|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-217 |
1.15e-104 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 305.06 E-value: 1.15e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIE 87
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPEFYPFLSGYENLTYFGRMNG---NVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTN 164
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGlprKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 822524621 165 GLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT 217
Cdd:COG1131 161 GLDPEARRELWELLRELA-AEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-212 |
5.69e-89 |
|
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: 264.08 E-value: 5.69e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkQQFESTAAKIGAVIE 87
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPEFYPFLSGYENLTYFGRMNGnVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLD 167
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLG-IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 822524621 168 PSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHG 212
Cdd:cd03268 159 PDGIKELRELILSLR-DQGITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
9-230 |
1.27e-80 |
|
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: 244.00 E-value: 1.27e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 9 KVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIET 88
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 89 PEFYPFLSGYENLTYFGRMNGNV---TEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNG 165
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFdeeLKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 822524621 166 LDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQHNQSEEMET 230
Cdd:COG4555 163 LDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
8-213 |
2.56e-79 |
|
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: 238.07 E-value: 2.56e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIE 87
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPEFYPFLSGYENLTyfgrmngnvteeridevvkllgmgqvidrkvkaYSLGMRQRLGIAQALIHDPDVLILDEPTNGLD 167
Cdd:cd03230 81 EPSLYENLTVRENLK---------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 822524621 168 PSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:cd03230 128 PESRREFWELLRELK-KEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-301 |
2.11e-73 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 227.68 E-value: 2.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQqfeSTAAKIGAVI 86
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP---EDRRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 ETPEFYPFLSGYENLTYFGRMNG---NVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPT 163
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLKGlskAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 164 NGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQH-NQSEEMETIRIRVDDANKAA 242
Cdd:COG4152 158 SGLDPVNVELLKDVIRELA-AKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEiRRQFGRNTLRLEADGDAGWL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822524621 243 EMLD--QDVLIKGNDLLIHVKDEEIPN-VIRILLEKNiQVYRVYEERKTLEEQFLELTGGKD 301
Cdd:COG4152 237 RALPgvTVVEEDGDGAELKLEDGADAQeLLRALLARG-PVREFEEVRPSLNEIFIEVVGEKA 297
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-216 |
6.16e-67 |
|
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: 208.38 E-value: 6.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIE 87
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPEFYPFLSGYENLTYFGRMNG---NVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTN 164
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGvpgAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 822524621 165 GLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIA 212
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
9-235 |
1.76e-66 |
|
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: 207.25 E-value: 1.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 9 KVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQqfeSTAAKIGAVIET 88
Cdd:TIGR03740 2 ETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR---KDLHKIGSLIES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 89 PEFYPFLSGYENLTYFGRMNGnVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDP 168
Cdd:TIGR03740 79 PPLYENLTARENLKVHTTLLG-LPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 169 SGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIqhNQSEEMETIRIRV 235
Cdd:TIGR03740 158 IGIQELRELIRSFP-EQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKI--NKSENLEKLFVEV 221
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
15-298 |
3.24e-66 |
|
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: 209.55 E-value: 3.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 15 KRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIETPEFYPF 94
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 95 LSGYENLTYFGRMNG---NVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGI 171
Cdd:TIGR01188 81 LTGRENLEMMGRLYGlpkDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 172 HEMRMYIKKIaHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA---TQNIQHNQSEEMETIR------IRVDDANKAA 242
Cdd:TIGR01188 161 RAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAegtPEELKRRLGKDTLESRprdiqsLKVEVSMLIA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822524621 243 EMLD-----QDVLIKGNDLLIHVK--DEEIPNVIRILLEKNIQVYRVYEERKTLEEQFLELTG 298
Cdd:TIGR01188 240 ELGEtglglLAVTVDSDRIKILVPdgDETVPEIVEAAIRNGIRIRSISTERPSLDDVFLKLTG 302
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-216 |
8.73e-66 |
|
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: 205.29 E-value: 8.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTL----VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKI 82
Cdd:cd03266 1 MITADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 83 GAVIETPEFYPFLSGYENLTYFGR---MNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLIL 159
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGlygLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 160 DEPTNGLDPSGIHEMRMYIKKIaHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
8-213 |
3.12e-64 |
|
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: 201.27 E-value: 3.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGeVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIE 87
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPEFYPFLSGYENLTYFGRMNGNVT---EERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTN 164
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSkevKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 822524621 165 GLDPSGIHEMRMYIKKIAheQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:cd03264 160 GLDPEERIRFRNLLSELG--EDRIVILSTHIVEDVESLCNQVAVLNKGK 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
8-207 |
8.51e-61 |
|
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: 192.31 E-value: 8.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIE 87
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPEFYPFLSGYENLTYFGRMNG-NVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGL 166
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGlRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 822524621 167 DPSGIhemRMYIKKIAH--EQGKAVLVSSHllSEVELMCDRVI 207
Cdd:COG4133 163 DAAGV---ALLAELIAAhlARGGAVLLTTH--QPLELAAARVL 200
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
8-222 |
1.17e-56 |
|
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: 181.93 E-value: 1.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKR--IGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAV 85
Cdd:cd03263 1 LQIRNLTKTykKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 86 ietPEF---YPFLSGYENLTYFGRMNGNVTEERIDEVVKLL---GMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLIL 159
Cdd:cd03263 81 ---PQFdalFDELTVREHLRFYARLKGLPKSEIKEEVELLLrvlGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822524621 160 DEPTNGLDPSGIHEMRMYIKKIAheQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQH 222
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVR--KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
8-297 |
3.28e-56 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 183.82 E-value: 3.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIE 87
Cdd:TIGR03522 3 IRVSSLTKLYGTQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNPKEVQRNIGYLPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPEFYPFLSGYENLTYFG---RMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTN 164
Cdd:TIGR03522 83 HNPLYLDMYVREYLQFIAgiyGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEPTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 165 GLDPSGIHEMRMYIKKIAheQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQH-NQSEEMETIRIRVDDA--NKA 241
Cdd:TIGR03522 163 GLDPNQLVEIRNVIKNIG--KDKTIILSTHIMQEVEAICDRVIIINKGKIVADKKLDElSAANKKQVIEVEFEEQidLQL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822524621 242 AEMLDQDVLIK---GNDLLIHVKDEE--IPNVIRILLEKNIQVYRVYEERKTLEEQFLELT 297
Cdd:TIGR03522 241 FETLEEISSVKntgGNTWKLTFETPNdtRPEIFKLAQQKGLKLISLQQNEKNLEQVFREIT 301
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
8-216 |
8.37e-54 |
|
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: 174.39 E-value: 8.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKqqfESTAAKIGAVIE 87
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPEFYPFLSGYENLTYFGRMNGNVTEE---RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTN 164
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEarrRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 822524621 165 GLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:cd03269 158 GLDPVNVELLKDVIRELA-RAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-217 |
1.13e-51 |
|
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: 168.85 E-value: 1.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkqqFESTAAK--IGAV 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV---TGVPPERrnIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 86 IETPEFYPFLSGYENLTYFGRMNGN---VTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEP 162
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVpkaEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 822524621 163 TNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT 217
Cdd:cd03259 158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-213 |
7.29e-51 |
|
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: 165.82 E-value: 7.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAA---KIGA 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlrrRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 85 VIETPEFYPFLSGYENLTYfgrmngnvteeridevvkllgmgqvidrkvkAYSLGMRQRLGIAQALIHDPDVLILDEPTN 164
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL-------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 822524621 165 GLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:cd03229 130 ALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
8-216 |
7.79e-51 |
|
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: 167.51 E-value: 7.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLT-KRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAA-KIGAV 85
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 86 IETPE---FYPflSGYENLTyFGRMNGNVTEE----RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLI 158
Cdd:COG1122 81 FQNPDdqlFAP--TVEEDVA-FGPENLGLPREeireRVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 822524621 159 LDEPTNGLDPSGIHEMRMYIKKIaHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-216 |
1.24e-49 |
|
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: 165.22 E-value: 1.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQfeST---AAKIG 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASL--SRrelARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 84 AV--IETPEF------------YPFLSGyenltyFGRMNGNvTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQA 149
Cdd:COG1120 79 YVpqEPPAPFgltvrelvalgrYPHLGL------FGRPSAE-DREAVEEALERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 150 LIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-216 |
1.77e-49 |
|
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: 162.22 E-value: 1.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 9 KVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIET 88
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 89 pefypflsgyenltyfgrmngnvteerideVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDP 168
Cdd:cd03214 81 ------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 822524621 169 SgiHEMRMY--IKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:cd03214 131 A--HQIELLelLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-298 |
1.82e-49 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 166.52 E-value: 1.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 6 SIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAV 85
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 86 IETPEFYPFLSGYENLTYFGR---MNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEP 162
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRyfgLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 163 TNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQHNQSEEM--ETIRIRVDDANK 240
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIgcDVIEIYGPDPVA 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822524621 241 AAEMLD---QDVLIKGNDLLIHVKDEEiPNVIRIlleKNIQVYRVYEERKTLEEQFLELTG 298
Cdd:PRK13537 245 LRDELAplaERTEISGETLFCYVRDPE-PLHARL---KGRAGLRYLHRPANLEDVFLRLTG 301
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-213 |
1.41e-48 |
|
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: 161.10 E-value: 1.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQ-QFESTAAKIGAVIETPE---FYP 93
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlSLKELRRKVGLVFQNPDdqfFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 94 -------FlsGYENLTyfgrMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGL 166
Cdd:cd03225 92 tveeevaF--GLENLG----LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 822524621 167 DPSGIHEMRMYIKKIaHEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:cd03225 166 DPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-217 |
4.03e-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: 167.77 E-value: 4.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 2 TNEQSIVKVERLTKR-----IGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFE 76
Cdd:COG1123 255 AAAEPLLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 77 ST----AAKIGAVIETPE--FYPFLSGYENLTY----FGRMNGNVTEERIDEVVKLLGMG-QVIDRKVKAYSLGMRQRLG 145
Cdd:COG1123 335 RSlrelRRRVQMVFQDPYssLNPRMTVGDIIAEplrlHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822524621 146 IAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT 217
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVED 486
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
4.58e-48 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 160.64 E-value: 4.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 1 MTNEqSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQfestAA 80
Cdd:COG1121 1 MMMM-PAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 KIGAVIETPEF---YPF------LSG-YENLTYFGRMNGNVtEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQAL 150
Cdd:COG1121 76 RIGYVPQRAEVdwdFPItvrdvvLMGrYGRRGLFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822524621 151 IHDPDVLILDEPTNGLDPSGIHEMRMYIKKIaHEQGKAVLVSSHLLSEVELMCDRVIIIQHG 212
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-212 |
7.59e-47 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 156.54 E-value: 7.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 9 KVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQfestAAKIGAVIET 88
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 89 PEF---YPfLSGYE----NLTYFGRMNGNVTEE---RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLI 158
Cdd:cd03235 77 RSIdrdFP-ISVRDvvlmGLYGHKGLFRRLSKAdkaKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 822524621 159 LDEPTNGLDPSGIHEMRMYIKKIaHEQGKAVLVSSHLLSEVELMCDRVI-----IIQHG 212
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLllnrtVVASG 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-298 |
4.49e-46 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 158.46 E-value: 4.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 13 LTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIETPEFY 92
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 93 PFLSGYENLTYFGR---MNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPS 169
Cdd:PRK13536 127 LEFTVRENLLVFGRyfgMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 170 GIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQHNQSEEM--ETIRIRVDDANKAAEMLD- 246
Cdd:PRK13536 207 ARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIgcQVIEIYGGDPHELSSLVKp 285
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 822524621 247 --QDVLIKGNDLLIHVKDeeiPNVIRILLEKNIQVyRVYEERKTLEEQFLELTG 298
Cdd:PRK13536 286 yaRRIEVSGETLFCYAPD---PEQVRVQLRGRAGL-RLLQRPPNLEDVFLRLTG 335
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-276 |
4.63e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 157.94 E-value: 4.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVietpefypF-------- 94
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVV--------Fgqrsqlww 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 95 -LSGYENLTYFGRMNG---NVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSG 170
Cdd:COG4586 110 dLPAIDSFRLLKAIYRipdAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 171 IHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQ--HNQSEEMETIRIRVDDANKAAEMLDQD 248
Cdd:COG4586 190 KEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEelKERFGPYKTIVLELAEPVPPLELPRGG 269
|
250 260 270
....*....|....*....|....*....|.
gi 822524621 249 VLIK--GNDLLIHVKDEE-IPNVIRILLEKN 276
Cdd:COG4586 270 EVIEreGNRVRLEVDPREsLAEVLARLLARY 300
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-213 |
7.76e-46 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 154.85 E-value: 7.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 10 VERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGqsvkqqfestaaKIGAVIE-- 87
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------------RVSALLElg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPeFYPFLSGYENLTYFGRMNG---NVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTN 164
Cdd:COG1134 97 AG-FHPELTGRENIYLNGRLLGlsrKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 822524621 165 GLDPS-------GIHEMRmyikkiahEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:COG1134 176 VGDAAfqkkclaRIRELR--------ESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-216 |
1.04e-45 |
|
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: 154.37 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV----KQQFESTAAKI 82
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 83 GAVietpefypFLSG--------YENLTYFGRMNGNVTEERIDEVV----KLLGMGQVIDRKVKAYSLGMRQRLGIAQAL 150
Cdd:COG1127 85 GML--------FQGGalfdsltvFENVAFPLREHTDLSEAEIRELVleklELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 822524621 151 IHDPDVLILDEPTNGLDP--SG-IHEMrmyIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPitSAvIDEL---IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-213 |
1.10e-45 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 151.63 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 9 KVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAK-IGAVIE 87
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 tpefypfLSGyenltyfgrmngnvteeridevvkllgmgqvidrkvkayslGMRQRLGIAQALIHDPDVLILDEPTNGLD 167
Cdd:cd00267 81 -------LSG-----------------------------------------GQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 822524621 168 PSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:cd00267 113 PASRERLLELLRELA-EEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-216 |
2.84e-45 |
|
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: 153.26 E-value: 2.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 19 SKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIETPEFY----PF 94
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLwwdlPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 95 LSGYENLTYFGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEM 174
Cdd:cd03267 113 IDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 822524621 175 RMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:cd03267 193 RNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-208 |
3.33e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 153.71 E-value: 3.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 1 MTNEQSIVKVERLTKR----IGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQqfe 76
Cdd:COG1116 1 MSAAAPALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 77 sTAAKIGAVIETPEFYPFLSGYENLTY---FGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHD 153
Cdd:COG1116 78 -PGPDRGVVFQEPALLPWLTVLDNVALgleLRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 822524621 154 PDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVII 208
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVV 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-213 |
6.56e-45 |
|
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: 151.87 E-value: 6.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGS----KTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFEST----- 78
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 79 AAKIGAVIETPEFYPFLSGYENLT---YFGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPD 155
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVElplLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 822524621 156 VLILDEPTNGLDP-SGIHEMRMyIKKIAHEQGKAVLVSSHLLsEVELMCDRVIIIQHGE 213
Cdd:cd03255 161 IILADEPTGNLDSeTGKEVMEL-LRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
8-212 |
7.78e-45 |
|
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: 151.64 E-value: 7.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkQQFESTAAKIGAVIE 87
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPEFYPFLSGYENLTYFGRMNG---NVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTN 164
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKvpkDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 822524621 165 GLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHG 212
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-217 |
1.60e-44 |
|
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: 151.50 E-value: 1.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV----KQQFESTAAKIG 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 84 AVIETPEFYPFLSGYENLTYFGRMNGNVTEERIDEVVKL----LGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLIL 159
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEkleaVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 822524621 160 DEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT 217
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-222 |
3.14e-44 |
|
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: 151.11 E-value: 3.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGS----KTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQF-ESTAAKI 82
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRrKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 83 GAVIETPE--FYPFLSGY----ENLTYFGRMNgnvTEERIDEVVKLLGMG-QVIDRKVKAYSLGMRQRLGIAQALIHDPD 155
Cdd:COG1124 82 QMVFQDPYasLHPRHTVDrilaEPLRIHGLPD---REERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 156 VLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQH 222
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-215 |
1.47e-43 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 149.05 E-value: 1.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 6 SIVKVERLTKR-IGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTA----A 80
Cdd:COG3638 1 PMLELRNLSKRyPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 KIGAVIETPEFYPFLSGYEN-LT-YFGRMN------GNVTEERIDEVVKLL---GMGQVIDRKVKAYSLGMRQRLGIAQA 149
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNvLAgRLGRTStwrsllGLFPPEDRERALEALervGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 150 LIHDPDVLILDEPTNGLDPSGIHE-MRmYIKKIAHEQGKAVLVSSHllsEVEL---MCDRVIIIQHGEYV 215
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQvMD-LLRRIAREDGITVVVNLH---QVDLarrYADRIIGLRDGRVV 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-217 |
2.71e-43 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 154.80 E-value: 2.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKqqFEST----AAKI 82
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR--IRSPrdaiALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 83 GAV------IETpefypfLSGYENL------TYFGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQAL 150
Cdd:COG3845 83 GMVhqhfmlVPN------LTVAENIvlglepTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 151 IHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT 217
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLA-AEGKSIIFITHKLREVMAIADRVTVLRRGKVVGT 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-213 |
7.30e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 146.73 E-value: 7.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 5 QSIVKVERLTKRIGSK----TLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAA 80
Cdd:COG1136 2 SPLLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 K-----IGAVIETPEFYPFLSGYENLT---YFGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIH 152
Cdd:COG1136 82 RlrrrhIGFVFQFFNLLPELTALENVAlplLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822524621 153 DPDVLILDEPTNGLDP-SGIHEMRMyIKKIAHEQGKAVLVSSHllsEVEL--MCDRVIIIQHGE 213
Cdd:COG1136 162 RPKLILADEPTGNLDSkTGEEVLEL-LRELNRELGTTIVMVTH---DPELaaRADRVIRLRDGR 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
8-213 |
1.18e-42 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 149.84 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQqfesTAAK---IGA 84
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD----LPPKdrnIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 85 VIETPEFYPFLSGYENLTyFG----RMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILD 160
Cdd:COG3839 80 VFQSYALYPHMTVYENIA-FPlklrKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 822524621 161 EPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGR 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-224 |
2.12e-42 |
|
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: 146.34 E-value: 2.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 5 QSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV--KQQFESTAAKI 82
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItgLPPHRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 83 GAVIETPEFYPFLSGYENLT--YFGRMNGNV----------------TEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRL 144
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVLvaAHARLGRGLlaallrlprarreereARERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 145 GIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT---QNIQ 221
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEgtpAEVR 241
|
...
