|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-238 |
1.57e-84 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 251.14 E-value: 1.57e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQKVGVQFQ 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 85 EGDYQPEIKVSELCGETACLY-----EAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTT 159
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYglprkEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 160 GLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQAKAvsgcEKFEDAYLMLSGEEV 238
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA----RLLEDVFLELTGEEA 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-207 |
1.64e-66 |
|
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: 203.40 E-value: 1.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQKVGVQFQ 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 85 EGDYQPEIKVSELcgetacLYeapadwkslceqfgigskignavksLSGGERQRLFIVLALIPNPELVFLDELTTGLDAK 164
Cdd:cd03230 81 EPSLYENLTVREN------LK-------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1045868222 165 ARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:cd03230 130 SRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-240 |
1.17e-63 |
|
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: 198.54 E-value: 1.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQKVGVQFQ 84
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 85 EGDYQPEIKVSELCGETACLY-----EAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTT 159
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYglfdeELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 160 GLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQAKAVSGCEKFEDAYLMLSGEEVG 239
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVALIGSEEG 241
|
.
gi 1045868222 240 E 240
Cdd:COG4555 242 E 242
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-214 |
1.42e-54 |
|
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: 174.62 E-value: 1.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAY--DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQKVGVQ 82
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 83 FQEGDYQPEIKVSE-------LCGETacLYEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLD 155
Cdd:cd03263 81 PQFDALFDELTVREhlrfyarLKGLP--KSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 156 ELTTGLDAKARRDVWKILQELKQgGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTV 214
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-224 |
1.31e-53 |
|
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: 174.50 E-value: 1.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 12 KAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQKVGVQFQegDYQPE 91
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQ--YASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 92 IKVS-----ELCGETACLYEAPADWKS--LCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAK 164
Cdd:TIGR01188 79 EDLTgrenlEMMGRLYGLPKDEAEERAeeLLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 165 ARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQAKAVSGCE 224
Cdd:TIGR01188 159 TRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKD 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-227 |
7.99e-53 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 172.60 E-value: 7.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNcNP--QKDRcrlfQKVGv 81
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG-EPldPEDR----RRIG- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 82 qfqegdYQPE-------IKVSElcgetACLY----------EAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLA 144
Cdd:COG4152 75 ------YLPEerglypkMKVGE-----QLVYlarlkglskaEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 145 LIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQAKAVSGCE 224
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRN 223
|
...
gi 1045868222 225 KFE 227
Cdd:COG4152 224 TLR 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-218 |
5.69e-50 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 162.92 E-value: 5.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQKVGVQFQ 84
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 85 EGDYQPEIKVSELCGETACLYEAP-ADWKS----LCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTT 159
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPgAERRErideLLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 160 GLDAKARRDVWKILQELKQ-GGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQAK 218
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-230 |
1.99e-46 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 154.48 E-value: 1.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRcrlfQKVG 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR----RRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 -V-QFQEGDYQPEIKVSE--LCGetaCLYEAP-------ADW----KSLcEQFGIGSKIGNAVKSLSGGERQRLFIVLAL 145
Cdd:COG1121 79 yVpQRAEVDWDFPITVRDvvLMG---RYGRRGlfrrpsrADReavdEAL-ERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 146 IPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKaVFYGTVEQakaVSGCEK 225
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGL-VAHGPPEE---VLTPEN 230
|
....*
gi 1045868222 226 FEDAY 230
Cdd:COG1121 231 LSRAY 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-217 |
8.15e-45 |
|
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: 149.79 E-value: 8.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAY-DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCR-LFQKVGVQ 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLReLRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 83 FQEGDYQpeikvseLCGETacLYE----------APADW-----KSLCEQFGIGSKIGNAVKSLSGGERQRLFI--VLAL 145
Cdd:COG1122 81 FQNPDDQ-------LFAPT--VEEdvafgpenlgLPREEirervEEALELVGLEHLADRPPHELSGGQKQRVAIagVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 146 ipNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQA 217
Cdd:COG1122 152 --EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-212 |
1.95e-44 |
|
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: 148.13 E-value: 1.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLfQKVGVQFQ 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL-RRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 85 EGDYQPEIKVSELCGETACLYEAP-ADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDA 163
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRkKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1045868222 164 KARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYG 212
Cdd:cd03268 160 DGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-215 |
1.06e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 147.16 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYD-------------NLL--------AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVS 62
Cdd:COG4586 1 IIEVENLSKTYRvyekepglkgalkGLFrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 63 ILNCNPQKDRCRLFQKVGVQFqeGdyQ--------PEIKVSELcgeTACLYEAPADW-----KSLCEQFGIGSKIGNAVK 129
Cdd:COG4586 81 VLGYVPFKRRKEFARRIGVVF--G--QrsqlwwdlPAIDSFRL---LKAIYRIPDAEykkrlDELVELLDLGELLDTPVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 130 SLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKA 208
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
....*..
