-value: 5.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQI-----HGGQVLWQGRpatvaDRRTFGYM 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGK-----DIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEErgLYVKQGVASQL-------IY----LG-QLAGM-SRPEARRSVTELLERFGLADRAKDKLESLSL--GNQQRVQIA 141
Cdd:cd03260 76 VLE--LRRRVGMVFQKpnpfpgsIYdnvaYGlRLHGIkLKEELDERVEEALRKAALWDEVKDRLHALGLsgGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 142 AAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTREgVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-191 |
1.78e-31 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 115.60 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 12 GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRP------ATVADRRTFGYM---PEERGL 82
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPldysrkGLLERRQRVGLVfqdPDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 83 Y--VKQGVASQLIYLGqlagMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGL 160
Cdd:TIGR01166 83 AadVDQDVAFGPLNLG----LSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|.
gi 1450037824 161 DPTSVDVMADLLREHTREGVPVLFSSHQLDL 191
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAEGMTVVISTHDVDL 189
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
7-220 |
5.00e-31 |
|
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: 118.68 E-value: 5.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 7 LTRRFGDHTAvdQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQ-----VLWQGRPATV---ADRRTFGYMPE 78
Cdd:TIGR02142 5 FSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEivlngRTLFDSRKGIflpPEKRRIGYVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 79 ERGLYVKQGVASQLIYlgqlaGMSR--PEARR----SVTELLERFGLADRAKDKLeslSLGNQQRVQIAAAVMSRPQALI 152
Cdd:TIGR02142 83 EARLFPHLSVRGNLRY-----GMKRarPSERRisfeRVIELLGIGHLLGRLPGRL---SGGEKQRVAIGRALLSSPRLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450037824 153 LDEPFSGLD-PTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRSAG 220
Cdd:TIGR02142 155 MDEPLAALDdPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-206 |
6.85e-31 |
|
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: 115.04 E-value: 6.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRF-GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRP-------ATVADRRT 72
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDvnrlrgrQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 73 FGYMPEERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALI 152
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 153 LDEPFSGLDP-TSVDVMaDLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGR 206
Cdd:TIGR02673 161 ADEPTGNLDPdLSERIL-DLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-216 |
7.52e-31 |
|
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: 115.57 E-value: 7.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLL-QIHGGQVLWQGRP---ATVAD-RRTFG- 74
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERrggEDVWElRKRIGl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 75 --------YMPEERGLYVkqgVASQL---IYLGQLAGmsrPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAA 143
Cdd:COG1119 83 vspalqlrFPRDETVLDV---VLSGFfdsIGLYREPT---DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 144 VMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVP-VLFSSHQL-DLVDRLSDGLvVLSKGRVVAQGTAEEL 216
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPtLVLVTHHVeEIPPGITHVL-LLKDGRVVAAGPKEEV 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
1.28e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.10 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHT-AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAdRRTFGYMPEE 79
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYS-RKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 80 RGLyVKQGVASQL--------IYLGQL-AGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQA 150
Cdd:PRK13636 84 VGM-VFQDPDNQLfsasvyqdVSFGAVnLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 151 LILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-216 |
1.52e-30 |
|
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: 115.43 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 5 QELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRR------------- 71
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrrkkismv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 72 --TFGYMPEergLYVKQGVASQLiylgQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQ 149
Cdd:cd03294 108 fqSFALLPH---RTVLENVAFGL----EVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPD 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1450037824 150 ALILDEPFSGLDPTSVDVMAD-LLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:cd03294 181 ILLMDEAFSALDPLIRREMQDeLLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-215 |
2.64e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.48 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGR------PATVADRRtfG 74
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwsPAELARRR--A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 75 YMPEERGL----YVKQGVASQLIYLGQlagmSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIA------AAV 144
Cdd:PRK13548 80 VLPQHSSLsfpfTVEEVVAMGRAPHGL----SRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArvlaqlWEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 145 MSRPQALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEE 215
Cdd:PRK13548 156 DGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-215 |
4.62e-30 |
|
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: 113.20 E-value: 4.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTaVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATV--ADRRTFGYMPEE 79
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNlpPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 80 RGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSG 159
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 160 LDP-TSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEE 215
Cdd:cd03299 160 LDVrTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-256 |
6.71e-30 |
|
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: 115.58 E-value: 6.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQeLTRRFGDHTAvdQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFgyMP-EE 79
Cdd:COG4148 2 MLEVD-FRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIF--LPpHR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 80 RGL-YVKQ--------GVASQLIYlgqlaGMSR---PEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSR 147
Cdd:COG4148 77 RRIgYVFQearlfphlSVRGNLLY-----GRKRaprAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 148 PQALILDEPFSGLD-PTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELrSAGPCRHRI 226
Cdd:COG4148 152 PRLLLMDEPLAALDlARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV-LSRPDLLPL 230
|
250 260 270
....*....|....*....|....*....|
gi 1450037824 227 VVSSDAGWVrdLSGvHVVDVDGTAALVELA 256
Cdd:COG4148 231 AGGEEAGSV--LEA-TVAAHDPDYGLTRLA 257
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-221 |
1.15e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.49 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGrpATVADRRTfgympEER 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKV-----DER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 GLYVKQGVASQLIYL--------------GQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMS 146
Cdd:PRK09493 74 LIRQEAGMVFQQFYLfphltalenvmfgpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450037824 147 RPQALILDEPFSGLDP----TSVDVMADLlrehTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRSAGP 221
Cdd:PRK09493 154 KPKLMLFDEPTSALDPelrhEVLKVMQDL----AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPP 228
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-216 |
1.27e-29 |
|
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: 114.75 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVA--DRRTFGYMPEE 79
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLppQKRDYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 80 RGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADrAKDKLES-LSLGNQQRVQIAAAVMSRPQALILDEPFS 158
Cdd:TIGR03265 85 YALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPG-SERKYPGqLSGGQQQRVALARALATSPGLLLLDEPLS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 159 GLDPtsvdvmadLLREHTRE---------GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:TIGR03265 164 ALDA--------RVREHLRTeirqlqrrlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEI 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-207 |
1.58e-29 |
|
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: 111.47 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATvADRRTFGYMPEERG 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 82 -----------LYVKQGVASQLIylgQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQA 150
Cdd:cd03262 80 mvfqqfnlfphLTVLENITLAPI---KVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 151 LILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRV 207
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-223 |
1.62e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 115.71 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFG----YM 76
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASrrvaSV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEERGLYVKQGVaSQLIYLGQLAGMSR-----PEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQAL 151
Cdd:PRK09536 83 PQDTSLSFEFDV-RQVVEMGRTPHRSRfdtwtETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 152 ILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRSAGPCR 223
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLR 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-220 |
1.68e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.41 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRP-ATVADR---RTFGYM 76
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPiSMLSSRqlaRRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEE----RGLYVKQGVA----SQLIYLGQLAGmsrpEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRP 148
Cdd:PRK11231 82 PQHhltpEGITVRELVAygrsPWLSLWGRLSA----EDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 149 QALILDEPFSGLDPT-SVDVMaDLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRSAG 220
Cdd:PRK11231 158 PVVLLDEPTTYLDINhQVELM-RLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-216 |
2.87e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.89 E-value: 2.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRfgdhTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD-----RRTFGY 75
Cdd:COG1129 256 VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSprdaiRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEER---GLYVKQGVASQLIY--LGQLAG---MSRPEARRSVTELLERFGL-ADRAKDKLESLSLGNQQRVQIAAAVMS 146
Cdd:COG1129 332 VPEDRkgeGLVLDLSIRENITLasLDRLSRgglLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 147 RPQALILDEPFSGldptsVDVMA-----DLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:COG1129 412 DPKVLILDEPTRG-----IDVGAkaeiyRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-216 |
3.15e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 111.52 E-value: 3.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGR-----PATVADRRTFGYM 76
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEERGLYVKQGVASQLIYLGQL-AGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 156 PFSGLDPTSVDVMADLLrEHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK10895 164 PFAGVDPISVIDIKRII-EHLRDsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
12-216 |
4.77e-29 |
|
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: 113.41 E-value: 4.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 12 GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD--------RRTFGYMPEERGLY 83
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSpvelrevrRKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 84 VKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPT 163
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 164 SVDVMAD-LLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:TIGR01186 164 IRDSMQDeLKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEI 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-208 |
6.65e-29 |
|
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: 109.65 E-value: 6.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRpaTVADRRtfgymPEERG 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR--DVTDLP-----PKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 82 ---------LYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALI 152
Cdd:cd03301 74 iamvfqnyaLYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 153 LDEPFSGLDPT-SVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVV 208
Cdd:cd03301 154 MDEPLSNLDAKlRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-203 |
9.62e-29 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 109.12 E-value: 9.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATvADRRTFgympeer 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR-RQRDEY------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 glyvkqgvASQLIYLGQLAG----------------MSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAV 144
Cdd:PRK13538 73 --------HQDLLYLGHQPGikteltalenlrfyqrLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLW 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1450037824 145 MSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQldLVDRLSDGLVVLS 203
Cdd:PRK13538 145 LTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQ--DLPVASDKVRKLR 201
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-216 |
1.50e-28 |
|
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: 114.40 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGD----HTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQ----IHGGQVLWQGRPATVADRRT 72
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 73 fgyMPEERG----------------LYVkqgVASQLIYLGQL-AGMSRPEARRSVTELLERFGLADrAKDKLES----LS 131
Cdd:COG4172 86 ---LRRIRGnriamifqepmtslnpLHT---IGKQIAEVLRLhRGLSGAAARARALELLERVGIPD-PERRLDAyphqLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 132 LGNQQRVQIAAAVMSRPQALILDEPFSGLDPTS----VDVMADLLREHtreGVPVLFSSHQLDLVDRLSDGLVVLSKGRV 207
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVqaqiLDLLKDLQREL---GMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
....*....
gi 1450037824 208 VAQGTAEEL 216
Cdd:COG4172 236 VEQGPTAEL 244
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-216 |
2.66e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 109.71 E-value: 2.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADR---------R 71
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllalrqqvA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 72 TFGYMPEERGLYVKqgVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQAL 151
Cdd:PRK13638 81 TVFQDPEQQIFYTD--IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 152 ILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-218 |
3.99e-28 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 110.98 E-value: 3.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTtmrmimGLLQIH-----GGQVLWQGRPATV---ADRRTF 73
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAHv*gpdAGRRPWRF*TWCAnrrALRRTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 74 G-YMPEERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALI 152
Cdd:NF000106 88 G*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 153 LDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRS 218
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-220 |
5.35e-28 |
|
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: 113.39 E-value: 5.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHT--AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGY 75
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDpaslRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEERGLY---VKQGVAsqliylgqlagMSRPEARRS-VTELLERFGLAD---RAKDKLE--------SLSLGNQQRVQI 140
Cdd:COG2274 554 VLQDVFLFsgtIRENIT-----------LGDPDATDEeIIEAARLAGLHDfieALPMGYDtvvgeggsNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 141 AAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTReGVPVLFSSHQLDLVdRLSDGLVVLSKGRVVAQGTAEELRSAG 220
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-221 |
5.45e-28 |
|
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: 112.93 E-value: 5.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGD-HTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFgympeer 80
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW------- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 glyvkqgvASQLIYLGQ----LAG-------MSRPEA-RRSVTELLERFGLAD---RAKDKLES--------LSLGNQQR 137
Cdd:COG4988 410 --------RRQIAWVPQnpylFAGtirenlrLGRPDAsDEELEAALEAAGLDEfvaALPDGLDTplgeggrgLSGGQAQR 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 138 VQIAAAVMSRPQALILDEPFSGLDPTS----VDVMADLLREHTregvpVLFSSHQLDLVdRLSDGLVVLSKGRVVAQGTA 213
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETeaeiLQALRRLAKGRT-----VILITHRLALL-AQADRILVLDDGRIVEQGTH 555
|
....*...
gi 1450037824 214 EELRSAGP 221
Cdd:COG4988 556 EELLAKNG 563
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-206 |
1.14e-27 |
|
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: 106.75 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHT-------AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVL--WQGRPATVAD-- 69
Cdd:COG4778 4 LLEVENLSKTFTLHLqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrHDGGWVDLAQas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 70 --------RRTFGY-------MPEERGLYVkqgVASQLIylgqLAGMSRPEARRSVTELLERFGLADRakdkLESL---- 130
Cdd:COG4778 84 preilalrRRTIGYvsqflrvIPRVSALDV---VAEPLL----ERGVDREEARARARELLARLNLPER----LWDLppat 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 131 -SLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGR 206
Cdd:COG4778 153 fSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-216 |
1.64e-27 |
|
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: 107.52 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRF--GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQV------------LWQGR---- 63
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVtvdgldtldeenLWEIRkkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 64 -----P------ATVADRRTFGymPEERGLyvkqgvasqliylgqlagmSRPEARRSVTELLERFGLADRAKDKLESLSL 132
Cdd:TIGR04520 81 mvfqnPdnqfvgATVEDDVAFG--LENLGV-------------------PREEMRKRVDEALKLVGMEDFRDREPHLLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 133 GNQQRVQIAAAVMSRPQALILDEPFSGLDPTS-VDVMADLLREHTREGVPVLFSSHQLDLVdRLSDGLVVLSKGRVVAQG 211
Cdd:TIGR04520 140 GQKQRVAIAGVLAMRPDIIILDEATSMLDPKGrKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEG 218
|
....*
gi 1450037824 212 TAEEL 216
Cdd:TIGR04520 219 TPREI 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-208 |
4.00e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.15 E-value: 4.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWqGrpATVadrrTFGYMPEER 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-G--ETV----KIGYFDQHQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 -GLYVKQGVasqLIYLGQLA-GMSRPEARRsvteLLERFGLA-DRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPF 157
Cdd:COG0488 388 eELDPDKTV---LDELRDGApGGTEQEVRG----YLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 158 SGLDPTSVDVMADLLREHtrEGVpVLFSSHQLDLVDRLSDGLVVLSKGRVV 208
Cdd:COG0488 461 NHLDIETLEALEEALDDF--PGT-VLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-188 |
5.41e-27 |
|
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: 104.36 E-value: 5.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPatvadrrtfgyMPEERG 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP-----------LAEQRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 82 LYvkqgvASQLIYLGQLAGMsRPE----------------ARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVM 145
Cdd:TIGR01189 70 EP-----HENILYLGHLPGL-KPElsalenlhfwaaihggAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1450037824 146 SRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQ 188
Cdd:TIGR01189 144 SRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQ 186
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-220 |
6.62e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.87 E-value: 6.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHT--AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRP---ATVAD-RRTFGY 75
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseETVWDvRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 M---PEER--GLYVKQGVASQLiylgQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQA 150
Cdd:PRK13635 86 VfqnPDNQfvGATVQDDVAFGL----ENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 151 LILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRlSDGLVVLSKGRVVAQGTAEELRSAG 220
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-216 |
6.86e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 107.12 E-value: 6.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRF-----------GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADR 70
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 71 RtfgympEERGL-----------Y--------VKQGVASQLIYLGQLagmSRPEARRSVTELLERFGLADRAKDKL--Es 129
Cdd:COG4608 88 R------ELRPLrrrmqmvfqdpYaslnprmtVGDIIAEPLRIHGLA---SKAERRERVAELLELVGLRPEHADRYphE- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 130 LSLGNQQRVQIAAAVMSRPQALILDEPFSGLDpTSV-----DVMADLLREHtreGVPVLFSSHQLDLVDRLSDGLVVLSK 204
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALD-VSIqaqvlNLLEDLQDEL---GLTYLFISHDLSVVRHISDRVAVMYL 233
|
250
....*....|..