gi 822524621 222 HNQ 224
Cdd:COG0411 242 ADP 244
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
9-213 |
2.33e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 144.96 E-value: 2.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 9 KVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkQQFESTA--AKIGAVI 86
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-SAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 ETPEFYPflsG--YENLTY-FGRMNGNVTEERIDEVVKLLGMGQ-VIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEP 162
Cdd:COG4619 81 QEPALWG---GtvRDNLPFpFQLRERKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 822524621 163 TNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-164 |
3.05e-42 |
|
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: 142.79 E-value: 3.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV-KQQFESTAAKIGAVIETPEFYPFLSGYENL 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 102 TYFGRMNGNVTEE---RIDEVVKLLGMG----QVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTN 164
Cdd:pfam00005 81 RLGLLLKGLSKREkdaRAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
4-213 |
3.15e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 148.71 E-value: 3.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 4 EQSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkqqfESTAA--- 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----TGLPPekr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 KIGAVietpeF--Y---PFLSGYENLTY---FGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIH 152
Cdd:COG3842 78 NVGMV-----FqdYalfPHLTVAENVAFglrMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822524621 153 DPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGR 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-213 |
4.47e-42 |
|
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: 144.60 E-value: 4.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 15 KRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQsVKQQFESTAAkigavietpeFYPF 94
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSLLGLGGG----------FNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 95 LSGYENLTYFGRMNGNVTEE---RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPsgi 171
Cdd:cd03220 99 LTGRENIYLNGRLLGLSRKEideKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA--- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 822524621 172 HEMRMYIKKIAH--EQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:cd03220 176 AFQEKCQRRLREllKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-217 |
5.38e-42 |
|
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: 144.89 E-value: 5.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 9 KVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV--KQQFESTAAKIGAVI 86
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItgLPPHEIARLGIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 ETPEFYPFLSGYENL--------TYFGRMNGNVTE-----ERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHD 153
Cdd:cd03219 82 QIPRLFPELTVLENVmvaaqartGSGLLLARARREerearERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822524621 154 PDVLILDEPTNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT 217
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-209 |
5.45e-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: 144.15 E-value: 5.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSK----TLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQfestAAKIG 83
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP----GPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 84 AVIETPEFYPFLSGYENLTYFGRMNGNVTEERIDEVVKLL---GMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILD 160
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLelvGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 822524621 161 EPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIII 209
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-213 |
5.48e-42 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 144.79 E-value: 5.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 6 SIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkqqfesTA------ 79
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI------THlpmhkr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 80 AKIG-------AVIetpefypF--LSGYENLTYFGRMNGNVTEERIDEVVKLL---GMGQVidRKVKAYSL--GMRQRLG 145
Cdd:COG1137 76 ARLGigylpqeASI-------FrkLTVEDNILAVLELRKLSKKEREERLEELLeefGITHL--RKSKAYSLsgGERRRVE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 822524621 146 IAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLK-ERGIGVLITDHNVRETLGICDRAYIISEGK 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
8-228 |
6.65e-42 |
|
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: 144.61 E-value: 6.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQ--FESTAAKIGAV 85
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 86 IETPEFYPFLSGYENLTYFGRMNGNVTEER---IDEVVKLLGMGQVidRKVKAYSL--GMRQRLGIAQALIHDPDVLILD 160
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEReekLEELLEEFHITHL--RKSKASSLsgGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 822524621 161 EPTNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAtqniqHNQSEEM 228
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKVLA-----EGTPEEI 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-256 |
2.75e-40 |
|
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: 146.97 E-value: 2.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 5 QSIVKVERLTKRI--GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMT---EGEVWIDGQSVKQQFEST- 78
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 79 AAKIGAVIETPEFYPFLSGYENLTYFGRMNGNVT----EERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDP 154
Cdd:COG1123 82 GRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSraeaRARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 155 DVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA---TQNIQHNQSEEMETI 231
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEdgpPEEILAAPQALAAVP 241
|
250 260
....*....|....*....|....*
gi 822524621 232 RIRVDDANKAAEMLDQDVLIKGNDL 256
Cdd:COG1123 242 RLGAARGRAAPAAAAAEPLLEVRNL 266
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-215 |
1.08e-39 |
|
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: 138.85 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 9 KVERLTKRIGS-KTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTA----AKIG 83
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlrRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 84 AVIETPEFYPFLSGYENLTY--FGRMN------GNVTEERIDEVVKLL---GMGQVIDRKVKAYSLGMRQRLGIAQALIH 152
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSgrLGRRStwrslfGLFPKEEKQRALAALervGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822524621 153 DPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-213 |
4.91e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 136.72 E-value: 4.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTLV-ENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV-KQQFESTAA---K 81
Cdd:COG2884 1 MIRFENVSKRYPGGREAlSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsRLKRREIPYlrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 82 IGAVietpeFYPF-----LSGYEN----LTYFGrMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIH 152
Cdd:COG2884 81 IGVV-----FQDFrllpdRTVYENvalpLRVTG-KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822524621 153 DPDVLILDEPTNGLDPSGIHE-MRMyIKKIaHEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEiMEL-LEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
7-215 |
7.14e-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: 7.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRI----GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV----KQQFEST 78
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 79 AAKIGAVietpeF-YPFLS-------G---YENLTYFGRMNGnvtEERIDEVVKLLGMG-----QVIDRKVKAYSLGMRQ 142
Cdd:cd03257 81 RKEIQMV-----FqDPMSSlnprmtiGeqiAEPLRIHGKLSK---KEARKEAVLLLLVGvglpeEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822524621 143 RLGIAQALIHDPDVLILDEPTNGLDPS---GIHEMrmyIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSvqaQILDL---LKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-216 |
1.29e-38 |
|
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: 144.21 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQ-QFESTAAKIGAVIETPEFYpflS 96
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGVVLQDVFLF---S 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 G--YENLTYFgrmNGNVTEERIDEVVKLLGMGQVIDRKVKAY-----------SLGMRQRLGIAQALIHDPDVLILDEPT 163
Cdd:COG2274 563 GtiRENITLG---DPDATDEEIIEAARLAGLHDFIEALPMGYdtvvgeggsnlSGGQRQRLAIARALLRNPRILILDEAT 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 822524621 164 NGLDPsgIHEMRM--YIKKIAheQGKAVLVSSHLLSEVELmCDRVIIIQHGEYVA 216
Cdd:COG2274 640 SALDA--ETEAIIleNLRRLL--KGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVE 689
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-221 |
1.33e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 142.08 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 4 EQSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkqQF----ESTA 79
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV--RFrsprDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 80 AKIGAVIETPEFYPFLSGYENL------TYFGRMNGNVTEERIDEVVKLLGMGqvID--RKVKAYSLGMRQRLGIAQALI 151
Cdd:COG1129 79 AGIAIIHQELNLVPNLSVAENIflgrepRRGGLIDWRAMRRRARELLARLGLD--IDpdTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822524621 152 HDPDVLILDEPTNGLDPSGIHemRMY--IKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQ 221
Cdd:COG1129 157 RDARVLILDEPTASLTEREVE--RLFriIRRLK-AQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVA 225
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
7-222 |
2.87e-38 |
|
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: 135.09 E-value: 2.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQ--FESTAAKIGA 84
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLpmHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 85 VIETPEFYPFLSGYEN----LTYFGRMNGNVTEERIDEVVKLLGMGQVidRKVKAYSL--GMRQRLGIAQALIHDPDVLI 158
Cdd:TIGR04406 81 LPQEASIFRKLTVEENimavLEIRKDLDRAEREERLEALLEEFQISHL--RDNKAMSLsgGERRRVEIARALATNPKFIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822524621 159 LDEPTNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQH 222
Cdd:TIGR04406 159 LDEPFAGVDPIAVGDIKKIIKHLK-ERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAE 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
12-212 |
3.88e-38 |
|
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: 133.96 E-value: 3.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 12 RLTKRIGSKTLveNISFEVKkGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQ----SVKQQFESTAA-KIGAVI 86
Cdd:cd03297 5 DIEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQrKIGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 ETPEFYPFLSGYENLTY-FGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNG 165
Cdd:cd03297 82 QQYALFPHLNVRENLAFgLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 822524621 166 LDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHG 212
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-217 |
7.33e-38 |
|
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: 131.78 E-value: 7.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkqQFESTAAKIGAVIE 87
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV--SFASPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TpefypflsgyenltyfgrmngnvteeridevvkllgmgqvidrkVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLD 167
Cdd:cd03216 79 M--------------------------------------------VYQLSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 822524621 168 PSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT 217
Cdd:cd03216 115 PAEVERLFKVIRRLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-215 |
1.77e-37 |
|
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: 133.19 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRI-GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFEST-AAKIGAV 85
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 86 IETPEFYPFLSGYENLTYFGRMNG---NVTEERIDEVVKLLGM--GQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILD 160
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKwpkEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 822524621 161 EPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
9-216 |
4.86e-37 |
|
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: 131.40 E-value: 4.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 9 KVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV--KQQFESTAAKIGAVI 86
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItgLPPHERARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 ETPEFYPFLSGYENLT---YFGRmnGNVTEERIDEVVKLLGM-GQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEP 162
Cdd:cd03224 82 EGRRIFPELTVEENLLlgaYARR--RAKRKARLERVYELFPRlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 822524621 163 TNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:cd03224 160 SEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVL 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-215 |
5.40e-37 |
|
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: 131.53 E-value: 5.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRM-----TEGEVWIDGQSVKQQFESTAA-- 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 -KIGAVIETPefYPF-LSGYENLTYFGRMNGNVTEERIDEVV----KLLGMGQVIDRKVKAYSL--GMRQRLGIAQALIH 152
Cdd:cd03260 81 rRVGMVFQKP--NPFpGSIYDNVAYGLRLHGIKLKEELDERVeealRKAALWDEVKDRLHALGLsgGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822524621 153 DPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQgkAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
12-225 |
7.68e-37 |
|
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: 134.47 E-value: 7.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 12 RLTKRIGSKTLveNISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDG---QSVKQQFESTAAK--IGAVI 86
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKGIFLPPEKrrIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 ETPEFYPFLSGYENLTY-FGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNG 165
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYgMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 166 LDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQHNQS 225
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-217 |
9.68e-37 |
|
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: 131.16 E-value: 9.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTK----RIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQ--FESTAA 80
Cdd:cd03258 1 MIELKNVSKvfgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 --KIGAVietpeFYPF--LSG---YENLTY---FGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQAL 150
Cdd:cd03258 81 rrRIGMI-----FQHFnlLSSrtvFENVALpleIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 151 IHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT 217
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-213 |
4.23e-36 |
|
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: 129.28 E-value: 4.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkQQFESTAAKIGAVIE 87
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPEFYPFLSGYENLTyFG----RMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPT 163
Cdd:cd03300 80 NYALFPHLTVFENIA-FGlrlkKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 822524621 164 NGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
18-216 |
6.10e-36 |
|
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: 135.66 E-value: 6.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFEST-AAKIGAVIETPefyPFLS 96
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlRRRIAVVPQRP---HLFD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 G--YENLtyfgRM-NGNVTEERIDEVVKLLGMGQVIDRKVKAY-----------SLGMRQRLGIAQALIHDPDVLILDEP 162
Cdd:COG4987 423 TtlRENL----RLaRPDATDEELWAALERVGLGDWLAALPDGLdtwlgeggrrlSGGERRRLALARALLRDAPILLLDEP 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 822524621 163 TNGLDPSGIHEMRMYIKkiAHEQGKAVLVSSHLLSEVELMcDRVIIIQHGEYVA 216
Cdd:COG4987 499 TEGLDAATEQALLADLL--EALAGRTVLLITHRLAGLERM-DRILVLEDGRIVE 549
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-215 |
1.53e-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: 126.99 E-value: 1.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQfeSTAAKIGAVIETPEFYPFLSG 97
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK--ERRKSIGYVMQDVDYQLFTDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 98 YENLTYFGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMY 177
Cdd:cd03226 89 VREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGEL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 822524621 178 IKKIAhEQGKAVLVSSHllsEVELM---CDRVIIIQHGEYV 215
Cdd:cd03226 169 IRELA-AQGKAVIVITH---DYEFLakvCDRVLLLANGAIV 205
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-206 |
1.95e-35 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 135.25 E-value: 1.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 13 LTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIETPEFY 92
Cdd:NF033858 272 LTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 93 PFLSGYENLTYFGR---MNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPs 169
Cdd:NF033858 352 GELTVRQNLELHARlfhLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP- 430
|
170 180 190
....*....|....*....|....*....|....*....
gi 822524621 170 GIHEM--RMYIkKIAHEQGKAVLVSSHLLSEVELmCDRV 206
Cdd:NF033858 431 VARDMfwRLLI-ELSREDGVTIFISTHFMNEAER-CDRI 467
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
24-212 |
2.70e-35 |
|
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: 128.34 E-value: 2.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 24 ENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV----KQQFESTAAKIGAVIETPEFYPFlsgyE 99
Cdd:TIGR04521 22 DDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakkKKKLKDLRKKVGLVFQFPEHQLF----E 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 100 NLTY----FGRMNGNVTEERIDEVVK--LLGMGqvIDRKVK-----AYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDP 168
Cdd:TIGR04521 98 ETVYkdiaFGPKNLGLSEEEAEERVKeaLELVG--LDEEYLerspfELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 822524621 169 SGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHG 212
Cdd:TIGR04521 176 KGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKG 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-216 |
2.90e-35 |
|
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: 126.94 E-value: 2.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAK-IGAVIETPE-FYPFLsgYEN 100
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRnIGYVPQDVTlFYGTL--RDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 101 LTYFgrmNGNVTEERIDEVVKLLGMGQVIDRKVKAYSL-----------GMRQRLGIAQALIHDPDVLILDEPTNGLDPS 169
Cdd:cd03245 98 ITLG---APLADDERILRAAELAGVTDFVNKHPNGLDLqigergrglsgGQRQAVALARALLNDPPILLLDEPTSAMDMN 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 822524621 170 G----IHEMRMYIKkiaheqGKAVLVSSHLLSEVELmCDRVIIIQHGEYVA 216
Cdd:cd03245 175 SeerlKERLRQLLG------DKTLIIITHRPSLLDL-VDRIIVMDSGRIVA 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-213 |
3.27e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 130.22 E-value: 3.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 1 MTNeQSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVK----QQFE 76
Cdd:PRK11432 1 MTQ-KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVThrsiQQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 77 staakIGAVIETPEFYPFLSGYENLTYFGRMNGNVTEE---RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHD 153
Cdd:PRK11432 80 -----ICMVFQSYALFPHMSLGENVGYGLKMLGVPKEErkqRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 154 PDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-213 |
3.98e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 132.88 E-value: 3.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 10 VERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWI----------------DGQSVKQ 73
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpkglrigylpqeppldDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 74 QFESTAAKIGAVI--------ETPEFYPFLSGYENL-TYFGRMNGNVTEERIDEVVKLLGMGQVI-DRKVKAYSLGMRQR 143
Cdd:COG0488 81 TVLDGDAELRALEaeleeleaKLAEPDEDLERLAELqEEFEALGGWEAEARAEEILSGLGFPEEDlDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822524621 144 LGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHeqgkAVLVSSH---LLSEVelmCDRVIIIQHGE 213
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG----TVLVVSHdryFLDRV---ATRILELDRGK 226
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
26-194 |
4.89e-35 |
|
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: 125.23 E-value: 4.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 26 ISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAA---KIGAVIETPE---FYPFLSgyE 99
Cdd:TIGR01166 11 LNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLErrqRVGLVFQDPDdqlFAADVD--Q 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 100 NLTyFGRMN----GNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMR 175
Cdd:TIGR01166 89 DVA-FGPLNlglsEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQML 167
|
170
....*....|....*....
gi 822524621 176 MYIKKIaHEQGKAVLVSSH 194
Cdd:TIGR01166 168 AILRRL-RAEGMTVVISTH 185
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
7-215 |
8.42e-35 |
|
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: 126.26 E-value: 8.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGS-KTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV----KQQFESTAAK 81
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklrGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 82 IGAVIETPEFYPFLSGYENLTY--FGRMN------GNVTEERIDEVVKLL---GMGQVIDRKVKAYSLGMRQRLGIAQAL 150
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHgrLGYKPtwrsllGRFSEEDKERALSALervGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 822524621 151 IHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-216 |
1.78e-34 |
|
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: 125.58 E-value: 1.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 5 QSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEG-EVWIDGQS--------VKQqf 75
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggedvweLRK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 76 estaaKIGAVieTPEFYPFLSGYEN-----LTYF----GRMNgNVTEE---RIDEVVKLLGMGQVIDRKVKAYSLGMRQR 143
Cdd:COG1119 79 -----RIGLV--SPALQLRFPRDETvldvvLSGFfdsiGLYR-EPTDEqreRARELLELLGLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822524621 144 LGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVeLMC-DRVIIIQHGEYVA 216
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEI-PPGiTHVLLLKDGRVVA 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
18-213 |
1.47e-33 |
|
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: 128.72 E-value: 1.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQ-QFESTAAKIGAVIETPEFYPfLS 96
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAWVPQNPYLFA-GT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 GYENLTyFGRMngNVTEERIDEVVKLLGMGQVIDRKVKAY-----------SLGMRQRLGIAQALIHDPDVLILDEPTNG 165
Cdd:COG4988 427 IRENLR-LGRP--DASDEELEAALEAAGLDEFVAALPDGLdtplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAH 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 822524621 166 LDPSGIHEMRMYIKKIAheQGKAVLVSSHLLSEVELMcDRVIIIQHGE 213
Cdd:COG4988 504 LDAETEAEILQALRRLA--KGRTVILITHRLALLAQA-DRILVLDDGR 548
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
10-216 |
1.65e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 123.34 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 10 VERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVietp 89
Cdd:PRK13548 5 ARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 90 efypfLSGYENLTY---------FGRM---NGNVTEERI-DEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALI----- 151
Cdd:PRK13548 81 -----LPQHSSLSFpftveevvaMGRAphgLSRAEDDALvAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 152 -HDPDVLILDEPTNGLDPS-GIHEMRMyIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLAhQHHVLRL-ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVA 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
9-217 |
2.43e-33 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 122.01 E-value: 2.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 9 KVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQ--FESTAAKIGAVI 86
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLppHRIARLGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 ETPEFYPFLSGYENLT--YFGRMNGNVTEERIDEVVKL---LG-MgqvidRKVKAYSL--GMRQRLGIAQALIHDPDVLI 158
Cdd:COG0410 85 EGRRIFPSLTVEENLLlgAYARRDRAEVRADLERVYELfprLKeR-----RRQRAGTLsgGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 822524621 159 LDEPTNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT 217
Cdd:COG0410 160 LDEPSLGLAPLIVEEIFEIIRRLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLE 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-212 |
3.50e-33 |
|
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: 122.06 E-value: 3.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQfESTAAKIGAVIE 87
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV-PVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPEFYPFLSGYENLTyFG--------RMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLIL 159
Cdd:cd03296 82 HYALFRHMTVFDNVA-FGlrvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 822524621 160 DEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHG 212
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-215 |
4.35e-33 |
|
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: 121.22 E-value: 4.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 19 SKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIR---MTEGEVWIDGQSVK-QQFEStaaKIGAVIETPEFYPF 94
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKpDQFQK---CVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 95 LSGYENLTYFGRM-------NGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLD 167
Cdd:cd03234 96 LTVRETLTYTAILrlprkssDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 822524621 168 PSGIHEMRMYIKKIAHEqGKAVLVSSHL-LSEVELMCDRVIIIQHGEYV 215
Cdd:cd03234 176 SFTALNLVSTLSQLARR-NRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-213 |
4.62e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 127.59 E-value: 4.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQ-QFESTAAKIGAVieTPEFYPFlS 96
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVV--PQDTFLF-S 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 G--YENLTYFgrmNGNVTEERIDEVVKLLGMGQVIDRKVKAY-----------SLGMRQRLGIAQALIHDPDVLILDEPT 163
Cdd:COG1132 428 GtiRENIRYG---RPDATDEEVEEAAKAAQAHEFIEALPDGYdtvvgergvnlSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 822524621 164 NGLDPSGIHEMRMYIKKIAheQGKAVLVSSHLLSEVElMCDRVIIIQHGE 213
Cdd:COG1132 505 SALDTETEALIQEALERLM--KGRTTIVIAHRLSTIR-NADRILVLDDGR 551
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-221 |
6.99e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 122.26 E-value: 6.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 4 EQSIVKVERLTKRIGSKT-LVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV---KQQFESTA 79
Cdd:PRK13636 2 EDYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 80 AKIGAVIETPEFYPF-LSGYENLTyFGRMNGNVTE----ERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDP 154
Cdd:PRK13636 82 ESVGMVFQDPDNQLFsASVYQDVS-FGAVNLKLPEdevrKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 155 DVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQ 221
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
28-234 |
9.39e-33 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 120.34 E-value: 9.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 28 FEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFestaAKIGAVIETPEF---YPF------LSGY 98
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGW----RHIGYVPQRHEFawdFPIsvahtvMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 99 ENLTYFGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYI 178
Cdd:TIGR03771 77 TGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 822524621 179 KKIAHEqGKAVLVSSHLLSEVELMCDRVIIIqHGEYVATQNIQHNQSEE--METIRIR 234
Cdd:TIGR03771 157 IELAGA-GTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDPApwMTTFGVS 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
8-221 |
1.26e-32 |
|
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: 120.52 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLvENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQqFESTAAKIGAVIE 87
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN-LPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPEFYPFLSGYENLTYFGRMNGNVTEE---RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTN 164
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEierKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 822524621 165 GLDPSgIHEMRMY-IKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQ 221
Cdd:cd03299 159 ALDVR-TKEKLREeLKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-208 |
2.74e-32 |
|
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: 121.70 E-value: 2.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSK----TLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIR---MTEGEVWIDGQSV----KQQF 75
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLlklsEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 76 -------------ESTAA-----KIGAVIEtpefypflsgyENLTYFGRMNGNVTEERIDEVVKLLGMGQVIDRkVKAY- 136
Cdd:COG0444 81 rkirgreiqmifqDPMTSlnpvmTVGDQIA-----------EPLRIHGGLSKAEARERAIELLERVGLPDPERR-LDRYp 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 822524621 137 ---SLGMRQRLGIAQALIHDPDVLILDEPTNGLDPS---GIHEMrmyIKKIAHEQGKAVLVSSHLLSEVELMCDRVII 208
Cdd:COG0444 149 helSGGMRQRVMIARALALEPKLLIADEPTTALDVTiqaQILNL---LKDLQRELGLAILFITHDLGVVAEIADRVAV 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-215 |
3.69e-32 |
|
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: 120.06 E-value: 3.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 11 ERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV-----KQQFESTAAKIGAV 85
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsrKELRELRRKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 86 IETPEFYPFLSGYENLTYFGRMNG---NVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEP 162
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGvprAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 822524621 163 TNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-213 |
4.72e-32 |
|
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: 118.02 E-value: 4.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV---KQQFESTAAKIGA 84
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 85 VIETPEFYPFLSGYENLT----YFGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILD 160
Cdd:cd03262 81 VFQQFNLFPHLTVLENITlapiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 822524621 161 EPTNGLDPSGIHEMRMYIKKIAHEqGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
18-213 |
5.91e-32 |
|
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: 116.71 E-value: 5.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQ-QFESTAAKIGAVIETPefypFLs 96
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAYVPQDP----FL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 gyenltyfgrMNGNVTEEridevvkLLgmgqvidrkvkaySLGMRQRLGIAQALIHDPDVLILDEPTNGLDPsgIHEMRM 176
Cdd:cd03228 88 ----------FSGTIREN-------IL-------------SGGQRQRIAIARALLRDPPILILDEATSALDP--ETEALI 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 822524621 177 Y--IKKIAheQGKAVLVSSHLLSEVElMCDRVIIIQHGE 213
Cdd:cd03228 136 LeaLRALA--KGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-226 |
8.47e-32 |
|
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: 125.13 E-value: 8.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 3 NEQSIVKVERLTKRIG--SKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAA 80
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQ 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 KIGAVIETPEFYPFLSGYENLTYFGRMNGnVTEERIDEV----VKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDV 156
Cdd:TIGR01257 2013 NMGYCPQFDAIDDLLTGREHLYLYARLRG-VPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 157 LILDEPTNGLDPSGIHEMRMYIKKIAHEqGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQHNQSE 226
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSK 2160
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
8.87e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.94 E-value: 8.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 1 MTNEQSIVKVERLTKR--IGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQ-FES 77
Cdd:PRK13632 1 IKNKSVMIKVENVSFSypNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 78 TAAKIGAVIETPEFYPFLSGYENLTYFGRMNGNVTEER----IDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHD 153
Cdd:PRK13632 81 IRKKIGIIFQNPDNQFIGATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 154 PDVLILDEPTNGLDPSGIHEMRMYIKKIaHEQGKAVLVS-SHLLSEVeLMCDRVIIIQHGEYVATQNIQH--NQSEEMET 230
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDL-RKTRKKTLISiTHDMDEA-ILADKVIVFSEGKLIAQGKPKEilNNKEILEK 238
|
...