gi 1045868222 209 VFYGTVE 215
Cdd:COG4586 234 IYDGSLE 240
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-212 |
1.89e-42 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 146.10 E-value: 1.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTA-IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSIlnCN---PQKDRcRLF 76
Cdd:PRK13537 3 MSVApIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISL--CGepvPSRAR-HAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 QKVGVQFQEGDYQPEIKVSE-------LCGETAClyEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNP 149
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVREnllvfgrYFGLSAA--AARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 150 ELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYG 212
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-212 |
3.08e-42 |
|
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: 142.42 E-value: 3.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNcNPQKDRCRlfQKVGVQFQ 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-KPLDIAAR--NRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 85 EGDYQPEIKVSELCGETACLY-----EAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTT 159
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKglkkeEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 160 GLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYG 212
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-212 |
3.23e-42 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 146.13 E-value: 3.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 3 TAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCnPQKDRCRLFQ-KVGV 81
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV-PVPARARLARaRIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 82 QFQEGDYQPEIKVSE-------LCGETAclYEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFL 154
Cdd:PRK13536 119 VPQFDNLDLEFTVREnllvfgrYFGMST--REIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1045868222 155 DELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYG 212
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-207 |
9.26e-41 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 136.99 E-value: 9.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 6 KVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNP-QKDRCRLFQKVGVQFQ 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 85 egdyqpeikvselcgetaclyeapadwkslceqfgigskignavksLSGGERQRLFIVLALIPNPELVFLDELTTGLDAK 164
Cdd:cd00267 81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1045868222 165 ARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:cd00267 115 SRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-212 |
2.61e-40 |
|
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: 137.88 E-value: 2.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNL----LAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNCNPQKDRCRLf 76
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdgfdVVKEPAEARRRL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 qkvGVQF-QEGDYqPEIKVSELCGETACLY-----EAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPE 150
Cdd:cd03266 81 ---GFVSdSTGLY-DRLTARENLEYFAGLYglkgdELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 151 LVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYG 212
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-212 |
6.32e-39 |
|
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: 134.24 E-value: 6.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGtVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQKVGVQFQ 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 85 EGDYQPEIKVSELCGETACLYE-APADWKSLC----EQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTT 159
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGiPSKEVKARVdevlELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 160 GLDAKARRDVWKILQELKQGGLTIFITsHFMDEVEILCDEICILKQGKAVFYG 212
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILST-HIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-207 |
6.54e-39 |
|
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: 134.13 E-value: 6.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 6 KVEQLSKAYDNL--LAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCR-LFQKVGVQ 82
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKeLRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 83 FQEGDYQpeikvseLCGET-------ACL------YEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNP 149
Cdd:cd03225 81 FQNPDDQ-------FFGPTveeevafGLEnlglpeEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1045868222 150 ELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-207 |
6.80e-39 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 133.08 E-value: 6.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSIL--NCNPQKDRCRLF-QKVGV 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgeDLTDLEDELPPLrRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 82 QFQEGDYQPEIKVSElcgetaclyeapadwkslceqfgigskigNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGL 161
Cdd:cd03229 81 VFQDFALFPHLTVLE-----------------------------NIALGLSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1045868222 162 DAKARRDVWKILQELKQG-GLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:cd03229 132 DPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-216 |
2.18e-37 |
|
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: 131.32 E-value: 2.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN----PQKDRCRlfqKV 79
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslSRRELAR---RI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 GVQFQEGDYQPEIKVSEL------------CGETACLYEApADWkSLcEQFGIGSKIGNAVKSLSGGERQRLFIVLALIP 147
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELvalgryphlglfGRPSAEDREA-VEE-AL-ERTGLEHLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 148 NPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-207 |
6.86e-37 |
|
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: 129.15 E-value: 6.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDN----LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNP------QKDRCR 74
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsekELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 75 LfQKVGVQFQEGDYQPEIKVSE-------LCGETAclYEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIP 147
Cdd:cd03255 81 R-RHIGFVFQSFNLLPDLTALEnvelpllLAGVPK--KERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1045868222 148 NPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEiLCDEICILKQGK 207
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELAE-YADRIIELRDGK 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-212 |
4.09e-36 |
|
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: 126.01 E-value: 4.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 6 KVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQK-DRCRLFQKVGVQFQ 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 85 egdyqpeikvselcgetaclyeapadwksLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAK 164
Cdd:cd03214 81 -----------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1045868222 165 ARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYG 212
Cdd:cd03214 132 HQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-212 |
6.50e-36 |
|
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: 126.49 E-value: 6.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 6 KVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRcrlfQKVGV--QF 83
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER----KRIGYvpQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 84 QEGDYQPEIKVSELCGeTACLYEAP-------ADWK---SLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVF 153
Cdd:cd03235 77 RSIDRDFPISVRDVVL-MGLYGHKGlfrrlskADKAkvdEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 154 LDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKaVFYG 212
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTV-VASG 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-212 |
9.07e-36 |
|
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: 126.68 E-value: 9.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYD---------------------NLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI 63
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligslkslfkrkyrEVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 64 LNCNPQKDRCRLFQKVGVQF-QEGDYQPEIKVSELCGETACLYEAPAD-----WKSLCEQFGIGSKIGNAVKSLSGGERQ 137
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPArfkkrLDELSELLDLEELLDTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1045868222 138 RLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYG 212
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-216 |
1.12e-35 |
|
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: 131.95 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 2 QTAIKVEQLSKAY-----DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN----PQKDR 72
Cdd:COG1123 258 EPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltklSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 73 CRLFQKVGVQFQEGDYQ--PEIKVSELCGETACLY------EAPADWKSLCEQFGIGSKIGNA-VKSLSGGERQRLFIVL 143
Cdd:COG1123 338 RELRRRVQMVFQDPYSSlnPRMTVGDIIAEPLRLHgllsraERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1045868222 144 ALIPNPELVFLDELTTGLDAKARRDVWKILQELKQ-GGLT-IFITsHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQReLGLTyLFIS-HDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
1.70e-34 |
|
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: 128.87 E-value: 1.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDN--LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILG--TKNAD-SGTVSI----LNCNPQKD 71
Cdd:COG1123 1 MTPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllPHGGRiSGEVLLdgrdLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 72 RCRlfqKVGVQFQEGDYQ--PeIKVSELCGETACLY-----EAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLA 144
Cdd:COG1123 81 RGR---RIGMVFQDPMTQlnP-VTVGDQIAEALENLglsraEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 145 LIPNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-216 |
2.03e-34 |
|
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: 123.07 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDN----LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN----PQKDRCRLF 76
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltllSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 QKVGVQFQ-----------------------EGDYQPEiKVSELCgetaclyeapadwkslcEQFGIGSKIGNAVKSLSG 133
Cdd:cd03258 82 RRIGMIFQhfnllssrtvfenvalpleiagvPKAEIEE-RVLELL-----------------ELVGLEDKADAYPAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 134 GERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYG 212
Cdd:cd03258 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEG 223
|
....
gi 1045868222 213 TVEQ 216
Cdd:cd03258 224 TVEE 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-209 |
2.45e-34 |
|
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: 120.61 E-value: 2.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNcnpqkdrcrlfQKVgvqfq 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-----------KEV----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 85 egdyqpeikvselcgETACLYEApadwkslcEQFGIGskignAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAK 164
Cdd:cd03216 65 ---------------SFASPRDA--------RRAGIA-----MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1045868222 165 ARRDVWKILQELKQGGLT-IFItSHFMDEVEILCDEICILKQGKAV 209
Cdd:cd03216 117 EVERLFKVIRRLRAQGVAvIFI-SHRLDEVFEIADRVTVLRDGRVV 161
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-219 |
6.20e-34 |
|
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: 122.01 E-value: 6.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN----PQKDRCRLF 76
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitglSEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 QKVGVQFQEG--------------------DY-QPEIK--VS---ELCG--ETACLYeaPADwkslceqfgigskignav 128
Cdd:COG1127 82 RRIGMLFQGGalfdsltvfenvafplrehtDLsEAEIRelVLeklELVGlpGAADKM--PSE------------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 129 ksLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQG-GLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:COG1127 142 --LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGK 219
|
250
....*....|..