gi 1450037824 205 GRVVAQGTAEEL 216
Cdd:COG4608 234 GKIVEIAPRDEL 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-216 |
9.30e-27 |
|
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: 109.00 E-value: 9.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRF-----------GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQiHGGQVLWQGRPATVADR 70
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 71 RT---------------FGY----MPEER----GLYVKQgvasqliylgqlAGMSRPEARRSVTELLERFGLADRAKDKL 127
Cdd:COG4172 355 RAlrplrrrmqvvfqdpFGSlsprMTVGQiiaeGLRVHG------------PGLSAAERRARVAEALEEVGLDPAARHRY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 128 --EsLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDptsVDVMA---DLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVV 201
Cdd:COG4172 423 phE-FSGGQRQRIAIARALILEPKLLVLDEPTSALD---VSVQAqilDLLRDLQREhGLAYLFISHDLAVVRALAHRVMV 498
|
250
....*....|....*
gi 1450037824 202 LSKGRVVAQGTAEEL 216
Cdd:COG4172 499 MKDGKVVEQGPTEQV 513
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-216 |
1.12e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 108.86 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQiHG---GQVLWQGRPATVAD-RRTfgym 76
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP-HGtyeGEIIFEGEELQASNiRDT---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 pEERGL--------YVKQGVASQLIYLGQLAG----MSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAV 144
Cdd:PRK13549 80 -ERAGIaiihqelaLVKELSVLENIFLGNEITpggiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 145 MSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
10-211 |
1.44e-26 |
|
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: 103.34 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 10 RFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD--RRTFGYMPEERGLYVKQG 87
Cdd:cd03298 7 RFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPpaDRPVSMLFQENNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 88 VAsQLIYLGQLAGMS-RPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVD 166
Cdd:cd03298 87 VE-QNVGLGLSPGLKlTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1450037824 167 VMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG 211
Cdd:cd03298 166 EMLDLVLDlHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-215 |
4.21e-26 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 103.00 E-value: 4.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQiHGGQVLWQGRP------ATVADRRtfGYMPEerglyvkQGVAS--- 90
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPlsdwsaAELARHR--AYLSQ-------QQSPPfam 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 91 ---QLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVM-------SRPQALILDEPFSGL 160
Cdd:COG4138 85 pvfQYLALHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 161 DPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEE 215
Cdd:COG4138 165 DVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-216 |
5.65e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 104.80 E-value: 5.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRpaTVADR----RTFGYMP 77
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE--DVTHRsiqqRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 78 EERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLA---DRAKDKLeslSLGNQQRVQIAAAVMSRPQALILD 154
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAgfeDRYVDQI---SGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 155 EPFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRElQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-220 |
6.71e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 103.27 E-value: 6.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFG---DHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTF 73
Cdd:PRK13650 4 IIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwdiRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 74 GYM---PEER--GLYVKQGVASQLiylgQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRP 148
Cdd:PRK13650 84 GMVfqnPDNQfvGATVEDDVAFGL----ENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 149 QALILDEPFSGLDPTS-VDVMADLLREHTREGVPVLFSSHQLDLVdRLSDGLVVLSKGRVVAQGTAEELRSAG 220
Cdd:PRK13650 160 KIIILDEATSMLDPEGrLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRG 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
9-215 |
1.58e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 101.31 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 9 RRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTfGYMPEERGLyvkqgv 88
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLELGA-GFHPELTGR------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 89 asQLIYL-GQLAGMSRPEARRSVTELLErF-GLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEpfsgldptsvd 166
Cdd:COG1134 107 --ENIYLnGRLLGLSRKEIDEKFDEIVE-FaELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE----------- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 167 VMA-----------DLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEE 215
Cdd:COG1134 173 VLAvgdaafqkkclARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-210 |
2.67e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 101.48 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFG----DHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATV--ADR---- 70
Cdd:COG4525 3 MLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGpgADRgvvf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 71 RTFGYMPeerGLYVKQGVASQLiylgQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQA 150
Cdd:COG4525 83 QKDALLP---WLNVLDNVAFGL----RLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 151 LILDEPFSGLDPTSVDVMADL-LREHTREGVPVLFSSHQLDLVDRLSDGLVVLSK--GRVVAQ 210
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELlLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVER 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-208 |
3.94e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.93 E-value: 3.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPAT--VADRrtfGYMPE 78
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpGAER---GVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 79 ERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFS 158
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 159 GLDPTSVDVMAD-LLREHTREGVPVLFSSHQLDLVDRLSDGLVVLS--KGRVV 208
Cdd:PRK11248 158 ALDAFTREQMQTlLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVV 210
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
16-216 |
4.52e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 100.98 E-value: 4.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 16 AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGYM---PEER--GLYVKQ 86
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNfeklRKHIGIVfqnPDNQfvGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 87 GVASQLiylgQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVD 166
Cdd:PRK13648 104 DVAFGL----ENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 167 VMADLLREHTRE-GVPVLFSSHqlDLVDRL-SDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13648 180 NLLDLVRKVKSEhNITIISITH--DLSEAMeADHVIVMNKGTVYKEGTPTEI 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-214 |
4.88e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.09 E-value: 4.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMI-------MGLLQIHGGQVLWQGRP---ATVADRR 71
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIAGHQFDFSQKPsekAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 72 TFGYMPEERGLYVKQGVASQLIYLG-QLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQA 150
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 151 LILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAE 214
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-211 |
7.95e-25 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 99.14 E-value: 7.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 10 RFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTfGYMPEERGLyvkqgva 89
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGG-GFNPELTGR------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 90 sQLIYL-GQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVM 168
Cdd:cd03220 103 -ENIYLnGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1450037824 169 ADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG 211
Cdd:cd03220 182 QRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-207 |
8.24e-25 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 97.89 E-value: 8.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRrfgdHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATV-----ADRRTFGY 75
Cdd:cd03215 4 VLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRrsprdAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEER---GLYVKQGVASQLIyLGQLagmsrpearrsvtellerfgladrakdklesLSLGNQQRVQIAAAVMSRPQALI 152
Cdd:cd03215 80 VPEDRkreGLVLDLSVAENIA-LSSL-------------------------------LSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 153 LDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRV 207
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-188 |
1.18e-24 |
|
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: 97.95 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPatvadrrtfgyMPEERG 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP-----------LDFQRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 82 LYvkqgvASQLIYLGQLAGMS-------------RPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRP 148
Cdd:cd03231 70 SI-----ARGLLYLGHAPGIKttlsvlenlrfwhADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1450037824 149 QALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQ 188
Cdd:cd03231 145 PLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
14-237 |
1.30e-24 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 99.96 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 14 HTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTF-GYMPEERGLYVKQGVASQL 92
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLvAYVPQSEEVDWSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 93 IYL----GQLAGMSRPEA--RRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVD 166
Cdd:PRK15056 100 VVMmgryGHMGWLRRAKKrdRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450037824 167 VMADLLREHTREGVPVLFSSHQLDLVDRLSDgLVVLSKGRVVAQG------TAEELRSA--GPCRHRIVVSSDAGWVRD 237
Cdd:PRK15056 180 RIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGptettfTAENLELAfsGVLRHVALNGSEESIITD 257
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-208 |
2.08e-24 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 98.02 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRF-GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD-------RRT 72
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnrevpflRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 73 FGYMPEERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALI 152
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 153 LDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVV 208
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-214 |
2.14e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.55 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMI-------MGLLQIHGGQVLWQGRP---ATVADRR 71
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNHFDFSKTPsdkAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 72 TFGYMPEERGLYVKQGVASQLIYLG-QLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQA 150
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 151 LILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAE 214
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-220 |
3.30e-24 |
|
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: 97.68 E-value: 3.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 12 GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGYMPEERGLYvkQG 87
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkslRSMIGVVLQDTFLF--SG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 88 VASQLIYLGqlagmsRPEARRSV----------TELLERF--GLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:cd03254 92 TIMENIRLG------RPNATDEEvieaakeagaHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 156 PFSGLDP-TSVDVMADLLRehTREGVPVLFSSHQLDLVdRLSDGLVVLSKGRVVAQGTAEELRSAG 220
Cdd:cd03254 166 ATSNIDTeTEKLIQEALEK--LMKGRTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-215 |
3.33e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.97 E-value: 3.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 16 AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG-----RPATVADRR-----TFGYmPEERgLYvK 85
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKLSDIRkkvglVFQY-PEYQ-LF-E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 86 QGVASQLIYLGQLAGMSRPEARRSVTELLERFGLA-DRAKDKLE-SLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPT 163
Cdd:PRK13637 99 ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 164 SVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEE 215
Cdd:PRK13637 179 GRDEILNKIKElHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-216 |
3.36e-24 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 101.83 E-value: 3.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQiHG---GQVLWQGRPATVADRRTfgymP 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYP-HGtwdGEIYWSGSPLKASNIRD----T 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 78 EERGL--------YVKQGVASQLIYLGQ---LAG--MSRPEARRSVTELLERFGL-ADRAKDKLESLSLGNQQRVQIAAA 143
Cdd:TIGR02633 76 ERAGIviihqeltLVPELSVAENIFLGNeitLPGgrMAYNAMYLRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 144 VMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-209 |
3.66e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 101.53 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRP---ATVADRRTFG---- 74
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfASTTAALAAGvaii 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 75 -----YMPEerglyvkQGVASQLiYLGQL---AGM-SRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVM 145
Cdd:PRK11288 85 yqelhLVPE-------MTVAENL-YLGQLphkGGIvNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 146 SRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVA 209
Cdd:PRK11288 157 RNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-216 |
3.98e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 98.16 E-value: 3.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLL----------QIHGGQVLWQGRPA--TVA 68
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdksagshiELLGRTVQREGRLArdIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 69 DRRTFGYMPEERGLYVKQGVASQLIyLGQLAGMS---------RPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQ 139
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVL-IGALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1450037824 140 IAAAVMSRPQALILDEPFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-206 |
4.52e-24 |
|
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: 95.53 E-value: 4.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 12 GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGYMPEERGLYvkqg 87
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDleslRKNIAYVPQDPFLF---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 88 vasqliylgqlagmsrpeaRRSVTELLerfgladrakdklesLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTS--- 164
Cdd:cd03228 89 -------------------SGTIRENI---------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETeal 134
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1450037824 165 -VDVMADLLREHTregvpVLFSSHQLDLVdRLSDGLVVLSKGR 206
Cdd:cd03228 135 iLEALRALAKGKT-----VIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-219 |
5.93e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 101.32 E-value: 5.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRF----GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLL-----QIHGGQVLWQGRPATVADRR 71
Cdd:PRK15134 5 LLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvVYPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 72 TFGYMPEERGLYVKQGVASQLIYL----GQLA-------GMSRPEARRSVTELLERFGL---ADRAKDKLESLSLGNQQR 137
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEPMVSLNPLhtleKQLYevlslhrGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 138 VQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
...
gi 1450037824 217 RSA 219
Cdd:PRK15134 245 FSA 247
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-194 |
1.10e-23 |
|
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: 95.76 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 4 VQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG--------RPATVADRRTFGY 75
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGqetpplnsKKASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1450037824 156 PFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDR 194
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQ 199
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-216 |
1.18e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.11 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHT-AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGYM 76
Cdd:PRK13647 5 IEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENekwvRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEERGLYVKQGVASQLIYLGQL-AGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:PRK13647 85 FQDPDDQVFSSTVWDDVAFGPVnMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 156 PFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-218 |
1.19e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 96.72 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATvadrrtfgYMPEER 80
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLT--------GLDEHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 -----------------GLYVKQ----------GVASQLiylgqLAGMSRPEARRsVTELLERFGLADRAKDKLESLSLG 133
Cdd:COG4674 82 iarlgigrkfqkptvfeELTVFEnlelalkgdrGVFASL-----FARLTAEERDR-IEEVLETIGLTDKADRLAGLLSHG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 134 NQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLRE----HTregvpVLFSSHQLDLVDRLSDGLVVLSKGRVVA 209
Cdd:COG4674 156 QKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSlagkHS-----VVVVEHDMEFVRQIARKVTVLHQGSVLA 230
|
....*....
gi 1450037824 210 QGTAEELRS 218
Cdd:COG4674 231 EGSLDEVQA 239
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-211 |
1.78e-23 |
|
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: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHG---GQVLWQGRPATVAD-RRTFGYMPEERGLYVKQGVASQLIYL 95
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQfQKCVAYVRQDDILLPGLTVRETLTYT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 96 GQLAGMSR-PEARRSV---TELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADL 171
Cdd:cd03234 106 AILRLPRKsSDAIRKKrveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVST 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1450037824 172 LREHTREGVPVLFSSHQ--LDLVdRLSDGLVVLSKGRVVAQG 211
Cdd:cd03234 186 LSQLARRNRIVILTIHQprSDLF-RLFDRILLLSSGEIVYSG 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-215 |
3.15e-23 |
|
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: 95.19 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDH----TAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRrtfgym 76
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 pEERGLYVKQGV-----ASQLIylgqlAGMS-------------RPEARRSVTELLERFGLADRAKDKLESLSLGNQQRV 138
Cdd:COG4181 82 -DARARLRARHVgfvfqSFQLL-----PTLTalenvmlplelagRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1450037824 139 QIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRlSDGLVVLSKGRVVAQGTAEE 215
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-216 |
3.43e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 95.62 E-value: 3.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 4 VQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFG----YMPEE 79
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFArkvaYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 80 ----RGLYVKQGVA-SQLIYLGQLaGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILD 154
Cdd:PRK10575 94 lpaaEGMTVRELVAiGRYPWHGAL-GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 155 EPFSGLD-PTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK10575 173 EPTSALDiAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-206 |
4.69e-23 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 92.13 E-value: 4.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWqgrpatvADRRTFGYMPeerg 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-------GSTVKIGYFE---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 82 lyvkqgvasqliylgQLAGmsrpearrsvtellerfgladrakdkleslslGNQQRVQIAAAVMSRPQALILDEPFSGLD 161
Cdd:cd03221 70 ---------------QLSG--------------------------------GEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1450037824 162 PTSVDVMADLLREHTREgvpVLFSSHQLDLVDRLSDGLVVLSKGR 206
Cdd:cd03221 103 LESIEALEEALKEYPGT---VILVSHDRYFLDQVATKIIELEDGK 144
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-221 |
6.79e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 98.31 E-value: 6.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 12 GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPatVAD------RRTFGYMPEERGLY-- 83
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD--IRDltleslRRQIGVVPQDTFLFsg 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 84 -VKQGVAsqliylgqlagMSRPEARRS-VTELLERFGLADRAK---DKLE--------SLSLGNQQRVQIAAAVMSRPQA 150
Cdd:COG1132 429 tIRENIR-----------YGRPDATDEeVEEAAKAAQAHEFIEalpDGYDtvvgergvNLSGGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 151 LILDEPFSGLDPTS----VDVMADLLREHTregvpVLFSSHQLDLVdRLSDGLVVLSKGRVVAQGTAEELRSAGP 221
Cdd:COG1132 498 LILDEATSALDTETealiQEALERLMKGRT-----TIVIAHRLSTI-RNADRILVLDDGRIVEQGTHEELLARGG 566
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-215 |
6.86e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 96.94 E-value: 6.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPAT--VADRRT------- 72
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIThvPAENRHvntvfqs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 73 ---FGYMPeerglyVKQGVASQLiylgQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQ 149
Cdd:PRK09452 95 yalFPHMT------VFENVAFGL----RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 150 ALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEE 215
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-219 |
9.83e-23 |
|
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: 95.64 E-value: 9.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 33 VGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATV--ADRRTFGYMPEERGLYVKQGVASQLIYLGQLAGMSRPEARRSV 110
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNvpPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 111 TELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMA-DLLREHTREGVPVLFSSHQL 189
Cdd:TIGR01187 82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQlELKTIQEQLGITFVFVTHDQ 161
|
170 180 190
....*....|....*....|....*....|
gi 1450037824 190 DLVDRLSDGLVVLSKGRVVAQGTAEELRSA 219
Cdd:TIGR01187 162 EEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-216 |
1.14e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.40 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELT-RRFGDHTAVDQVSFTVPDGQLIGFVG--GNGagKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTF----- 73
Cdd:COG3845 258 LEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGvaGNG--QSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlgv 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 74 GYMPEER-------GLYVKQGVASQLIYLGQLAG---MSRPEARRSVTELLERFGL-ADRAKDKLESLSLGNQQRVQIAA 142