gi 822524621 231 IRI 233
Cdd:PRK13632 239 AKI 241
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-213 |
1.53e-31 |
|
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: 116.74 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTL-VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV----KQQFESTAAKI 82
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 83 GAVIETPEFYPFLSGYENLTYFGRMNG---NVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLIL 159
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGvppREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 822524621 160 DEPTNGLDPSGIHEMRMYIKKIaHEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-236 |
1.80e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 118.37 E-value: 1.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV-KQQFESTAAKIGAVIETPEFYPFLS 96
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItKENIREVRKFVGLVFQNPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 GYENLTYFGRMNGNVTEE----RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIH 172
Cdd:PRK13652 95 TVEQDIAFGPINLGLDEEtvahRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822524621 173 EMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQHNQSEEMETIRIRVD 236
Cdd:PRK13652 175 ELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVHLD 238
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
12-216 |
2.48e-31 |
|
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: 119.82 E-value: 2.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 12 RLTKRIGSKTLveNISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQ----SVKQQFESTAA-KIGAVI 86
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLPPHRrRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 ETPEFYPFLSGYENLTY-FGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNG 165
Cdd:COG4148 84 QEARLFPHLSVRGNLLYgRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 822524621 166 LDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:COG4148 164 LDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVA 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-216 |
2.70e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 114.61 E-value: 2.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 6 SIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQ--SVKQQFESTAAKIG 83
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdiSLLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 84 AVIETPEFYPFLSGYENLTYFGRMNGNVTEE----RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLIL 159
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIRDDLSAEqredRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 160 DEPTNGLDPSGIHEMRMYIKKIaHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-213 |
5.21e-30 |
|
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: 111.75 E-value: 5.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTkrigSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKqqFESTAAKIGAVI 86
Cdd:cd03215 4 VLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT--RRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 etpefypflsgyenltyfgrmnGNVTEERIDEVVkLLGMGqVIDRKVKAYSL--GMRQRLGIAQALIHDPDVLILDEPTN 164
Cdd:cd03215 78 ----------------------AYVPEDRKREGL-VLDLS-VAENIALSSLLsgGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 822524621 165 GLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:cd03215 134 GVDVGAKAEIYRLIRELA-DAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
9-221 |
7.26e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 112.93 E-value: 7.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 9 KVERLTKRIGSKTLveNISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkqqfesTAAKIG----A 84
Cdd:COG3840 3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL------TALPPAerpvS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 85 VI--ETPEFyPFLSGYENLtYFG-RMNGNVTEE---RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLI 158
Cdd:COG3840 75 MLfqENNLF-PHLTVAQNI-GLGlRPGLKLTAEqraQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822524621 159 LDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQ 221
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTA 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-217 |
9.75e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.43 E-value: 9.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRigskTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKqqFEST----AAKI 82
Cdd:COG1129 256 VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR--IRSPrdaiRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 83 GAVietPE------FYPFLSGYENLT--------YFGRMNGNVTEERIDEVVKLLGmgqV----IDRKVKAYSLGMRQRL 144
Cdd:COG1129 330 AYV---PEdrkgegLVLDLSIRENITlasldrlsRGGLLDRRRERALAEEYIKRLR---IktpsPEQPVGNLSGGNQQKV 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822524621 145 GIAQALIHDPDVLILDEPTNGLDP---SGIHEMrmyIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT 217
Cdd:COG1129 404 VLAKWLATDPKVLILDEPTRGIDVgakAEIYRL---IRELA-AEGKAVIVISSELPELLGLSDRILVMREGRIVGE 475
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-194 |
2.67e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 112.10 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVI- 86
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 ETPEFYPFLSGYEnLTYFGRM---NGNVTEE---RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILD 160
Cdd:COG4604 82 QENHINSRLTVRE-LVAFGRFpysKGRLTAEdreIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
170 180 190
....*....|....*....|....*....|....
gi 822524621 161 EPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSH 194
Cdd:COG4604 161 EPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLH 194
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-213 |
2.68e-29 |
|
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: 108.69 E-value: 2.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGqsvkqqfestAAKIGavie 87
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS----------TVKIG---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 tpeFYPFLSGyenltyfgrmngnvteeridevvkllgmgqvidrkvkayslGMRQRLGIAQALIHDPDVLILDEPTNGLD 167
Cdd:cd03221 67 ---YFEQLSG-----------------------------------------GEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 822524621 168 PSGIHEMRMYIKKiahEQGkAVLVSSH---LLSEVelmCDRVIIIQHGE 213
Cdd:cd03221 103 LESIEALEEALKE---YPG-TVILVSHdryFLDQV---ATKIIELEDGK 144
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
24-208 |
2.85e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 112.26 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 24 ENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkqqfESTAAKIGAVIETPEFYPFLSGYENLTy 103
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV----TGPGADRGVVFQKDALLPWLNVLDNVA- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 104 FG-RMNGNVTEER---IDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIK 179
Cdd:COG4525 99 FGlRLRGVPKAERrarAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLL 178
|
170 180
....*....|....*....|....*....
gi 822524621 180 KIAHEQGKAVLVSSHLLSEVELMCDRVII 208
Cdd:COG4525 179 DVWQRTGKGVFLITHSVEEALFLATRLVV 207
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-213 |
3.44e-29 |
|
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: 109.95 E-value: 3.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRM--TEGEVWIDGQSVKQQfeSTAAKIGAVIETPEFYPFL 95
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKR--SFRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 96 SGYENLTYfgrmngnvteerideVVKLLGMgqvidrkvkaySLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMR 175
Cdd:cd03213 98 TVRETLMF---------------AAKLRGL-----------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 822524621 176 MYIKKIAHeQGKAVLVSSH-LLSEVELMCDRVIIIQHGE 213
Cdd:cd03213 152 SLLRRLAD-TGRTIICSIHqPSSEIFELFDKLLLLSQGR 189
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
8-212 |
4.56e-29 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 116.29 E-value: 4.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKR--IGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQ-QFESTAAKIGA 84
Cdd:TIGR01842 317 LSVENVTIVppGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwDRETFGKHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 85 VIETPEFYPFLSGyENLTYFGRmngNVTEERIDEVVKLLGMGQVIDRKVKAY-----------SLGMRQRLGIAQALIHD 153
Cdd:TIGR01842 397 LPQDVELFPGTVA-ENIARFGE---NADPEKIIEAAKLAGVHELILRLPDGYdtvigpggatlSGGQRQRIALARALYGD 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 822524621 154 PDVLILDEPTNGLDPSGIHEMRMYIKKiAHEQGKAVLVSSHLLSEVELMcDRVIIIQHG 212
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKA-LKARGITVVVITHRPSLLGCV-DKILVLQDG 529
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-212 |
4.61e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 113.70 E-value: 4.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 6 SIVkVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAV 85
Cdd:COG1118 2 SIE-VRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 86 ietpeF--Y---PFLSGYENLTyFGRMNGNVTEERIDEVV----KLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDV 156
Cdd:COG1118 81 -----FqhYalfPHMTVAENIA-FGLRVRPPSKAEIRARVeellELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 822524621 157 LILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHG 212
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQG 210
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-217 |
4.65e-29 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 115.78 E-value: 4.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 25 NISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSvkQQFESTAAKIG---AVI-ETPEFYPFLSGYEN 100
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE--MRFASTTAALAagvAIIyQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 101 LtYFGRM---NGNVTEERIDEVV--KLLGMGQVID--RKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHE 173
Cdd:PRK11288 100 L-YLGQLphkGGIVNRRLLNYEAreQLEHLGVDIDpdTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 822524621 174 MRMYIKKIaHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT 217
Cdd:PRK11288 179 LFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
7-216 |
9.29e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.98 E-value: 9.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRI--GSKTLvENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFES-TAAKIG 83
Cdd:PRK13647 4 IIEVEDLHFRYkdGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 84 AVIETPEFYPFLSGYENLTYFGRMN----GNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLIL 159
Cdd:PRK13647 83 LVFQDPDDQVFSSTVWDDVAFGPVNmgldKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 160 DEPTNGLDPSGIHEMrMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:PRK13647 163 DEPMAYLDPRGQETL-MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLA 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-216 |
9.62e-29 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 113.20 E-value: 9.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkQQFESTAAKIGAVIE 87
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-NDVPPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPEFYPFLSGYENLTyFG----RMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPT 163
Cdd:PRK11000 83 SYALYPHLSVAENMS-FGlklaGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 822524621 164 NGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGeYVA 216
Cdd:PRK11000 162 SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAG-RVA 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
10-213 |
1.45e-28 |
|
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: 107.69 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 10 VERLTKRIG--SKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQfestaakigavie 87
Cdd:cd03246 3 VENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 tpefypflsgyeNLTYFGRMNGNVTEEridevVKLLGmGQVIDrkvKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLD 167
Cdd:cd03246 70 ------------DPNELGDHVGYLPQD-----DELFS-GSIAE---NILSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 822524621 168 PSG-------IHEMRMyikkiaheQGKAVLVSSHLLSEVElMCDRVIIIQHGE 213
Cdd:cd03246 129 VEGeralnqaIAALKA--------AGATRIVIAHRPETLA-SADRILVLEDGR 172
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
10-194 |
2.51e-28 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 107.83 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 10 VERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIETP 89
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 90 EFYPFLSGYENLTYFGRMNGnvTEER-IDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDP 168
Cdd:TIGR01189 83 GLKPELSALENLHFWAAIHG--GAQRtIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180 190
....*....|....*....|....*....|.
gi 822524621 169 SGI----HEMRmyikkiAH-EQGKAVLVSSH 194
Cdd:TIGR01189 161 AGVallaGLLR------AHlARGGIVLLTTH 185
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-168 |
2.70e-28 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 114.45 E-value: 2.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQF--ESTAAKIgA 84
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARhrRAVCPRI-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 85 VIetPE-----FYPFLSGYENLTYFGRMNGNVTEE---RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDV 156
Cdd:NF033858 80 YM--PQglgknLYPTLSVFENLDFFGRLFGQDAAErrrRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170
....*....|..
gi 822524621 157 LILDEPTNGLDP 168
Cdd:NF033858 158 LILDEPTTGVDP 169
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-215 |
3.20e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 110.94 E-value: 3.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSK----TLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQfeSTAA-- 80
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAL--SERElr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 ----KIGAVietpeFYPF--LSG---YENLTY---FGRMNGNVTEERIDEVVKLLGMGqviDRKvKAY----SLGMRQRL 144
Cdd:COG1135 79 aarrKIGMI-----FQHFnlLSSrtvAENVALpleIAGVPKAEIRKRVAELLELVGLS---DKA-DAYpsqlSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822524621 145 GIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
8-212 |
4.57e-28 |
|
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: 113.30 E-value: 4.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRI--GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQqfeSTAAKIGAV 85
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ---WDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 86 IetpefypflsGY-------------ENLtyfGRMnGNVTEERIDEVVKLLGMGQVIDRKVKAY-----------SLGMR 141
Cdd:COG4618 408 I----------GYlpqdvelfdgtiaENI---ARF-GDADPEKVVAAAKLAGVHEMILRLPDGYdtrigeggarlSGGQR 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 142 QRLGIAQALIHDPDVLILDEPTNGLDPSG-------IHEMRmyikkiahEQGKAVLVSSH---LLSEvelmCDRVIIIQH 211
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLDDEGeaalaaaIRALK--------ARGATVVVITHrpsLLAA----VDKLLVLRD 541
|
.
gi 822524621 212 G 212
Cdd:COG4618 542 G 542
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
10-207 |
4.88e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 107.27 E-value: 4.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 10 VERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQsvkqqfESTAAKIGAVIEtp 89
Cdd:PRK13539 5 GEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG------DIDDPDVAEACH-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 90 efY--------PFLSGYENLTYFGRMNGNvTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDE 161
Cdd:PRK13539 77 --YlghrnamkPALTVAENLEFWAAFLGG-EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 822524621 162 PTNGLDPSGIhemRMYIKKIAH--EQGKAVLVSSHllSEVELMCDRVI 207
Cdd:PRK13539 154 PTAALDAAAV---ALFAELIRAhlAQGGIVIAATH--IPLGLPGAREL 196
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
25-217 |
4.93e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.40 E-value: 4.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 25 NISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAA---KIGAVIETPEFYPFLSGYENL 101
Cdd:PRK13639 20 GINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEvrkTVGIVFQNPDDQLFAPTVEED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 102 TYFGRMNGNVTEE----RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMY 177
Cdd:PRK13639 100 VAFGPLNLGLSKEevekRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 822524621 178 IKKIaHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT 217
Cdd:PRK13639 180 LYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-216 |
5.02e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 108.66 E-value: 5.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 10 VERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIE-- 87
Cdd:COG4559 4 AENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPqh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 -TPEFyPFLSgyENLTYFGRMNGNVT----EERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQAL--IHDPD----- 155
Cdd:COG4559 84 sSLAF-PFTV--EEVVALGRAPHGSSaaqdRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEPVdggpr 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822524621 156 VLILDEPTNGLDPSgiHE---MRMyIKKIAHEQGkAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:COG4559 161 WLFLDEPTSALDLA--HQhavLRL-ARQLARRGG-GVVAVLHDLNLAAQYADRILLLHQGRLVA 220
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
10-195 |
5.09e-28 |
|
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: 107.19 E-value: 5.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 10 VERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIETP 89
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 90 EFYPFLSGYENLTYFGRMNGNVT-EERIDEVvkllGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDP 168
Cdd:cd03231 83 GIKTTLSVLENLRFWHADHSDEQvEEALARV----GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180
....*....|....*....|....*...
gi 822524621 169 SGIHEMRMYIKkiAH-EQGKAVLVSSHL 195
Cdd:cd03231 159 AGVARFAEAMA--GHcARGGMVVLTTHQ 184
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-216 |
8.81e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.56 E-value: 8.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 3 NEQSIVKVERLTKRI--GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKqqfESTA- 79
Cdd:PRK13635 1 MKEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS---EETVw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 80 ---AKIGAVIETPEFYPFLSGYENLTYFGRMNGNVTE----ERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIH 152
Cdd:PRK13635 78 dvrRQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPReemvERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822524621 153 DPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVeLMCDRVIIIQHGEYVA 216
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILE 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-213 |
1.02e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.08 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIdGQSVK-----QQFEstaak 81
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKigyfdQHQE----- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 82 igavietpEFYPFLSGYENLTYFGRmngNVTEEridEVVKLLGM----GQVIDRKVKAYSLGMRQRLGIAQALIHDPDVL 157
Cdd:COG0488 389 --------ELDPDKTVLDELRDGAP---GGTEQ---EVRGYLGRflfsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 822524621 158 ILDEPTNGLDPSGIHEMRMYIKKIaheQGkAVLVSSH---LLSEVelmCDRVIIIQHGE 213
Cdd:COG0488 455 LLDEPTNHLDIETLEALEEALDDF---PG-TVLLVSHdryFLDRV---ATRILEFEDGG 506
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-221 |
1.40e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 111.80 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIE 87
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPEFYPF--LSGYENLtYFGR------MNGNVTE-----ERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDP 154
Cdd:PRK09700 86 YQELSVIdeLTVLENL-YIGRhltkkvCGVNIIDwremrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 155 DVLILDEPTNGLDPSGIHEMRMYIKKIAHEqGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQ 221
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-212 |
1.59e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.04 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 1 MTNEQSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkQQFESTAA 80
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 KIGAVIETPEFYPFLSGYENLTYFGRMNGNVTEE---RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVL 157
Cdd:PRK09452 87 HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEitpRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 822524621 158 ILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHG 212
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
7-213 |
1.80e-27 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 106.62 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV---KQQFESTAAKIG 83
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdsKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 84 AVIETPEFYPFLSGYENLTY----FGRMNGNVTEERIDEVVKLLGMGQvidrKVKAY----SLGMRQRLGIAQALIHDPD 155
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLapikVKKMSKAEAEERAMELLERVGLAD----KADAYpaqlSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822524621 156 VLILDEPTNGLDPSGIHEMRMYIKKIAHEqGKAVLVSSHLLS---EVelmCDRVIIIQHGE 213
Cdd:COG1126 157 VMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGfarEV---ADRVVFMDGGR 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-215 |
2.73e-27 |
|
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: 106.42 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 22 LVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQ-QFESTAAKIGAVIEtpefypflsgyEN 100
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQ-----------EN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 101 LTYFGRMNGNVT-------EERIDEVVKL-----------LGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEP 162
Cdd:cd03252 86 VLFNRSIRDNIAladpgmsMERVIEAAKLagahdfiselpEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 822524621 163 TNGLDPSGIHEMRMYIKKIAheQGKAVLVSSHLLSEVelMC-DRVIIIQHGEYV 215
Cdd:cd03252 166 TSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTV--KNaDRIIVMEKGRIV 215
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
6-257 |
5.50e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 106.35 E-value: 5.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 6 SIVKVERLTKRIGS---KTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQ-FESTAAK 81
Cdd:PRK13650 3 NIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 82 IGAVIETPEFYPFLSGYENLTYFGRMNGNVT----EERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVL 157
Cdd:PRK13650 83 IGMVFQNPDNQFVGATVEDDVAFGLENKGIPheemKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 158 ILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELmCDRVIIIQHG--EYVATQNIQHNQSEEMETIRIRV 235
Cdd:PRK13650 163 ILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVAL-SDRVLVMKNGqvESTSTPRELFSRGNDLLQLGLDI 241
|
250 260
....*....|....*....|..
gi 822524621 236 DDANKAAEMLDQDVLIKGNDLL 257
Cdd:PRK13650 242 PFTTSLVQSLRQNGYDLPEGYL 263
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
8-213 |
1.85e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 105.13 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVE-----NISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV---KQQFESTA 79
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEkkaldNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 80 AKIGAVIETPEFYPFLSGYENLTYFGRMNGNVTEERIDEVVK----LLGMG--QVIDRKVKAYSLGMRQRLGIAQALIHD 153
Cdd:PRK13637 83 KKVGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKramnIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 154 PDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-215 |
1.85e-26 |
|
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: 106.04 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 38 LLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQfESTAAKIGAVIETPEFYPFLSGYENLTYFGRMNGNVTEE--- 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV-PPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEikp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 115 RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSH 194
Cdd:TIGR01187 80 RVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTH 159
|
170 180
....*....|....*....|.
gi 822524621 195 LLSEVELMCDRVIIIQHGEYV 215
Cdd:TIGR01187 160 DQEEAMTMSDRIAIMRKGKIA 180
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-168 |
2.00e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 104.35 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 1 MTNEQSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRM-----TEGEVWIDGQSVkqqF 75
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDI---Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 76 ESTA------AKIGAVIETPEfyPF-LSGYENLTYFGRMNGNVTEERIDEVVK--LLGMG---QVIDR-KVKAYSL--GM 140
Cdd:COG1117 82 DPDVdvvelrRRVGMVFQKPN--PFpKSIYDNVAYGLRLHGIKSKSELDEIVEesLRKAAlwdEVKDRlKKSALGLsgGQ 159
|
170 180
....*....|....*....|....*...
gi 822524621 141 RQRLGIAQALIHDPDVLILDEPTNGLDP 168
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDP 187
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-216 |
2.36e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 104.70 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 16 RIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV---KQQFESTAAKIGAVIETPEFY 92
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 93 PFLSGYENLTYFGRMNGNVTEE----RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDP 168
Cdd:PRK13638 90 IFYTDIDSDIAFSLRNLGVPEAeitrRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 822524621 169 SGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:PRK13638 170 AGRTQMIAIIRRIV-AQGNHVIISSHDIDLIYEISDAVYVLRQGQILT 216
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-208 |
3.91e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 105.20 E-value: 3.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 1 MTNEQSIVKVERLTKR--IGSKTL---------VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQ 69
Cdd:COG4608 1 AAMAEPLLEVRDLKKHfpVRGGLFgrtvgvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 70 SV-------------KQQ--FESTAA------KIGAVIETPefypflsgyenLTYFGRMNGNVTEERIDEVVKLLGMG-Q 127
Cdd:COG4608 81 DItglsgrelrplrrRMQmvFQDPYAslnprmTVGDIIAEP-----------LRIHGLASKAERRERVAELLELVGLRpE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 128 VIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPS---GIHEMRMYIKKiahEQGKAVLVSSHLLSEVELMCD 204
Cdd:COG4608 150 HADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSiqaQVLNLLEDLQD---ELGLTYLFISHDLSVVRHISD 226
|
....
gi 822524621 205 RVII 208
Cdd:COG4608 227 RVAV 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
25-222 |
4.25e-26 |
|
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: 103.07 E-value: 4.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 25 NISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQ-QFESTAAKIGAVIETpefyPFL-SG--YEN 100
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQD----TFLfSGtiMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 101 LTYFgrmNGNVTEERIDEVVKLLGMGQVIDRKVKAY-----------SLGMRQRLGIAQALIHDPDVLILDEPTNGLDPS 169
Cdd:cd03254 97 IRLG---RPNATDEEVIEAAKEAGAHDFIMKLPNGYdtvlgenggnlSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 822524621 170 GIHEMRMYIKKIAHeqGKAVLVSSHLLSEVElMCDRVIIIQHGEYVATQNIQH 222
Cdd:cd03254 174 TEKLIQEALEKLMK--GRTSIIIAHRLSTIK-NADKILVLDDGKIIEEGTHDE 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-209 |
5.04e-26 |
|
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: 107.37 E-value: 5.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAK-IGAVIETPEFYPfLS 96
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDqIAWVPQHPFLFA-GT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 GYENLTyFGRmnGNVTEERIDEVVKLLG-------MGQVIDRKV----KAYSLGMRQRLGIAQALIHDPDVLILDEPTNG 165
Cdd:TIGR02857 412 IAENIR-LAR--PDASDAEIREALERAGldefvaaLPQGLDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 822524621 166 LDPSGIHEMRMYIKKIAheQGKAVLVSSHLLSEVELMcDRVIII 209
Cdd:TIGR02857 489 LDAETEAEVLEALRALA--QGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-216 |
8.77e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.78 E-value: 8.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 6 SIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQ----QFESTAAK 81
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlssrQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 82 IGAVIETPEFYPF--LSGYEN---LTYFGRMNGNvTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDV 156
Cdd:PRK11231 81 LPQHHLTPEGITVreLVAYGRspwLSLWGRLSAE-DNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 157 LILDEPTNGLDPSGIHEMrMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:PRK11231 160 VLLDEPTTYLDINHQVEL-MRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-233 |
9.80e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 106.55 E-value: 9.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 13 LTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMT--EGEVWIDGQSVKQQFESTAAKIGAVIETPE 90
Cdd:PRK13549 11 ITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTERAGIAIIHQE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 91 F--YPFLSGYEN------LTYFGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEP 162
Cdd:PRK13549 91 LalVKELSVLENiflgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822524621 163 TNGLDPSGIhEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIqhnqsEEMETIRI 233
Cdd:PRK13549 171 TASLTESET-AVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPA-----AGMTEDDI 235
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
10-194 |
9.95e-26 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 101.03 E-value: 9.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 10 VERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAK---IGAVi 86
Cdd:PRK13538 4 ARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllyLGHQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 etPEFYPFLSGYENLTYFGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGL 166
Cdd:PRK13538 83 --PGIKTELTALENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|....*....