gi 1045868222 208 AVFYGTVEQAKA 219
Cdd:COG1127 220 IIAEGTPEELLA 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-216 |
1.15e-33 |
|
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: 121.00 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV-----SILNCNPQKdRCRL---- 75
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeDITGLPPHE-IARLgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 76 -FQK--------------VGVQFQEGDYQPEIKVSElcGETACLYEApadwKSLCEQFGIGSKIGNAVKSLSGGERQRLF 140
Cdd:cd03219 80 tFQIprlfpeltvlenvmVAAQARTGSGLLLARARR--EEREARERA----EELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1045868222 141 IVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-219 |
2.62e-33 |
|
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: 120.68 E-value: 2.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDNLL----AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNCNPQKDRCRl 75
Cdd:COG1124 1 MLEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgrpVTRRRRKAFRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 76 fqKVGVQFQ--EGDYQPEIKVSELCGETACLYEAPADWK---SLCEQFGIGSkignAVKS-----LSGGERQRLFIVLAL 145
Cdd:COG1124 80 --RVQMVFQdpYASLHPRHTVDRILAEPLRIHGLPDREEriaELLEQVGLPP----SFLDryphqLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1045868222 146 IPNPELVFLDELTTGLDAKARRDVWKILQELK-QGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQAKA 219
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-216 |
4.02e-33 |
|
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: 119.57 E-value: 4.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN----PQKDRCRL----- 75
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklPMHKRARLgigyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 76 ------FQKVGV--------QFQEGDYQPEIKVSElcgetaclyeapadwkSLCEQFGIGSKIGNAVKSLSGGERQRLFI 141
Cdd:cd03218 81 pqeasiFRKLTVeenilavlEIRGLSKKEREEKLE----------------ELLEEFHITHLRKSKASSLSGGERRRVEI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1045868222 142 VLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:cd03218 145 ARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEE 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-212 |
7.47e-33 |
|
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: 118.76 E-value: 7.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDN----LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNCNPQKDRCRLF 76
Cdd:cd03257 2 LEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdgkdLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 QKVGVQFQegDYQ----PEIKVSELCGETA----CLYEAPADWKSLCE---QFGIGSKIGNA-VKSLSGGERQRLFIVLA 144
Cdd:cd03257 82 KEIQMVFQ--DPMsslnPRMTIGEQIAEPLrihgKLSKKEARKEAVLLllvGVGLPEEVLNRyPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 145 LIPNPELVFLDELTTGLDAKARRDVWKILQELKQG-GLTIFITSHFMDEVEILCDEICILKQGKAVFYG 212
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-200 |
2.94e-32 |
|
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: 116.81 E-value: 2.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQKVGVQFQ 84
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 85 EGDYQPEIKVSELCGETACLYEAPAD---WKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGL 161
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADreaIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 1045868222 162 DAKARRDVWKILQELKQGGLTIFITSHfmDEVEILCDEI 200
Cdd:COG4133 163 DAAGVALLAELIAAHLARGGAVLLTTH--QPLELAAARV 199
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-213 |
4.10e-32 |
|
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: 117.28 E-value: 4.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLL-AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCR----LFQKV 79
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 GVQFQEGDYQPEIKVSE--LCGetaCLYEAPAdWKSL---------------CEQFGIGSKIGNAVKSLSGGERQRLFIV 142
Cdd:cd03256 81 GMIFQQFNLIERLSVLEnvLSG---RLGRRST-WRSLfglfpkeekqralaaLERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 143 LALIPNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGT 213
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGP 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-240 |
4.80e-32 |
|
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: 117.45 E-value: 4.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV-----SILNCNPQKdRCRL 75
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIlfdgrDITGLPPHR-IARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 76 -----FQ--------------KVGVQFQEGdyqpeikvselCGETACLYEAPADWKS----------LCEQFGIGSKIGN 126
Cdd:COG0411 80 giartFQnprlfpeltvlenvLVAAHARLG-----------RGLLAALLRLPRARREereareraeeLLERVGLADRADE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 127 AVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQG-GLTIFITSHFMDEVEILCDEICILKQ 205
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDF 228
|
250 260 270
....*....|....*....|....*....|....*
gi 1045868222 206 GKAVFYGTVEQakaVSGCEKFEDAYLmlsGEEVGE 240
Cdd:COG0411 229 GRVIAEGTPAE---VRADPRVIEAYL---GEEAAA 257
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-226 |
9.34e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 111.14 E-value: 9.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNCNPQKDRCRlfQKVG 80
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedISLLPLHARAR--RGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQFQEGD-------YQPEIKVSELCGE-TACLYEAPADwkSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELV 152
Cdd:PRK10895 82 YLPQEASifrrlsvYDNLMAVLQIRDDlSAEQREDRAN--ELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 153 FLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTV------EQAKAVSGCEKF 226
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPteilqdEHVKRVYLGEDF 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-207 |
1.16e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 110.52 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDN----LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN----PQKDR 72
Cdd:COG1136 1 MSPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDisslSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 73 CRL-FQKVGVQFQegDYQ--PEIKVSE-------LCGETAclYEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIV 142
Cdd:COG1136 81 ARLrRRHIGFVFQ--FFNllPELTALEnvalpllLAGVSR--KERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1045868222 143 LALIPNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHfmDEvEIL--CDEICILKQGK 207
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTH--DP-ELAarADRVIRLRDGR 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-219 |
2.31e-29 |
|
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: 109.90 E-value: 2.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNP----QKDRCRLFQKVG 80
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQFQEG---DyqpeikvSELCGETAC--LYEAPADWKSLC--------EQFGIGSKIGNAVKSLSGGERQRLFIVLALIP 147
Cdd:cd03261 81 MLFQSGalfD-------SLTVFENVAfpLREHTRLSEEEIreivleklEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 148 NPELVFLDELTTGLDAKARRDVWKILQELKQ-GGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQAKA 219
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-212 |
3.54e-29 |
|
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: 108.92 E-value: 3.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 30 GTVYGLLGANGAGKSTTIECILGTKNADSGTVSI-----------LNCNPQKdrcrlfQKVGVQFQEGDYQPEIKVSE-- 96
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdsrkkINLPPQQ------RKIGLVFQQYALFPHLNVREnl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 97 LCGETAClyeAPADWKSLCEQ----FGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKI 172
Cdd:cd03297 97 AFGLKRK---RNREDRISVDElldlLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1045868222 173 LQELKQ--GGLTIFITsHFMDEVEILCDEICILKQGKAVFYG 212
Cdd:cd03297 174 LKQIKKnlNIPVIFVT-HDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-209 |
1.15e-28 |
|
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: 107.61 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNCNPQKDRcrlfqKVG 80
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgrdVTGVPPERR-----NIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQFQegDYqpeikvselcgetaCLY---------------------EAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRL 139