Cdd:COG3845 336 AYIPEDRlgrglvpDMSVAENLILGRYRRPPFSRggfLDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILAR 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 143 AVMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:COG3845 416 ELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-216 |
1.21e-22 |
|
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: 97.53 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRF--GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGY 75
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDeddlRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEErglyvkqgvasqlIYL--GQLAG---MSRPEA-RRSVTELLERFGLAD---RAKDKLES--------LSLGNQQRV 138
Cdd:COG4987 414 VPQR-------------PHLfdTTLREnlrLARPDAtDEELWAALERVGLGDwlaALPDGLDTwlgeggrrLSGGERRRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1450037824 139 QIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVpVLFSSHQLDLVDRLsDGLVVLSKGRVVAQGTAEEL 216
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRT-VLLITHRLAGLERM-DRILVLEDGRIVEQGTHEEL 556
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-188 |
1.42e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.63 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADrrtfgympeer 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 glyvkqgVASQLIYLGQLAGMSRP---------------EARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVM 145
Cdd:PRK13539 71 -------VAEACHYLGHRNAMKPAltvaenlefwaaflgGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1450037824 146 SRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQ 188
Cdd:PRK13539 144 SNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-216 |
1.59e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.48 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 16 AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIH--------------GGQVLWQGRP---------------AT 66
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpnskitvdgitlTAKTVWDIREkvgivfqnpdnqfvgAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 67 VADRRTFGYmpEERGLyvkqgvasqliylgqlagmSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMS 146
Cdd:PRK13640 102 VGDDVAFGL--ENRAV-------------------PRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 147 RPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFS-SHQLDLVDrLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISiTHDIDEAN-MADQVLVLDDGKLLAQGSPVEI 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-216 |
2.15e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 93.49 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPAT----------VADRR 71
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 72 TFGYMpEERGLYVKQ--GVASQLIYLG-------QLAGMSRPEARRSVTELLERFGLADRAKDKLES-LSLGNQQRVQIA 141
Cdd:PRK10619 86 QLRLL-RTRLTMVFQhfNLWSHMTVLEnvmeapiQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 142 AAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-211 |
2.28e-22 |
|
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: 92.27 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 13 DHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVL------WQGRPATVadRRTFGYMPEERGLY--- 83
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLldgtdiRQLDPADL--RRNIGYVPQDVTLFygt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 84 VKQGVAsqliylgqlagMSRPEAR-RSVTELLERFGLADRAKD-----------KLESLSLGNQQRVQIAAAVMSRPQAL 151
Cdd:cd03245 94 LRDNIT-----------LGAPLADdERILRAAELAGVTDFVNKhpngldlqigeRGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 152 ILDEPFSGLDPTS----VDVMADLLREHTregvpVLFSSHQ---LDLVDRlsdgLVVLSKGRVVAQG 211
Cdd:cd03245 163 LLDEPTSAMDMNSeerlKERLRQLLGDKT-----LIIITHRpslLDLVDR----IIVMDSGRIVADG 220
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-216 |
2.38e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.13 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 17 VDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATV-ADRRTFGYMPEERGLyVKQGVASQL--- 92
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKKLRKKVSL-VFQFPEAQLfen 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 93 -----IYLGQLA-GMSRPEARRSVTELLERFGLADRAKDKLE-SLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSV 165
Cdd:PRK13641 102 tvlkdVEFGPKNfGFSEDEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 166 DVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13641 182 KEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-211 |
2.74e-22 |
|
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: 91.46 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 17 VDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHG--GQVLWQGRPatvADRRTF----GYMPEErglyvkqgvas 90
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRP---LDKRSFrkiiGYVPQD----------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 91 qLIYLGQLagmsrpearrSVTELLeRFGLadrakdKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMAD 170
Cdd:cd03213 91 -DILHPTL----------TVRETL-MFAA------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1450037824 171 LLREHTREGVPVLFSSHQL-DLVDRLSDGLVVLSKGRVVAQG 211
Cdd:cd03213 153 LLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-215 |
2.75e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 96.23 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTrrfgdHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATV---ADRRTFG--YM 76
Cdd:PRK10762 258 LKVDNLS-----GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrspQDGLANGivYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEER-------GLYVKQGVA-SQLIYLGQLAG-MSRPEARRSVTELLERFGLADRAKDK-LESLSLGNQQRVQIAAAVMS 146
Cdd:PRK10762 333 SEDRkrdglvlGMSVKENMSlTALRYFSRAGGsLKHADEQQAVSDFIRLFNIKTPSMEQaIGLLSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 147 RPQALILDEPFSGldptsVDVMA-----DLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEE 215
Cdd:PRK10762 413 RPKVLILDEPTRG-----VDVGAkkeiyQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQ 481
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-223 |
5.08e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.52 E-value: 5.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD--RRTFGYMPE 78
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPpyQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 79 ERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFS 158
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450037824 159 GLDPTSVDVM----ADLLRehtREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRSAGPCR 223
Cdd:PRK11607 179 ALDKKLRDRMqlevVDILE---RVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-216 |
7.01e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 93.23 E-value: 7.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 16 AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATvadrrtfgYMPEERGLYVKQGVasQLIYL 95
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLL--------GMKDDEWRAVRSDI--QMIFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 96 GQLAG---------------------MSRPEARRSVTELLERFGLadrakdkLESL--------SLGNQQRVQIAAAVMS 146
Cdd:PRK15079 106 DPLASlnprmtigeiiaeplrtyhpkLSRQEVKDRVKAMMLKVGL-------LPNLinryphefSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 147 RPQALILDEPFSGLDptsVDVMA---DLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK15079 179 EPKLIICDEPVSALD---VSIQAqvvNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-216 |
7.33e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 91.74 E-value: 7.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMI------------MGLLQIHGGQVLWQGRPATVA 68
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIDTARSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 69 DRRTFGYMPEERGLYVKQGVASQLIYlG--QLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMS 146
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIE-GpvIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 147 RPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-207 |
9.82e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.66 E-value: 9.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFGYMPEERG 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 82 LYVKQGVASqlIYLGqLAGMSRPEARRSvtelLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLD 161
Cdd:PRK11247 93 LPWKKVIDN--VGLG-LKGQWRDAALQA----LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1450037824 162 PTSVDVMADLL----REHtreGVPVLFSSHQLDLVDRLSDGLVVLSKGRV 207
Cdd:PRK11247 166 ALTRIEMQDLIeslwQQH---GFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-231 |
1.67e-21 |
|
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: 90.60 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 17 VDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVA--DR----RTFGYMPeerGLYVKQGVAs 90
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpDRmvvfQNYSLLP---WLTVRENIA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 91 qLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDP-TSVDVMA 169
Cdd:TIGR01184 77 -LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAlTRGNLQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 170 DLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRSAGPcRHRIVVSSD 231
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVPFPRP-RDRLEVVED 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-211 |
2.87e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 90.37 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFGyMPEER 80
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALS-EAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 GL------YVKQ--------------GVASQLIYLGQlagmsR--PEARRSVTELLERFGL-ADRAKDKLESLSLGNQQR 137
Cdd:PRK11701 85 RLlrtewgFVHQhprdglrmqvsaggNIGERLMAVGA-----RhyGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1450037824 138 VQIAAAVMSRPQALILDEPFSGLDptsVDVMA---DLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG 211
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLD---VSVQArllDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-216 |
3.47e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 89.55 E-value: 3.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGR-----PATVADRRTFGY 75
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEERGLYVKQGVASQLIYLGQLAGMSRPEAR-RSVTELLERfgLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILD 154
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQFQERiKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 155 EPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-215 |
5.48e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 89.76 E-value: 5.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFG-----DHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATvadrrtfgY 75
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT--------K 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEE-RGLYV-------KQGVASQLIYLGQLA-----GMSRPeARRSVT--------ELLERF--GLADRAKDKLESLSL 132
Cdd:COG1101 73 LPEYkRAKYIgrvfqdpMMGTAPSMTIEENLAlayrrGKRRG-LRRGLTkkrrelfrELLATLglGLENRLDTKVGLLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 133 GNQQRVQIAAAVMSRPQALILDEPFSGLDP-TSVDVMA---DLLREHtreGVPVLFSSHQ----LDLVDRlsdgLVVLSK 204
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPkTAALVLElteKIVEEN---NLTTLMVTHNmeqaLDYGNR----LIMMHE 224
|
250
....*....|.
gi 1450037824 205 GRVVAQGTAEE 215
Cdd:COG1101 225 GRIILDVSGEE 235
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-218 |
7.18e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 89.44 E-value: 7.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG-------RPATVADRRTF 73
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenipamsRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 74 GYMPEERGLYVKQGVASQLIY-LGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALI 152
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYpLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 153 LDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRS 218
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-216 |
7.48e-21 |
|
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: 88.89 E-value: 7.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMI--MGLL--------QIH-GGQVLWQGRPATVADR 70
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrMNDLvpgvriegKVLfDGQDIYDKKIDVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 71 RTFGYMPEERGLYVKQgVASQLIYLGQLAGM-SRPEARRSVTELLERFGLADRAKDKLE----SLSLGNQQRVQIAAAVM 145
Cdd:TIGR00972 82 RRVGMVFQKPNPFPMS-IYDNIAYGPRLHGIkDKKELDEIVEESLKKAALWDEVKDRLHdsalGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 146 SRPQALILDEPFSGLDPTSVDVMADLLREhTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQE-LKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQI 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-233 |
9.41e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 89.36 E-value: 9.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 7 LTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATV---ADRRTFgympeeRGly 83
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnrAQRKAF------RR-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 84 vkqgvASQLIY--------------------LGQLAGMSRPEARRSVTELLERFGLADRAKDKL-ESLSLGNQQRVQIAA 142
Cdd:PRK10419 90 -----DIQMVFqdsisavnprktvreiirepLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRpPQLSGGQLQRVCLAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 143 AVMSRPQALILDEPFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVaqgtaeELRSAGP 221
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKlQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV------ETQPVGD 238
|
250
....*....|..
gi 1450037824 222 CRHrivVSSDAG 233
Cdd:PRK10419 239 KLT---FSSPAG 247
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-216 |
1.63e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 89.78 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRF----GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHG---GQVLWQGRPATVADRRTF 73
Cdd:PRK09473 12 LLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 74 GYMPEER------------GLYVKqgVASQLIYLGQL-AGMSRPEARRSVTELLERFGLAD---RAKDKLESLSLGNQQR 137
Cdd:PRK09473 92 NKLRAEQismifqdpmtslNPYMR--VGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 138 VQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-218 |
1.69e-20 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 91.61 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHT--AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRP--ATVAD-RRTFGY 75
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSilTNISDvHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 156 PFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRS 218
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKS 2159
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-217 |
1.72e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 91.34 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 3 EVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRP-ATVADRRTFG----YMP 77
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDmADARHRRAVCpriaYMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 78 EERG--LYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLA---DRAKDKlesLSLGNQQRVQIAAAVMSRPQALI 152
Cdd:NF033858 83 QGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLApfaDRPAGK---LSGGMKQKLGLCCALIHDPDLLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450037824 153 LDEPFSGLDPTSV----DVMADLLREhtREGVPVLFSSHQLDLVDRLsDGLVVLSKGRVVAQGTAEELR 217
Cdd:NF033858 160 LDEPTTGVDPLSRrqfwELIDRIRAE--RPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELL 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-207 |
2.92e-20 |
|
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: 2.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 4 VQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVlwqgrpaTVADRRTFGYMPEERGLY 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-------SIPKGLRIGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 84 ----VKQGVASQLIYLGQL--------AGMSRPE--------------------ARRSVTELLERFGLADRAKD-KLESL 130
Cdd:COG0488 74 ddltVLDTVLDGDAELRALeaeleeleAKLAEPDedlerlaelqeefealggweAEARAEEILSGLGFPEEDLDrPVSEL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 131 SLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLRehTREGvPVLFSSHQLDLVDRLSDGLVVLSKGRV 207
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLK--NYPG-TVLVVSHDRYFLDRVATRILELDRGKL 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-220 |
4.05e-20 |
|
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: 86.77 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 16 AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGYMPEERGLY---VKQGV 88
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADpawlRRQVGVVLQENVLFnrsIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 89 AS--------QLIYLGQLAGmsrpeARRSVTELLERFG--LADRAKdkleSLSLGNQQRVQIAAAVMSRPQALILDEPFS 158
Cdd:cd03252 97 ALadpgmsmeRVIEAAKLAG-----AHDFISELPEGYDtiVGEQGA----GLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 159 GLDPTSVDV----MADLLREHTregvpVLFSSHQLDLVdRLSDGLVVLSKGRVVAQGTAEELRSAG 220
Cdd:cd03252 168 ALDYESEHAimrnMHDICAGRT-----VIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-188 |
5.06e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 85.77 E-value: 5.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPatvadrrtfgyMPEER 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS-----------IKKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 GLYVKqgvasQLIYLGQLAGMSRPEARRS--------------VTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMS 146
Cdd:PRK13540 70 CTYQK-----QLCFVGHRSGINPYLTLREnclydihfspgavgITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1450037824 147 RPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQ 188
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-215 |
5.69e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 86.53 E-value: 5.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQiHGGQVLWQGRP------ATVADRRTfgympeerglYVKQGVAS--- 90
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPleawsaAELARHRA----------YLSQQQTPpfa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 91 ----QLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVM-----SRP--QALILDEPFSG 159
Cdd:PRK03695 84 mpvfQYLTLHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 160 LDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEE 215
Cdd:PRK03695 164 LDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-219 |
6.01e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 87.87 E-value: 6.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHT----AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQiHGGQVLWQgrpATVADRRTFGYM 76
Cdd:PRK11022 3 LLNVDKLSVHFGDESapfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAE---KLEFNGQDLQRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PE-ERGLYVKQGVAsqLIY--------------------LGQLAGMSRPEARRSVTELLERFGLADRAKdKLE----SLS 131
Cdd:PRK11022 79 SEkERRNLVGAEVA--MIFqdpmtslnpcytvgfqimeaIKVHQGGNKKTRRQRAIDLLNQVGIPDPAS-RLDvyphQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 132 LGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQ 210
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLElQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
....*....
gi 1450037824 211 GTAEELRSA 219
Cdd:PRK11022 236 GKAHDIFRA 244
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-216 |
6.57e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 87.38 E-value: 6.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 16 AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVlwqgrpaTVADRR-TFGYMPEE-RGLYVKQGVA---- 89
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV-------TIGERViTAGKKNKKlKPLRKKVGIVfqfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 90 -SQL--------IYLGQLA-GMSRPEARRSVTELLERFGLAD--RAKDKLEsLSLGNQQRVQIAAAVMSRPQALILDEPF 157
Cdd:PRK13634 95 eHQLfeetvekdICFGPMNfGVSEEDAKQKAREMIELVGLPEelLARSPFE-LSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 158 SGLDPTSVDVMADLL-REHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13634 174 AGLDPKGRKEMMEMFyKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-216 |
6.68e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.22 E-value: 6.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATV--ADRRTFGYMPEE 79
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlhARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 80 RGLYVKQGVASQLIY-LGQLAGMSRPEA---RRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:PRK10851 83 YALFRHMTVFDNIAFgLTVLPRRERPNAaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 156 PFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQlHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-201 |
8.66e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 85.23 E-value: 8.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIH---GGQVLWQGRPATV--ADRRTFGY 75
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAlpAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEERGLYVKQGVASQLIYlGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAF-ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1450037824 156 PFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHqlDLVDRLSDGLVV 201
Cdd:COG4136 160 PFSKLDAALRAQFREFVFEQIRQrGIPALLVTH--DEEDAPAAGRVL 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-216 |
1.11e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 88.71 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRF-----GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVL------W--------- 60
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdeWvdmtkpgpd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 61 -QGRPatvadRRTFGYMPEERGLYVKQGVasqLIYLGQLAGMSRPE--ARRSVTELLERFGLAD-RAKDKLE----SLSL 132
Cdd:TIGR03269 359 gRGRA-----KRYIGILHQEYDLYPHRTV---LDNLTEAIGLELPDelARMKAVITLKMVGFDEeKAEEILDkypdELSE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 133 GNQQRVQIAAAVMSRPQALILDEPFSGLDP-TSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG 211
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPiTKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
....*
gi 1450037824 212 TAEEL 216
Cdd:TIGR03269 511 DPEEI 515
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-219 |
1.11e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.57 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRP---ATVADRRTFG-YM 76
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPcarLTPAKAHQLGiYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 -PEERGLYVKQGVASQLiylgqLAGMSRPEAR-RSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILD 154
Cdd:PRK15439 91 vPQEPLLFPNLSVKENI-----LFGLPKRQASmQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 155 EPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRSA 219
Cdd:PRK15439 166 EPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
1.25e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.83 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHT-----AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQ----------IHGGQVLWQGRPA 65
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKskygtiqvgdIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 66 TVADRRTFGYMPEERGL--YVKQGVASQL--------IYLGQLA-GMSRPEARRSVTELLERFGLADrakDKLE----SL 130
Cdd:PRK13631 101 TNPYSKKIKNFKELRRRvsMVFQFPEYQLfkdtiekdIMFGPVAlGVKKSEAKKLAKFYLNKMGLDD---SYLErspfGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 131 SLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQ 210
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
....*.