gi 822524621 167 DPSGIHEMRMYIkkIAH-EQGKAVLVSSH 194
Cdd:PRK13538 161 DKQGVARLEALL--AQHaEQGGMVILTTH 187
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-212 |
1.02e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.47 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkqqfESTAAKIGAVI 86
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV----EGPGAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 ETPEFYPFLSGYENLTYFGRMNGNVTEERID---EVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPT 163
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEiahQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 822524621 164 NGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHG 212
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-215 |
1.05e-25 |
|
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: 101.92 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 19 SKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQ-QFESTAAKIGAVIE-TPEFYPFLs 96
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQdTVLFNDTI- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 gYENLTYfGRMngNVTEERIDEVVKLLGMGQVIDRKVKAY-----------SLGMRQRLGIAQALIHDPDVLILDEPTNG 165
Cdd:cd03253 92 -GYNIRY-GRP--DATDEEVIEAAKAAQIHDKIMRFPDGYdtivgerglklSGGEKQRVAIARAILKNPPILLLDEATSA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 822524621 166 LDPSGIHEMRMYIKKIAheQGKAVLVSSHLLSEVeLMCDRVIIIQHGEYV 215
Cdd:cd03253 168 LDTHTEREIQAALRDVS--KGRTTIVIAHRLSTI-VNADKIIVLKDGRIV 214
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
13-222 |
1.15e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 102.84 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 13 LTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkQQFESTAAK----------- 81
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL-AKLNRAQRKafrrdiqmvfq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 82 --IGAVieTPEFYPFLSGYENLTYFGRMNGNVTEERIDEVVKLLGMG-QVIDRKVKAYSLGMRQRLGIAQALIHDPDVLI 158
Cdd:PRK10419 97 dsISAV--NPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822524621 159 LDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQH 222
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGD 238
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-199 |
1.52e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.39 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 16 RIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQS----VKQQFESTAAKIGAVIETPE- 90
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArvayVPQRSEVPDSLPLTVRDLVAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 91 -FYPFLSGYENLTYFGRMngnvteeRIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPS 169
Cdd:NF040873 81 gRWARRGLWRRLTRDDRA-------AVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180 190
....*....|....*....|....*....|
gi 822524621 170 GIHEMRMYIKKiAHEQGKAVLVSSHLLSEV 199
Cdd:NF040873 154 SRERIIALLAE-EHARGATVVVVTHDLELV 182
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
23-215 |
1.79e-25 |
|
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: 101.54 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQ-QFESTAAKIGAVIETpefyPFL---SGY 98
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGLVSQD----VFLfndTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 99 ENLTYfGRMngNVTEERIDEVVKLLGMGQVIDRKVKAY-----------SLGMRQRLGIAQALIHDPDVLILDEPTNGLD 167
Cdd:cd03251 94 ENIAY-GRP--GATREEVEEAARAANAHEFIMELPEGYdtvigergvklSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 822524621 168 psgiHEMRMYIKKIAHE--QGKAVLVSSHLLSEVElMCDRVIIIQHGEYV 215
Cdd:cd03251 171 ----TESERLVQAALERlmKNRTTFVIAHRLSTIE-NADRIVVLEDGKIV 215
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
20-213 |
2.22e-25 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 100.71 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 20 KTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAkIGAVIETPEFYPFLSGYE 99
Cdd:TIGR01277 11 EHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP-VSMLFQENNLFAHLTVRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 100 NLTyFG-----RMNGnVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEM 174
Cdd:TIGR01277 90 NIG-LGlhpglKLNA-EQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEM 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 822524621 175 RMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:TIGR01277 168 LALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
8-212 |
2.39e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.15 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVI- 86
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 -ETPEFYPF-------LSGYENLTYFGRMnGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLI 158
Cdd:PRK09536 84 qDTSLSFEFdvrqvveMGRTPHRSRFDTW-TETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 822524621 159 LDEPTNGLDPSgiHEMRMY--IKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHG 212
Cdd:PRK09536 163 LDEPTASLDIN--HQVRTLelVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-218 |
2.53e-25 |
|
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: 100.26 E-value: 2.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 30 VKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQfESTAAKIGAVIETPEFYPFLSGYENLTyFGRMNG 109
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA-PPADRPVSMLFQENNLFAHLTVEQNVG-LGLSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 110 ----NVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQ 185
Cdd:cd03298 99 lkltAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAET 178
|
170 180 190
....*....|....*....|....*....|...
gi 822524621 186 GKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQ 218
Cdd:cd03298 179 KMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-215 |
4.09e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 103.38 E-value: 4.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkQQFESTAAKIGAVI 86
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 ETPEFYPFLSGYENLTyFG----RMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEP 162
Cdd:PRK11607 98 QSYALFPHMTVEQNIA-FGlkqdKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 822524621 163 TNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-217 |
4.92e-25 |
|
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: 104.50 E-value: 4.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 4 EQSIVKVERLTKRI-----GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEV-------WIDGQSV 71
Cdd:TIGR03269 276 GEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKP 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 72 KQQFESTAAK-IGAVIETPEFYPFLSGYENLT---------YFGRMNGNVTeeridevVKLLGMGQ-----VIDRKVKAY 136
Cdd:TIGR03269 356 GPDGRGRAKRyIGILHQEYDLYPHRTVLDNLTeaiglelpdELARMKAVIT-------LKMVGFDEekaeeILDKYPDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 137 SLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
.
gi 822524621 217 T 217
Cdd:TIGR03269 509 I 509
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-215 |
5.51e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 100.59 E-value: 5.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 6 SIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMM-------VGMIRMteGEVWIDG-QSVKQQ--- 74
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRV--GDITIDTaRSLSQQkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 75 FESTAAKIGAVIETPEFYPFLSGYENLtyfgrMNGNV---------TEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLG 145
Cdd:PRK11264 80 IRQLRQHVGFVFQNFNLFPHRTVLENI-----IEGPVivkgepkeeATARARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 146 IAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVsSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIV-THEMSFARDVADRAIFMDQGRIV 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-224 |
1.20e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 99.84 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 3 NEQSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV----KQQFEST 78
Cdd:PRK11831 3 SVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 79 AAKIGAVIETPEFYPFLSGYENLTYFGRMNGNVTEERID-------EVVKLLGMGQVIDRKVkaySLGMRQRLGIAQALI 151
Cdd:PRK11831 83 RKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHstvmmklEAVGLRGAAKLMPSEL---SGGMARRAALARAIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822524621 152 HDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA---TQNIQHNQ 224
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAhgsAQALQANP 235
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-206 |
1.41e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 99.42 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 1 MTNEQSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV--KQQFEST 78
Cdd:COG4674 4 DTMHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLtgLDEHEIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 79 AAKIGAVIETPEFYPFLSGYENL------------TYFGRMNGNVtEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGI 146
Cdd:COG4674 84 RLGIGRKFQKPTVFEELTVFENLelalkgdrgvfaSLFARLTAEE-RDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 147 AQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAheQGKAVLVSSHLLSEVELMCDRV 206
Cdd:COG4674 163 GMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLA--GKHSVVVVEHDMEFVRQIARKV 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-208 |
1.54e-24 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 103.35 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 2 TNEQSIVKVERLTKRIGSKTL-VEniSFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWID------GQSVKQQ 74
Cdd:PRK13409 335 SERETLVEYPDLTKKLGDFSLeVE--GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykPQYIKPD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 75 FESTA----AKIGAVIETPEFYPflsgyenltyfgrmngnvteeridEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQAL 150
Cdd:PRK13409 413 YDGTVedllRSITDDLGSSYYKS------------------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822524621 151 IHDPDVLILDEPTNGLDPsgihEMRM----YIKKIAHEQGKAVLVSSHLLSEVELMCDRVII 208
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDV----EQRLavakAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
5-217 |
1.65e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.29 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 5 QSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGA 84
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 85 V-------------------------IETpefyPFLSGYENLTYFGRMNGNVTeERIDEVVKLLGMGQVIDRKVKAYSLG 139
Cdd:PRK11300 83 VrtfqhvrlfremtvienllvaqhqqLKT----GLFSGLLKTPAFRRAESEAL-DRAATWLERVGLLEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 822524621 140 MRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT 217
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
13-180 |
1.78e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 101.07 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 13 LTKRIGSKTLV-ENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkQQFESTAAKIGAVIETPEF 91
Cdd:PRK11650 9 VRKSYDGKTQViKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-NELEPADRDIAMVFQNYAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 92 YPFLSGYENLTYfGRMNGNVT----EERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLD 167
Cdd:PRK11650 88 YPHMSVRENMAY-GLKIRGMPkaeiEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
170
....*....|...
gi 822524621 168 PSGIHEMRMYIKK 180
Cdd:PRK11650 167 AKLRVQMRLEIQR 179
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-212 |
1.97e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 98.63 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKqqfeSTAAKI---- 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN----DPKVDErlir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 83 ---GAVIETPEFYPFLSGYENLTyFG--RMNGNVTEERIDEVVKLL---GMGQVIDRKVKAYSLGMRQRLGIAQALIHDP 154
Cdd:PRK09493 77 qeaGMVFQQFYLFPHLTALENVM-FGplRVRGASKEEAEKQARELLakvGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 822524621 155 DVLILDEPTNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHG 212
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-208 |
4.47e-24 |
|
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: 101.78 E-value: 4.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 2 TNEQSIVKVERLTKRIGSKTL-VEniSFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVwiDGQ---SVKQQFES 77
Cdd:COG1245 336 KEEETLVEYPDLTKSYGGFSLeVE--GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDlkiSYKPQYIS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 78 TAAKiGAVIEtpefypFLSGyenlTYFGRMNGNVTEEridEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVL 157
Cdd:COG1245 412 PDYD-GTVEE------FLRS----ANTDDFGSSYYKT---EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLY 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 822524621 158 ILDEPTNGLDPsgihEMRM----YIKKIAHEQGKAVLVSSHLLSEVELMCDRVII 208
Cdd:COG1245 478 LLDEPSAHLDV----EQRLavakAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-215 |
5.47e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 98.62 E-value: 5.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 19 SKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVK--QQFESTAAKIGAVIETPEFYPFLS 96
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeENLWDIRNKAGMVFQNPDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 GYENLTYFGRMNGNVTEE----RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIH 172
Cdd:PRK13633 102 IVEEDVAFGPENLGIPPEeireRVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 822524621 173 EMRMYIKKIAHEQGKAVLVSSHLLSEVeLMCDRVIIIQHGEYV 215
Cdd:PRK13633 182 EVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVV 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
13-215 |
5.79e-24 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 101.66 E-value: 5.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 13 LTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLM-----RMMVGMIRmtEGEVWIDGQSVKQQFEStaaKIGAVIE 87
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVKG--SGSVLLNGMPIDAKEMR---AISAYVQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPE-FYPFLSGYENLTYFG--RMNGNVTE----ERIDEVVKLLGMGQVIDRK------VKAYSLGMRQRLGIAQALIHDP 154
Cdd:TIGR00955 106 QDDlFIPTLTVREHLMFQAhlRMPRRVTKkekrERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822524621 155 DVLILDEPTNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEvELMC--DRVIIIQHGEYV 215
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQPSS-ELFElfDKIILMAEGRVA 246
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
7-212 |
5.88e-24 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 97.04 E-value: 5.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRI--GSKTL--VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKI 82
Cdd:TIGR02211 1 LLKCENLGKRYqeGKLDTrvLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 83 -----GAVIETPEFYPFLSGYENLTY---FGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDP 154
Cdd:TIGR02211 81 rnkklGFIYQFHHLLPDFTALENVAMpllIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822524621 155 DVLILDEPTNGLD---PSGIHEMrmyIKKIAHEQGKAVLVSSHLLSEVELMcDRVIIIQHG 212
Cdd:TIGR02211 161 SLVLADEPTGNLDnnnAKIIFDL---MLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDG 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
7-217 |
3.77e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.84 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKT-----LVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAK 81
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 82 -----------------IGAVIETPEFYPFLSGYENLTYFGRMNGNVTEERIDEVVK--LLGMG---QVIDRKVKAYSLG 139
Cdd:PRK13631 101 tnpyskkiknfkelrrrVSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKfyLNKMGlddSYLERSPFGLSGG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 822524621 140 MRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMrMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT 217
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-211 |
4.80e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 95.18 E-value: 4.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 1 MTNeqsIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQsvkqqfestaA 80
Cdd:PRK09544 1 MTS---LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK----------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 KIGAVIETPEFYPFLSgyenLTY--FGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLI 158
Cdd:PRK09544 68 RIGYVPQKLYLDTTLP----LTVnrFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 822524621 159 LDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQH 211
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-218 |
5.37e-23 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 98.36 E-value: 5.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 13 LTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMT--EGEVWIDGQSVKQQFESTAAKIGAVIETPE 90
Cdd:TIGR02633 7 IVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 91 --FYPFLSGYEN------LTYFG-RMNGNVTEERIDEVVKLLGMGQVID-RKVKAYSLGMRQRLGIAQALIHDPDVLILD 160
Cdd:TIGR02633 87 ltLVPELSVAENiflgneITLPGgRMAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 822524621 161 EPTNGLDPSGIhEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQ 218
Cdd:TIGR02633 167 EPSSSLTEKET-EILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATK 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-247 |
5.73e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.86 E-value: 5.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 25 NISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIdGQSV------KQQFESTAAKIGAVIETPEFYPFLSGY 98
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkkNKKLKPLRKKVGIVFQFPEHQLFEETV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 99 ENLTYFGRMNGNVTEE----RIDEVVKLLGMGQ-VIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHE 173
Cdd:PRK13634 104 EKDICFGPMNFGVSEEdakqKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKE 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822524621 174 MRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQH--NQSEEMETIRIRVDDANKAAEMLDQ 247
Cdd:PRK13634 184 MMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREifADPDELEAIGLDLPETVKFKRALEE 259
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-216 |
5.89e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.96 E-value: 5.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 25 NISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEG-----EVWIDGQSVKQQFESTAAKIGAVIETPEFYPFLSGYE 99
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 100 NLTYFGRMNGNVTEERIDEV----VKLLGMGQVI-DRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEM 174
Cdd:PRK13643 104 KDVAFGPQNFGIPKEKAEKIaaekLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 822524621 175 RMYIKKIaHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:PRK13643 184 MQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-228 |
7.37e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 95.67 E-value: 7.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAK-----IGAVIETPEFYPFLSG 97
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKklrkkVSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 98 YENLTYFGRMNGNVTEERIDEV----VKLLGMG-QVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIH 172
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKEKalkwLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 822524621 173 EMrMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYvatqnIQHNQSEEM 228
Cdd:PRK13641 183 EM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL-----IKHASPKEI 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-215 |
9.87e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.85 E-value: 9.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 13 LTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRmTEGEVWIDGQSVKQ----QFESTAAKIGAVIET 88
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNlnrrQLLPVRHRIQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 89 P--EFYPFLSGY----ENLT-YFGRMNGNVTEERIDEVVKLLGMGQVI-DRKVKAYSLGMRQRLGIAQALIHDPDVLILD 160
Cdd:PRK15134 371 PnsSLNPRLNVLqiieEGLRvHQPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 822524621 161 EPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-242 |
1.22e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 94.31 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 5 QSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMI---RMTEGEVWIDGQSVKQQ------F 75
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREgrlardI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 76 ESTAAKIGAVIETPEFYPFLSGYEN---------------LTYFGRmngnVTEERIDEVVKLLGMGQVIDRKVKAYSLGM 140
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENvligalgstpfwrtcFSWFTR----EQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 141 RQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNI 220
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
250 260
....*....|....*....|....*
gi 822524621 221 QHNQSEEMETIRI---RVDDANKAA 242
Cdd:PRK09984 238 QQFDNERFDHLYRsinRVEENAKAA 262
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-196 |
1.23e-22 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 97.43 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFES-TAAKIGAVIETPEFYPfLS 96
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDeVRRRVSVCAQDAHLFD-TT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 GYENLTyFGRmnGNVTEERIDEV---VKLL--------GMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNG 165
Cdd:TIGR02868 425 VRENLR-LAR--PDATDEELWAAlerVGLAdwlralpdGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180 190
....*....|....*....|....*....|.
gi 822524621 166 LDPSGihEMRMYIKKIAHEQGKAVLVSSHLL 196
Cdd:TIGR02868 502 LDAET--ADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-217 |
1.82e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.54 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkQQFESTAAKIGAVIE 87
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPEFYPFLSGYENLTyFG--------RMNGNVTEERideVVKLLGMGQV---IDRKVKAYSLGMRQRLGIAQALIHDPDV 156
Cdd:PRK10851 82 HYALFRHMTVFDNIA-FGltvlprreRPNAAAIKAK---VTQLLEMVQLahlADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 822524621 157 LILDEPTNGLDPSGIHEMRMYIKKIaHEQGK--AVLVsSHLLSEVELMCDRVIIIQHG--EYVAT 217
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQL-HEELKftSVFV-THDQEEAMEVADRVVVMSQGniEQAGT 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-212 |
1.97e-22 |
|
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: 97.78 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 25 NISFevKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIETPEFYPFLSGYENLTYF 104
Cdd:TIGR01257 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 105 GRMNGNVTEERIDEVVKLL---GMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKi 181
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLedtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK- 1106
|
170 180 190
....*....|....*....|....*....|.
gi 822524621 182 aHEQGKAVLVSSHLLSEVELMCDRVIIIQHG 212
Cdd:TIGR01257 1107 -YRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
25-213 |
3.12e-22 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 96.50 E-value: 3.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 25 NISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQsvkqqfeSTAAKIGAVIETPefypfLSGYENLTYF 104
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-------AALIAISSGLNGQ-----LTGIENIELK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 105 GRMNGnVTEERIDE----VVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMrmyIKK 180
Cdd:PRK13545 110 GLMMG-LTKEKIKEiipeIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC---LDK 185
|
170 180 190
....*....|....*....|....*....|....*
gi 822524621 181 IAH--EQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:PRK13545 186 MNEfkEQGKTIFFISHSLSQVKSFCTKALWLHYGQ 220
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
12-208 |
3.30e-22 |
|
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: 92.86 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 12 RLTKRIGSKTL-VENISFevKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDG-------QSVKQQFESTAAKIG 83
Cdd:cd03237 5 TMKKTLGEFTLeVEGGSI--SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtvsykpQYIKADYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 84 AVIeTPEFYpflsgyeNLTYFgrmngnvteerIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPT 163
Cdd:cd03237 83 SSI-TKDFY-------THPYF-----------KTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 822524621 164 NGLDPsgihEMRMY----IKKIAHEQGKAVLVSSHLLSEVELMCDRVII 208
Cdd:cd03237 144 AYLDV----EQRLMaskvIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-213 |
5.79e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.89 E-value: 5.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 1 MTNEQSIVKVERLTKRIGSKT--LVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQ-FES 77
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDnFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 78 TAAKIGAVIETPE--FYPFLSGYEnlTYFGRMNGNVT----EERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALI 151
Cdd:PRK13648 81 LRKHIGIVFQNPDnqFVGSIVKYD--VAFGLENHAVPydemHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822524621 152 HDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVeLMCDRVIIIQHGE 213
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGT 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-216 |
7.93e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 92.36 E-value: 7.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 1 MTNEQSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkQQFES--T 78
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI-QHYASkeV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 79 AAKIGAVIE---TP-----EFYPFLSGYENLTYFGRMNGNvTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQAL 150
Cdd:PRK10253 80 ARRIGLLAQnatTPgditvQELVARGRYPHQPLFTRWRKE-DEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822524621 151 IHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
8-215 |
8.08e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 92.84 E-value: 8.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVE-----NISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEV-WIDGQSVKQQ----FES 77
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIFKDEKNKKktkeKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 78 TAAK--------------------IGAVIETPEFYPFLSGYENLTYFGRMNGNVT----EERIDEVVKLLGMGQ-VIDRK 132
Cdd:PRK13651 83 VLEKlviqktrfkkikkikeirrrVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSkeeaKKRAAKYIELVGLDEsYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 133 VKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIaHEQGKAVLVSSHLLSEVELMCDRVIIIQHG 212
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
...
gi 822524621 213 EYV 215
Cdd:PRK13651 242 KII 244
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-231 |
9.78e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.16 E-value: 9.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 2 TNEQSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAK 81
Cdd:PRK10575 6 NHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 82 igAVIETPEFYPFLSGY--ENLTYFGRMN--------GNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALI 151
Cdd:PRK10575 86 --KVAYLPQQLPAAEGMtvRELVAIGRYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 152 HDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQN-IQHNQSEEMET 230
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTpAELMRGETLEQ 243
|
.