Cdd:cd03259 76 MVFQ--DY--------------ALFphltvaeniafglklrgvpkaEIRARVRELLELVGLEGLLNRYPHELSGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1045868222 140 FIVLALIPNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAV 209
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-219 |
1.90e-28 |
|
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: 107.13 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVS-----ILNCNPQKdRCRLfqkv 79
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfdgrdITGLPPHE-RARA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 GVQfqegdYQPEIK-------VSE---LCGETACLYEAPADWKSLCEQFGI-GSKIGNAVKSLSGGERQRLFIVLALIPN 148
Cdd:cd03224 76 GIG-----YVPEGRrifpeltVEEnllLGAYARRRAKRKARLERVYELFPRlKERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1045868222 149 PELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQAKA 219
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-216 |
7.79e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 105.88 E-value: 7.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVsILNcnpQKD--------RCRL- 75
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI-FLD---GEDithlpmhkRARLg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 76 ----------FQKVGV--------QFQEGDY-QPEIKVSELCGEtaclyeapadwkslceqFGIGSKIGNAVKSLSGGER 136
Cdd:COG1137 80 igylpqeasiFRKLTVednilavlELRKLSKkEREERLEELLEE-----------------FGITHLRKSKAYSLSGGER 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 137 QRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:COG1137 143 RRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEE 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-207 |
8.05e-28 |
|
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: 104.00 E-value: 8.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDN--LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQK-DRCRLFQKVGV 81
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 82 QFQEgdyqpeikvselcgetACLYEApadwkSLCEQFgigskignavksLSGGERQRLFIVLALIPNPELVFLDELTTGL 161
Cdd:cd03228 81 VPQD----------------PFLFSG-----TIRENI------------LSGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1045868222 162 DAKARRDVWKILQELKQGGLTIFITsHFMDEVEiLCDEICILKQGK 207
Cdd:cd03228 128 DPETEALILEALRALAKGKTVIVIA-HRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-207 |
1.73e-27 |
|
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: 104.53 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNcNPQKDRCRLFQKVG 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdglkLT-DDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQFQEGDYQPEIKVSELCGEtACLY-------EAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVF 153
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITL-APIKvkgmskaEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1045868222 154 LDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-159 |
1.99e-27 |
|
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: 102.34 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQK-VGVQFQEGDYQPEIKVSELCGET 101
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKeIGYVFQDPQLFPRLTVRENLRLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1045868222 102 ACLYEAPADWKS-----LCEQFGIG----SKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTT 159
Cdd:pfam00005 84 LLLKGLSKREKDaraeeALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-213 |
4.30e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.07 E-value: 4.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 2 QTAIKVEQLSKAYDN--LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQ-K 78
Cdd:PRK13632 5 SVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRkK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 79 VGVQFQEGDYQpeikvseLCGETA-----------CL--YEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFI--VL 143
Cdd:PRK13632 85 IGIIFQNPDNQ-------FIGATVeddiafglenkKVppKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIasVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1045868222 144 ALipNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVeILCDEICILKQGKAVFYGT 213
Cdd:PRK13632 158 AL--NPEIIIFDESTSMLDPKGKREIKKIMVDLrKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-188 |
8.12e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 102.82 E-value: 8.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDN-LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN----PQKDRCRLFQKV 79
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrlKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 GVQFQegDYQ--PEIKVSE-------LCGETaclyeaPADWKS----LCEQFGIGSKIGNAVKSLSGGERQRLFIVLALI 146
Cdd:COG2884 82 GVVFQ--DFRllPDRTVYEnvalplrVTGKS------RKEIRRrvreVLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1045868222 147 PNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSH 188
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATH 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-232 |
1.09e-26 |
|
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: 108.18 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLL--AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQKVGV- 81
Cdd:TIGR01257 1938 LRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYc 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 82 -QFQEGD-----YQPEIKVSELCGETACLYEAPADWKslCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLD 155
Cdd:TIGR01257 2018 pQFDAIDdlltgREHLYLYARLRGVPAEEIEKVANWS--IQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLD 2095
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1045868222 156 ELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQAKAvsgceKFEDAYLM 232
Cdd:TIGR01257 2096 EPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKS-----KFGDGYIV 2167
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-209 |
1.64e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.64 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVsILNCNPQKdrcrlF---- 76
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEI-LLDGEPVR-----Frspr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 --QKVGVQ--FQEGDYQPEIKVselcGETACLYEAPA-----DWKS-------LCEQFGIGSKIGNAVKSLSGGERQRLF 140
Cdd:COG1129 75 daQAAGIAiiHQELNLVPNLSV----AENIFLGREPRrggliDWRAmrrrareLLARLGLDIDPDTPVGDLSVAQQQLVE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 141 IVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAV 209
Cdd:COG1129 151 IARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLV 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-207 |
1.96e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 101.43 E-value: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV-----SILNCNPQKDRCR---LF 76
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkPLSAMPPPEWRRQvayVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 QK-------VGVQFQEGDYQPEIKVSelcgetaclyeaPADWKSLCEQFGIGSKIGNA-VKSLSGGERQRLFIVLALIPN 148
Cdd:COG4619 81 QEpalwggtVRDNLPFPFQLRERKFD------------RERALELLERLGLPPDILDKpVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 149 PELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-216 |
1.99e-26 |
|
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: 104.81 E-value: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 22 KINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLF-----QKVGVQFQEGDYQPEIKVSE 96
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlppekRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 97 --LCGETACL-YEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKIL 173
Cdd:TIGR02142 95 nlRYGMKRARpSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1045868222 174 QELKQG-GLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:TIGR02142 175 ERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAE 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-212 |
3.30e-26 |
|
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: 100.70 E-value: 3.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 10 LSKAYDNLLavDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKN--ADSGTVSIlncNPQKDRCRLFQK-VGVQFQEG 86
Cdd:cd03213 17 PSKSGKQLL--KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLI---NGRPLDKRSFRKiIGYVPQDD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 87 DYQPEIKVSELCGETACLyeapadwkslceqfgigskignavKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKAR 166