gi 1450037824 211 GTAEEL 216
Cdd:PRK13631 258 GTPYEI 263
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-196 |
1.46e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.25 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGD---HTAV-DQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRP------ATVADR 70
Cdd:PRK11629 5 LLQCDNLCKRYQEgsvQTDVlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmsklssAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 71 RT----FGY-----MPEERGLyvkQGVASQLIylgqLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIA 141
Cdd:PRK11629 85 RNqklgFIYqfhhlLPDFTAL---ENVAMPLL----IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 142 AAVMSRPQALILDEPFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLS 196
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGElNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-216 |
1.59e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 85.91 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQ---VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTF 73
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 74 GYM---PEERglYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQA 150
Cdd:PRK13642 84 GMVfqnPDNQ--FVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 151 LILDEPFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRlSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEiKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-208 |
2.72e-19 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 87.54 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQiHG---GQVLWQGRPATVADRRTfgymP 77
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGsyeGEILFDGEVCRFKDIRD----S 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 78 EERGLYV-KQGVA--SQL-----IYLG--QLAG--MSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVM 145
Cdd:NF040905 76 EALGIVIiHQELAliPYLsiaenIFLGneRAKRgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 146 SRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVV 208
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-211 |
4.10e-19 |
|
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: 84.50 E-value: 4.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFGYMPEER 80
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 GLYVKQGVASQLIYLGQLAGMS-------RPEA---------RRSVTELLERFGL-ADRAKDKLESLSLGNQQRVQIAAA 143
Cdd:TIGR02323 83 LMRTEWGFVHQNPRDGLRMRVSaganigeRLMAigarhygniRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450037824 144 VMSRPQALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG 211
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-218 |
4.74e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.65 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHT-AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGrpatvADRRTFGYMPEE 79
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG-----IDTGDFSKLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 80 RGL-----------YVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRP 148
Cdd:PRK13644 76 RKLvgivfqnpetqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 149 QALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVdRLSDGLVVLSKGRVVAQGTAEELRS 218
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-216 |
5.52e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 84.08 E-value: 5.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMI-------MGLLQIHGGQVLWQGRP---ATVADR 70
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCInlletpdSGEIRVGGEEIRLKPDRdgeLVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 71 RTFGYMPEERGLyVKQG--VASQLIYLG-------QLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIA 141
Cdd:COG4598 88 RQLQRIRTRLGM-VFQSfnLWSHMTVLEnvieapvHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450037824 142 AAVMSRPQALILDEPFSGLDPTSVD----VMADLlrehTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGevlkVMRDL----AEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-216 |
8.02e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 86.01 E-value: 8.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIH--GGQVL----------WQGRPATVAD 69
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIIyhvalcekcgYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 70 -----------------------------------RRTFGympeergLYVKQGVASQLIYLGQLAGMSRPEARRSVTELL 114
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsdklrrrirkriaimlQRTFA-------LYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 115 ERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVD 193
Cdd:TIGR03269 154 EMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEVIE 233
|
250 260
....*....|....*....|...
gi 1450037824 194 RLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTPDEV 256
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-218 |
1.09e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.90 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 16 AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGR--PATVADRRTFGYMPEERGLYVK-------Q 86
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaiPANLKKIKEVKRLRKEIGLVFQfpeyqlfQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 87 GVASQLIYLGQL-AGMSRPEARRSVTELLERFGLA-DRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPT- 163
Cdd:PRK13645 106 ETIEKDIAFGPVnLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKg 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 164 SVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRS 218
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-216 |
1.34e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 84.70 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 11 FGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLwqgrpatVADRRTFGYMPEERG--------- 81
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLF-------IGEKRMNDVPPAERGvgmvfqsya 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 82 LYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLD 161
Cdd:PRK11000 86 LYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1450037824 162 PT-SVDVMADLLREHTREGVPVLFSSHqlDLVD--RLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK11000 166 AAlRVQMRIEISRLHKRLGRTMIYVTH--DQVEamTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-216 |
1.34e-18 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 84.77 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 5 QELTRRFGDHTAVDQVSFTVPDGQLigFV--GGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD-------RRT--- 72
Cdd:COG4175 31 DEILEKTGQTVGVNDASFDVEEGEI--FVimGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSkkelrelRRKkms 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 73 -----FGYMPEergLYVKQGVAsqliyLG-QLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMS 146
Cdd:COG4175 109 mvfqhFALLPH---RTVLENVA-----FGlEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALAT 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 147 RPQALILDEPFSGLDPTSVDVMAD-LLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:COG4175 181 DPDILLMDEAFSALDPLIRREMQDeLLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEI 251
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-220 |
1.75e-18 |
|
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: 82.28 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHT--AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG---RPATVAD-RRTFGY 75
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTLASlRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEERGLYvkQGVASQLIYLGQLaGMSRPEARRS-----VTELLERF--GLADRAKDKLESLSLGNQQRVQIAAAVMSRP 148
Cdd:cd03251 81 VSQDVFLF--NDTVAENIAYGRP-GATREEVEEAaraanAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 149 QALILDEPFSGLDPTSVDVMADLLrEHTREGVPVLFSSHQLDLVdRLSDGLVVLSKGRVVAQGTAEELRSAG 220
Cdd:cd03251 158 PILILDEATSALDTESERLVQAAL-ERLMKNRTTFVIAHRLSTI-ENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
12-216 |
1.76e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 84.12 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 12 GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLwqgrpatVADRRTFGYMPEERG---------L 82
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIW-------IGGRVVNELEPADRDiamvfqnyaL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 83 YVKQGVASQLIYLGQLAGMSRPEARRSVTE---LLERFGLADRakdKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSG 159
Cdd:PRK11650 88 YPHMSVRENMAYGLKIRGMPKAEIEERVAEaarILELEPLLDR---KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 160 LDPT-SVDVMADLLREHTREGVPVLFSSH-QLD---LVDRlsdgLVVLSKGRVVAQGTAEEL 216
Cdd:PRK11650 165 LDAKlRVQMRLEIQRLHRRLKTTSLYVTHdQVEamtLADR----VVVMNGGVAEQIGTPVEV 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-202 |
1.89e-18 |
|
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: 85.03 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHT-AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFGympeER 80
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWR----DQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 GLYVKQgvaSQLIYLGQLA---GMSRPEARRS-VTELLERFGLADRAKDKLES-----------LSLGNQQRVQIAAAVM 145
Cdd:TIGR02857 398 IAWVPQ---HPFLFAGTIAeniRLARPDASDAeIREALERAGLDEFVAALPQGldtpigeggagLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 146 SRPQALILDEPFSGLDPTSVDVMADLLREhTREGVPVLFSSHQLDLVdRLSDGLVVL 202
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRA-LAQGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-216 |
2.20e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 84.31 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRP-ATVAD-------RRTF 73
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiAKISDaelrevrRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 74 GYMPEERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALIL 153
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 154 DEPFSGLDPTSVDVMAD-LLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDeLVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-216 |
2.48e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 83.48 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 16 AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRT---------------FGYM-PEE 79
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrqkiqivfqnpYGSLnPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 80 RglyVKQGVASQLIYLGQLagmSRPEARRSVTELLERFGL----ADRAKdklESLSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:PRK11308 110 K---VGQILEEPLLINTSL---SAAERREKALAMMAKVGLrpehYDRYP---HMFSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 156 PFSGLDpTSV-----DVMADLLREHtreGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK11308 181 PVSALD-VSVqaqvlNLMMDLQQEL---GLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
2.87e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 82.35 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHT--AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGrpaTVADRRTFGYMPE 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG---ITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 79 ERGLyVKQGVASQLIylGQLA------GM-----SRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSR 147
Cdd:PRK13632 84 KIGI-IFQNPDNQFI--GATVeddiafGLenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 148 PQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFS-SHQLDLVdRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-216 |
3.72e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.07 E-value: 3.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRtfgyMPEER 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK----LAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 GL---YVKQGVASQL-----IYLGQLAG--------MSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAV 144
Cdd:PRK09700 81 GIgiiYQELSVIDELtvlenLYIGRHLTkkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 145 MSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-216 |
4.71e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.83 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 17 VDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQ-IHGGQVLWQGRPATV-----ADRRTFGYMPEER---GLYVKQG 87
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIrnpqqAIAQGIAMVPEDRkrdGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 88 VASQ--LIYLGQLAGMSRPEARRSVTELLERFglaDRAKDK-------LESLSLGNQQRVQIAAAVMSRPQALILDEPFS 158
Cdd:PRK13549 358 VGKNitLAALDRFTGGSRIDDAAELKTILESI---QRLKVKtaspelaIARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 159 GldptsVDVMA-----DLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13549 435 G-----IDVGAkyeiyKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNL 492
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-215 |
5.36e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 82.61 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQeLTRRFGDHTAvdQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFgYMPEER 80
Cdd:PRK11144 1 MLELN-FKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIC-LPPEKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 GL-YVKQ--------GVASQLIYlgqlaGMSR--PEARRSVTE------LLERFGLadrakdkleSLSLGNQQRVQIAAA 143
Cdd:PRK11144 77 RIgYVFQdarlfphyKVRGNLRY-----GMAKsmVAQFDKIVAllgiepLLDRYPG---------SLSGGEKQRVAIGRA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 144 VMSRPQALILDEPFSGLD-PTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEE 215
Cdd:PRK11144 143 LLTAPELLLMDEPLASLDlPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-216 |
6.62e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 81.11 E-value: 6.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIH-----GGQVLWQGR-----PATVADRR 71
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQdifkmDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 72 T---FGYMPEERGLYVKQGVASQLiYLGQLAGmSRPEARRSVTELLERFGLADRAKDKLE----SLSLGNQQRVQIAAAV 144
Cdd:PRK14247 84 VqmvFQIPNPIPNLSIFENVALGL-KLNRLVK-SKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 145 MSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFsSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLV-THFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-216 |
8.92e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.86 E-value: 8.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHG------GQVLWQGRPATVAD----R 70
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIFQIDaiklR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 71 RTFGYMPEERGLYVKQGVASQLIYLGQLAGMS-RPEARRSVTELLERFGLADRAKDKLES----LSLGNQQRVQIAAAVM 145
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 146 SRPQALILDEPFSGLDPTSVDVMADLLREHTREgVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-219 |
8.94e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.22 E-value: 8.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 7 LTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGgQVLWQGRPATVADRRTFgyMPEERG----- 81
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQG-EIWFDGQPLHNLNRRQL--LPVRHRiqvvf 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 82 ----------LYVKQGVASQL-IYLGQLAGMSRpEARrsVTELLERFGLADRAKDKLES-LSLGNQQRVQIAAAVMSRPQ 149
Cdd:PRK15134 369 qdpnsslnprLNVLQIIEEGLrVHQPTLSAAQR-EQQ--VIAVMEEVGLDPETRHRYPAeFSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 150 ALILDEPFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRSA 219
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSlQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAA 516
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-197 |
9.28e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 80.98 E-value: 9.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMR-------MIMGLLQ----IHGGQVLWQGRPATVADR 70
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRVegkvTFHGKNLYAPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 71 RTFGYMPEERGLYVKQgVASQLIYLGQLAGMsrpeaRRSVTELLER----FGLADRAKDKLE----SLSLGNQQRVQIAA 142
Cdd:PRK14243 91 RRIGMVFQKPNPFPKS-IYDNIAYGARINGY-----KGDMDELVERslrqAALWDEVKDKLKqsglSLSGGQQQRLCIAR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 143 AVMSRPQALILDEPFSGLDPTSVDVMADLLREhTREGVPVLFSSHQLDLVDRLSD 197
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHE-LKEQYTIIIVTHNMQQAARVSD 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-219 |
1.01e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.91 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 7 LTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQI-----HGGQVLWQGRPA-----TVADRRTFGYM 76
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfnyrdVLEFRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEERGLYVKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLES----LSLGNQQRVQIAAAVMSRPQALI 152
Cdd:PRK14271 107 FQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 153 LDEPFSGLDPTSVDVMADLLREhTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRSA 219
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRS-LADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-215 |
1.12e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.91 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRfgDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG-----RPATVADRRTFGY 75
Cdd:PRK09700 265 VFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdispRSPLDAVKKGMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEER---GLY----VKQGVA-SQLIYLGQLAGM-----SRPEARrsvtellerfgLADRAKDKLE-----------SLS 131
Cdd:PRK09700 343 ITESRrdnGFFpnfsIAQNMAiSRSLKDGGYKGAmglfhEVDEQR-----------TAENQRELLAlkchsvnqnitELS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 132 LGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG 211
Cdd:PRK09700 412 GGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQIL 491
|
....
gi 1450037824 212 TAEE 215
Cdd:PRK09700 492 TNRD 495
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-218 |
1.23e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.60 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHT---------AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADrr 71
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 72 tFGYMpEERGLYVKQGVASQL---IYLGQL--------AGMSRPEARRSVTELLERFGL-ADRAKDKLESLSLGNQQRVQ 139
Cdd:PRK15112 82 -YSYR-SQRIRMIFQDPSTSLnprQRISQIldfplrlnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 140 IAAAVMSRPQALILDEPFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG-TAEELR 217
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGsTADVLA 239
|
.
gi 1450037824 218 S 218
Cdd:PRK15112 240 S 240
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
20-220 |
1.63e-17 |
|
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: 79.58 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGYMPEERGL----------YVK 85
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTldslRRAIGVVPQDTVLfndtigynirYGR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 86 QGVASQLIYLGQLAG------MSRPEARRsvTELLERfGLadrakdkleSLSLGNQQRVQIAAAVMSRPQALILDEPFSG 159
Cdd:cd03253 100 PDATDEEVIEAAKAAqihdkiMRFPDGYD--TIVGER-GL---------KLSGGEKQRVAIARAILKNPPILLLDEATSA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 160 LD-PTSVDVMADLLRehTREGVPVLFSSHQL-DLVDrlSDGLVVLSKGRVVAQGTAEELRSAG 220
Cdd:cd03253 168 LDtHTEREIQAALRD--VSKGRTTIVIAHRLsTIVN--ADKIIVLKDGRIVERGTHEELLAKG 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-216 |
1.83e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.97 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRT-----FGY 75
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsqeagIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEERGLYVKQGVASQlIYLGQ-----LAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQA 150
Cdd:PRK10762 84 IHQELNLIPQLTIAEN-IFLGRefvnrFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 151 LILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-206 |
1.99e-17 |
|
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: 78.67 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGR-----------PATVADRRTFGY-MPEERglYVKQG 87
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiayvsqepwiqNGTIRENILFGKpFDEER--YEKVI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 88 VASQLIY-LGQLAGmsrpearRSVTELLERfGLadrakdkleSLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDP-TSV 165
Cdd:cd03250 102 KACALEPdLEILPD-------GDLTEIGEK-GI---------NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAhVGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1450037824 166 DVMADLLREHTREGVPVLFSSHQLDLVDRlSDGLVVLSKGR 206
Cdd:cd03250 165 HIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-219 |
2.15e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.03 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG----RPATVADRRTFGYMP 77
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 78 EER---GLYVKQGVASQLIYLGQ-LAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALIL 153
Cdd:PRK10253 88 QNAttpGDITVQELVARGRYPHQpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 154 DEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRSA 219
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-218 |
2.93e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.86 E-value: 2.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFgDHTAVdQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRP--ATVADRRTFGYMPE 78
Cdd:PRK10771 1 MLKLTDITWLY-HHLPM-RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhtTTPPSRRPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 79 ERGLYVKQGVAsQLIYLGQLAGMS-RPEARRSVTELLERFGLADRAkDKLES-LSLGNQQRVQIAAAVMSRPQALILDEP 156
Cdd:PRK10771 79 ENNLFSHLTVA-QNIGLGLNPGLKlNAAQREKLHAIARQMGIEDLL-ARLPGqLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 157 FSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRS 218
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-187 |
4.32e-17 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 77.97 E-value: 4.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 22 FTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADR-RTFGYMPEERGLYVKQGVASQLIYLGQLAG 100
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRsRFMAYLGHLPGLKADLSTLENLHFLCGLHG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 101 MsrpEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGV 180
Cdd:PRK13543 112 R---RAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGG 188
|
....*..