gi 822524621 231 I 231
Cdd:PRK10575 244 I 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-215 |
1.01e-21 |
|
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: 94.75 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRmTEGEVWIDGQSV----KQQFESTAAKIGAVIETPefypflsgy 98
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLdglsRRALRPLRRRMQVVFQDP--------- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 99 enltyFG----RMN--------------GNVTEERIDEVVKLL---GM-GQVIDRKVKAYSLGMRQRLGIAQALIHDPDV 156
Cdd:COG4172 372 -----FGslspRMTvgqiiaeglrvhgpGLSAAERRARVAEALeevGLdPAARHRYPHEFSGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822524621 157 LILDEPTNGLDPSgiheMRMYI----KKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:COG4172 447 LVLDEPTSALDVS----VQAQIldllRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-194 |
1.02e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 90.39 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 22 LVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIETPEFYPFLSGYENL 101
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 102 TYfgRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMrmyIKKI 181
Cdd:PRK13540 96 LY--DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI---ITKI 170
|
170
....*....|....*
gi 822524621 182 -AH-EQGKAVLVSSH 194
Cdd:PRK13540 171 qEHrAKGGAVLLTSH 185
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-215 |
1.10e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 93.33 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTK--RIGSKTL--VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQ--QFESTAA- 80
Cdd:PRK11153 2 IELKNISKvfPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlsEKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 -KIGAVietpeFYPFlsgyeNL----TYFGrmngNVT-------------EERIDEVVKLLGMGQVIDRKVKAYSLGMRQ 142
Cdd:PRK11153 82 rQIGMI-----FQHF-----NLlssrTVFD----NVAlplelagtpkaeiKARVTELLELVGLSDKADRYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822524621 143 RLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-230 |
1.10e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.17 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 19 SKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQ-QFESTAAKIGAVIETPEFYPfLSG 97
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLFS-GSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 98 YENLTYFGRmngNVTEERIDEVVKLLGMGQVIDRKVKAY-----------SLGMRQRLGIAQALIHDPDVLILDEPTNGL 166
Cdd:TIGR00958 572 RENIAYGLT---DTPDEEIMAAAKAANAHDFIMEFPNGYdtevgekgsqlSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822524621 167 DPSGIHEMRMYIKKiaheQGKAVLVSSHLLSEVElMCDRVIIIQHGEYVatQNIQHNQSEEMET 230
Cdd:TIGR00958 649 DAECEQLLQESRSR----ASRTVLLIAHRLSTVE-RADQILVLKKGSVV--EMGTHKQLMEDQG 705
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-216 |
1.29e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 94.35 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 26 ISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGA--VIETPEFYPFLSGYENLTy 103
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIylVPQEPLLFPNLSVKENIL- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 104 FGRMNGNVTEERIDEVVKLLGMGqvIDRKVKAYSLGM--RQRLGIAQALIHDPDVLILDEPTNGLDPsgiHEMRMYIKKI 181
Cdd:PRK15439 109 FGLPKRQASMQKMKQLLAALGCQ--LDLDSSAGSLEVadRQIVEILRGLMRDSRILILDEPTASLTP---AETERLFSRI 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 822524621 182 A--HEQGKAVLVSSHLLSEVELMCDRVIIIQHGeYVA 216
Cdd:PRK15439 184 RelLAQGVGIVFISHKLPEIRQLADRISVMRDG-TIA 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-216 |
1.35e-21 |
|
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: 89.68 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 19 SKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIETPEFYPfLSGY 98
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFD-TTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 99 ENLtyfGRmngnvteeridevvkllgmgqvidrkvkAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPsgIHEMRMYI 178
Cdd:cd03247 93 NNL---GR----------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDP--ITERQLLS 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 822524621 179 KKIAHEQGKAVLVSSHLLSEVELMcDRVIIIQHGEYVA 216
Cdd:cd03247 140 LIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
11-215 |
1.63e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.56 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 11 ERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVK-----QQFESTAAKIGAV 85
Cdd:PRK10070 32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdaELREVRRKKIAMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 86 IETPEFYPFLSGYENLTYFGRMNGNVTEERIDEVVKLL---GMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEP 162
Cdd:PRK10070 112 FQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALrqvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 822524621 163 TNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-215 |
2.15e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.20 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVK--QQFESTAAKIGAVIETPEFYPFLSGYEN 100
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfSKLQGIRKLVGIVFQNPETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 101 LTYFGRMNGNV----TEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDP-SGIHEMR 175
Cdd:PRK13644 98 DLAFGPENLCLppieIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPdSGIAVLE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 822524621 176 MyIKKIaHEQGKAVLVSSHLLSEVElMCDRVIIIQHGEYV 215
Cdd:PRK13644 178 R-IKKL-HEKGKTIVYITHNLEELH-DADRIIVMDRGKIV 214
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-215 |
2.44e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.88 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 5 QSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV---KQQFESTAAK 81
Cdd:PRK14246 8 EDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 82 ----IGAVIETPEFYPFLSGYENLTYFGRMNGnVTEER-----IDEVVKLLGM-GQVIDR---KVKAYSLGMRQRLGIAQ 148
Cdd:PRK14246 88 lrkeVGMVFQQPNPFPHLSIYDNIAYPLKSHG-IKEKReikkiVEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 149 ALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQgkAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-215 |
2.89e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.96 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 25 NISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQ-----FESTAAKIGAVIETPEFYPFLSGYE 99
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkdIKQIRKKVGLVFQFPESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 100 NLTYFGRMNGNVTEERID----EVVKLLGMGQ-VIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEM 174
Cdd:PRK13649 105 KDVAFGPQNFGVSQEEAEalarEKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKEL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 822524621 175 rMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:PRK13649 185 -MTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-212 |
3.40e-21 |
|
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: 88.84 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGmiRMT----EGEVWIDGQSVKQQFESTaakIGAVIETPEFYP 93
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTagviTGEILINGRPLDKNFQRS---TGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 94 FLSGYENLTYfgrmngnvteeridevvkllgmgqviDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHE 173
Cdd:cd03232 93 NLTVREALRF--------------------------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 822524621 174 MRMYIKKIAhEQGKAVLVSSHLLSEVEL-MCDRVIIIQHG 212
Cdd:cd03232 147 IVRFLKKLA-DSGQAILCTIHQPSASIFeKFDRLLLLKRG 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-213 |
4.77e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 92.68 E-value: 4.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIR-MTEGEVWIDGQSVKQQ--FESTAAKIGAVIETPEFY---PFLS 96
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRnpQQAIAQGIAMVPEDRKRDgivPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 GYENLTY-----FGRMNgnvteeRIDEVVKLLGMGQVIDR-KVKAYSL---------GMRQRLGIAQALIHDPDVLILDE 161
Cdd:PRK13549 358 VGKNITLaaldrFTGGS------RIDDAAELKTILESIQRlKVKTASPelaiarlsgGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 822524621 162 PTNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:PRK13549 432 PTRGIDVGAKYEIYKLINQLV-QQGVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-237 |
5.64e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.51 E-value: 5.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 26 ISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRmTEGEVWIDGQSVKQQFESTAAKIGAVI---ETPEFypFLSGYENLT 102
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHRAYLsqqQSPPF--AMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 103 YFGRMNGNVT--EERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQAL--IH---DPD--VLILDEPTNGLDpsgIHE 173
Cdd:COG4138 92 LHQPAGASSEavEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqVWptiNPEgqLLLLDEPMNSLD---VAQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822524621 174 MRMYIKKIAH--EQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA---TQNI--QHNQSE--EMETIRIRVDD 237
Cdd:COG4138 169 QAALDRLLRElcQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVAsgeTAEVmtPENLSEvfGVKFRRLEVEG 241
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-224 |
6.80e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.58 E-value: 6.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 24 ENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIeTPEFYPFlSGY--ENL 101
Cdd:PRK11160 357 KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVV-SQRVHLF-SATlrDNL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 102 TYfgrMNGNVTEERIDEVVKLLGMGQVI--DRKVKAY--------SLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGI 171
Cdd:PRK11160 435 LL---AAPNASDEALIEVLQQVGLEKLLedDKGLNAWlgeggrqlSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 822524621 172 HEMRMYIKKiaHEQGKAVLVSSHLLSEVELMcDRVIIIQHGEYVATQNiqHNQ 224
Cdd:PRK11160 512 RQILELLAE--HAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGT--HQE 559
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
7-215 |
7.41e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.77 E-value: 7.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTLVEN---ISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVK-QQFESTAAKI 82
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 83 GAVIETPEFYPFLSGYENLTYFGRMNGNVTEE----RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLI 158
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVAFGMENQGIPREemikRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 159 LDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVElMCDRVIIIQHGEYV 215
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEII 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-216 |
9.16e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 88.84 E-value: 9.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 26 ISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIrMTEGEVWIDGQSVKQQFESTAAKIGAVI---ETPEF------YPFLS 96
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLsqqQTPPFampvfqYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 GYENLtyfgrmNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIH-DPDV------LILDEPTNGLDPS 169
Cdd:PRK03695 94 QPDKT------RTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLDVA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 822524621 170 GIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:PRK03695 168 QQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLA 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-227 |
1.40e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.38 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 3 NEQSIVKVERLTKRIGSKtlVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAK- 81
Cdd:PRK09700 261 AHETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKk 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 82 -IGAVIETPE---FYPFLSGYENLTY-----FGRMNGNV------TEERI-DEVVKLLGMG-QVIDRKVKAYSLGMRQRL 144
Cdd:PRK09700 339 gMAYITESRRdngFFPNFSIAQNMAIsrslkDGGYKGAMglfhevDEQRTaENQRELLALKcHSVNQNITELSGGNQQKV 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 145 GIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQHNQ 224
Cdd:PRK09700 419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDM 497
|
...
gi 822524621 225 SEE 227
Cdd:PRK09700 498 SEE 500
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-222 |
1.69e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 89.77 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 19 SKTL--VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEV-WID----GQSVKQQ----------FESTAAK 81
Cdd:PRK15079 31 PKTLkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLGkdllGMKDDEWravrsdiqmiFQDPLAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 82 ------IGAVIETP--EFYPFLSGYEnltyfgrmngnvTEERIDEVVKLLGM-GQVIDRKVKAYSLGMRQRLGIAQALIH 152
Cdd:PRK15079 111 lnprmtIGEIIAEPlrTYHPKLSRQE------------VKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 153 DPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVII------IQHGEYVAT-QNIQH 222
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVmylghaVELGTYDEVyHNPLH 255
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-213 |
2.86e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 87.14 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 5 QSIVKVERLT--KRIGSKTLV-ENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQ-QFESTAA 80
Cdd:cd03248 9 KGIVKFQNVTfaYPTRPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 KIGAVIETPEFYPfLSGYENLTYfGRmnGNVTEERIDEVVKLLGMGQVIDRKVKAY-----------SLGMRQRLGIAQA 149
Cdd:cd03248 89 KVSLVGQEPVLFA-RSLQDNIAY-GL--QSCSFECVKEAAQKAHAHSFISELASGYdtevgekgsqlSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822524621 150 LIHDPDVLILDEPTNGLDPSGIHEMRMYIKKiaHEQGKAVLVSSHLLSEVElMCDRVIIIQHGE 213
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYD--WPERRTVLVIAHRLSTVE-RADQILVLDGGR 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
11-242 |
3.59e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.36 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 11 ERLT-KRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkqQFESTAAKIGA-VIET 88
Cdd:PRK11288 256 VRLRlDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI--DIRSPRDAIRAgIMLC 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 89 PE------FYPFLSGYENLTYFGR---------MNGNVTEERIDEVVKLLGMGQ-VIDRKVKAYSLGMRQRLGIAQALIH 152
Cdd:PRK11288 334 PEdrkaegIIPVHSVADNINISARrhhlragclINNRWEAENADRFIRSLNIKTpSREQLIMNLSGGNQQKAILGRWLSE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 153 DPDVLILDEPTNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAtqNIQHNQSEEMETIR 232
Cdd:PRK11288 414 DMKVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRIAG--ELAREQATERQALS 490
|
250
....*....|
gi 822524621 233 IRVDDANKAA 242
Cdd:PRK11288 491 LALPRTSAAV 500
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
26-194 |
4.29e-20 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 86.44 E-value: 4.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 26 ISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQfeSTAAKIGAVIETPEFYPFLSGYENLTYFG 105
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG--DRSRFMAYLGHLPGLKADLSTLENLHFLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 106 RMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQ 185
Cdd:PRK13543 108 GLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGG 187
|
....*....
gi 822524621 186 GkAVLVSSH 194
Cdd:PRK13543 188 G-AALVTTH 195
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-215 |
4.98e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 87.91 E-value: 4.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQ-----FESTAAKIGAVIETPEFYPFLSG 97
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkyIRPVRKRIGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 98 YENLTYFGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSL-----GMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIH 172
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPfqmsgGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 822524621 173 EMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:PRK13646 183 QVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-300 |
5.39e-20 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 88.64 E-value: 5.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 5 QSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAG--KTTLMRMMVGMirmtegevwiDGQSVKQQFESTAAKI 82
Cdd:NF000106 11 RNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GP----------DAGRRPWRF*TWCANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 83 GAVIETPEFY--------PFLSGYENLTYFGR---MNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALI 151
Cdd:NF000106 81 RALRRTIG*Hrpvr*grrESFSGRENLYMIGR*ldLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 152 HDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEqGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQHNQSE-EMET 230
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKvGGRT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 231 IRIRVDDANKAAEM---LDQDVL--IKG-----NDLLIH---VKDEEIPNVIRILLEKNIQVYRVYEERKTLEEQFLELT 297
Cdd:NF000106 240 LQIRPAHAAELDRMvgaIAQAGLdgIAGatadhEDGVVNvpiVSDEQLSAVVGMLGERGFTISGHQHPSAQL*EVFLAIT 319
|
...
gi 822524621 298 GGK 300
Cdd:NF000106 320 GQK 322
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
8-227 |
5.44e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 86.61 E-value: 5.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQ--SVKQQFESTAA----- 80
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAIrllrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 KIGAVIETPEFYPFLSGYENLT----YFGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDV 156
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIeapcKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 157 LILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVsSHllsEVEL---MCDRVIIIQHG---EYVATQNIQHNQSEE 227
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIV-TH---EVEFarkVASQVVYMEKGriiEQGDASHFTQPQTEA 235
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-197 |
5.48e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.41 E-value: 5.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 3 NEQSIVKVERLTKRIG----SKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQfeST 78
Cdd:PRK11629 1 MNKILLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKL--SS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 79 AAK-------IGAVIETPEFYPFLSGYENLTY---FGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQ 148
Cdd:PRK11629 79 AAKaelrnqkLGFIYQFHHLLPDFTALENVAMpllIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIAR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 822524621 149 ALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLS 197
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ 207
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-221 |
5.56e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.68 E-value: 5.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 12 RLTKRIGSKTL---------VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV--KQQFESTAA 80
Cdd:PRK10762 248 RLDKAPGEVRLkvdnlsgpgVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtRSPQDGLAN 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 KI----------GAVIEtpefypfLSGYEN-----LTYFGRMNGNV--TEERI--DEVVKLL-----GMGQVIdrkvKAY 136
Cdd:PRK10762 328 GIvyisedrkrdGLVLG-------MSVKENmsltaLRYFSRAGGSLkhADEQQavSDFIRLFniktpSMEQAI----GLL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 137 SLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHlLSEVELMCDRVIIIQHG---- 212
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSE-MPEVLGMSDRILVMHEGrisg 475
|
....*....
gi 822524621 213 EYVATQNIQ 221
Cdd:PRK10762 476 EFTREQATQ 484
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-228 |
5.88e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 86.75 E-value: 5.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 5 QSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRM-----TEGEVWIDGQSVKQQFESTA 79
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIYSPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 80 ---AKIGAVIETPEFYPFlSGYENLTYFGRMNGNVTEERIDEVVKLLGMGQVIDRKVK--------AYSLGMRQRLGIAQ 148
Cdd:PRK14239 83 dlrKEIGMVFQQPNPFPM-SIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKdrlhdsalGLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 149 ALIHDPDVLILDEPTNGLDP--SGIHEMRMYIKKiaheQGKAVLVSSHLLSEVELMCDRVIIIQHGEYvatqnIQHNQSE 226
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPisAGKIEETLLGLK----DDYTMLLVTRSMQQASRISDRTGFFLDGDL-----IEYNDTK 232
|
..
gi 822524621 227 EM 228
Cdd:PRK14239 233 QM 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-227 |
6.03e-20 |
|
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: 89.50 E-value: 6.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIR-MTEGEVWIDGQSV--KQQFESTAAKIGAVIETPE---FYPFLS 96
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVdiRNPAQAIRAGIAMVPEDRKrhgIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 GYENLTyFGRMNGNVTEERIDEVVKLLGMGQVIDR-KVKAYSL---------GMRQRLGIAQALIHDPDVLILDEPTNGL 166
Cdd:TIGR02633 356 VGKNIT-LSVLKSFCFKMRIDAAAELQIIGSAIQRlKVKTASPflpigrlsgGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822524621 167 DPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQnIQHNQSEE 227
Cdd:TIGR02633 435 DVGAKYEIYKLINQLA-QEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDF-VNHALTQE 493
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
6-215 |
6.54e-20 |
|
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: 85.78 E-value: 6.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 6 SIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMT---EGEVWIDGQSVKQQFESTAAKI 82
Cdd:cd03233 6 WRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 83 GAVIETPEFYPFLSGYENLTYFGRMNGNvteeridEVVkllgmgqvidRKVkaySLGMRQRLGIAQALIHDPDVLILDEP 162
Cdd:cd03233 86 IYVSEEDVHFPTLTVRETLDFALRCKGN-------EFV----------RGI---SGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 822524621 163 TNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLS-EVELMCDRVIIIQHGEYV 215
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQI 199
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-215 |
6.81e-20 |
|
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: 89.36 E-value: 6.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 1 MTNEqSIVKVERLTKRIGS----KTLVENISFEVKKGEVVGLLGPNGAGKT----TLMRMMVGMIRMTEGEVWIDGQSVK 72
Cdd:COG4172 1 MMSM-PLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 73 QQFESTAAKI-GAVI-----EtpefyPFLS-------G---YENLTYFGRMNGNVTEERIDEVVKLLGmgqvID---RKV 133
Cdd:COG4172 80 GLSERELRRIrGNRIamifqE-----PMTSlnplhtiGkqiAEVLRLHRGLSGAAARARALELLERVG----IPdpeRRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 134 KAY----SLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIII 209
Cdd:COG4172 151 DAYphqlSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVM 230
|
....*.
gi 822524621 210 QHGEYV 215
Cdd:COG4172 231 RQGEIV 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
10-213 |
7.00e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 86.66 E-value: 7.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 10 VERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAkigaVIETP 89
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRL----MFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 90 EFYPFLSGYENLTYFGRMNGNVTEERIDEVVKLlgmgqvIDRKVK---AYSLGMRQRLGIAQALIHDPDVLILDEPTNGL 166
Cdd:PRK11247 91 RLLPWKKVIDNVGLGLKGQWRDAALQALAAVGL------ADRANEwpaALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 822524621 167 DPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:PRK11247 165 DALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-214 |
1.03e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.95 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 3 NEQSIVKVERLTKRiGSKtlveNISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQqfESTAAKI 82
Cdd:PRK15439 264 AGAPVLTVEDLTGE-GFR----NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINA--LSTAQRL 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 83 --------------GAVIETPEFYPFLS-GYENLTYF---GRMNGNVTEERIDEVVKLLGmgqvIDRKVKAYSLGMRQRL 144
Cdd:PRK15439 337 arglvylpedrqssGLYLDAPLAWNVCAlTHNRRGFWikpARENAVLERYRRALNIKFNH----AEQAARTLSGGNQQKV 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 145 GIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEY 214
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-233 |
1.32e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 85.73 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 5 QSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRM-----TEGEVWIDGQSV-KQQFEST 78
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIfKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 79 AAKIGAVIETPEFYPFLSGYENLTYFGRMNGNVT-----EERIDEVVKLLGMGQVIDRKVKA----YSLGMRQRLGIAQA 149
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKskkelQERVRWALEKAQLWDEVKDRLDApagkLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 150 LIHDPDVLILDEPTNGLDP---SGIHEMRMYIKKiaheqGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT-------QN 219
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPentAKIESLFLELKK-----DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWgptrevfTN 235
|
250
....*....|....
gi 822524621 220 IQHNQSEEMETIRI 233
Cdd:PRK14247 236 PRHELTEKYVTGRL 249
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-213 |
2.01e-19 |
|
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: 88.30 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 31 KKGEVVGLLGPNGAGKTTLMRMMVGMIR----MTEGEVWID-------GQSVKQQFE-------STAAKIGAVIETPEFY 92
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKpnlgDYDEEPSWDevlkrfrGTELQDYFKklangeiKVAHKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 93 pflsgyenltyfgrmNGNV------TEER--IDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTN 164
Cdd:COG1245 177 ---------------KGTVrellekVDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 822524621 165 GLDpsgIHE-MRM--YIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIqHGE 213
Cdd:COG1245 242 YLD---IYQrLNVarLIRELA-EEGKYVLVVEHDLAILDYLADYVHIL-YGE 288
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-217 |
2.62e-19 |
|
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: 83.73 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 9 KVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGM--IRMTEGEVWIDGQSVKQQFESTAAKIG--- 83
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGifl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 84 AVIETPEFypflSGYENLTYFGRMNgnvteeridevvkllgmgqvidrkvKAYSLGMRQRLGIAQALIHDPDVLILDEPT 163
Cdd:cd03217 82 AFQYPPEI----PGVKNADFLRYVN-------------------------EGFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 164 NGLDPSGIHEMRMYIKKIaHEQGKAVLVSSH---LLSEVElmCDRVIIIQHGEYVAT 217
Cdd:cd03217 133 SGLDIDALRLVAEVINKL-REEGKSVLIITHyqrLLDYIK--PDRVHVLYDGRIVKS 186
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-217 |
3.02e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.98 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 3 NEQSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQS------------ 70
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlyalsea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 71 ------------VKQQFE-------STAAKIGavietpefypflsgyENLTYFG-RMNGNVTEERIDevvkllGMGQV-- 128
Cdd:PRK11701 82 errrllrtewgfVHQHPRdglrmqvSAGGNIG---------------ERLMAVGaRHYGDIRATAGD------WLERVei 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 129 ----IDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCD 204
Cdd:PRK11701 141 daarIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAH 220
|
250
....*....|...