Cdd:cd03213 92 ILHPTLTVRETLMFAAKL------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1045868222 167 RDVWKILQELKQGGLTIFITSH-FMDEVEILCDEICILKQGKAVFYG 212
Cdd:cd03213 148 LQVMSLLRRLADTGRTIICSIHqPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-215 |
1.06e-25 |
|
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: 100.49 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLlAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVS-----ILNCNPQKDRcrlfqkV 79
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkdITNLPPEKRD------I 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 GVQFQEGDYQPEIKVSE-----LCGETACLYEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFL 154
Cdd:cd03299 74 SYVPQNYALFPHMTVYKniaygLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 155 DELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVE 215
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-216 |
1.15e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 102.53 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI------LNCNPQkDRcrlfqK 78
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLngrdlfTNLPPR-ER-----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 79 VGVQFQegDY----------------------QPEI--KVSELcgetaclyeapadwksLcEQFGIgSKIGNAVKS-LSG 133
Cdd:COG1118 77 VGFVFQ--HYalfphmtvaeniafglrvrppsKAEIraRVEEL----------------L-ELVQL-EGLADRYPSqLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 134 GERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQEL--KQGGLTIFITsHFMDEVEILCDEICILKQGKAVFY 211
Cdd:COG1118 137 GQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhdELGGTTVFVT-HDQEEALELADRVVVMNQGRIEQV 215
|
....*
gi 1045868222 212 GTVEQ 216
Cdd:COG1118 216 GTPDE 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-216 |
3.42e-25 |
|
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: 99.39 E-value: 3.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 2 QTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTtiecILGTKNAD-----SGTVSILNCnpQKDRCRLF 76
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKST----LLSLITGDlpptyGNDVRLFGE--RRGGEDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 ---QKVGV---QFQEgDYQPEIKVSE--LCGETA--CLYEAPADW-----KSLCEQFGIGSKIGNAVKSLSGGERQRLFI 141
Cdd:COG1119 75 elrKRIGLvspALQL-RFPRDETVLDvvLSGFFDsiGLYREPTDEqreraRELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1045868222 142 VLALIPNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEV--EIlcDEICILKQGKAVFYGTVEQ 216
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIppGI--THVLLLKDGRVVAAGPKEE 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-215 |
4.56e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.41 E-value: 4.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI------LNcNPQKDRcR 74
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdgkpvrIR-SPRDAI-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 75 LfqKVGVQFQ------------------EGDYQPEIKVSELCGETaclyeapadwKSLCEQFGI----GSKIGNavksLS 132
Cdd:COG3845 80 L--GIGMVHQhfmlvpnltvaenivlglEPTKGGRLDRKAARARI----------RELSERYGLdvdpDAKVED----LS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 133 GGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVfyG 212
Cdd:COG3845 144 VGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV--G 221
|
...
gi 1045868222 213 TVE 215
Cdd:COG3845 222 TVD 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-216 |
7.15e-25 |
|
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: 98.02 E-value: 7.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECI-----LGTKNADSGTVSILN---CNPQKDRCRLF 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGkdiYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 QKVGVQFQE------------------GDYQPEIKVSELCGEtaCLYEApADWKSLCEQFGIGSkignavksLSGGERQR 138
Cdd:cd03260 81 RRVGMVFQKpnpfpgsiydnvayglrlHGIKLKEELDERVEE--ALRKA-ALWDEVKDRLHALG--------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1045868222 139 LFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQgGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-222 |
8.94e-25 |
|
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: 102.22 E-value: 8.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDNL--LAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQK-DRCRLFQKVG 80
Cdd:COG2274 473 DIELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQFQEGD------------YQPEIKVSEL--CGETACLYEA----PAdwkslceqfGIGSKIGNAVKSLSGGERQRLFIV 142
Cdd:COG2274 553 VVLQDVFlfsgtirenitlGDPDATDEEIieAARLAGLHDFiealPM---------GYDTVVGEGGSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 143 LALIPNPELVFLDELTTGLDAKARRDVWKILQELKQgGLTIFITSHFMDEVEiLCDEICILKQGKAVFYGTVEQAKAVSG 222
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLARKG 701
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-219 |
1.31e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.77 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 3 TAIKVEQLSKAY-DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVsILNCNP----QKDRCRLFQ 77
Cdd:PRK13636 4 YILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPidysRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 78 KVGVQFQEGDYQP-EIKVSELCGETACLYEAPADW-----KSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPEL 151
Cdd:PRK13636 83 SVGMVFQDPDNQLfSASVYQDVSFGAVNLKLPEDEvrkrvDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 152 VFLDELTTGLDAKARRDVWKILQELKQG-GLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQAKA 219
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-207 |
1.96e-24 |
|
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: 96.32 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAY-DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCR----LFQKV 79
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 GVQFQEGDYQPEIKVSE-LCGETACLYEAPADW----KSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFL 154
Cdd:cd03292 81 GVVFQDFRLLPDRNVYEnVAFALEVTGVPPREIrkrvPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 155 DELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-216 |
3.68e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 98.23 E-value: 3.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYD----NLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNCNPQKDRCRLF 76
Cdd:COG1135 2 IELENLSKTFPtkggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVdgvdLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 QKVGVQFQ--------------------EGDYQPEI--KVSELcgetaclyeapadwksLcEQFGIGSKIGNAVKSLSGG 134
Cdd:COG1135 82 RKIGMIFQhfnllssrtvaenvalpleiAGVPKAEIrkRVAEL----------------L-ELVGLSDKADAYPSQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 135 ERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGT 213
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGP 224
|
...
gi 1045868222 214 VEQ 216
Cdd:COG1135 225 VLD 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-213 |
6.07e-24 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 100.09 E-value: 6.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQKVGVQFQEGDYQPEIKVSELC 98
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 99 GETACLY-----EAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKIL 173
Cdd:TIGR01257 1025 LFYAQLKgrsweEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1045868222 174 QELKQgGLTIFITSHFMDEVEILCDEICILKQGKAVFYGT 213
Cdd:TIGR01257 1105 LKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-225 |
8.36e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.66 E-value: 8.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYD-----NLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLF--- 76
Cdd:PRK13637 3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 QKVGVQFQEGDYQpeikvseLCGETacLYEAPAdwkslceqFG---IG---SKIGNAVKS-------------------L 131
Cdd:PRK13637 83 KKVGLVFQYPEYQ-------LFEET--IEKDIA--------FGpinLGlseEEIENRVKRamnivgldyedykdkspfeL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 132 SGGERQRLFI--VLALipNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKA 208
Cdd:PRK13637 146 SGGQKRRVAIagVVAM--EPKILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
250
....*....|....*...