gi 1450037824 181 PVLFSSH 187
Cdd:PRK13543 189 AALVTTH 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-207 |
5.97e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 5.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPAT---VADRRTFG--YMPEER---GLYVKQGVA-- 89
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINalsTAQRLARGlvYLPEDRqssGLYLDAPLAwn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 90 -SQLIYlGQLAGMSRPEARRSVtelLERFGLA-----DRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPT 163
Cdd:PRK15439 362 vCALTH-NRRGFWIKPARENAV---LERYRRAlnikfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1450037824 164 SVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRV 207
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-216 |
6.38e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.48 E-value: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 27 GQLIGFVGGNGAGKTTTMRMIMGL----LQIhGGQVLWQGRPATVADRRtfgympeERGLYVKQ--------GVASQLIY 94
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRspkgVKG-SGSVLLNGMPIDAKEMR-------AISAYVQQddlfiptlTVREHLMF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 95 LGQL---AGMSRPEARRSVTELLERFGLADRAK------DKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSV 165
Cdd:TIGR00955 123 QAHLrmpRRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 166 DVMADLLREHTREGVPVLFSSHQ--LDLVDrLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:TIGR00955 203 YSVVQVLKGLAQKGKTIICTIHQpsSELFE-LFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-207 |
9.12e-17 |
|
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: 77.51 E-value: 9.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 13 DHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGYMPEERGLYVKQgV 88
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEhkylHSKVSLVGQEPVLFARS-L 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 89 ASQLIY-LGQLAGMSRPEARR-----SVTELLERfGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDP 162
Cdd:cd03248 105 QDNIAYgLQSCSFECVKEAAQkahahSFISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1450037824 163 TSVDVMADLLRE-HTREGVPVLfsSHQLDLVDRlSDGLVVLSKGRV 207
Cdd:cd03248 184 ESEQQVQQALYDwPERRTVLVI--AHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-216 |
9.75e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.21 E-value: 9.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGD------HTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQV------------LWQG 62
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtsdeenLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 63 RPAT---------------VADRRTFGymPEERGLYVKqgvasqliylgqlagmsrpEARRSVTELLERFGLADRAKDKL 127
Cdd:PRK13633 84 RNKAgmvfqnpdnqivatiVEEDVAFG--PENLGIPPE-------------------EIRERVDESLKKVGMYEYRRHAP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 128 ESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTS-VDVMADLLREHTREGVPVLFSSHQLDLVDRlSDGLVVLSKGR 206
Cdd:PRK13633 143 HLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGrREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGK 221
|
250
....*....|
gi 1450037824 207 VVAQGTAEEL 216
Cdd:PRK13633 222 VVMEGTPKEI 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-216 |
1.01e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 78.24 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 16 AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD--------RRTFGYM---PEERglYV 84
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeikpvRKKVGVVfqfPESQ--LF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 85 KQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLADRAKDKLE-SLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPT 163
Cdd:PRK13643 99 EETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 164 SVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13643 179 ARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-217 |
1.42e-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: 76.41 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGL--LQIHGGQVLWQGRPATVADrrtfgymPEE 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLP-------PEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 80 RglyVKQGvasqlIYLGqlagMSRPEARRSVTellerfgLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSG 159
Cdd:cd03217 74 R---ARLG-----IFLA----FQYPPEIPGVK-------NADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1450037824 160 LDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLV-VLSKGRVVAQGTAEELR 217
Cdd:cd03217 135 LDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVhVLYDGRIVKSGDKELAL 193
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-209 |
2.08e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.10 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 17 VDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQ-IHGGQVLWQGRPATV-----ADRRTFGYMPEERGlyvKQGVAS 90
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIrnpaqAIRAGIAMVPEDRK---RHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 91 QL-----IYLGQL---AGMSRPEA---RRSVTELLERFGLADRAKD-KLESLSLGNQQRVQIAAAVMSRPQALILDEPFS 158
Cdd:TIGR02633 353 ILgvgknITLSVLksfCFKMRIDAaaeLQIIGSAIQRLKVKTASPFlPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 159 GLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVA 209
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-212 |
3.09e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 76.71 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 16 AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADR-RTFGYMPEERGLyVKQGVASQL-- 92
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQIRKKVGL-VFQFPESQLfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 93 ------IYLG-QLAGMSRPEARRSVTELLERFGLADRAKDKLE-SLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTS 164
Cdd:PRK13649 101 etvlkdVAFGpQNFGVSQEEAEALAREKLALVGISESLFEKNPfELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1450037824 165 VDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGT 212
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-219 |
5.88e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 76.76 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRF----GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHggqvlWQgrpaTVADRRTFGYM 76
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDN-----WR----VTADRMRFDDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 ------PEERGLYVKQGVA-----------------SQLI-------YLGQLAGMSRPEARRSVtELLERFGLADRaKDK 126
Cdd:PRK15093 74 dllrlsPRERRKLVGHNVSmifqepqscldpservgRQLMqnipgwtYKGRWWQRFGWRKRRAI-ELLHRVGIKDH-KDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 127 LES----LSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLL-REHTREGVPVLFSSHQLDLVDRLSDGLVV 201
Cdd:PRK15093 152 MRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLtRLNQNNNTTILLISHDLQMLSQWADKINV 231
|
250
....*....|....*...
gi 1450037824 202 LSKGRVVAQGTAEELRSA 219
Cdd:PRK15093 232 LYCGQTVETAPSKELVTT 249
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-227 |
7.31e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.46 E-value: 7.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRF--GDHT--AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRmIMGLL--------QIHGGQVLWQGRPATVA 68
Cdd:PRK10535 4 LLELKDIRRSYpsGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdkptsgtyRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 69 DRRT-FGYMPEERGLY----VKQGVASQLIYlgqlAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAA 143
Cdd:PRK10535 83 LRREhFGFIFQRYHLLshltAAQNVEVPAVY----AGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 144 VMSRPQALILDEPFSGLDPTS-VDVMAdLLREHTREGVPVLFSSH------QLDLVDRLSDGLVVL---SKGRVVAQGTA 213
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSgEEVMA-ILHQLRDRGHTVIIVTHdpqvaaQAERVIEIRDGEIVRnppAQEKVNVAGGT 237
|
250
....*....|....
gi 1450037824 214 EELRSAGPCRHRIV 227
Cdd:PRK10535 238 EPVVNTASGWRQFV 251
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-211 |
1.04e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.20 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 16 AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG-RPATVADRR--------TFGYMPEERGLYVKQ 86
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqRIDTLSPGKlqalrrdiQFIFQDPYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 87 GVASQLIYLGQLAGMSRPE-ARRSVTELLERFGL-ADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTS 164
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKaAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1450037824 165 VDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQG 211
Cdd:PRK10261 499 RGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-194 |
1.97e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 73.66 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFG--DH--TAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFGYM 76
Cdd:PRK10584 6 IVEVHHLKKSVGqgEHelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEERGLYVKQGVA----------SQLIYLgqLAGMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMS 146
Cdd:PRK10584 86 RAKHVGFVFQSFMliptlnalenVELPAL--LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1450037824 147 RPQALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDR 194
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAAR 212
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-175 |
2.63e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 75.61 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTA-VDQVSFTVPDGQ--LIgfVGGNGAGKTTTMRMIMGLlqihggqvlW---QGRPATVADRRTFg 74
Cdd:COG4178 362 ALALEDLTLRTPDGRPlLEDLSLSLKPGErlLI--TGPSGSGKSTLLRAIAGL---------WpygSGRIARPAGARVL- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 75 YMPEErgLYVKQG-VASQLIYLGQLAGMSRPEARrsvtELLERFGLADRAkDKLES-------LSLGNQQRVQIAAAVMS 146
Cdd:COG4178 430 FLPQR--PYLPLGtLREALLYPATAEAFSDAELR----EALEAVGLGHLA-ERLDEeadwdqvLSLGEQQRLAFARLLLH 502
|
170 180
....*....|....*....|....*....
gi 1450037824 147 RPQALILDEPFSGLDPTSVDVMADLLREH 175
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLLREE 531
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-219 |
3.09e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.58 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 17 VDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLL----QIHGGQVLWQGRPATVAD---RRTFGYMPEERGLYVK-QGV 88
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPVAPCAlrgRKIATIMQNPRSAFNPlHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 89 ASQLIYLGQLAGMSRPEARrsVTELLERFGLADRAKdKLES----LSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTS 164
Cdd:PRK10418 99 HTHARETCLALGKPADDAT--LTAALEAVGLENAAR-VLKLypfeMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1450037824 165 ----VDVMADLLREHtreGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRSA 219
Cdd:PRK10418 176 qariLDLLESIVQKR---ALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-219 |
3.93e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 74.17 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 16 AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHggqvlWQGRpatvADRRTFGYM------PEERGLYVKQGVA 89
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN-----WHVT----ADRFRWNGIdllklsPRERRKIIGREIA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 90 -----------------SQL---IYLGQLAG--MSRPEAR-RSVTELLERFGLADRaKDKLES----LSLGNQQRVQIAA 142
Cdd:COG4170 93 mifqepsscldpsakigDQLieaIPSWTFKGkwWQRFKWRkKRAIELLHRVGIKDH-KDIMNSypheLTEGECQKVMIAM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 143 AVMSRPQALILDEPFSGLDPTSvdvMADLLREHTR----EGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRS 218
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTT---QAQIFRLLARlnqlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILK 248
|
.
gi 1450037824 219 A 219
Cdd:COG4170 249 S 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-211 |
4.62e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.97 E-value: 4.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHT-----AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLW----------QGRPAT 66
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkkTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 67 VADRRTFGYMPEERGLYVKQ-----GVASQL-------------IYLGQLA-GMSRPEARRSVTELLERFGLADRAKDKL 127
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKEirrrvGVVFQFaeyqlfeqtiekdIIFGPVSmGVSKEEAKKRAAKYIELVGLDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 128 E-SLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGR 206
Cdd:PRK13651 163 PfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
....*
gi 1450037824 207 VVAQG 211
Cdd:PRK13651 243 IIKDG 247
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-207 |
5.56e-15 |
|
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: 71.09 E-value: 5.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGD--HTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGY 75
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDpnelGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEERGLyvkqgvasqliylgqLAGmsrpearrSVTELLerfgladrakdklesLSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:cd03246 81 LPQDDEL---------------FSG--------SIAENI---------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 156 PFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVdRLSDGLVVLSKGRV 207
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-208 |
5.62e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 5.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 3 EVQELTRRFG------DHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLqihggqvlwQGRPATVADRRTFGYM 76
Cdd:COG2401 26 RVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL---------KGTPVAGCVDVPDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEERGLyvkqgvasqliylgqLAGMSRPEARRSVTELLERFGLADRA--KDKLESLSLGNQQRVQIAAAVMSRPQALILD 154
Cdd:COG2401 97 GREASL---------------IDAIGRKGDFKDAVELLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 155 EPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLS-DGLVVLSKGRVV 208
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGYGGVP 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-214 |
8.10e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.45 E-value: 8.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQgrpatvaDRRTFGYMPEEr 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN-------GKLRIGYVPQK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 gLYVKQGVASQLIYLGQLagmsRPEARRS-VTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSG 159
Cdd:PRK09544 76 -LYLDTTLPLTVNRFLRL----RPGTKKEdILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 160 LDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSkGRVVAQGTAE 214
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPE 205
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-227 |
1.31e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 73.99 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 21 SFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGYMPEERGLY---VKQGVASQLI 93
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhhylHRQVALVGQEPVLFsgsVRENIAYGLT 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 94 YLGQ---LAGMSRPEARRSVTELLErfGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDptsVDVMAD 170
Cdd:TIGR00958 581 DTPDeeiMAAAKAANAHDFIMEFPN--GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD---AECEQL 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 171 LLREHTREGVPVLFSSHQLDLVDRlSDGLVVLSKGRVVAQGTAEELRSAGPCRHRIV 227
Cdd:TIGR00958 656 LQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
13-193 |
1.43e-14 |
|
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: 69.88 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 13 DHTAVDQVSFTVPDGQ--LIgfVGGNGAGKTTTMRMIMGLLQIHGGQVlwqGRPAtvaDRRTFgYMPEERglYVKQGV-A 89
Cdd:cd03223 13 GRVLLKDLSFEIKPGDrlLI--TGPSGTGKSSLFRALAGLWPWGSGRI---GMPE---GEDLL-FLPQRP--YLPLGTlR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 90 SQLIYlgqlagmsrPEARRsvtellerfgladrakdklesLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMA 169
Cdd:cd03223 82 EQLIY---------PWDDV---------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170 180 190
....*....|....*....|....*....|..
gi 1450037824 170 DLLREHT--------REGVPVLFsSHQLDLVD 193
Cdd:cd03223 132 QLLKELGitvisvghRPSLWKFH-DRVLDLDG 162
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-214 |
1.58e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 71.25 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGL--LQIHGGQVLWQGRPATVADrrtfgymPEE 79
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELS-------PDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 80 R---GLYVK-Q------GVA-SQLIY--LGQLAG--MSRPEARRSVTELLERFGL----ADRAKDklESLSLGNQQRVQI 140
Cdd:COG0396 74 RaraGIFLAfQypveipGVSvSNFLRtaLNARRGeeLSAREFLKLLKEKMKELGLdedfLDRYVN--EGFSGGEKKRNEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 141 AAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLS-DGLVVLSKGRVVAQGTAE 214
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIKpDFVHVLVDGRIVKSGGKE 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
13-216 |
3.24e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 71.35 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 13 DHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG------------RPAtvadRRTFGYM---P 77
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyiRPV----RKRIGMVfqfP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 78 EERgLYvKQGVASQLIYLGQLAGMSRPEARRSVTELLERFGLAdraKDKLES----LSLGNQQRVQIAAAVMSRPQALIL 153
Cdd:PRK13646 95 ESQ-LF-EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS---RDVMSQspfqMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 154 DEPFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSlQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-161 |
3.92e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 72.28 E-value: 3.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVlwqgrpaTVADRRTFGYMPEER- 80
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-------EIGETVKLAYVDQSRd 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 GLYVKQGV------ASQLIYLGQLAGMSRpearrsvtELLERFGL--ADRAKdKLESLSLGNQQRVQIAAAVMSRPQALI 152
Cdd:TIGR03719 396 ALDPNKTVweeisgGLDIIKLGKREIPSR--------AYVGRFNFkgSDQQK-KVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
....*....
gi 1450037824 153 LDEPFSGLD 161
Cdd:TIGR03719 467 LDEPTNDLD 475
|
|
| DUF4162 |
pfam13732 |
Domain of unknown function (DUF4162); This domain is found at the C-terminus of bacterial ABC ... |
211-292 |
3.96e-14 |
|
Domain of unknown function (DUF4162); This domain is found at the C-terminus of bacterial ABC transporter proteins. The function is not known.
Pssm-ID: 463971 [Multi-domain] Cd Length: 82 Bit Score: 66.46 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 211 GTAEELR-SAGpcRHRIVVS-SDAGWVRDLSGVHVVDVDGTAALVELADETAKQALLAEALSRGSLSEFTPVRPSLSEIY 288
Cdd:pfam13732 1 GTLEEIKrSYG--RNRIEVEtADAEELLELPGVEEVEEEGGGLELKLEDEEAANELLAALLSGGEIRSFEEEEPSLNDIF 78
|
....
gi 1450037824 289 REVT 292
Cdd:pfam13732 79 IEKV 82
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-212 |
5.46e-14 |
|
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: 69.44 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDH--TAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGY 75
Cdd:cd03244 3 IEFKNVSLRYRPNlpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGlhdlRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEERGLYvkqgvasqliylgqlAGMSR----PEARRSVTEL---LERFGLADRAKDKL-----------ESLSLGNQQR 137
Cdd:cd03244 83 IPQDPVLF---------------SGTIRsnldPFGEYSDEELwqaLERVGLKEFVESLPggldtvveeggENLSVGQRQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 138 VQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTReGVPVLFSSHQLD-LVDrlSDGLVVLSKGRVVAQGT 212
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK-DCTVLTIAHRLDtIID--SDRILVLDKGRVVEFDS 220
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-215 |
5.65e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.83 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 6 ELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHG--GQVLWQGRPATVADRRTFGYMPEERGLY 83
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKRTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 84 VKQGVASQLIYLGQL---AGMSRPEARRSVTELLERFGLAdrakdKLESLSLGN----------QQRVQIAAAVMSRPQA 150
Cdd:PLN03211 153 PHLTVRETLVFCSLLrlpKSLTKQEKILVAESVISELGLT-----KCENTIIGNsfirgisggeRKRVSIAHEMLINPSL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 151 LILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQ-LDLVDRLSDGLVVLSKGRVVAQGTAEE 215
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-211 |
6.40e-14 |
|
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: 68.49 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 13 DHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFGYMpeerglyvkqGVASQL 92
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLI----------SVLNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 93 IYLGQlagmsrpearrsvTELLERFGladrakdklESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLL 172
Cdd:cd03247 84 PYLFD-------------TTLRNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 1450037824 173 REHTREGVpVLFSSHQLDLVDRLsDGLVVLSKGRVVAQG 211
Cdd:cd03247 142 FEVLKDKT-LIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
13-216 |
6.42e-14 |
|
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: 69.49 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 13 DHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG---RPATVAD-RRTFGYMPEERGLYvkQGV 88
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdiRDLNLRWlRSQIGLVSQEPVLF--DGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 89 ASQLIYLGqlagmsRPEARRSVTELLERFGLADRAKDKLE------------SLSLGNQQRVQIAAAVMSRPQALILDEP 156
Cdd:cd03249 93 IAENIRYG------KPDATDEEVEEAAKKANIHDFIMSLPdgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 157 FSGLDPTSVDVMADLLrEHTREGVPVLFSSHQLDLVdRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:cd03249 167 TSALDAESEKLVQEAL-DRAMKGRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQGTHDEL 224
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-220 |
6.56e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 71.46 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWqgrpatvADRRTFGYMPEER- 80
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-------SENANIGYYAQDHa 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 -------------GLYVKQGVASQLI--YLGQLAgmsrpearrsvtellerFGlADRAKDKLESLSLGNQQRVQIAAAVM 145
Cdd:PRK15064 393 ydfendltlfdwmSQWRQEGDDEQAVrgTLGRLL-----------------FS-QDDIKKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 146 SRPQALILDEPFSGLDPTSVDVMADLLREHtrEGVpVLFSSHQLDLVDRLSDGLVVLSKGRVVA-QGTAEE-LRSAG 220
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMESIESLNMALEKY--EGT-LIFVSHDREFVSSLATRIIEITPDGVVDfSGTYEEyLRSQG 528
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-216 |
8.17e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 69.68 E-value: 8.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQ-IHG----GQVLWQGR----PAT--VADR 70
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlIPGarveGEILLDGEdiydPDVdvVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 71 RTFGyMpeerglyvkqgVASQL------IY----LG-QLAGM-SRPEARRSVTELLERFGLADRAKDKLE----SLSLGN 134
Cdd:COG1117 92 RRVG-M-----------VFQKPnpfpksIYdnvaYGlRLHGIkSKSELDEIVEESLRKAALWDEVKDRLKksalGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 135 QQRVQIAAAVMSRPQALILDEPFSGLDPTSV----DVMADLLREHTregvpVLFSSHQLDLVDRLSDGLVVLSKGRVVAQ 210
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTakieELILELKKDYT-----IVIVTHNMQQAARVSDYTAFFYLGELVEF 234
|
....*.