gi 822524621 205 RVIIIQHGEYVAT 217
Cdd:PRK11701 221 RLLVMKQGRVVES 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-209 |
3.33e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 87.56 E-value: 3.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 30 VKKGEVVGLLGPNGAGKTTLMRMMVGMIR----MTEGEVWID-------GQSVKQQFESTAAKIGAVIETPEFYPFLSGY 98
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIpnlgDYEEEPSWDevlkrfrGTELQNYFKKLYNGEIKVVHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 99 enltyfgrMNGNV------TEER--IDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDpsg 170
Cdd:PRK13409 176 --------FKGKVrellkkVDERgkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--- 244
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 822524621 171 IHE-MRM--YIKKIAheQGKAVLVSSHLLSEVELMCDRVIII 209
Cdd:PRK13409 245 IRQrLNVarLIRELA--EGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-221 |
3.79e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 85.09 E-value: 3.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMtEGEVWIDG------QSVKQQ---FEST 78
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGrveffnQNIYERrvnLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 79 AAKIGAVIETPEFYPfLSGYENLTYFGRMNGNVTEERIDEVV----KLLGMGQVIDRKVKAYSL----GMRQRLGIAQAL 150
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVesalKDADLWDEIKHKIHKSALdlsgGQQQRLCIARAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822524621 151 IHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQ 221
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVE 236
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-215 |
5.77e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.06 E-value: 5.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVK------QQFESTAAKIGAVIETPEFYPFLS 96
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPanlkkiKEVKRLRKEIGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 GYENLTYFGRMN-GNVTEERIDEVVKLLGMGQVIDRKVK----AYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGI 171
Cdd:PRK13645 107 TIEKDIAFGPVNlGENKQEAYKKVPELLKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 822524621 172 HEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:PRK13645 187 EDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
10-212 |
6.02e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 84.25 E-value: 6.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 10 VERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV--------------KQQF 75
Cdd:PRK10619 8 VIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvadKNQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 76 ESTAAKIGAVIETPEFYPFLSGYENLTYFG-RMNGNVTEERIDEVVKLLGMGQVIDRKVKAY----SLGMRQRLGIAQAL 150
Cdd:PRK10619 88 RLLRTRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERAQGKYpvhlSGGQQQRVSIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822524621 151 IHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHG 212
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-167 |
7.48e-19 |
|
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: 86.53 E-value: 7.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIdGQSVK-----QQFESTAAK 81
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKlayvdQSRDALDPN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 82 --IGAVIETPEFYPFLSGYE--NLTYFGRMNgnvteeridevvkllGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVL 157
Cdd:TIGR03719 401 ktVWEEISGGLDIIKLGKREipSRAYVGRFN---------------FKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170
....*....|
gi 822524621 158 ILDEPTNGLD 167
Cdd:TIGR03719 466 LLDEPTNDLD 475
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-221 |
1.00e-18 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 86.10 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEV-WidgqsvkqqfeSTAAKIGavi 86
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkW-----------SENANIG--- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 etpeFYPFLSGYE---NLTYFGRMNGNVTEERIDEVV-----KLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLI 158
Cdd:PRK15064 386 ----YYAQDHAYDfenDLTLFDWMSQWRQEGDDEQAVrgtlgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822524621 159 LDEPTNGLDPSGIHEMRMYIKKIaheQGKAVLVS------SHLLSEV-ELMCDRVIIIQ--HGEYVATQNIQ 221
Cdd:PRK15064 462 MDEPTNHMDMESIESLNMALEKY---EGTLIFVShdrefvSSLATRIiEITPDGVVDFSgtYEEYLRSQGIE 530
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-212 |
1.91e-18 |
|
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: 82.59 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 25 NISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQ-FESTAAKIGAVIETPEFYPfLSGYENLTY 103
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLnLRWLRSQIGLVSQEPVLFD-GTIAENIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 104 fGRmnGNVTEERIDEVVKLLGMGQVIDRKVKAY-----------SLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIH 172
Cdd:cd03249 100 -GK--PDATDEEVEEAAKKANIHDFIMSLPDGYdtlvgergsqlSGGQKQRIAIARALLRNPKILLLDEATSALDAESEK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 822524621 173 EMRMYIKKIAheQGKAVLVSSHLLSEVElMCDRVIIIQHG 212
Cdd:cd03249 177 LVQEALDRAM--KGRTTIVIAHRLSTIR-NADLIAVLQNG 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-215 |
1.98e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 85.40 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQ-QFESTAAKIGAVIETPEFYPfLS 96
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAGLFN-RS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 GYENLTyFGRMNGnvTEERIDEVVKLLGMGQVIDRKVKAY-----------SLGMRQRLGIAQALIHDPDVLILDEPTNG 165
Cdd:PRK13657 425 IEDNIR-VGRPDA--TDEEMRAAAERAQAHDFIERKPDGYdtvvgergrqlSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 822524621 166 LDPSGIHEMRMYIKKIAHeqGKAVLVSSHLLSEVElMCDRVIIIQHGEYV 215
Cdd:PRK13657 502 LDVETEAKVKAALDELMK--GRTTFIIAHRLSTVR-NADRILVFDNGRVV 548
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
23-215 |
2.14e-18 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 85.15 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDG--------QSVKQQ----------FESTAAkiga 84
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdladytlASLRRQvalvsqdvvlFNDTIA---- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 85 vietpefypflsgyENLTYfGRMnGNVTEERIDEVVKL-----------LGMGQVIDRKVKAYSLGMRQRLGIAQALIHD 153
Cdd:TIGR02203 424 --------------NNIAY-GRT-EQADRAEIERALAAayaqdfvdklpLGLDTPIGENGVLLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822524621 154 PDVLILDEPTNGLDPSGIHEMRMYIKKIahEQGKAVLVSSHLLSEVElMCDRVIIIQHGEYV 215
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERL--MQGRTTLVIAHRLSTIE-KADRIVVMDDGRIV 546
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-219 |
2.57e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.54 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 13 LTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDgqsvkqqfestaakigavIETPEFY 92
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQFG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 93 PFLSGYENLTyfgrMNGNvteerIDEVVKLLGMGQVID-----RKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLD 167
Cdd:COG2401 98 REASLIDAIG----RKGD-----FKDAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 822524621 168 PSGIHEMRMYIKKIAHEQGKAVLVSSHlLSEVE--LMCDRVIIIQHGEYVATQN 219
Cdd:COG2401 169 RQTAKRVARNLQKLARRAGITLVVATH-HYDVIddLQPDLLIFVGYGGVPEEKR 221
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
9-212 |
2.74e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 84.93 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 9 KVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMT--EGEVWIDGQSVKQQfesTAAKIGAVI 86
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQ---ILKRTGFVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 ETPEFYPFLSGYENLTYFG--RMNGNVT-EERI---DEVVKLLGMGQ-----VIDRKVKAYSLGMRQRLGIAQALIHDPD 155
Cdd:PLN03211 147 QDDILYPHLTVRETLVFCSllRLPKSLTkQEKIlvaESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 822524621 156 VLILDEPTNGLDPSGIHEMRMYIKKIAHeQGKAVLVSSHL-LSEVELMCDRVIIIQHG 212
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMHQpSSRVYQMFDSVLVLSEG 283
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-196 |
3.17e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 81.98 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQsvkqQFESTAA------- 80
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN----HFDFSKTpsdkair 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 ----KIGAVIETPEFYPFLSGYENLT-----YFGrMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALI 151
Cdd:PRK11124 79 elrrNVGMVFQQYNLWPHLTVQQNLIeapcrVLG-LSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 822524621 152 HDPDVLILDEPTNGLDP-------SGIHEMR-MYIKKI--AHEQGKAVLVSSHLL 196
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPeitaqivSIIRELAeTGITQVivTHEVEVARKTASRVV 212
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-215 |
3.18e-18 |
|
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: 81.39 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 16 RIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkqqfestaAKIG--------AVIe 87
Cdd:cd03244 13 RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI--------SKIGlhdlrsriSII- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 tPEfYPFL-SGY--ENLTYFGRmngnVTEERIDEVVKLLGMGQVIDRKVKA-----------YSLGMRQRLGIAQALIHD 153
Cdd:cd03244 84 -PQ-DPVLfSGTirSNLDPFGE----YSDEELWQALERVGLKEFVESLPGGldtvveeggenLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822524621 154 PDVLILDEPTNGLDPsgihEMRMYIKKIAHEQ--GKAVLVSSHLLSEVeLMCDRVIIIQHGEYV 215
Cdd:cd03244 158 SKILVLDEATASVDP----ETDALIQKTIREAfkDCTVLTIAHRLDTI-IDSDRILVLDKGRVV 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-216 |
3.83e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.28 E-value: 3.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 5 QSIVKVERLTKRI-GSKTLvENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV--KQQFESTAAK 81
Cdd:PRK10762 2 QALLQLKGIDKAFpGVKAL-SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 82 IGAVIETPEFYPFLSGYENL-------TYFGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDP 154
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIflgrefvNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 822524621 155 DVLILDEPTNGLDP-------SGIHEMRmyikkiahEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:PRK10762 161 KVIIMDEPTDALTDteteslfRVIRELK--------SQGRGIVYISHRLKEIFEICDDVTVFRDGQFIA 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-217 |
4.03e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.31 E-value: 4.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLT-KRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQ--FESTAAKIG 83
Cdd:COG3845 257 VLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLspRERRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 84 AVIE-------TPEFypflSGYEN--LTYF--------GRMNGNVTEERIDEVVKLLG-MGQVIDRKVKAYSLGMRQRLG 145
Cdd:COG3845 337 YIPEdrlgrglVPDM----SVAENliLGRYrrppfsrgGFLDRKAIRAFAEELIEEFDvRTPGPDTPARSLSGGNQQKVI 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822524621 146 IAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT 217
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELR-DAGAAVLLISEDLDEILALSDRIAVMYEGRIVGE 483
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
21-210 |
5.38e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.85 E-value: 5.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 21 TLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQF-ESTAAKIGAVIETPEFYPFLsgYE 99
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALqKNLVAYVPQSEEVDWSFPVL--VE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 100 NLTYFGRMnGNV---------TEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSG 170
Cdd:PRK15056 99 DVVMMGRY-GHMgwlrrakkrDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 822524621 171 IHEMRMYIKKIAHEqGKAVLVSSHLLSEVELMCDRVIIIQ 210
Cdd:PRK15056 178 EARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-195 |
6.49e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.43 E-value: 6.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMT-----EGEVWIDGQSV---KQQFESTAAKIGAVIETP 89
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIyspDVDPIEVRREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 90 EFYPFLSGYENLTYFGRMNGNV-TEERIDEVV----KLLGMGQVIDRKVKAY----SLGMRQRLGIAQALIHDPDVLILD 160
Cdd:PRK14267 95 NPFPHLTIYDNVAIGVKLNGLVkSKKELDERVewalKKAALWDEVKDRLNDYpsnlSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 822524621 161 EPTNGLDPSG---IHEMRMYIKK------IAHEQGKAVLVSSHL 195
Cdd:PRK14267 175 EPTANIDPVGtakIEELLFELKKeytivlVTHSPAQAARVSDYV 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-212 |
7.30e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.78 E-value: 7.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 27 SFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSvkqQFESTAAK--IGAVIETPEFYPFLSGYENLTyF 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD---HTTTPPSRrpVSMLFQENNLFSHLTVAQNIG-L 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 105 G-----RMNGnVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIK 179
Cdd:PRK10771 95 GlnpglKLNA-AQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190
....*....|....*....|....*....|...
gi 822524621 180 KIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHG 212
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-169 |
8.30e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 81.29 E-value: 8.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGS-----KTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV-KQQFESTAA 80
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 KIGAVIETPefypfLSG-------YENLT--YF-GRMNG---NVTEERID---EVVKLLGMG--QVIDRKVKAYSLGMRQ 142
Cdd:COG1101 81 YIGRVFQDP-----MMGtapsmtiEENLAlaYRrGKRRGlrrGLTKKRRElfrELLATLGLGleNRLDTKVGLLSGGQRQ 155
|
170 180
....*....|....*....|....*..
gi 822524621 143 RLGIAQALIHDPDVLILDEPTNGLDPS 169
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPK 182
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-167 |
1.13e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.21 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 5 QSIVKVERLTKRIGSK----TLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAA 80
Cdd:PRK10584 4 ENIVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 K-----IGAVIETPEFYPFLSGYENLTYFGRMNG---NVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIH 152
Cdd:PRK10584 84 KlrakhVGFVFQSFMLIPTLNALENVELPALLRGessRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170
....*....|....*
gi 822524621 153 DPDVLILDEPTNGLD 167
Cdd:PRK10584 164 RPDVLFADEPTGNLD 178
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
6-216 |
1.22e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.00 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 6 SIVKVERL--TKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMI---RMTEGEVWIDGQSVKQQ-FESTA 79
Cdd:PRK13640 4 NIVEFKHVsfTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKtVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 80 AKIGAVIETPEFYPFLSGYENLTYFGRMNGNVTEER----IDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPD 155
Cdd:PRK13640 84 EKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEmikiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822524621 156 VLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVElMCDRVIIIQHGEYVA 216
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLA 223
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-215 |
2.18e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.20 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 20 KTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMtEGEVWIDGQSVKQ-QFESTAAKIGAVIETPE-FYPFLSg 97
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRElDPESWRKHLSWVGQNPQlPHGTLR- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 98 yENLTyFGrmNGNVTEERIDEVVKLLGMGQVIDRKVKAY-----------SLGMRQRLGIAQALIHDPDVLILDEPTNGL 166
Cdd:PRK11174 441 -DNVL-LG--NPDASDEQLQQALENAWVSEFLPLLPQGLdtpigdqaaglSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 822524621 167 DpsgIHEMRMYIKKIAHE-QGKAVLVSSHLLSEVElMCDRVIIIQHGEYV 215
Cdd:PRK11174 517 D---AHSEQLVMQALNAAsRRQTTLMVTHQLEDLA-QWDQIWVMQDGQIV 562
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
18-217 |
2.27e-17 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 82.48 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLvENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkQQFESTAAK--IGAVIETPefYPFL 95
Cdd:TIGR01193 486 GSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL-KDIDRHTLRqfINYLPQEP--YIFS 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 96 -SGYENLTYfgRMNGNVTEERIDEVVKL-----------LGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPT 163
Cdd:TIGR01193 562 gSILENLLL--GAKENVSQDEIWAACEIaeikddienmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 822524621 164 NGLDPsgIHEMRMyIKKIAHEQGKAVLVSSHLLSeVELMCDRVIIIQHGEYVAT 217
Cdd:TIGR01193 640 SNLDT--ITEKKI-VNNLLNLQDKTIIFVAHRLS-VAKQSDKIIVLDHGKIIEQ 689
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-256 |
2.27e-17 |
|
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: 82.16 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGM--IRMTEGEV-----------WIDGQSVKQQ 74
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 75 ----FESTAAKIGA---VIETPEFYPF-----------LSGYENLTYFGRM------NGNVTEERIDEVVKLLGMGQVID 130
Cdd:TIGR03269 81 pcpvCGGTLEPEEVdfwNLSDKLRRRIrkriaimlqrtFALYGDDTVLDNVlealeeIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 131 RKV---KAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSG---IHEMrmyIKKIAHEQGKAVLVSSHLLSEVELMCD 204
Cdd:TIGR03269 161 RIThiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTaklVHNA---LEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 822524621 205 RVIIIQHGEYVATQNIQHNQSEEMETirirVDDANKAAEMLDQDVLIKGNDL 256
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVAVFMEG----VSEVEKECEVEVGEPIIKVRNV 285
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-167 |
6.52e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 80.93 E-value: 6.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIdGQSVK-----QQFESTAAK 81
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKlayvdQSRDALDPN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 82 --IGAVIEtpefypflSGYENLT----------YFGRMNgnvteeridevvkLLGMGQviDRKVKAYSLGMRQRLGIAQA 149
Cdd:PRK11819 403 ktVWEEIS--------GGLDIIKvgnreipsraYVGRFN-------------FKGGDQ--QKKVGVLSGGERNRLHLAKT 459
|
170
....*....|....*...
gi 822524621 150 LIHDPDVLILDEPTNGLD 167
Cdd:PRK11819 460 LKQGGNVLLLDEPTNDLD 477
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
9-217 |
7.12e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.19 E-value: 7.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 9 KVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVG--MIRMTEGEVWIDGQSVKQqfestaakigavi 86
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILE------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 ETPE-------FYPF-----LSGYENLTYFGRMNGNVTEERID---------EVVKLLGMGQ-VIDRKVKA-YSLGMRQR 143
Cdd:COG0396 69 LSPDeraragiFLAFqypveIPGVSVSNFLRTALNARRGEELSareflkllkEKMKELGLDEdFLDRYVNEgFSGGEKKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 144 LGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIaHEQGKAVLVSSH---LLSEVElmCDRVIIIQHGEYVAT 217
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKL-RSPDRGILIITHyqrILDYIK--PDFVHVLVDGRIVKS 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-212 |
1.23e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.85 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 20 KTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGmirmtegeVWIDGQsvkqqfestaakiGaVIETPE-----FYP- 93
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG--------LWPYGS-------------G-RIARPAgarvlFLPq 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 94 ---FLSG--YENLTYfGRMNGNVTEERIDEVVKLLGMGQVIDR--KVKAY----SLGMRQRLGIAQALIHDPDVLILDEP 162
Cdd:COG4178 434 rpyLPLGtlREALLY-PATAEAFSDAELREALEAVGLGHLAERldEEADWdqvlSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 822524621 163 TNGLDPSGihEMRMYiKKIAHEQGKAVLVS-SHlLSEVELMCDRVIIIQHG 212
Cdd:COG4178 513 TSALDEEN--EAALY-QLLREELPGTTVISvGH-RSTLAAFHDRVLELTGD 559
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4-215 |
1.56e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 77.23 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 4 EQSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAK-- 81
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMRea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 82 IGAVIETPEFYPFLSGYENLTYFGRM-NGNVTEERIDEVVKLLgmGQVIDRKVK---AYSLGMRQRLGIAQALIHDPDVL 157
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMGGFFaERDQFQERIKWVYELF--PRLHERRIQragTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 822524621 158 ILDEPTNGLDPSGIHEMRMYIKKIaHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-184 |
1.97e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.51 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 1 MTNEQSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMR---MMVGMIR--MTEGEVWIDGQSVKQQF 75
Cdd:PRK14243 4 LNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPgfRVEGKVTFHGKNLYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 76 ESTAA---KIGAVIETPefYPF-LSGYENLTYFGRMNGnvTEERIDEVVKLLGMGQVIDRKVK--------AYSLGMRQR 143
Cdd:PRK14243 84 VDPVEvrrRIGMVFQKP--NPFpKSIYDNIAYGARING--YKGDMDELVERSLRQAALWDEVKdklkqsglSLSGGQQQR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 822524621 144 LGIAQALIHDPDVLILDEPTNGLDPsgIHEMRmyIKKIAHE 184
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDP--ISTLR--IEELMHE 196
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-220 |
2.12e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.05 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 22 LVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGM----IRMTEGEVWIDGQSVKQQfESTAAKIGAVIETPE--FYPFL 95
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVAPC-ALRGRKIATIMQNPRsaFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 96 S----GYENLTYFGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDpsGI 171
Cdd:PRK10418 97 TmhthARETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD--VV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 822524621 172 HEMRM--YIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNI 220
Cdd:PRK10418 175 AQARIldLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDV 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-213 |
2.27e-16 |
|
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: 75.91 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSK--TLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQ-QFESTAAKIGA 84
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 85 VIETPEfypFLSGY--ENLTYFGRMngnvTEERIDEVVKLLGMGQVIdrkvkaySLGMRQRLGIAQALIHDPDVLILDEP 162
Cdd:cd03369 87 IPQDPT---LFSGTirSNLDPFDEY----SDEEIYGALRVSEGGLNL-------SQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 822524621 163 TNGLDPSGIHEmrmyIKKIAHE--QGKAVLVSSHLLSEVeLMCDRVIIIQHGE 213
Cdd:cd03369 153 TASIDYATDAL----IQKTIREefTNSTILTIAHRLRTI-IDYDKILVMDAGE 200
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-224 |
2.36e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 78.99 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 19 SKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQ-QFESTAAKIGAVIETPefYPFLSG 97
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAVVSQTP--FLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 98 YENLTYFGRmnGNVTEERIDEVVKLLGMGQVIDRKVKAY-----------SLGMRQRLGIAQALIHDPDVLILDEPTNGL 166
Cdd:PRK10789 405 VANNIALGR--PDATQQEIEHVARLASVHDDILRLPQGYdtevgergvmlSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 822524621 167 DPSGIHEMRMYIKKIAheQGKAVLVSSHLLSEVElMCDRVIIIQHGEyvATQNIQHNQ 224
Cdd:PRK10789 483 DGRTEHQILHNLRQWG--EGRTVIISAHRLSALT-EASEILVMQHGH--IAQRGNHDQ 535
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-210 |
2.90e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 76.29 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 1 MTNEQSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkqqfeSTAa 80
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI-----STL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 kigavieTPEFY----------PFLSG---YENLTYFGRMNGNVTEER--IDEVVKLLGMGQVIDRKVKAYSLGMRQRLG 145
Cdd:PRK10247 75 -------KPEIYrqqvsycaqtPTLFGdtvYDNLIFPWQIRNQQPDPAifLDDLERFALPDTILTKNIAELSGGEKQRIS 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 822524621 146 IAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVElMCDRVIIIQ 210
Cdd:PRK10247 148 LIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEIN-HADKVITLQ 211
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
23-208 |
4.37e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 77.31 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMmVGMIRM-TEGEVWIDGQSVKQQFESTAA--------------------- 80
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARL-LTMIETpTGGELYYQGQDLLKADPEAQKllrqkiqivfqnpygslnprk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 81 KIGAVIETPefypfLSGYENLTyfgrmngnvTEERIDEVVKLlgMGQV------IDRKVKAYSLGMRQRLGIAQALIHDP 154
Cdd:PRK11308 110 KVGQILEEP-----LLINTSLS---------AAERREKALAM--MAKVglrpehYDRYPHMFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 155 DVLILDEPTNGLDPS---GIHEMRMYIKKiahEQGKAVLVSSHLLSEVELMCDRVII 208
Cdd:PRK11308 174 DVVVADEPVSALDVSvqaQVLNLMMDLQQ---ELGLSYVFISHDLSVVEHIADEVMV 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
23-215 |
6.35e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.98 E-value: 6.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDG------------QSVKQQFE--STA----AKIGA 84
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsQRIRMIFQdpSTSlnprQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 85 VIETPefypflsgyenLTYFGRMNGNVTEERIDEVVKLLGMgqvidRKVKAY------SLGMRQRLGIAQALIHDPDVLI 158
Cdd:PRK15112 109 ILDFP-----------LRLNTDLEPEQREKQIIETLRQVGL-----LPDHASyyphmlAPGQKQRLGLARALILRPKVII 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822524621 159 LDEPTNGLDPSgiheMRMYIKKIAHE----QGKAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:PRK15112 173 ADEALASLDMS----MRSQLINLMLElqekQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
24-224 |
9.02e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.46 E-value: 9.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 24 ENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKI-----GAVIETPEFYPFLSGY 98
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrrehfGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 99 ENL----TYFGrMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEM 174
Cdd:PRK10535 105 QNVevpaVYAG-LERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 822524621 175 rMYIKKIAHEQGKAVLVSSHlLSEVELMCDRVIIIQHGEYVATQNIQHNQ 224
Cdd:PRK10535 184 -MAILHQLRDRGHTVIIVTH-DPQVAAQAERVIEIRDGEIVRNPPAQEKV 231
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-212 |
2.30e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 76.69 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 22 LVENISFEVKKGEVVGLLGPNGAGKTTLM-----RMMVGMIrmTEGEVWIDGQSVKQQFESTaakIGAVIETPEFYPFLS 96
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGVI--TGGDRLVNGRPLDSSFQRS---IGYVQQQDLHLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 GYENLTY--FGRMNGNVTEER----IDEVVKLLGMGQVIDRKVKAYSLGM----RQRLGIAQALIHDPDVLI-LDEPTNG 165
Cdd:TIGR00956 853 VRESLRFsaYLRQPKSVSKSEkmeyVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 822524621 166 LDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVeLMC--DRVIIIQHG 212
Cdd:TIGR00956 933 LDSQTAWSICKLMRKLA-DHGQAILCTIHQPSAI-LFEefDRLLLLQKG 979
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-196 |
2.73e-15 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 74.07 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 1 MTNEQSI-VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVK------- 72
Cdd:COG4598 1 MTDTAPPaLEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 73 -------QQFESTAAKIGAVietpeFYPFlsgyeNLtyFGRMN--GNVTE-----------ERIDEVVKLL---GMGQVI 129
Cdd:COG4598 81 elvpadrRQLQRIRTRLGMV-----FQSF-----NL--WSHMTvlENVIEapvhvlgrpkaEAIERAEALLakvGLADKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 130 DrkvkAY----SLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIA----------HEQGKAVLVSSHL 195
Cdd:COG4598 149 D----AYpahlSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAeegrtmlvvtHEMGFARDVSSHV 224
|
.