gi 1045868222 209 VFYGTVEQA-KAVSGCEK 225
Cdd:PRK13637 224 ELQGTPREVfKEVETLES 241
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
11-209 |
8.88e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.83 E-value: 8.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 11 SKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSIlNCNPQK---DRCRLFQKVGVQFQEGD 87
Cdd:PRK11288 11 GKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILI-DGQEMRfasTTAALAAGVAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 88 YQPEIKVSE------------LCGETACLYEAPADWKSLCEQFGIGSKignaVKSLSGGERQRLFIVLALIPNPELVFLD 155
Cdd:PRK11288 90 LVPEMTVAEnlylgqlphkggIVNRRLLNYEAREQLEHLGVDIDPDTP----LKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1045868222 156 ELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAV 209
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYV 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-209 |
1.68e-23 |
|
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: 93.86 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 7 VEQLSKAY-DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSIlnCNPQKDRCRLFQKVGVQFQE 85
Cdd:cd03226 2 IENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILL--NGKPIKAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 86 GDYQpeikvseLCGETA---CLYEAPADWKSLCEQFGIGSKIG-NAVK-----SLSGGERQRLFIVLALIPNPELVFLDE 156
Cdd:cd03226 80 VDYQ-------LFTDSVreeLLLGLKELDAGNEQAETVLKDLDlYALKerhplSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1045868222 157 LTTGLDAKARRDVWKILQELKQGGLTIFITSH---FMDEVeilCDEICILKQGKAV 209
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHdyeFLAKV---CDRVLLLANGAIV 205
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-231 |
2.45e-23 |
|
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: 93.89 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 6 KVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV-----SILNCNPQKdRCRLfqkvG 80
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIrfdgeDITGLPPHR-IARL----G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQfqegdYQPEIK-------VSE--LCGETACLYEAPADWkSLCEQFGI----GSKIGNAVKSLSGGERQRLFIVLALIP 147
Cdd:COG0410 80 IG-----YVPEGRrifpsltVEEnlLLGAYARRDRAEVRA-DLERVYELfprlKERRRQRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 148 NPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTveqAKAVSGCEKFE 227
Cdd:COG0410 154 RPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGT---AAELLADPEVR 230
|
....
gi 1045868222 228 DAYL 231
Cdd:COG0410 231 EAYL 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-219 |
2.74e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 93.99 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAY-----------DNLL-----------AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADS 58
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkELLLrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 59 GTVSIlncnpqkdRCR---LFQkVGVQFQegdyqpeikvSELCG----------------ETACLYEApadwkslCEQF- 118
Cdd:COG1134 81 GRVEV--------NGRvsaLLE-LGAGFH----------PELTGreniylngrllglsrkEIDEKFDE-------IVEFa 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 119 GIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDE-LTTGlDA----KARRdvwkILQELKQGGLTIFITSHFMDEV 193
Cdd:COG1134 135 ELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEvLAVG-DAafqkKCLA----RIRELRESGRTVIFVSHSMGAV 209
|
250 260
....*....|....*....|....*.
gi 1045868222 194 EILCDEICILKQGKAVFYGTVEQAKA 219
Cdd:COG1134 210 RRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-222 |
3.56e-23 |
|
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: 97.52 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDN-LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNCNPQKDRCRLFQK 78
Cdd:COG4988 336 SIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIngvdLSDLDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 79 VGvqfQE------------GDYQPEIKVSELCG--ETACLYEapadwksLCEQF--GIGSKIGNAVKSLSGGERQRLFIV 142
Cdd:COG4988 416 VP---QNpylfagtirenlRLGRPDASDEELEAalEAAGLDE-------FVAALpdGLDTPLGEGGRGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 143 LALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITsHFMDEVEiLCDEICILKQGKAVFYGTVEQAKAVSG 222
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRLALLA-QADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-231 |
4.23e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 97.50 E-value: 4.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 3 TAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTvsilncnpqkdrCRLF-QKVGv 81
Cdd:NF033858 265 PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE------------AWLFgQPVD- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 82 qfqEGDYQPEIKV----------SELcgeT--------ACLYEAPADW-----KSLCEQFGIGSKIGNAVKSLSGGERQR 138
Cdd:NF033858 332 ---AGDIATRRRVgymsqafslyGEL---TvrqnlelhARLFHLPAAEiaarvAEMLERFDLADVADALPDSLPLGIRQR 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 139 LFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEiLCDEICILKQGKAVFYGTVEQA 217
Cdd:NF033858 406 LSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELsREDGVTIFISTHFMNEAE-RCDRISLMHAGRVLASDTPAAL 484
|
250
....*....|....*..
gi 1045868222 218 KAVSGCEKFEDA---YL 231
Cdd:NF033858 485 VAARGAATLEEAfiaYL 501
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-216 |
7.61e-23 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 94.78 E-value: 7.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV-----SILNCNPQKDRcrl 75
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIlldgrDVTGLPPEKRN--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 76 fqkVGVQFQegDY----------------------QPEI--KVSElcgetaclyeapadwksLCEQFGIGSKIGNAVKSL 131
Cdd:COG3842 79 ---VGMVFQ--DYalfphltvaenvafglrmrgvpKAEIraRVAE-----------------LLELVGLEGLADRYPHQL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 132 SGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVW----KILQELkqgGLT-IFITsHFMDEVEILCDEICILKQG 206
Cdd:COG3842 137 SGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMReelrRLQREL---GITfIYVT-HDQEEALALADRIAVMNDG 212
|
250
....*....|
gi 1045868222 207 KavfygtVEQ 216
Cdd:COG3842 213 R------IEQ 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-193 |
1.52e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.76 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 13 AYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSilncnpQKDRCRLfqKVGVQFQEGDYQPEI 92
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------RAGGARV--AYVPQRSEVPDSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 93 KVSELCgeTACLYEAPADWKSL-----------CEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGL 161
Cdd:NF040873 73 TVRDLV--AMGRWARRGLWRRLtrddraavddaLERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|..