gi 1450037824 211 GTAEEL 216
Cdd:COG1117 235 GPTEQI 240
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-215 |
1.36e-13 |
|
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: 70.55 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTF----GYMPEERGLY---VKQGVA--- 89
Cdd:COG4618 351 VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELgrhiGYLPQDVELFdgtIAENIArfg 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 90 ---SQLIYL-GQLAGmsrpearrsVTELLERF--GLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPT 163
Cdd:COG4618 431 dadPEKVVAaAKLAG---------VHEMILRLpdGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDE 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 164 SVDVMADLLREHTREGVPVLFSSHQ---LDLVDRlsdgLVVLSKGRVVAQGTAEE 215
Cdd:COG4618 502 GEAALAAAIRALKARGATVVVITHRpslLAAVDK----LLVLRDGRVQAFGPRDE 552
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
27-205 |
6.55e-13 |
|
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: 66.11 E-value: 6.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 27 GQLIGFVGGNGAGKTTTM-----RMIMGLLqihGGQVLWQGRPATVADRRTFGYmpeerglyVKQgvasQLIYLGQLagm 101
Cdd:cd03232 33 GTLTALMGESGAGKTTLLdvlagRKTAGVI---TGEILINGRPLDKNFQRSTGY--------VEQ----QDVHSPNL--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 102 srpearrSVTELLeRFGLADRAkdklesLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVP 181
Cdd:cd03232 95 -------TVREAL-RFSALLRG------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQA 160
|
170 180
....*....|....*....|....*.
gi 1450037824 182 VLFSSHQ--LDLVDRLsDGLVVLSKG 205
Cdd:cd03232 161 ILCTIHQpsASIFEKF-DRLLLLKRG 185
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-189 |
7.23e-13 |
|
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: 68.54 E-value: 7.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRF-GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGYM 76
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqdevRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEERGLYvkqgvASQLiyLGQLAgMSRPEAR-RSVTELLERFGLAD---RAKDKLE--------SLSLGNQQRVQIAAAV 144
Cdd:TIGR02868 415 AQDAHLF-----DTTV--RENLR-LARPDATdEELWAALERVGLADwlrALPDGLDtvlgeggaRLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1450037824 145 MSRPQALILDEPFSGLDP-TSVDVMADLLRehTREGVPVLFSSHQL 189
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAeTADELLEDLLA--ALSGRTVVLITHHL 530
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-216 |
7.92e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 68.45 E-value: 7.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 12 GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMrmimGLLQ----IHGGQVLWQG---RPATVAD-RRTFGYMPEERGLY 83
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLLQrvfdPQSGRILIDGtdiRTVTRASlRRNIAVVFQDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 84 VKQgvASQLIYLGQ----LAGMSRPEARRSVTELLER--FGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPF 157
Cdd:PRK13657 422 NRS--IEDNIRVGRpdatDEEMRAAAERAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 158 SGLD-PTSVDVMADLlrEHTREGVPVLFSSHQLDLVdRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13657 500 SALDvETEAKVKAAL--DELMKGRTTFIIAHRLSTV-RNADRILVFDNGRVVESGSFDEL 556
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-216 |
8.28e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHT----AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQV-----LWQGRPATVADRR 71
Cdd:PRK10261 12 VLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 72 TF--GYMPEERG-----------------LYVKQGVASQlIYLGQlaGMSRPEARRSVTELLERFGLADrAKDKL----E 128
Cdd:PRK10261 92 EQsaAQMRHVRGadmamifqepmtslnpvFTVGEQIAES-IRLHQ--GASREEAMVEAKRMLDQVRIPE-AQTILsrypH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 129 SLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGRV 207
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
....*....
gi 1450037824 208 VAQGTAEEL 216
Cdd:PRK10261 248 VETGSVEQI 256
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-220 |
9.95e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.95 E-value: 9.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 13 DHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQiHGGQVLWQGRPATVADrrtfgyMPEERglyvkqgvaSQL 92
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELD------PESWR---------KHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 93 IYLGQ----LAG-------MSRPEA----------RRSVTELLERF--GLADRAKDKLESLSLGNQQRVQIAAAVMSRPQ 149
Cdd:PRK11174 426 SWVGQnpqlPHGtlrdnvlLGNPDAsdeqlqqaleNAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 150 ALILDEPFSGLDPTSVD-VMADLlrEHTREGVPVLFSSHQLDLVDRLsDGLVVLSKGRVVAQGTAEELRSAG 220
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQlVMQAL--NAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
3-216 |
1.33e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 67.61 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 3 EVQELTRRFGD---HTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAdrrtfgympee 79
Cdd:PRK13545 23 KLKDLFFRSKDgeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIA----------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 80 rglyVKQGVASQLIYL------GQLAGMSRPEARRSVTELLErfgLADRAK---DKLESLSLGNQQRVQIAAAVMSRPQA 150
Cdd:PRK13545 92 ----ISSGLNGQLTGIenielkGLMMGLTKEKIKEIIPEIIE---FADIGKfiyQPVKTYSSGMKSRLGFAISVHINPDI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 151 LILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13545 165 LVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-190 |
1.37e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.51 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATV----ADRRTFGYM 76
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlkpeIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 77 PEERGLYvKQGVASQLIYLGQLAGmSRPEARRSVTElLERFGLADRAKDK-LESLSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:PRK10247 87 AQTPTLF-GDTVYDNLIFPWQIRN-QQPDPAIFLDD-LERFALPDTILTKnIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1450037824 156 PFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLD 190
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKD 199
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-205 |
3.19e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.06 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 18 DQVSFTVPDGQLIGFVGGNGAGKTTTM-----RMIMGLlqIHGGQVLWQGRPATVADRRTFGYMpEERGLYVKQG-VASQ 91
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGV--ITGGDRLVNGRPLDSSFQRSIGYV-QQQDLHLPTStVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 92 LI---YLGQLAGMSRPEARRSVTELLERFGLADRAkDKL-----ESLSLGNQQRVQIAAAVMSRPQALI-LDEPFSGLDP 162
Cdd:TIGR00956 857 LRfsaYLRQPKSVSKSEKMEYVEEVIKLLEMESYA-DAVvgvpgEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS 935
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1450037824 163 TSVDVMADLLREHTREGVPVLFSSHQ--LDLVDRLsDGLVVLSKG 205
Cdd:TIGR00956 936 QTAWSICKLMRKLADHGQAILCTIHQpsAILFEEF-DRLLLLQKG 979
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-197 |
3.37e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 65.18 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMI--MGLLQ---------IHGGQVLWQGRPATVAD 69
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNpevtitgsiVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 70 RRtfgympeERGLYVKQ------GVASQLIYLGQLAGMSRPEA-RRSVTELLERFGLADRAKDKLE----SLSLGNQQRV 138
Cdd:PRK14239 85 RK-------EIGMVFQQpnpfpmSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIWDEVKDRLHdsalGLSGGQQQRV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1450037824 139 QIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREhTREGVPVLFSSHQLDLVDRLSD 197
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLG-LKDDYTMLLVTRSMQQASRISD 215
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-238 |
4.19e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 66.27 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 13 DHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADrrtfgyMPEERGlyvKQGVASQL 92
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ------LDSWRS---RLAVVSQT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 93 IYL------GQLAgMSRPEARRSVTELLERfgLADRAKDKLE--------------SLSLGNQQRVQIAAAVMSRPQALI 152
Cdd:PRK10789 398 PFLfsdtvaNNIA-LGRPDATQQEIEHVAR--LASVHDDILRlpqgydtevgergvMLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 153 LDEPFSGLD-PTSVDVMADLLRehTREGVPVLFSSHQLD-LVDrlSDGLVVLSKGRVVAQGTAEELrsagpcrhrivvSS 230
Cdd:PRK10789 475 LDDALSAVDgRTEHQILHNLRQ--WGEGRTVIISAHRLSaLTE--ASEILVMQHGHIAQRGNHDQL------------AQ 538
|
....*...
gi 1450037824 231 DAGWVRDL 238
Cdd:PRK10789 539 QSGWYRDM 546
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-197 |
5.15e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.67 E-value: 5.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTT------TMRMIMGLLQIHG-----GQVLWQGRPATVADR 70
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTflkclnRMNELESEVRVEGrveffNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 71 RTFGYMPEERGLYvKQGVASQLIYLGQLAGMsRP--EARRSVTELLERFGLADRAKDKLES----LSLGNQQRVQIAAAV 144
Cdd:PRK14258 88 RQVSMVHPKPNLF-PMSVYDNVAYGVKIVGW-RPklEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 145 MSRPQALILDEPFSGLDP-TSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSD 197
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPiASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-190 |
8.81e-12 |
|
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: 64.11 E-value: 8.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRF--GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHG----GQVLWQGRPATVAdRRTFGY 75
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGdiqiDGVSWNSVPLQKW-RKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEErglyvkqgvasQLIYLGQLAGMSRPEARRSVTELL---ERFGLA---DRAKDKLE--------SLSLGNQQRVQIA 141
Cdd:cd03289 82 IPQK-----------VFIFSGTFRKNLDPYGKWSDEEIWkvaEEVGLKsviEQFPGQLDfvlvdggcVLSHGHKQLMCLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1450037824 142 AAVMSRPQALILDEPFSGLDPTSVDVMADLLReHTREGVPVLFSSHQLD 190
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLK-QAFADCTVILSEHRIE 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-216 |
9.38e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.14 E-value: 9.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 16 AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRP-----ATVADRRTFGYMPEERGLyVKQGVAS 90
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfksSKEALENGISMVHQELNL-VLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 91 QLIYLGQ--LAGMSRPEAR--RSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVD 166
Cdd:PRK10982 92 DNMWLGRypTKGMFVDQDKmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVN 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1450037824 167 VMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK10982 172 HLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-221 |
1.02e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.53 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 12 GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMG-LLQIHGGQVLWQGR-----------PATVADRRTFGyMPEE 79
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTvayvpqvswifNATVRDNILFG-SPFD 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 80 RGLYVKQGVASQLIY-LGQLAGmsrpearRSVTELLERfGLadrakdkleSLSLGNQQRVQIAAAVMSRPQALILDEPFS 158
Cdd:PLN03130 707 PERYERAIDVTALQHdLDLLPG-------GDLTEIGER-GV---------NISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 159 GLDP-TSVDVMADLLREHTREGVPVLFSS--HQLDLVDRlsdgLVVLSKGRVVAQGTAEELRSAGP 221
Cdd:PLN03130 770 ALDAhVGRQVFDKCIKDELRGKTRVLVTNqlHFLSQVDR----IILVHEGMIKEEGTYEELSNNGP 831
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-260 |
1.06e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.04 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMG-LLQIHGGQVLWQGRPATVA----------- 68
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGeLPLLSGERQSQFSHITRLSfeqlqklvsde 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 69 --DRRTFGYMPEER--GLyvkqgVASQLIYLGqlagmSRPEARrsVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAV 144
Cdd:PRK10938 83 wqRNNTDMLSPGEDdtGR-----TTAEIIQDE-----VKDPAR--CEQLAQQFGITALLDRRFKYLSTGETRKTLLCQAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 145 MSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEELRSagpcrh 224
Cdd:PRK10938 151 MSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ------ 224
|
250 260 270
....*....|....*....|....*....|....*.
gi 1450037824 225 RIVVSSDAgWVRDLSGVHVVDVDGTAALVELADETA 260
Cdd:PRK10938 225 QALVAQLA-HSEQLEGVQLPEPDEPSARHALPANEP 259
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-161 |
2.68e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVlwqgrpaTVADRRTFGYMPEER- 80
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-------KIGETVKLAYVDQSRd 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 GLYVKQGV------ASQLIYLGQLAGMSRpearrsvtELLERFGL--ADRAKdKLESLSLGNQQRVQIAAAVMSRPQALI 152
Cdd:PRK11819 398 ALDPNKTVweeisgGLDIIKVGNREIPSR--------AYVGRFNFkgGDQQK-KVGVLSGGERNRLHLAKTLKQGGNVLL 468
|
....*....
gi 1450037824 153 LDEPFSGLD 161
Cdd:PRK11819 469 LDEPTNDLD 477
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-220 |
2.84e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQihggqvlwQGRPATVADRRTFGYMPEERGLYvkQGVASQLIYLGQLA 99
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELS--------HAETSSVVIRGSVAYVPQVSWIF--NATVRENILFGSDF 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 100 GMSRPEARRSVTEL---LERFGLADRAK--DKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSV-----DVMA 169
Cdd:PLN03232 706 ESERYWRAIDVTALqhdLDLLPGRDLTEigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAhqvfdSCMK 785
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 170 DLLREHTRegVPVLFSSHQLDLVDRlsdgLVVLSKGRVVAQGTAEELRSAG 220
Cdd:PLN03232 786 DELKGKTR--VLVTNQLHFLPLMDR----IILVSEGMIKEEGTFAELSKSG 830
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-216 |
2.85e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.17 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHggqvlwqgRPATV-ADRRTFG---YMP 77
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELN--------EEARVeGEVRLFGrniYSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 78 EERGLYVKQ--GVASQL--------IYLGQLAGMSRPEARRSVTELLERFGLA-----------DRAKDKLESLSLGNQQ 136
Cdd:PRK14267 77 DVDPIEVRRevGMVFQYpnpfphltIYDNVAIGVKLNGLVKSKKELDERVEWAlkkaalwdevkDRLNDYPSNLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 137 RVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFsSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLV-THSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-215 |
4.33e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.88 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 17 VDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGllQIHG----GQVLWQGRPA---TVAD--RRTFGYMPEER---GLYV 84
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG--RSYGrnisGTVFKDGKEVdvsTVSDaiDAGLAYVTEDRkgyGLNL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 85 KQGVASQlIYLGQLAGMSRpearRSVTELLERFGLADRAKDKL-----------ESLSLGNQQRVQIAAAVMSRPQALIL 153
Cdd:NF040905 354 IDDIKRN-ITLANLGKVSR----RGVIDENEEIKVAEEYRKKMniktpsvfqkvGNLSGGNQQKVVLSKWLFTDPDVLIL 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 154 DEPFSGldptsVDVMAD-----LLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEE 215
Cdd:NF040905 429 DEPTRG-----IDVGAKyeiytIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREE 490
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-218 |
4.60e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGrpatvADRRTFGYMPEERGLYVKQgvASQLIYLGQL- 98
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD-----CDVAKFGLTDLRRVLSIIP--QSPVLFSGTVr 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 99 -----------AGMSRPEARRSVTELLER--FGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSgldptSV 165
Cdd:PLN03232 1328 fnidpfsehndADLWEALERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATA-----SV 1402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1450037824 166 DVMADLLREHT-RE---GVPVLFSSHQLD-LVDrlSDGLVVLSKGRVVAQGTAEELRS 218
Cdd:PLN03232 1403 DVRTDSLIQRTiREefkSCTMLVIAHRLNtIID--CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-190 |
5.18e-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: 63.39 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRF--GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLL------QIHGgqVLWQGrpATVAD-RRT 72
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLstegeiQIDG--VSWNS--VTLQTwRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 73 FGYMPEErglyvkqgvasQLIYLGQLAGMSRPEARRSVTEL---LERFGLA---DRAKDKLE--------SLSLGNQQRV 138
Cdd:TIGR01271 1294 FGVIPQK-----------VFIFSGTFRKNLDPYEQWSDEEIwkvAEEVGLKsviEQFPDKLDfvlvdggyVLSNGHKQLM 1362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 139 QIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLReHTREGVPVLFSSHQLD 190
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLK-QSFSNCTVILSEHRVE 1413
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-202 |
6.13e-11 |
|
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: 62.49 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 27 GQLIGFVGGNGAGKTTTMRMIMGLLQ----IHGGQVLWQgrpaTVAD--RRT--FGYMpeeRGLY---VKQGVASQLIYL 95
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKpnlgDYDEEPSWD----EVLKrfRGTelQDYF---KKLAngeIKVAHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 96 ---------GQLagMSRPEARRSVTELLERFGLA---DRakdKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPT 163
Cdd:COG1245 172 ipkvfkgtvREL--LEKVDERGKLDELAEKLGLEnilDR---DISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246
|
170 180 190
....*....|....*....|....*....|....*....