gi 822524621 196 L 196
Cdd:COG4598 225 V 225
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-194 |
4.62e-15 |
|
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: 75.22 E-value: 4.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 26 ISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV--------KQQFestaakigAVIETpEFYPFlsg 97
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtadnreayRQLF--------SAVFS-DFHLF--- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 98 yENLtyFGrMNGNVTEERIDEVVKLLGMgqviDRKVK---------AYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDP 168
Cdd:COG4615 419 -DRL--LG-LDGEADPARARELLERLEL----DHKVSvedgrfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDP 490
|
170 180 190
....*....|....*....|....*....|....
gi 822524621 169 SG--------IHEMRmyikkiahEQGKAVLVSSH 194
Cdd:COG4615 491 EFrrvfytelLPELK--------ARGKTVIAISH 516
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-232 |
4.88e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.21 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLvENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGM--IRMTEGEVWIDGQsvKQQFESTAA--KIGAVIETPE--F 91
Cdd:NF040905 13 GVKAL-DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGE--VCRFKDIRDseALGIVIIHQElaL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 92 YPFLSGYENL------TYFGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNG 165
Cdd:NF040905 90 IPYLSIAENIflgnerAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822524621 166 LDPSG-------IHEMRmyikkiahEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQHNQSEEMETIR 232
Cdd:NF040905 170 LNEEDsaalldlLLELK--------AQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRADEVTEDRIIR 235
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
8-194 |
6.13e-15 |
|
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: 71.03 E-value: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGS-KTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEvwidgqsvkqqfestaakigavI 86
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGR----------------------I 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 ETPE-----FYPflsgyeNLTYFGRmnGNVTEeridevvkllgmgQVI---DRKVkaySLGMRQRLGIAQALIHDPDVLI 158
Cdd:cd03223 59 GMPEgedllFLP------QRPYLPL--GTLRE-------------QLIypwDDVL---SGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 822524621 159 LDEPTNGLDPSGihEMRMYikKIAHEQGKAVLVSSH 194
Cdd:cd03223 115 LDEATSALDEES--EDRLY--QLLKELGITVISVGH 146
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-212 |
6.30e-15 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 72.93 E-value: 6.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGqsvkqqfESTAAKIGAVIETPefypfLSGYENLT 102
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-------EVSVIAISAGLSGQ-----LTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 103 Y------FGRMNgnvTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPS------- 169
Cdd:PRK13546 108 FkmlcmgFKRKE---IKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTfaqkcld 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 822524621 170 GIHEMRmyikkiahEQGKAVLVSSHLLSEVELMCDRVIIIQHG 212
Cdd:PRK13546 185 KIYEFK--------EQNKTIFFVSHNLGQVRQFCTKIAWIEGG 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-213 |
6.80e-15 |
|
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: 71.73 E-value: 6.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 24 ENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQS--VKQQfestaakigavietpefyPFL-SG--Y 98
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIayVSQE------------------PWIqNGtiR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 99 ENLTYFGRMNgnvtEERIDEVVK---------LLGMG---QVIDRKVkaySL--GMRQRLGIAQALIHDPDVLILDEPTN 164
Cdd:cd03250 84 ENILFGKPFD----EERYEKVIKacalepdleILPDGdltEIGEKGI---NLsgGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 822524621 165 GLDPS-GIHEMRMYIKKIAHEqGKAVLVSSHLLSEVELmCDRVIIIQHGE 213
Cdd:cd03250 157 AVDAHvGRHIFENCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-167 |
7.92e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.60 E-value: 7.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 22 LVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDgQSVK----QQ----------FESTAAKIGAVIE 87
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIvarlQQdpprnvegtvYDFVAEGIEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPEFYPFLS-------GYENLTYFGRM-------NGNVTEERIDEVVKLLGMGQviDRKVKAYSLGMRQRLGIAQALIHD 153
Cdd:PRK11147 97 YLKRYHDIShlvetdpSEKNLNELAKLqeqldhhNLWQLENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSN 174
|
170
....*....|....
gi 822524621 154 PDVLILDEPTNGLD 167
Cdd:PRK11147 175 PDVLLLDEPTNHLD 188
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-215 |
1.62e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.74 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVK----QQFESTAAKIGAVIETPefYPFLS-- 96
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspGKLQALRRDIQFIFQDP--YASLDpr 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 ---GY---ENLTYFGRMNGNVTEERIDEVVKLLGM-GQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPS 169
Cdd:PRK10261 418 qtvGDsimEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 822524621 170 GIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-221 |
1.65e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.74 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDG---------------QSVKQQFESTAAKIGAVIE 87
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvielseQSAAQMRHVRGADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TP--EFYPFLSGYENLTYFGRMNGNVTEE-------RIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLI 158
Cdd:PRK10261 112 EPmtSLNPVFTVGEQIAESIRLHQGASREeamveakRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822524621 159 LDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQ 221
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVE 254
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-217 |
3.24e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.83 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 35 VVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVkqqFESTAA--------KIGAVIETPEFYPFLSGYENLTYfGr 106
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL---FDAEKGiclppekrRIGYVFQDARLFPHYKVRGNLRY-G- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 107 MNgNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQG 186
Cdd:PRK11144 101 MA-KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREIN 179
|
170 180 190
....*....|....*....|....*....|.
gi 822524621 187 KAVLVSSHLLSEVELMCDRVIIIQHGEYVAT 217
Cdd:PRK11144 180 IPILYVSHSLDEILRLADRVVVLEQGKVKAF 210
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-219 |
5.21e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.90 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKR-IGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAA----K 81
Cdd:PRK10908 1 MIRFEHVSKAyLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrrQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 82 IGAVIETPEFYPFLSGYENLTYFGRMNGNVTEERIDEVVKLLGMGQVIDrKVKAY----SLGMRQRLGIAQALIHDPDVL 157
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLD-KAKNFpiqlSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822524621 158 ILDEPTNGLDpSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQN 219
Cdd:PRK10908 160 LADEPTGNLD-DALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVG 220
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-217 |
5.92e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.06 E-value: 5.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 1 MTNEQSIVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVG--MIRMTEGEVWIDGQSVKQQFEST 78
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 79 AAKIGAVIetpEF-YPF-LSGYEN-----LTYFGRMNG-NVTE-------ERIDEVVKLLGMGQV-IDRKV-KAYSLGMR 141
Cdd:CHL00131 81 RAHLGIFL---AFqYPIeIPGVSNadflrLAYNSKRKFqGLPEldpleflEIINEKLKLVGMDPSfLSRNVnEGFSGGEK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 822524621 142 QRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSH---LLSEVelMCDRVIIIQHGEYVAT 217
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLM-TSENSIILITHyqrLLDYI--KPDYVHVMQNGKIIKT 233
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-213 |
7.74e-14 |
|
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: 69.70 E-value: 7.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 30 VKKGEVVGLLGPNGAGKTTLMRMMVGMI-----RMTEGEVWID------GQSVKQQFESTAAKIGAVIETPEFYPFLSGy 98
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLkpnlgKFDDPPDWDEildefrGSELQNYFTKLLEGDVKVIVKPQYVDLIPK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 99 enltyfgRMNGNV------TEER--IDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDpsg 170
Cdd:cd03236 102 -------AVKGKVgellkkKDERgkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD--- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 822524621 171 IHEmRMYIKKIAHE---QGKAVLVSSHLLSEVELMCDrVIIIQHGE 213
Cdd:cd03236 172 IKQ-RLNAARLIRElaeDDNYVLVVEHDLAVLDYLSD-YIHCLYGE 215
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-175 |
1.37e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 70.69 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 13 LTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWID-----GQSVKQQF------------ 75
Cdd:PRK15064 7 ITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlGKLRQDQFafeeftvldtvi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 76 ----ESTAAK-----IGAVIE-TPEFYPFLSGYEnlTYFGRMNGNVTEERIDEVvkLLGMGQVIDR---KVKAYSLGMRQ 142
Cdd:PRK15064 87 mghtELWEVKqerdrIYALPEmSEEDGMKVADLE--VKFAEMDGYTAEARAGEL--LLGVGIPEEQhygLMSEVAPGWKL 162
|
170 180 190
....*....|....*....|....*....|...
gi 822524621 143 RLGIAQALIHDPDVLILDEPTNGLDpsgIHEMR 175
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD---INTIR 192
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-216 |
1.43e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.59 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMI--RMTEGEVWIDGQSVkqQFESTAAKIGAvietpefypflsgyeN 100
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEV--DVSTVSDAIDA---------------G 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 101 LTYfgrmngnVTEER-------IDEV---VKLLGMGQV----------------------------IDRKVKAYSLGMRQ 142
Cdd:NF040905 339 LAY-------VTEDRkgyglnlIDDIkrnITLANLGKVsrrgvideneeikvaeeyrkkmniktpsVFQKVGNLSGGNQQ 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822524621 143 RLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:NF040905 412 KVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELA-AEGKGVIVISSELPELLGMCDRIYVMNEGRITG 484
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
22-167 |
2.15e-13 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 70.65 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 22 LVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGmiRMT----EGEVWIDGQSVKQQfesTAAKIGAVIETPEFY-PFLS 96
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPKKQE---TFARISGYCEQNDIHsPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 GYENLTY--FGRMNGNVTEER----IDEVVKLLGMGQVIDR-----KVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNG 165
Cdd:PLN03140 970 VRESLIYsaFLRLPKEVSKEEkmmfVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
..
gi 822524621 166 LD 167
Cdd:PLN03140 1050 LD 1051
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-215 |
2.65e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.58 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 13 LTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEG-----EVWIDGQSV--KQQFESTAAKIGAV 85
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnYRDVLEFRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 86 IETPEFYPF------LSGYENLTYFGRMN-GNVTEERIDEVvkllGMGQVIDRKVK----AYSLGMRQRLGIAQALIHDP 154
Cdd:PRK14271 107 FQRPNPFPMsimdnvLAGVRAHKLVPRKEfRGVAQARLTEV----GLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822524621 155 DVLILDEPTNGLDPSGIHEMRMYIKKIAHEQgkAVLVSSHLLSEVELMCDRVIIIQHGEYV 215
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLV 241
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-167 |
3.11e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 69.58 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 4 EQSIVKVERLTKRIGSKTLV-ENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIdgqsvkqqfeSTAAKI 82
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP----------QPGIKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 83 GAVIETPEFYPFLSGYEN-----------LTYFGRMNGNVTEERiDEVVKLLG-MGQVIDR------------------- 131
Cdd:TIGR03719 71 GYLPQEPQLDPTKTVRENveegvaeikdaLDRFNEISAKYAEPD-ADFDKLAAeQAELQEIidaadawdldsqleiamda 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 822524621 132 --------KVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLD 167
Cdd:TIGR03719 150 lrcppwdaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-221 |
3.37e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.37 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLvENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIETPEFYPFL-- 95
Cdd:PRK10982 10 GVKAL-DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLqr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 96 SGYENLtYFGR--MNGN-VTEERIDEVVKLLGMGQVID----RKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDP 168
Cdd:PRK10982 89 SVMDNM-WLGRypTKGMfVDQDKMYRDTKAIFDELDIDidprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 822524621 169 SGIHEMRMYIKKIaHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQ 221
Cdd:PRK10982 168 KEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLA 219
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
18-226 |
3.91e-13 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 67.96 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRmTEGEVWIDGQSVKQQFESTAAKIGAVIETPEFYPFLSG 97
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 98 YENLTYFGRMNgnvtEERIDEVVKLLGMGQVIDR---KVK--------AYSLGMRQRLGIAQALIHDPDVLILDEPTNGL 166
Cdd:cd03289 94 RKNLDPYGKWS----DEEIWKVAEEVGLKSVIEQfpgQLDfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 167 DPSGIHEMRMYIKKIAheQGKAVLVSSHLLsEVELMCDRVIIIQHGEYVATQNIQHNQSE 226
Cdd:cd03289 170 DPITYQVIRKTLKQAF--ADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
24-215 |
5.65e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.89 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 24 ENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIeTPEFYPFLSGYENLTY 103
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALV-SQNVHLFNDTIANNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 104 FGRmNGNVTEERIDEVVKLL-----------GMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIH 172
Cdd:PRK11176 439 YAR-TEQYSREQIEEAARMAyamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESER 517
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 822524621 173 EMRMYIKKIahEQGKAVLVSSHLLSEVElMCDRVIIIQHGEYV 215
Cdd:PRK11176 518 AIQAALDEL--QKNRTSLVIAHRLSTIE-KADEILVVEDGEIV 557
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-192 |
8.21e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.44 E-value: 8.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 10 VERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVwidgqsvkqqfestaaKIGAVIEtp 89
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----------------HCGTKLE-- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 90 efypflsgyenLTYFGRMNGNVTEERidEVVKLLGMGQ----VIDRK--------------------VKAYSLGMRQRLG 145
Cdd:PRK11147 384 -----------VAYFDQHRAELDPEK--TVMDNLAEGKqevmVNGRPrhvlgylqdflfhpkramtpVKALSGGERNRLL 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 822524621 146 IAQALIHDPDVLILDEPTNGLDpsgIHEMRMYIKKIAHEQGKAVLVS 192
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLD---VETLELLEELLDSYQGTVLLVS 494
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-210 |
8.44e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 68.78 E-value: 8.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRmTEGEVWIDGQSVKQQFESTAAKIGAVIetPEFYPFLSG 97
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVI--PQKVFIFSG 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 98 yenlTYfgRMNGNVTEERIDE----VVKLLGMGQVIDR---KVK--------AYSLGMRQRLGIAQALIHDPDVLILDEP 162
Cdd:TIGR01271 1307 ----TF--RKNLDPYEQWSDEeiwkVAEEVGLKSVIEQfpdKLDfvlvdggyVLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 822524621 163 TNGLDPSGIHEMRMYIKKIAHEQgkAVLVSSHLLsEVELMCDRVIIIQ 210
Cdd:TIGR01271 1381 SAHLDPVTLQIIRKTLKQSFSNC--TVILSEHRV-EALLECQQFLVIE 1425
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
8-210 |
2.53e-12 |
|
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: 64.13 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISfEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQsvkqqfestaakigavie 87
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 88 TPEFYPflsgyenltyfgrmngnvteeridEVVKLLGmgqvidrkvkayslGMRQRLGIAQALIHDPDVLILDEPTNGLD 167
Cdd:cd03222 62 TPVYKP------------------------QYIDLSG--------------GELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 822524621 168 PSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQ 210
Cdd:cd03222 104 IEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-228 |
7.23e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 7.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 13 LTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIetPEFY 92
Cdd:PLN03232 1242 LRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSII--PQSP 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 93 PFLSGYE--NLTYFGRMNG-----NVTEERIDEVVKLLGMGqvIDRKV----KAYSLGMRQRLGIAQALIHDPDVLILDE 161
Cdd:PLN03232 1320 VLFSGTVrfNIDPFSEHNDadlweALERAHIKDVIDRNPFG--LDAEVseggENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 822524621 162 PTNGLDPsgihEMRMYIKKIAHEQGKA--VLVSSHLLSEVeLMCDRVIIIQHGeyvatQNIQHNQSEEM 228
Cdd:PLN03232 1398 ATASVDV----RTDSLIQRTIREEFKSctMLVIAHRLNTI-IDCDKILVLSSG-----QVLEYDSPQEL 1456
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-216 |
9.79e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 9.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 19 SKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMI---------RMTeGEVWIDGQSVKQQFESTAAKIGAVIETP 89
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgaRVT-GDVTLNGEPLAAIDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 90 EFYPFLSGYENLTYFGRM----NGNVTEER----IDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQAL---------IH 152
Cdd:PRK13547 92 AQPAFAFSAREIVLLGRYpharRAGALTHRdgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822524621 153 DPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVA 216
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVA 235
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-220 |
1.26e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 64.36 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKT----TLMRMMVGMIRmTEGEVWIDGQSV-----KQQFESTAAKIGAVIET 88
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREIlnlpeKELNKLRAEQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 89 P--EFYPFLSGYENLT----YFGRMNGNvteERIDEVVKLLGMGQVID-RK-VKAY----SLGMRQRLGIAQALIHDPDV 156
Cdd:PRK09473 106 PmtSLNPYMRVGEQLMevlmLHKGMSKA---EAFEESVRMLDAVKMPEaRKrMKMYphefSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 157 LILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHG---EYVATQNI 220
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGrtmEYGNARDV 249
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
8-194 |
1.42e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.88 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMV-----GM-----IRMTEGEVWIDGQSVKQ---- 73
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGIpkncqILHVEQEVVGDDTTALQcvln 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 74 ------QFESTAAKIGAVIETPEFyPFLSGYENLTYFGRMNGNVTEERIDEVVKLLgmgQVID----------------- 130
Cdd:PLN03073 258 tdiertQLLEEEAQLVAQQRELEF-ETETGKGKGANKDGVDKDAVSQRLEEIYKRL---ELIDaytaearaasilaglsf 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 131 ------RKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAheqgKAVLVSSH 194
Cdd:PLN03073 334 tpemqvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP----KTFIVVSH 399
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-192 |
1.99e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.42 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 13 LTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQS----VKQqfESTAAKIGA---V 85
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWqlawVNQ--ETPALPQPAleyV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 86 IETPEFYPFLS-----------GYENLTYFGRM---NGNVTEERIDEVVKLLGMGQV-IDRKVKAYSLGMRQRLGIAQAL 150
Cdd:PRK10636 85 IDGDREYRQLEaqlhdanerndGHAIATIHGKLdaiDAWTIRSRAASLLHGLGFSNEqLERPVSDFSGGWRMRLNLAQAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 822524621 151 IHDPDVLILDEPTNGLDPSGIHEMRMYIKKIaheQGKAVLVS 192
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY---QGTLILIS 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-221 |
2.31e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 20 KTLVENISFEVKKGEVVGLLGPNGAGKT----TLMRMMVG-MIRMTEGEVWIDGQSVKQQFEST-----AAKIGAVIETP 89
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSpPVVYPSGDIRFHGESLLHASEQTlrgvrGNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 90 --EFYPFLSG----YENLTYFGRMNGNVTEERIDEVVKLLGMGQVIDRkVKAY----SLGMRQRLGIAQALIHDPDVLIL 159
Cdd:PRK15134 102 mvSLNPLHTLekqlYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKR-LTDYphqlSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822524621 160 DEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQ 221
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-212 |
5.60e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.20 E-value: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 19 SKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMM----VGMIRMTEGEVWIDGQS---VKQQFESTAAKIGaviETPEF 91
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITpeeIKKHYRGDVVYNA---ETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 92 YPFLSGYENLTYFGRMNG------NVTEE-----RIDEVVKLLGMGQVIDRKV-----KAYSLGMRQRLGIAQALIHDPD 155
Cdd:TIGR00956 150 FPHLTVGETLDFAARCKTpqnrpdGVSREeyakhIADVYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAK 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 822524621 156 VLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSE--VELMcDRVIIIQHG 212
Cdd:TIGR00956 230 IQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQdaYELF-DKVIVLYEG 287
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
7-194 |
6.89e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.88 E-value: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWID-----GQSVKQQFESTAAK 81
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkgiklGYFAQHQLEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 82 igaviETPefypflsgyenLTYFGRMNGNVTEERIDEVVKLLGM-GQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILD 160
Cdd:PRK10636 392 -----ESP-----------LQHLARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180 190
....*....|....*....|....*....|....
gi 822524621 161 EPTNGLDpsgiHEMRMYIKKIAHEQGKAVLVSSH 194
Cdd:PRK10636 456 EPTNHLD----LDMRQALTEALIDFEGALVVVSH 485
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
6-217 |
9.16e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 61.68 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 6 SIVKVERLTKRIGSKTL----VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMI----RMTEGEVWIDGQ-----SVK 72
Cdd:PRK11022 2 ALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQdlqriSEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 73 QQFESTAAKIGAVIETP--EFYP-FLSGYENLTYFGRMNGNVTEERIDEVVKLLGMGQVID--RKVKAY----SLGMRQR 143
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPmtSLNPcYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpaSRLDVYphqlSGGMSQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822524621 144 LGIAQALIHDPDVLILDEPTNGLD---PSGIHEMRMYIKKiahEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVAT 217
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDvtiQAQIIELLLELQQ---KENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-167 |
1.07e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.06 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 12 RLTKRIGSKTLV-ENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIdgqsvkqqfeSTAAKIGAVIETPE 90
Cdd:PRK11819 11 RVSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP----------APGIKVGYLPQEPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 91 FYPflsgyeNLTYFgrmnGNVTE---------ERIDEVVKLLG------------MGQV-----------IDRK------ 132
Cdd:PRK11819 81 LDP------EKTVR----ENVEEgvaevkaalDRFNEIYAAYAepdadfdalaaeQGELqeiidaadawdLDSQleiamd 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 822524621 133 ----------VKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLD 167
Cdd:PRK11819 151 alrcppwdakVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-213 |
1.67e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.53 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 26 ISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV-KQQFESTAAKIGAVIEtpEFYPFlsgyENLTyf 104
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPEDYRKLFSAVFT--DFHLF----DQLL-- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 105 GRMNGNVTEERIDEVVKLLGM--------GQVIDRKVkaySLGMRQRLGIAQALIHDPDVLILDEPTNGLDPsgiHEMRM 176
Cdd:PRK10522 414 GPEGKPANPALVEKWLERLKMahkleledGRISNLKL---SKGQKKRLALLLALAEERDILLLDEWAADQDP---HFRRE 487
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 822524621 177 YIKKI---AHEQGKAVLVSSHLLSEVElMCDRVIIIQHGE 213
Cdd:PRK10522 488 FYQVLlplLQEMGKTIFAISHDDHYFI-HADRLLEMRNGQ 526
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-215 |
2.02e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.27 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 20 KTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVIETPEFYPFLSGYE 99
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 100 NLTyFGRmngNVTEERI---DEVVKLL--------GMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDp 168
Cdd:PRK10790 434 NVT-LGR---DISEEQVwqaLETVQLAelarslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANID- 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 822524621 169 SGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVElmCDRVIIIQHGEYV 215
Cdd:PRK10790 509 SGTEQAIQQALAAVREHTTLVVIAHRLSTIVE--ADTILVLHRGQAV 553
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-228 |
1.25e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRigSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVI 86
Cdd:PRK10982 250 ILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 87 ETPE-----FYPFLS-GYENL-----TYFGRMnGNVTEERIDEVVKLlgmgqVIDR-KVK---------AYSLGMRQRLG 145
Cdd:PRK10982 328 VTEErrstgIYAYLDiGFNSLisnirNYKNKV-GLLDNSRMKSDTQW-----VIDSmRVKtpghrtqigSLSGGNQQKVI 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 146 IAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAhEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQHNQS 225
Cdd:PRK10982 402 IGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELA-KKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQ 480
|
...