gi 1045868222 162 DAKARRDVWKILQELKQGGLTIFITSHFMDEV 193
Cdd:NF040873 151 DAESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-207 |
1.66e-22 |
|
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: 91.55 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNCNPQKDRcrlfqKVG 80
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIggrdVTDLPPKDR-----DIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQFQEGDYQPEIKVSELCGETACLYEAPADW-----KSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLD 155
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKLRKVPKDEidervREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1045868222 156 ELTTGLDAKARRdvwKILQELK-----QGGLTIFITsHFMDEVEILCDEICILKQGK 207
Cdd:cd03301 156 EPLSNLDAKLRV---QMRAELKrlqqrLGTTTIYVT-HDQVEAMTMADRIAVMNDGQ 208
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-213 |
1.90e-22 |
|
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: 91.53 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV-----SILNCNPQKdrcrlfQKV 79
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlldgkDITNLPPHK------RPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 GVQFQEGDYQPEIKVSE-------LCGETACLYEAPADWksLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELV 152
Cdd:cd03300 75 NTVFQNYALFPHLTVFEniafglrLKKLPKAEIKERVAE--ALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 153 FLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGT 213
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-222 |
9.35e-22 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 93.29 E-value: 9.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 2 QTAIKVEQLSKAYDN--LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQK-DRCRLFQK 78
Cdd:COG4987 331 GPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 79 VGVQFQE--------------GDyqPEIKVSELCG--ETACLyeapADW-KSLCEqfGIGSKIGNAVKSLSGGERQRLFI 141
Cdd:COG4987 411 IAVVPQRphlfdttlrenlrlAR--PDATDEELWAalERVGL----GDWlAALPD--GLDTWLGEGGRRLSGGERRRLAL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 142 VLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITsHFMDEVEiLCDEICILKQGKAVFYGTVEQAKAVS 221
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLIT-HRLAGLE-RMDRILVLEDGRIVEQGTHEELLAQN 560
|
.
gi 1045868222 222 G 222
Cdd:COG4987 561 G 561
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-216 |
1.24e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.07 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 3 TAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSiLNCNPQK---DRcRLFQKV 79
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVF-LGDKPISmlsSR-QLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 GVQFQEgDYQPE-IKVSELCGetaclY-EAPadWKSL---------------CEQFGIGSKIGNAVKSLSGGERQRLFIV 142
Cdd:PRK11231 79 ALLPQH-HLTPEgITVRELVA-----YgRSP--WLSLwgrlsaednarvnqaMEQTRINHLADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1045868222 143 LALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-215 |
1.42e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 91.40 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYD----NLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN----PQKDRCRLF 76
Cdd:PRK11153 2 IELKNISKVFPqggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltalSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 QKVGVQFQ--------------------EGDYQPEIK--VSELCgetaclyeapadwkslcEQFGIGSKIGNAVKSLSGG 134
Cdd:PRK11153 82 RQIGMIFQhfnllssrtvfdnvalplelAGTPKAEIKarVTELL-----------------ELVGLSDKADRYPAQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 135 ERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGT 213
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
..
gi 1045868222 214 VE 215
Cdd:PRK11153 225 VS 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-207 |
1.45e-21 |
|
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: 87.87 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 3 TAIKVEQLSKAydnlLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQKVGVQ 82
Cdd:cd03215 3 PVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 83 FqegdyqpeikvselcgetaclyeAPADWKS--LCEQFGIGSKIGNAVkSLSGGERQRLFIVLALIPNPELVFLDELTTG 160
Cdd:cd03215 79 Y-----------------------VPEDRKRegLVLDLSVAENIALSS-LLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1045868222 161 LDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:cd03215 135 VDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-216 |
1.67e-21 |
|
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: 90.88 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYD----NLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILG---TKNADSGTVSILNCN----PQKDRC 73
Cdd:COG0444 2 LEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDllklSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 74 RL--------FQ----------KVGVQFQEGdyqpeIKVSELCGETaclyEAPADWKSLCEQFGIGSKiGNAVKS----L 131
Cdd:COG0444 82 KIrgreiqmiFQdpmtslnpvmTVGDQIAEP-----LRIHGGLSKA----EARERAIELLERVGLPDP-ERRLDRypheL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 132 SGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQG-GLT-IFITsHFMDEVEILCDEICILKQGKAV 209
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAiLFIT-HDLGVVAEIADRVAVMYAGRIV 230
|
....*..
gi 1045868222 210 FYGTVEQ 216
Cdd:COG0444 231 EEGPVEE 237
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-216 |
2.41e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 90.08 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 18 LAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNC-----NPQKDRCRLFQKVGVQFQegdyQPEi 92
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitagKKNKKLKPLRKKVGIVFQ----FPE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 93 kvSELCGETA----CL---------YEAPADWKSLCEQFGIGSKIgnAVKS---LSGGERQRLFI--VLALipNPELVFL 154
Cdd:PRK13634 96 --HQLFEETVekdiCFgpmnfgvseEDAKQKAREMIELVGLPEEL--LARSpfeLSGGQMRRVAIagVLAM--EPEVLVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 155 DELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPRE 232
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-216 |
3.08e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.99 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN----PQKDrcrLFQKVG 80
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDvattPSRE---LAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQFQEGDYQPEIKVSELCG----------ETAclyeapADWK----SLcEQFGIGSKIGNAVKSLSGGERQRLFIVLALI 146
Cdd:COG4604 79 ILRQENHINSRLTVRELVAfgrfpyskgrLTA------EDREiideAI-AYLDLEDLADRYLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1045868222 147 PNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHfmdevEI-----LCDEICILKQGKAVFYGTVEQ 216
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLH-----DInfascYADHIVAMKDGRVVAQGTPEE 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-211 |
3.42e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.66 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 7 VEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI--------LNCNPQ--------- 69
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpkglrigyLPQEPPldddltvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 70 ------KDRCRL---FQKVGVQFQEGDYQPEiKVSELCGETACL--YEAPADWKSLCEQFGIGSKIGNA-VKSLSGGERQ 137
Cdd:COG0488 81 tvldgdAELRALeaeLEELEAKLAEPDEDLE-RLAELQEEFEALggWEAEARAEEILSGLGFPEEDLDRpVSELSGGWRR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1045868222 138 RLFIVLALIPNPELVFLDELTTGLDAKARRdvWkiLQE-LKQGGLTIFITSH---FMDEVeilCDEICILKQGKAVFY 211
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIE--W--LEEfLKNYPGTVLVVSHdryFLDRV---ATRILELDRGKLTLY 230
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-200 |
4.41e-21 |
|
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: 91.19 E-value: 4.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAY-DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNCNPQKDRCR---- 74