gi 1450037824 164 SVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVL 202
Cdd:COG1245 247 QRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-213 |
6.91e-11 |
|
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: 61.27 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 23 TVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWqgrpatvaDRRTFGYMPEerglYVK---QGVASQLIYlGQLA 99
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI--------ELDTVSYKPQ----YIKadyEGTVRDLLS-SITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 100 GM-SRPEARRSVTELLERFGLADRakdKLESLSLGNQQRVQIAAAvMSRPQAL-ILDEPFSGLDPTSVDVMADLLR---E 174
Cdd:cd03237 88 DFyTHPYFKTEIAKPLQIEQILDR---EVPELSGGELQRVAIAAC-LSKDADIyLLDEPSAYLDVEQRLMASKVIRrfaE 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1450037824 175 HTREGVPVLfsSHQLDLVDRLSDGLVVLSkGRVVAQGTA 213
Cdd:cd03237 164 NNEKTAFVV--EHDIIMIDYLADRLIVFE-GEPSVNGVA 199
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
5-202 |
8.24e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 60.84 E-value: 8.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 5 QELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQ----IHGGQVLWQGRPATVADRRTFGYMPEER 80
Cdd:cd03236 4 DEPVHRYGPNSFKLHRLPVPREGQVLGLVGPNGIGKSTALKILAGKLKpnlgKFDDPPDWDEILDEFRGSELQNYFTKLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 GLYVKQGVASQLIYL---------GQLagMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQAL 151
Cdd:cd03236 84 EGDVKVIVKPQYVDLipkavkgkvGEL--LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 152 ILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVL 202
Cdd:cd03236 162 FFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-210 |
9.51e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.85 E-value: 9.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRR---TFGYM--PEERglyvKQgvasqliy 94
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdaiRAGIMlcPEDR----KA-------- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 95 LGQLAGMSRPE-----ARRSVTelleRFGL----------ADR-----------AKDKLESLSLGNQQRVQIAAAVMSRP 148
Cdd:PRK11288 340 EGIIPVHSVADninisARRHHL----RAGClinnrweaenADRfirslniktpsREQLIMNLSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 149 QALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQ 210
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-212 |
9.77e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.00 E-value: 9.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHG--------GQVLWQGRPATVADRRT 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 73 FGYMpeeRGLYVKQG------VASQLIYLGQLagmsrPEARRS----------VTELLERFGLADRAKDKLESLSLGNQQ 136
Cdd:PRK13547 81 LARL---RAVLPQAAqpafafSAREIVLLGRY-----PHARRAgalthrdgeiAWQALALAGATALVGRDVTTLSGGELA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 137 RVQIAAAV---------MSRPQALILDEPFSGLDPTSVDVMADLLREHTRE-GVPVLFSSHQLDLVDRLSDGLVVLSKGR 206
Cdd:PRK13547 153 RVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGA 232
|
....*.
gi 1450037824 207 VVAQGT 212
Cdd:PRK13547 233 IVAHGA 238
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-212 |
1.03e-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: 60.12 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDH--TAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGY 75
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPledlRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEErglyvkqgvasQLIYLGQLAGMSRPEARRSVTELLErfglADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:cd03369 87 IPQD-----------PTLFSGTIRSNLDPFDEYSDEEIYG----ALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 156 PFSgldptSVDVMAD-LLREHTRE---GVPVLFSSHQLDLVDRLsDGLVVLSKGRVVAQGT 212
Cdd:cd03369 152 ATA-----SIDYATDaLIQKTIREeftNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-217 |
1.62e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 11 FGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQV----------LWQGRPATVADrRTFGYMPE-- 78
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiyeqdlivarLQQDPPRNVEG-TVYDFVAEgi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 79 -ERGLYVKQ-GVASQLI-------YLGQLA---------GMSRPEARrsVTELLERFGLAdrAKDKLESLSLGNQQRVQI 140
Cdd:PRK11147 92 eEQAEYLKRyHDISHLVetdpsekNLNELAklqeqldhhNLWQLENR--INEVLAQLGLD--PDAALSSLSGGWLRKAAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 141 AAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHtrEGvPVLFSSHQLDLVDRLSDGLVVLSKGRVVA---------QG 211
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QG-SIIFISHDRSFIRNMATRIVDLDRGKLVSypgnydqylLE 244
|
....*.
gi 1450037824 212 TAEELR 217
Cdd:PRK11147 245 KEEALR 250
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-201 |
3.26e-10 |
|
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: 60.57 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 27 GQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQgrpATVAdrrtfgYMPEerglYVKQGVASQLIYLgqLAGMSRPEA 106
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED---LKIS------YKPQ----YISPDYDGTVEEF--LRSANTDDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 107 RRSV--TELLERFGLaDRAKDK-LESLSLGNQQRVQIAAAvMSRPQAL-ILDEPFSGLDPTSVDVMADLLREHTRE-GVP 181
Cdd:COG1245 431 GSSYykTEIIKPLGL-EKLLDKnVKDLSGGELQRVAIAAC-LSRDADLyLLDEPSAHLDVEQRLAVAKAIRRFAENrGKT 508
|
170 180
....*....|....*....|
gi 1450037824 182 VLFSSHQLDLVDRLSDGLVV 201
Cdd:COG1245 509 AMVVDHDIYLIDYISDRLMV 528
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-216 |
4.09e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.12 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHTAVDQ-VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTfgympeer 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQnINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV-------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 glyVKQGVAsqliyLGQ-----LAG-------MSRPEARRSVTELLERFGLADRAK---DKLES--------LSLGNQQR 137
Cdd:PRK10790 413 ---LRQGVA-----MVQqdpvvLADtflanvtLGRDISEEQVWQALETVQLAELARslpDGLYTplgeqgnnLSVGQKQL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 138 VQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREhTREGVPVLFSSHQLD-LVDrlSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDSGTEQAIQQALAA-VREHTTLVVIAHRLStIVE--ADTILVLHRGQAVEQGTHQQL 561
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-216 |
4.89e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 59.84 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 12 GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADrrtfgympeERGLYVKQGVASQ 91
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS---------EAALRQAISVVSQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 92 LIYL--GQLAG---MSRPEARRS-VTELLERFGLADRAKDK--LES--------LSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:PRK11160 422 RVHLfsATLRDnllLAAPNASDEaLIEVLQQVGLEKLLEDDkgLNAwlgeggrqLSGGEQRRLGIARALLHDAPLLLLDE 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 156 PFSGLDPTSVDVMADLLREHTReGVPVLFSSHQLDLVDRLsDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK11160 502 PTEGLDAETERQILELLAEHAQ-NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQEL 560
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-188 |
5.90e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 10 RFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMG--------LLQIHGGQvlwQGRPATVAD-RRTFGYMP--- 77
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysnDLTLFGRR---RGSGETIWDiKKHIGYVSssl 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 78 --EER-----------------GLYvkQGVASQLIYLGQlagmsrpearrsvtELLERFGLADR-AKDKLESLSLGNQQR 137
Cdd:PRK10938 346 hlDYRvstsvrnvilsgffdsiGIY--QAVSDRQQKLAQ--------------QWLDILGIDKRtADAPFHSLSWGQQRL 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1450037824 138 VQIAAAVMSRPQALILDEPFSGLDPTS-------VDVMadllrehTREG-VPVLFSSHQ 188
Cdd:PRK10938 410 ALIVRALVKHPTLLILDEPLQGLDPLNrqlvrrfVDVL-------ISEGeTQLLFVSHH 461
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-202 |
6.23e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 23 TVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD--RRT--FGYMpeeRGLY---VKQGVASQLIYL 95
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVLKrfRGTelQNYF---KKLYngeIKVVHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 96 ---------GQLagMSRPEARRSVTELLERFGLA---DRakdKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPT 163
Cdd:PRK13409 172 ipkvfkgkvREL--LKKVDERGKLDEVVERLGLEnilDR---DISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180 190
....*....|....*....|....*....|....*....
gi 1450037824 164 SVDVMADLLREHTrEGVPVLFSSHQLDLVDRLSDGLVVL 202
Cdd:PRK13409 247 QRLNVARLIRELA-EGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-216 |
1.62e-09 |
|
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: 58.29 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG---RPATVAD-RRTFGYMPEERGLYvKQGVASQLIYl 95
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDVTQASlRAAIGIVPQDTVLF-NDTIAYNIAY- 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 96 gqlagmSRPEARRSvtELLERFGLA------DRAKDKLES--------LSLGNQQRVQIAAAVMSRPQALILDEPFSGLD 161
Cdd:COG5265 455 ------GRPDASEE--EVEAAARAAqihdfiESLPDGYDTrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 162 -PTSVDVMADLL---REHTregvpVLFSSHqldlvdRLS-----DGLVVLSKGRVVAQGTAEEL 216
Cdd:COG5265 527 sRTERAIQAALRevaRGRT-----TLVIAH------RLStivdaDEILVLEAGRIVERGTHAEL 579
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-203 |
2.15e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 27 GQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQgrpATVAdrrtfgYMPEerglYVKqgvASQLIYLGQLAGMSRPEA 106
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKIS------YKPQ----YIK---PDYDGTVEDLLRSITDDL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 107 RRSV--TELLERFGLADRAKDKLESLSLGNQQRVQIAAAvMSRPQAL-ILDEPFSGLDPTSVDVMADLLREHTRE-GVPV 182
Cdd:PRK13409 429 GSSYykSEIIKPLQLERLLDKNVKDLSGGELQRVAIAAC-LSRDADLyLLDEPSAHLDVEQRLAVAKAIRRIAEErEATA 507
|
170 180
....*....|....*....|.
gi 1450037824 183 LFSSHQLDLVDRLSDGLVVLS 203
Cdd:PRK13409 508 LVVDHDIYMIDYISDRLMVFE 528
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-207 |
2.87e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRfgDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG-----RPATVADRRTFGY 75
Cdd:PRK10982 250 ILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkinnHNANEAINHGFAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 76 MPEER---GLYVKQGVA-SQLIylgqlagmsrpearRSVTELLERFGLADRAKDK--------------------LESLS 131
Cdd:PRK10982 328 VTEERrstGIYAYLDIGfNSLI--------------SNIRNYKNKVGLLDNSRMKsdtqwvidsmrvktpghrtqIGSLS 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 132 LGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRV 207
Cdd:PRK10982 394 GGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-155 |
2.90e-09 |
|
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: 57.50 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFgympeerglyvkqgvaSQLI------ 93
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAY----------------RQLFsavfsd 414
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 94 -YL-GQLAGMSRPEARRSVTELLERFGLADraKDKLE-------SLSLGNQQRVQIAAAVMSRPQALILDE 155
Cdd:COG4615 415 fHLfDRLLGLDGEADPARARELLERLELDH--KVSVEdgrfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-215 |
3.16e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.87 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVlWQGRP------------ATVADRRTFgyMPEERGLYVKQG 87
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSiayvpqqawimnATVRGNILF--FDEEDAARLADA 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 88 V-ASQL-IYLGQLAGmsrpearrsvtellerfGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDP-TS 164
Cdd:PTZ00243 756 VrVSQLeADLAQLGG-----------------GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhVG 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 165 VDVMADLLREHTREGVPVLfSSHQLDLVDRlSDGLVVLSKGRVVAQGTAEE 215
Cdd:PTZ00243 819 ERVVEECFLGALAGKTRVL-ATHQVHVVPR-ADYVVALGDGRVEFSGSSAD 867
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-188 |
3.94e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.26 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 34 GGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFGYMPEERGLYVKQGVASQLIYLGQLAgmsrpEARRSVTEL 113
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIY-----NSAETLYAA 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 114 LERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQ 188
Cdd:PRK13541 108 IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHL 182
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-216 |
5.19e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.98 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 16 AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAdrrtfgympeerglyVKQGVASQLIYL 95
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIA---------------ISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 96 GQLA------GMSRPEARRSVTELLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMA 169
Cdd:PRK13546 104 ENIEfkmlcmGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1450037824 170 DLLREHTREGVPVLFSSHQLDLVDRLSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK13546 184 DKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-207 |
7.50e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVlwqgrpaTVADRRTFGYMPEER 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------GLAKGIKLGYFAQHQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 GLYVKQGvASQLIYLGQLAGMsrpEARRSVTELLERFGL-ADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSG 159
Cdd:PRK10636 385 LEFLRAD-ESPLQHLARLAPQ---ELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1450037824 160 LDPTSVDVMADLLREHtrEGVPVLFsSHQLDLVDRLSDGLVVLSKGRV 207
Cdd:PRK10636 461 LDLDMRQALTEALIDF--EGALVVV-SHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-216 |
2.23e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.02 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 13 DHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQG---RPATVADRRTfgympeerglyvKQGVA 89
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTLASLRN------------QVALV 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 90 SQLIYL------GQLAGMSRPEARRSVTELLERFGLADRAKDKLE------------SLSLGNQQRVQIAAAVMSRPQAL 151
Cdd:PRK11176 423 SQNVHLfndtiaNNIAYARTEQYSREQIEEAARMAYAMDFINKMDngldtvigengvLLSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1450037824 152 ILDEPFSGLDPTSVDVMADLLREhTREGVPVLFSSHQLDLVDRlSDGLVVLSKGRVVAQGTAEEL 216
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDE-LQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAEL 565
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-218 |
4.76e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.36 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGrpatvADRRTFGYMPEERGLyvkqGVASQLIYLgqLA 99
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG-----CDISKFGLMDLRKVL----GIIPQAPVL--FS 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 100 GMSR----PEARRSVTEL---LER-----------FGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSgld 161
Cdd:PLN03130 1327 GTVRfnldPFNEHNDADLwesLERahlkdvirrnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA--- 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 162 ptSVDVMADLLREHT-RE---GVPVLFSSHQLD-LVDrlSDGLVVLSKGRVVAQGTAEELRS 218
Cdd:PLN03130 1404 --AVDVRTDALIQKTiREefkSCTMLIIAHRLNtIID--CDRILVLDAGRVVEFDTPENLLS 1461
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-191 |
8.60e-08 |
|
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: 53.21 E-value: 8.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 17 VDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGqvlwqgRPATVADRRTFgYMPEERglYVKQG-VASQLIYL 95
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG------RLTKPAKGKLF-YVPQRP--YMTLGtLRDQIIYP 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 96 GQLAGMSRPEARRSVTE----------LLERFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLdptSV 165
Cdd:TIGR00954 539 DSSEDMKRRGLSDKDLEqildnvqlthILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV---SV 615
|
170 180
....*....|....*....|....*..
gi 1450037824 166 DvMADLLREHTREGVPVLFS-SHQLDL 191
Cdd:TIGR00954 616 D-VEGYMYRLCREFGITLFSvSHRKSL 641
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-163 |
9.80e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.05 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 2 LEVQELTRRFGDHT-AVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVADRRTFgympeeR 80
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY------R 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 81 GLYvkQGVASQLIYLGQLAGmsrPEARRSVTEL----LERFGLadraKDKLE---------SLSLGNQQRVQIAAAVMSR 147
Cdd:PRK10522 397 KLF--SAVFTDFHLFDQLLG---PEGKPANPALvekwLERLKM----AHKLEledgrisnlKLSKGQKKRLALLLALAEE 467
|
170
....*....|....*.
gi 1450037824 148 PQALILDEPFSGLDPT 163
Cdd:PRK10522 468 RDILLLDEWAADQDPH 483
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
30-176 |
1.00e-07 |
|
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: 53.02 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 30 IGFVGGNGAGKTTTMRMIMGLLQIHGGQvlwqgrpATVADRRTFGYMPEERGL--------YVKQGVASQLIYLGQL--- 98
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAGVDKDFNGE-------ARPQPGIKVGYLPQEPQLdptktvreNVEEGVAEIKDALDRFnei 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 99 -AGMSRPEARRSV-----TELLERFGLAD---------RAKDKL---------ESLSLGNQQRVQIAAAVMSRPQALILD 154
Cdd:TIGR03719 107 sAKYAEPDADFDKlaaeqAELQEIIDAADawdldsqleIAMDALrcppwdadvTKLSGGERRRVALCRLLLSKPDMLLLD 186
|
170 180
....*....|....*....|..