gi 822524621 226 EEM 228
Cdd:PRK10982 481 NEI 483
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-215 |
2.30e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.21 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 26 ISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSVKQQFESTAAKIGAVI-ETPEFYpflSGYE--NLT 102
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIpQAPVLF---SGTVrfNLD 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 103 YFGRMN-GNVTE--ER--IDEVVKL--LGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDpsgiheMR 175
Cdd:PLN03130 1335 PFNEHNdADLWEslERahLKDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD------VR 1408
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 822524621 176 M--YIKKIAHEQGKA--VLVSSHLLSEVeLMCDRVIIIQHGEYV 215
Cdd:PLN03130 1409 TdaLIQKTIREEFKSctMLIIAHRLNTI-IDCDRILVLDAGRVV 1451
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-196 |
5.33e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 55.41 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEV-WIDGQSVKQQFESTAAKIGAVIETPEFYPFL---SGY 98
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWSNKNESEPSFEATRSRNRYSVAYAAQKPWLlnaTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 99 ENLTYFGRMNGNVTEERIDEV-----VKLLGMG---QVIDRKVKaYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPS- 169
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACslqpdIDLLPFGdqtEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 175
|
170 180
....*....|....*....|....*..
gi 822524621 170 GIHEMRMYIKKIAHEQGKAVLVSSHLL 196
Cdd:cd03290 176 SDHLMQEGILKFLQDDKRTLVLVTHKL 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-167 |
1.71e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 27 SFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQS-VKQQFEstaaKIGAVIETpEF----YPFLSGYENL 101
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHiTRLSFE----QLQKLVSD-EWqrnnTDMLSPGEDD 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822524621 102 TyfGR------MNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLD 167
Cdd:PRK10938 98 T--GRttaeiiQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-167 |
1.88e-08 |
|
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: 55.69 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 22 LVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGqsvkqqfestaaKIGAVIETPEFYP-------- 93
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQTSWIMPgtikdnii 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 94 FLSGYENLTYFGRMNGNVTEERI------DEVVklLGMGQVidrkvkAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLD 167
Cdd:TIGR01271 509 FGLSYDEYRYTSVIKACQLEEDIalfpekDKTV--LGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-198 |
2.80e-08 |
|
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: 51.99 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 32 KGEVVGLLGPNGAGKTTLMRMMVGMI-RMTEGEVWIDGqsvkqqfestaakigavietpefypflsgyenltyfgrmngn 110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELgPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 111 vteERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYI-----KKIAHEQ 185
Cdd:smart00382 39 ---EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSEK 115
|
170
....*....|...
gi 822524621 186 GKAVLVSSHLLSE 198
Cdd:smart00382 116 NLTVILTTNDEKD 128
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-213 |
3.68e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVG-------------MIRMTEGE-VWidgqSVKQqfestaaKIG 83
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltlfGRRRGSGEtIW----DIKK-------HIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 84 AVietpefypflSGYENLTYfgRMNGNV-----------------TEER----IDEVVKLLGM-GQVIDRKVKAYSLGmR 141
Cdd:PRK10938 340 YV----------SSSLHLDY--RVSTSVrnvilsgffdsigiyqaVSDRqqklAQQWLDILGIdKRTADAPFHSLSWG-Q 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822524621 142 QRLG-IAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKK-IAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGE 213
Cdd:PRK10938 407 QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLFVSHHAEDAPACITHRLEFVPDGD 480
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
95-232 |
7.04e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 95 LSGYENLTyFGRMNGnvTEERIDEVVKLLGMGQVI-------DRKV----KAYSLGMRQRLGIAQALIHDPDVLILDEPT 163
Cdd:PTZ00265 1310 MSIYENIK-FGKEDA--TREDVKRACKFAAIDEFIeslpnkyDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEAT 1386
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 822524621 164 NGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVElMCDRVIIIQHGEYVATQNIQHNQSEEMETIR 232
Cdd:PTZ00265 1387 SSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIK-RSDKIVVFNNPDRTGSFVQAHGTHEELLSVQ 1454
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-213 |
8.65e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 25 NISFEVKKGEVVGLLGPNGAGKTTLMRMMVG-MIRMTEGEVWIDGQ-----SVKQQFESTAAkiGAVIETPEFYPflSGY 98
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTvayvpQVSWIFNATVR--DNILFGSPFDP--ERY 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 99 ENLTyfgrmngNVTEERIDevVKLLGMG---QVIDRKVKaYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPsgiHEMR 175
Cdd:PLN03130 711 ERAI-------DVTALQHD--LDLLPGGdltEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA---HVGR 777
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 822524621 176 MYIKK-IAHE-QGKA-VLVSS--HLLSEVelmcDRVIIIQHGE 213
Cdd:PLN03130 778 QVFDKcIKDElRGKTrVLVTNqlHFLSQV----DRIILVHEGM 816
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-212 |
9.92e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 9.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 19 SKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMI-RMTEGEVWIDGQ-----SVKQQFESTAAkigavietpEFY 92
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELsHAETSSVVIRGSvayvpQVSWIFNATVR---------ENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 93 PFLSGYENLTYFGRMNGNVTEERIDeVVKLLGMGQVIDRKVKAySLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIH 172
Cdd:PLN03232 700 LFGSDFESERYWRAIDVTALQHDLD-LLPGRDLTEIGERGVNI-SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 822524621 173 EmrMYIKKIAHE-QGKAVLVSSHLLSEVELMcDRVIIIQHG 212
Cdd:PLN03232 778 Q--VFDSCMKDElKGKTRVLVTNQLHFLPLM-DRIILVSEG 815
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-246 |
1.06e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.24 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 19 SKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQ--SVKQQfestAAKIGAVIEtpefypfls 96
Cdd:PTZ00243 672 PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSiaYVPQQ----AWIMNATVR--------- 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 97 gyENLTYFGRMNgnvtEERIDEVVKLL-----------GMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNG 165
Cdd:PTZ00243 739 --GNILFFDEED----AARLADAVRVSqleadlaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 166 LDPS-GIHEMRMYIkkIAHEQGKAVLVSSHLLSEVELmCDRVIIIQHG---------EYVATQNIQHNQSEEMETIRIRV 235
Cdd:PTZ00243 813 LDAHvGERVVEECF--LGALAGKTRVLATHQVHVVPR-ADYVVALGDGrvefsgssaDFMRTSLYATLAAELKENKDSKE 889
|
250
....*....|.
gi 822524621 236 DDANKAAEMLD 246
Cdd:PTZ00243 890 GDADAEVAEVD 900
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
18-197 |
1.15e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 18 GSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVwidgqsvkqqFESTAAKIgAVIETPEFYPFLSG 97
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV----------FRSAKVRM-AVFSQHHVDGLDLS 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 98 YENLTYFGRMNGNVTEERIDEVVKLLGM-GQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMrm 176
Cdd:PLN03073 589 SNPLLYMMRCFPGVPEQKLRAHLGSFGVtGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL-- 666
|
170 180
....*....|....*....|...
gi 822524621 177 yIKKIAHEQGKAVLVS--SHLLS 197
Cdd:PLN03073 667 -IQGLVLFQGGVLMVShdEHLIS 688
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
7-167 |
1.19e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.72 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 7 IVKVERLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGM--IRMTEGEVWIDGQSVKQQFESTAAKIGA 84
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 85 VIETPefYPF-LSGYENLTYFGRMNGNVTEER-------------IDEVVKLLGMGQ-VIDRKVK-AYSLGMRQRLGIAQ 148
Cdd:PRK09580 81 FMAFQ--YPVeIPGVSNQFFLQTALNAVRSYRgqepldrfdfqdlMEEKIALLKMPEdLLTRSVNvGFSGGEKKRNDILQ 158
|
170
....*....|....*....
gi 822524621 149 ALIHDPDVLILDEPTNGLD 167
Cdd:PRK09580 159 MAVLEPELCILDESDSGLD 177
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-199 |
1.25e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 24 ENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWI-DGQSVKQ-QFESTAAKIGAVIETPEFYP-------- 93
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDiNLKWWRSKIGVVSQDPLLFSnsiknnik 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 94 ----FLSGYENLTYFGRMNGNVTEERID-----------------------EVVKLLGMGQVID--------RKV----- 133
Cdd:PTZ00265 482 yslySLKDLEALSNYYNEDGNDSQENKNkrnscrakcagdlndmsnttdsnELIEMRKNYQTIKdsevvdvsKKVlihdf 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 134 ----------------KAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLS 197
Cdd:PTZ00265 562 vsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS 641
|
..
gi 822524621 198 EV 199
Cdd:PTZ00265 642 TI 643
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
8-167 |
4.09e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 50.29 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 8 VKVERLTKRIGS--KTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV-KQQFESTAAKIGA 84
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIsKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 85 VIETPefypflsgyenLTYFGRMNGNVTEER---------------IDEVVKLL--GMGQVIDRKVKAYSLGMRQRLGIA 147
Cdd:cd03288 100 ILQDP-----------ILFSGSIRFNLDPECkctddrlwealeiaqLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLA 168
|
170 180
....*....|....*....|
gi 822524621 148 QALIHDPDVLILDEPTNGLD 167
Cdd:cd03288 169 RAFVRKSSILIMDEATASID 188
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-167 |
8.45e-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: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 22 LVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVwidGQSVKQQFESTAAKI--GAVIETpefYPFLSGYE 99
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---KHSGRISFSSQFSWImpGTIKEN---IIFGVSYD 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822524621 100 NLTYFGRMNGNVTEERIDEVVK----LLGMGQVIdrkvkaYSLGMRQRLGIAQALIHDPDVLILDEPTNGLD 167
Cdd:cd03291 126 EYRYKSVVKACQLEEDITKFPEkdntVLGEGGIT------LSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-213 |
1.18e-06 |
|
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: 49.94 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 16 RIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV-KQQFESTAAKIGAVIETPEFYpf 94
Cdd:TIGR00957 1295 REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIaKIGLHDLRFKITIIPQDPVLF-- 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 95 lSGYEnltyfgRMN----GNVTEERI---DEVVKLLGMGQVIDRKV--------KAYSLGMRQRLGIAQALIHDPDVLIL 159
Cdd:TIGR00957 1373 -SGSL------RMNldpfSQYSDEEVwwaLELAHLKTFVSALPDKLdhecaeggENLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 822524621 160 DEPTNGLDpsgiHEMRMYIKKIAHEQGK--AVLVSSHLLSEVeLMCDRVIIIQHGE 213
Cdd:TIGR00957 1446 DEATAAVD----LETDNLIQSTIRTQFEdcTVLTIAHRLNTI-MDYTRVIVLDKGE 1496
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
23-222 |
1.34e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 49.13 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMI----RMTEGEVWIDGQ-----SVKQQFESTAAKIGAVIETPEFY- 92
Cdd:COG4170 23 VDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIdllklSPRERRKIIGREIAMIFQEPSSCl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 93 -PFLSGYENL------TYFGRMNGNVTEERIDEVVKLLGMGQVIDRKV--KAY----SLGMRQRLGIAQALIHDPDVLIL 159
Cdd:COG4170 103 dPSAKIGDQLieaipsWTFKGKWWQRFKWRKKRAIELLHRVGIKDHKDimNSYphelTEGECQKVMIAMAIANQPRLLIA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822524621 160 DEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNIQH 222
Cdd:COG4170 183 DEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQ 245
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-194 |
3.61e-06 |
|
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: 48.21 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 22 LVENISFEVKKGEVVGLLGPNGAGKTTLMRMMvgmirmteGEVWidgqsvkqqfestaAKIGAVIETPE----FY----P 93
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRIL--------GELW--------------PVYGGRLTKPAkgklFYvpqrP 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 94 FLSG---YENLTY-------FGRMNGNVTEERIDEVVKL-------LGMGQVIDRKvKAYSLGMRQRLGIAQALIHDPDV 156
Cdd:TIGR00954 525 YMTLgtlRDQIIYpdssedmKRRGLSDKDLEQILDNVQLthilereGGWSAVQDWM-DVLSGGEKQRIAMARLFYHKPQF 603
|
170 180 190
....*....|....*....|....*....|....*...
gi 822524621 157 LILDEPTNGLDPsgihEMRMYIKKIAHEQGKAVLVSSH 194
Cdd:TIGR00954 604 AILDECTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
40-199 |
1.42e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 40 GPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV----KQQFESTAAKIGAVIEtpefypfLSGYENLTYFGRMNGNVteER 115
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniaKPYCTYIGHNLGLKLE-------MTVFENLKFWSEIYNSA--ET 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 116 IDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIkKIAHEQGKAVLVSSHL 195
Cdd:PRK13541 104 LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI-VMKANSGGIVLLSSHL 182
|
....
gi 822524621 196 LSEV 199
Cdd:PRK13541 183 ESSI 186
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
12-212 |
2.50e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.93 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 12 RLTKRIGSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWIDGQSV--------KQQF-------- 75
Cdd:PTZ00243 1315 QMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIgayglrelRRQFsmipqdpv 1394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 76 --------------ESTAAKIGAVIEtpefypfLSGyenltyfgrMNGNVTEER--IDEVVKLLGMGqvidrkvkaYSLG 139
Cdd:PTZ00243 1395 lfdgtvrqnvdpflEASSAEVWAALE-------LVG---------LRERVASESegIDSRVLEGGSN---------YSVG 1449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822524621 140 MRQRLGIAQALIHDPDVLIL-DEPTNGLDPSGIHEMRMYIKKI--AHeqgkAVLVSSHLLSEVElMCDRVIIIQHG 212
Cdd:PTZ00243 1450 QRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAfsAY----TVITIAHRLHTVA-QYDKIIVMDHG 1520
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
32-195 |
2.81e-05 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 43.91 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 32 KGEVVGLLGPNGAGKTTLmrMMVGMIRMTEGEVWIDGQSVKQQ--------------FESTAAKIGAVIETPEFYPFLSG 97
Cdd:pfam13481 32 AGGLGLLAGAPGTGKTTL--ALDLAAAVATGKPWLGGPRVPEQgkvlyvsaegpadeLRRRLRAAGADLDLPARLLFLSL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 98 YENLTYFGRMNGNvteERIDEVVKLLgmgqviDRKVKAyslgmrqrlgiaqalIHDPDVLILD--EPTNGLDPSGIHEMR 175
Cdd:pfam13481 110 VESLPLFFLDRGG---PLLDADVDAL------EAALEE---------------VEDPDLVVIDplARALGGDENSNSDVG 165
|
170 180
....*....|....*....|...
gi 822524621 176 MYIKK---IAHEQGKAVLVSSHL 195
Cdd:pfam13481 166 RLVKAldrLARRTGATVLLVHHV 188
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
23-228 |
8.27e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.64 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 23 VENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGM----IRMTEGEVWIDG-----QSVKQQFESTAAKIGAVIETPEfyP 93
Cdd:PRK15093 23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDidllrLSPRERRKLVGHNVSMIFQEPQ--S 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 94 FLSGYENL-----------TYFGRMNGNVtEERIDEVVKLLGMGQVIDRK--VKAYSL----GMRQRLGIAQALIHDPDV 156
Cdd:PRK15093 101 CLDPSERVgrqlmqnipgwTYKGRWWQRF-GWRKRRAIELLHRVGIKDHKdaMRSFPYelteGECQKVMIAIALANQPRL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822524621 157 LILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSSHLLSEVELMCDRVIIIQHGeyvatQNIQHNQSEEM 228
Cdd:PRK15093 180 LIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCG-----QTVETAPSKEL 246
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
130-218 |
8.42e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.77 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 130 DRKVKAYSL--GMRQRLGIAqALIHDPD---VLILDEPTNGLDPSGIHEMRMYIKKIAHE-QgkaVLVSSH---LLSEVE 200
Cdd:COG4637 251 DRPFPARELsdGTLRFLALL-AALLSPRpppLLCIEEPENGLHPDLLPALAELLREASERtQ---VIVTTHspaLLDALE 326
|
90
....*....|....*...
gi 822524621 201 LmcDRVIIIQHGEYVATQ 218
Cdd:COG4637 327 P--EEVLVLEREDDGETR 342
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
12-264 |
2.54e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 12 RLTKRIgSKTLVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMT---EGEVWIDGQSVKqQF--ESTAAKIG--- 83
Cdd:PLN03140 171 NLAKKT-KLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLN-EFvpRKTSAYISqnd 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 84 ------AVIETPEFYPFLSG----YENLTYFGR---------------------MNGNVTEERIDEVVKLLGMG-----Q 127
Cdd:PLN03140 249 vhvgvmTVKETLDFSARCQGvgtrYDLLSELARrekdagifpeaevdlfmkataMEGVKSSLITDYTLKILGLDickdtI 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 128 VIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGIHEMRMYIKKIAHEQGKAVLVSshLLS---EVELMCD 204
Cdd:PLN03140 329 VGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMS--LLQpapETFDLFD 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 205 RVIIIQHGEYVaTQNIQHNQSEEMETIRIRVDDANKAAEMLdQDVLIKgndllihvKDEE 264
Cdd:PLN03140 407 DIILLSEGQIV-YQGPRDHILEFFESCGFKCPERKGTADFL-QEVTSK--------KDQE 456
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
22-220 |
3.98e-04 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 40.81 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 22 LVENISFEVKKGEVVGLLGPNGAGKTTLMRMMVGMIRMTEGEVWidgqsvkqQFESTAAKIGAvieTPEFYPFLSGYENL 101
Cdd:PRK15177 2 VLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFI--------GLRGDALPLGA---NSFILPGLTGEENA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 102 TYFGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHDPDVLILDEPTNGLDPSGihEMRMYIKKI 181
Cdd:PRK15177 71 RMMASLYGLDGDEFSHFCYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNAT--QLRMQAALA 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 822524621 182 AHEQGKAVLVSSHLLSEVELMCDRVIIIQHGEYVATQNI 220
Cdd:PRK15177 149 CQLQQKGLIVLTHNPRLIKEHCHAFGVLLHGKITMCEDL 187
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-212 |
5.33e-04 |
|
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: 40.00 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 25 NISFEVKKGEVVGLLGPNGAGKTTLmrmmvgmirmtegevwidgqsVKQQFEstAAKIGAVIETPEFYPflsgyENLTYF 104
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTL---------------------VNEGLY--ASGKARLISFLPKFS-----RNKLIF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 105 grmngnvteerIDEVVKLLGMG---QVIDRKVKAYSLGMRQRLGIAQALIHDPD--VLILDEPTNGLDPSGIHEMRMYIK 179
Cdd:cd03238 65 -----------IDQLQFLIDVGlgyLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIK 133
|
170 180 190
....*....|....*....|....*....|....*
gi 822524621 180 KIAhEQGKAVLVSSHllsEVELMC--DRVIIIQHG 212
Cdd:cd03238 134 GLI-DLGNTVILIEH---NLDVLSsaDWIIDFGPG 164
|
|
| DUF4162 |
pfam13732 |
Domain of unknown function (DUF4162); This domain is found at the C-terminus of bacterial ABC ... |
229-297 |
1.16e-03 |
|
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: 37.19 E-value: 1.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 229 ETIRIRVDDANKAAEMLDQDVL-IKGNDLLIHVKDEEIPNVIRILLEKNIQVYRVYEERKTLEEQFLELT 297
Cdd:pfam13732 13 NRIEVETADAEELLELPGVEEVeEEGGGLELKLEDEEAANELLAALLSGGEIRSFEEEEPSLNDIFIEKV 82
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-209 |
1.40e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 130 DRKVKAYSLGMRQRLGIAQALIHDPD--VLILDEPTNGLDPSGIHEMRMYIKKIaHEQGKAVLVSSHLLSEVELmCDRVI 207
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQMISL-ADRII 548
|
..
gi 822524621 208 II 209
Cdd:PRK00635 549 DI 550
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
10-194 |
2.37e-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: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 10 VERLT-KRIGSKTLVENISFEvkkGEVVGLLGPNGAGKTTLM---------------RMMVGMIRM-TEGEVwidGQSVK 72
Cdd:cd03240 1 IDKLSiRNIRSFHERSEIEFF---SPLTLIVGQNGAGKTTIIealkyaltgelppnsKGGAHDPKLiREGEV---RAQVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 73 QQFESTAAKIGAVIETPEFYpflsgyENLTYF--GRMNGNVTEERidevvKLLGMGQvidrKVKAySLGMRqrLGIAQAL 150
Cdd:cd03240 75 LAFENANGKKYTITRSLAIL------ENVIFChqGESNWPLLDMR-----GRCSGGE----KVLA-SLIIR--LALAETF 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 822524621 151 IHDPDVLILDEPTNGLDPSGIHE-MRMYIKKIAHEQGKAVLVSSH 194
Cdd:cd03240 137 GSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQKNFQLIVITH 181
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
98-194 |
2.40e-03 |
|
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: 38.91 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 98 YENLTYFGRMNGNVTEERIDEVVKLLGMGQVIDRKVKAYSLGMRQRLGIAQALIHD---PDVLILDEPTNGLDPSGIHEM 174
Cdd:pfam13304 199 LSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLSAlpkGGLLLIDEPESGLHPKLLRRL 278
|
90 100
....*....|....*....|
gi 822524621 175 rMYIKKIAHEQGKAVLVSSH 194
Cdd:pfam13304 279 -LELLKELSRNGAQLILTTH 297
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-207 |
3.10e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822524621 131 RKVKAYSLGMRQRLGIAQALIH---DPDVLILDEPTNGLDPSGIHEMRMYIKKIAHeQGKAVLVSSHLLSEVELmCDRVI 207
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTH-QGHTVVIIEHNMHVVKV-ADYVL 882
|
|
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