gi 1450037824 155 EPFSGLDPTSVDVMADLLREHT 176
Cdd:TIGR03719 187 EPTNHLDAESVAWLERHLQEYP 208
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-216 |
1.60e-07 |
|
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: 52.64 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 12 GDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPAtvadrrtfgYMPEERglYVKQGVASQ 91
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVA---------YVPQQA--WIQNDSLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 92 LIYLGQLAgmsRPEARRSVTEL------LERFGLADRAK--DKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPT 163
Cdd:TIGR00957 718 NILFGKAL---NEKYYQQVLEAcallpdLEILPSGDRTEigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 164 SVDVMAD-------LLREHTRegvpvLFSSHQLDLVDRLsDGLVVLSKGRVVAQGTAEEL 216
Cdd:TIGR00957 795 VGKHIFEhvigpegVLKNKTR-----ILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 848
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-221 |
2.73e-07 |
|
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: 51.83 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGR-----------PATVADRRTFGYMPEERgLYVKQGV 88
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRisfspqtswimPGTIKDNIIFGLSYDEY-RYTSVIK 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 89 ASQLiylgqlagmsrpeaRRSVTELLErfgladraKDKLE------SLSLGNQQRVQIAAAVMSRPQALILDEPFSGLD- 161
Cdd:TIGR01271 524 ACQL--------------EEDIALFPE--------KDKTVlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDv 581
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 162 PTSVDV----MADLLREHTRegvpVLFSShQLDLVDRlSDGLVVLSKGRVVAQGTAEELRSAGP 221
Cdd:TIGR01271 582 VTEKEIfescLCKLMSNKTR----ILVTS-KLEHLKK-ADKILLLHEGVCYFYGTFSELQAKRP 639
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-214 |
3.10e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.41 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMG--LLQIHGGQVLWQGRPATVADrrtfgymPE 78
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLE-------PE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 79 ERglyvkqgvaSQL-IYLG-----QLAGMSRPE-------ARRSVTEL-----LERFGLadrAKDKL------------- 127
Cdd:CHL00131 80 ER---------AHLgIFLAfqypiEIPGVSNADflrlaynSKRKFQGLpeldpLEFLEI---INEKLklvgmdpsflsrn 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 128 --ESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLV-VLSK 204
Cdd:CHL00131 148 vnEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVhVMQN 227
|
250
....*....|
gi 1450037824 205 GRVVAQGTAE 214
Cdd:CHL00131 228 GKIIKTGDAE 237
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-211 |
4.76e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTtmrmimgLLQihggQVLW-QGRPATVADRRTFGYMPeerglyvkqgvasqLIYLGQL 98
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKST-------LVN----EGLYaSGKARLISFLPKFSRNK--------------LIFIDQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 99 agmsrpearRSVTEL------LERfgladrakdKLESLSLGNQQRVQIAAAVMSRPQA--LILDEPFSGLDPTSVDVMAD 170
Cdd:cd03238 69 ---------QFLIDVglgyltLGQ---------KLSTLSGGELQRVKLASELFSEPPGtlFILDEPSTGLHQQDINQLLE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1450037824 171 LLREHTREGVPVLFSSHQLDLVDRlSDGLVVLSK------GRVVAQG 211
Cdd:cd03238 131 VIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPgsgksgGKVVFSG 176
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-221 |
7.18e-07 |
|
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: 49.47 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGR-----------PATVADRRTFGYMPEE-RGLYVKQg 87
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRisfssqfswimPGTIKENIIFGVSYDEyRYKSVVK- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 88 vASQLiylgQLAGMSRPEARRSVtelLERFGLadrakdkleSLSLGNQQRVQIAAAVMSRPQALILDEPFSGLD-PTSVD 166
Cdd:cd03291 135 -ACQL----EEDITKFPEKDNTV---LGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDvFTEKE 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1450037824 167 V----MADLLREHTRegvpVLFSSHQLDLvdRLSDGLVVLSKGRVVAQGTAEELRSAGP 221
Cdd:cd03291 198 IfescVCKLMANKTR----ILVTSKMEHL--KKADKILILHEGSSYFYGTFSELQSLRP 250
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
129-193 |
1.27e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 48.93 E-value: 1.27e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1450037824 129 SLSLGNQQRVQIAAAVMSRPQA---LILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVD 193
Cdd:pfam13304 236 ELSDGTKRLLALLAALLSALPKgglLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-202 |
2.11e-06 |
|
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: 47.18 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 24 VPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWqgrpatvaDRRTFGYMPEerglYVKqgvasqliylgqlagmsr 103
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW--------DGITPVYKPQ----YID------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 104 pearrsvtellerfgladrakdklesLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTREGV-PV 182
Cdd:cd03222 72 --------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTA 125
|
170 180
....*....|....*....|
gi 1450037824 183 LFSSHQLDLVDRLSDGLVVL 202
Cdd:cd03222 126 LVVEHDLAVLDYLSDRIHVF 145
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-211 |
2.56e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGL--LQIHGGQVLWQGRPATVADrrtfgymPE 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELS-------PE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 79 ERGlyvKQGVASQLIYLGQLAGMSRP-------EARRSV--TELLERFGLADRAKDKLESLSL---------------GN 134
Cdd:PRK09580 74 DRA---GEGIFMAFQYPVEIPGVSNQfflqtalNAVRSYrgQEPLDRFDFQDLMEEKIALLKMpedlltrsvnvgfsgGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 135 QQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMA---DLLREHTREGVPVLFSSHQLDLVDrlSDGLVVLSKGRVVAQG 211
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKIVAdgvNSLRDGKRSFIIVTHYQRILDYIK--PDYVHVLYQGRIVKSG 228
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-206 |
2.71e-06 |
|
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: 46.21 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 27 GQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVlwqgrpatvadrrtfgympeerglyvkqgvasqlIYLGqlagmsrPEA 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV----------------------------------IYID-------GED 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 107 RRSVTELLERFGLADRAKdklESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTS------VDVMADLLREHTREGV 180
Cdd:smart00382 41 ILEEVLDQLLLIIVGGKK---ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllLEELRLLLLLKSEKNL 117
|
170 180 190
....*....|....*....|....*....|.
gi 1450037824 181 PVLFSSHQL-----DLVDRLSDGLVVLSKGR 206
Cdd:smart00382 118 TVILTTNDEkdlgpALLRRRFDRRIVLLLIL 148
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
27-212 |
3.60e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.30 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 27 GQLIGFVGGNGAGKTTTMRMIMGLlQIHG---GQVLWQGRPA---TVAdrRTFGYMpEERGLYVKQ-GVASQLIYLGQL- 98
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGR-KTGGyieGDIRISGFPKkqeTFA--RISGYC-EQNDIHSPQvTVRESLIYSAFLr 981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 99 --AGMSRPEARRSVTELLERFGLaDRAKDKL------ESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMAD 170
Cdd:PLN03140 982 lpKEVSKEEKMMFVDEVMELVEL-DNLKDAIvglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMR 1060
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1450037824 171 LLREHTREGVPVLFSSHQ--LDLVDRLSDGLVVLSKGRVVAQGT 212
Cdd:PLN03140 1061 TVRNTVDTGRTVVCTIHQpsIDIFEAFDELLLMKRGGQVIYSGP 1104
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
20-195 |
5.87e-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: 45.43 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIgfVGGNGAGKTTTMRMImGLLqihggqvlwqgrpATVADRRTFGYMPEERGLYVKQGVASQLIYLGQLA 99
Cdd:cd03227 16 VTFGEGSLTII--TGPNGSGKSTILDAI-GLA-------------LGGAQSATRRRSGVKAGCIVAAVSAELIFTRLQLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 100 GmsrpeARRSVTELLERFGLADRAKDKLeslslgnqqrvqiaaavmsrpqaLILDEPFSGLDPTSVDVMADLLREHTREG 179
Cdd:cd03227 80 G-----GEKELSALALILALASLKPRPL-----------------------YILDEIDRGLDPRDGQALAEAILEHLVKG 131
|
170
....*....|....*.
gi 1450037824 180 VPVLFSSHQLDLVDRL 195
Cdd:cd03227 132 AQVIVITHLPELAELA 147
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-211 |
6.83e-06 |
|
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: 45.72 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 9 RRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHG---GQVLWQGRPATVADRRTFGympeerglyvk 85
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPG----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 86 qgvasQLIYLGQ----LAGMSrpearrsVTELLErFGLADRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLD 161
Cdd:cd03233 84 -----EIIYVSEedvhFPTLT-------VRETLD-FALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 162 PTSVDVMADLLREHTRE-GVPVLFSSHQ-----LDLVDRlsdgLVVLSKGRVVAQG 211
Cdd:cd03233 151 SSTALEILKCIRTMADVlKTTTFVSLYQasdeiYDLFDK----VLVLYEGRQIYYG 202
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
128-219 |
6.99e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 128 ESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADLLRE-HTREGVPVLFSSHQLDLVDRlSDGLVVLSK-- 204
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDiKDKADKTIITIAHRIASIKR-SDKIVVFNNpd 1435
|
90
....*....|....*...
gi 1450037824 205 --GRVV-AQGTAEELRSA 219
Cdd:PTZ00265 1436 rtGSFVqAHGTHEELLSV 1453
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-197 |
9.45e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 9.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 1 MLEVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGG--------QVLWQGRPATVADRRT 72
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGsytfpgnwQLAWVNQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 73 FGYM----PEERGLYVKQGVASQ-----LIYL--GQLAGMSRPEARRSVTELLERFGLA-DRAKDKLESLSLGNQQRVQI 140
Cdd:PRK10636 81 LEYVidgdREYRQLEAQLHDANErndghAIATihGKLDAIDAWTIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1450037824 141 AAAVMSRPQALILDEPFSGLDPTSVDVMADLLREHTreGVPVLFsSHQLDLVDRLSD 197
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQ--GTLILI-SHDRDFLDPIVD 214
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
30-166 |
1.29e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 30 IGFVGGNGAGKTTTMRMIMGLLQIHGGQvlwqgrpATVADRRTFGYMPEE---------RGLyVKQGVASQLIYLGQL-- 98
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVDKEFEGE-------ARPAPGIKVGYLPQEpqldpektvREN-VEEGVAEVKAALDRFne 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 99 --AGMSRPEArrSVTELLERFG-LAD---------------RAKDKL---------ESLSLGNQQRVQIAAAVMSRPQAL 151
Cdd:PRK11819 108 iyAAYAEPDA--DFDALAAEQGeLQEiidaadawdldsqleIAMDALrcppwdakvTKLSGGERRRVALCRLLLEKPDML 185
|
170
....*....|....*
gi 1450037824 152 ILDEPFSGLDPTSVD 166
Cdd:PRK11819 186 LLDEPTNHLDAESVA 200
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-216 |
1.38e-05 |
|
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: 46.48 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTtmrMIMGLLQIH---GGQVLWQGrpATVAD------RRTFGYMPEERGLYVkqgvAS 90
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSS---LTLGLFRINesaEGEIIIDG--LNIAKiglhdlRFKITIIPQDPVLFS----GS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 91 QLIYLGQLAGMSRPEARRSVtELLERFGLADRAKDKL--------ESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDP 162
Cdd:TIGR00957 1376 LRMNLDPFSQYSDEEVWWAL-ELAHLKTFVSALPDKLdhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 163 TSVDVMADLLREHTrEGVPVLFSSHQLDLVDRLSDgLVVLSKGRVVAQGTAEEL 216
Cdd:TIGR00957 1455 ETDNLIQSTIRTQF-EDCTVLTIAHRLNTIMDYTR-VIVLDKGEVAEFGAPSNL 1506
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
140-205 |
2.12e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 45.31 E-value: 2.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450037824 140 IAAAVMS--RPQALILDEPFSGLDPTSVDVMADLLREHTREGvPVLFSSHQLDLVDRLSDG-LVVLSKG 205
Cdd:COG4637 269 LLAALLSprPPPLLCIEEPENGLHPDLLPALAELLREASERT-QVIVTTHSPALLDALEPEeVLVLERE 336
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-207 |
5.17e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 30 IGFVGGNGAGKTTTMRMIMGLLQIHGGQVLwqgrpatvadrrtfgympeeRGLYVKQGVASQ------------LIYlgq 97
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVF--------------------RSAKVRMAVFSQhhvdgldlssnpLLY--- 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 98 lagMSR-----PEARrsVTELLERFGLA-DRAKDKLESLSLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTSVDVMADL 171
Cdd:PLN03073 595 ---MMRcfpgvPEQK--LRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQG 669
|
170 180 190
....*....|....*....|....*....|....*.
gi 1450037824 172 LRehTREGvPVLFSSHQLDLVDRLSDGLVVLSKGRV 207
Cdd:PLN03073 670 LV--LFQG-GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
129-212 |
1.95e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 42.22 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 129 SLSLGNQQRVQIAAAvMSRPQA----LILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVdRLSDGLVVLSK 204
Cdd:cd03271 169 TLSGGEAQRIKLAKE-LSKRSTgktlYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVI-KCADWIIDLGP 246
|
90
....*....|....
gi 1450037824 205 ------GRVVAQGT 212
Cdd:cd03271 247 eggdggGQVVASGT 260
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-58 |
3.53e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.86 E-value: 3.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1450037824 3 EVQELTRRFGDHTAVDQVSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQV 58
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-216 |
5.79e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVLWQGRPATVAD----RRTFGYMPEERGLY---VKQGVASQL 92
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGlrelRRQFSMIPQDPVLFdgtVRQNVDPFL 1408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 93 iylgqlagmsrpEARRS-VTELLERFGLADRAKDKLESL-----------SLGNQQRVQIAAAVMSRPQALIL-DEPFSG 159
Cdd:PTZ00243 1409 ------------EASSAeVWAALELVGLRERVASESEGIdsrvleggsnySVGQRQLMCMARALLKKGSGFILmDEATAN 1476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1450037824 160 LDPT-----SVDVMAdLLREHTregvpVLFSSHQLDLVDRLsDGLVVLSKGRVVAQGTAEEL 216
Cdd:PTZ00243 1477 IDPAldrqiQATVMS-AFSAYT-----VITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPREL 1531
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-164 |
6.89e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 20 VSFTVPDGQLIGFVGGNGAGKTTTMRMIMGLLQIHGGQVL--------------WQGRPATVADR--------------- 70
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIindshnlkdinlkwWRSKIGVVSQDpllfsnsiknnikys 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 71 ----RTFGYMPEErglYVKQGVASQ----------LIYLGQLAGMSRPEARRSVTELLERFGLADRAK------------ 124
Cdd:PTZ00265 484 lyslKDLEALSNY---YNEDGNDSQenknkrnscrAKCAGDLNDMSNTTDSNELIEMRKNYQTIKDSEvvdvskkvlihd 560
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1450037824 125 ------DKLESL--------SLGNQQRVQIAAAVMSRPQALILDEPFSGLDPTS 164
Cdd:PTZ00265 561 fvsalpDKYETLvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
116-212 |
8.24e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 40.37 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 116 RFGLADRAKDKLESLSLGNQQRVQIAA----AVMSRPQA---LILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQ 188
Cdd:COG3593 149 SLRIEDGKELPLDRLGSGFQRLILLALlsalAELKRAPAnpiLLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHS 228
|
90 100
....*....|....*....|....*
gi 1450037824 189 LDLVDRLS-DGLVVLSKGRVVAQGT 212
Cdd:COG3593 229 PHLLSEVPlENIRRLRRDSGGTTST 253
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
129-197 |
2.17e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 38.36 E-value: 2.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450037824 129 SLSLgnqqRVQIAAAVMSRPQALILDEPFSGLDPTSVD-VMADLLREHTREGVP-VLFSSHQLDLVDRLSD 197
Cdd:cd03240 125 SLII----RLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQKNFqLIVITHDEELVDAADH 191
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
129-201 |
4.01e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 37.63 E-value: 4.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1450037824 129 SLSLGNQQRVQIAAAVmsRPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVDRLSDGLVV 201
Cdd:cd03279 135 SLALALSEVLQNRGGA--RLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRLEV 205
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-216 |
4.33e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 129 SLSLGNQQRVQIAAAVMSR---PQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVdRLSDGLVVLSK- 204
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVI-KTADYIIDLGPe 907
|
90
....*....|....*..
gi 1450037824 205 -----GRVVAQGTAEEL 216
Cdd:TIGR00630 908 ggdggGTVVASGTPEEV 924
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
127-216 |
5.56e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450037824 127 LESLSLGNQQRVQIAAAVMS---RPQALILDEPFSGLDPTSVDVMADLLREHTREGVPVLFSSHQLDLVdRLSDGLVVLS 203
Cdd:PRK00635 807 LSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVV-KVADYVLELG 885
|
90
....*....|....*....
gi 1450037824 204 K------GRVVAQGTAEEL 216
Cdd:PRK00635 886 PeggnlgGYLLASCSPEEL 904
|
|
| |