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpLADADADSWRDqiaw 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 75 ------LFQKV---GVQFQEGDYQPE--IKVSELCGETACLYEAPAdwkslceqfGIGSKIGNAVKSLSGGERQRLFIVL 143
Cdd:TIGR02857 401 vpqhpfLFAGTiaeNIRLARPDASDAeiREALERAGLDEFVAALPQ---------GLDTPIGEGGAGLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1045868222 144 ALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITsHfMDEVEILCDEI 200
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVT-H-RLALAALADRI 526
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-222 |
5.92e-21 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 89.79 E-value: 5.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 2 QTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAG--KSTTIECILGtknADSGTvsilncNPQKDRCRLFQKV 79
Cdd:NF000106 11 RNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGR------RPWRF*TWCANRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 GVQFQEGDYQP-EIKVSELCGETACLY-----------EAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIP 147
Cdd:NF000106 82 ALRRTIG*HRPvR*GRRESFSGRENLYmigr*ldlsrkDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1045868222 148 NPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQAKAVSG 222
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-215 |
8.20e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 8.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVsilncnpqkdrcrlfqKVG--VQ 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----------------KLGetVK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 83 F----QEGDY-QPEIKVSE-LCGETACLYEAPAdwKSLCEQFGI-GSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLD 155
Cdd:COG0488 380 IgyfdQHQEElDPDKTVLDeLRDGAPGGTEQEV--RGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1045868222 156 ELTTGLDAKARRdvwkILQELKQG--GlTIFITSH---FMDEVeilCDEICILKQGKAVFY-GTVE 215
Cdd:COG0488 458 EPTNHLDIETLE----ALEEALDDfpG-TVLLVSHdryFLDRV---ATRILEFEDGGVREYpGGYD 515
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-213 |
1.20e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 87.91 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNC---NPQKDRC--RLFQKVGVQFQegdyQPEIK 93
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDItitHKTKDKYirPVRKRIGMVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 94 VSELCGETACLY----------EAPADWKSLCEQFGIGSKIGNAVK-SLSGGERQRLFIVLALIPNPELVFLDELTTGLD 162
Cdd:PRK13646 98 LFEDTVEREIIFgpknfkmnldEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 163 AKARRDVWKILQELK-QGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGT 213
Cdd:PRK13646 178 PQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTS 229
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-209 |
1.38e-20 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 89.79 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 10 LSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVsilncnpqkdrcrLFQKVGVQFQEGDYQ 89
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI-------------LFQGKEIDFKSSKEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 90 PEIKVSELCGETACLYEAPA-----------------------DWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALI 146
Cdd:PRK10982 71 LENGISMVHQELNLVLQRSVmdnmwlgryptkgmfvdqdkmyrDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 147 PNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAV 209
Cdd:PRK10982 151 YNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-216 |
3.21e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.61 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGT---VSILNCNPQKDRcRLFQ 77
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQREG-RLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 78 KV-------GVQFQEGDYQPEIKVSE--LCGETAC--LYEAPADWKSLCEQ---FGIGSKIGNA------VKSLSGGERQ 137
Cdd:PRK09984 80 DIrksrantGYIFQQFNLVNRLSVLEnvLIGALGStpFWRTCFSWFTREQKqraLQALTRVGMVhfahqrVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 138 RLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQG-GLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
19-191 |
3.33e-20 |
|
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: 84.78 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVsILNCNP----QKDRCRLFQKVGVQFQEGDYQ---PE 91
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAV-LIDGEPldysRKGLLERRQRVGLVFQDPDDQlfaAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 92 I--KVS----ELCGETAclyEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKA 165
Cdd:TIGR01166 86 VdqDVAfgplNLGLSEA---EVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180
....*....|....*....|....*.
gi 1045868222 166 RRDVWKILQELKQGGLTIFITSHFMD 191
Cdd:TIGR01166 163 REQMLAILRRLRAEGMTVVISTHDVD 188
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-216 |
3.77e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 86.28 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAY-DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVsILNCNP----QKDRCRLFQKV 79
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEV-LIKGEPikydKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 GVQFQEGDYQ---PEIKVSELCGetaclyeaPADWKSLCEQfgIGSKIGNAVKS-------------LSGGERQRLFIVL 143
Cdd:PRK13639 81 GIVFQNPDDQlfaPTVEEDVAFG--------PLNLGLSKEE--VEKRVKEALKAvgmegfenkpphhLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 144 ALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKE 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-207 |
4.11e-20 |
|
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: 83.27 E-value: 4.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSIlncnpqkdrcrlfqkvgvqfq 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 85 egdyQPEIKVSELcgetaclyeapadwkslcEQfgigskignavksLSGGERQRLFIVLALIPNPELVFLDELTTGLDAK 164
Cdd:cd03221 60 ----GSTVKIGYF------------------EQ-------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1045868222 165 ARRDVWKILQELKQgglTIFITSH---FMDEVeilCDEICILKQGK 207
Cdd:cd03221 105 SIEALEEALKEYPG---TVILVSHdryFLDQV---ATKIIELEDGK 144
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-195 |
6.11e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 85.07 E-value: 6.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILN------CNPQ-KDRCRLF 76
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSdKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 QKVGVQFQEGDYQPEIKVSELCGETACLY------EAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPE 150
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEAPCRVlglskdQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1045868222 151 LVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHfmdEVEI 195
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTH---EVEV 203
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
34-216 |
8.85e-20 |
|
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: 86.69 E-value: 8.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 34 GLLGANGAGKSTTIECILGTKNADSGTVSI----LncnpQKDRCRLFQK-----VGVQFQEGDYQPEIKVSE-Lcgetac 103
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevL----QDSARGIFLPphrrrIGYVFQEARLFPHLSVRGnL------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 104 LY--------EAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQE 175
Cdd:COG4148 99 LYgrkrapraERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLER 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1045868222 176 L-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:COG4148 179 LrDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAE 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-216 |
9.39e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.55 E-value: 9.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNL-----LAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKD-------- 71
Cdd:TIGR03269 280 IKVRNVSKRYISVdrgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDmtkpgpdg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 72 RCRLFQKVGVQFQEGDYQPEIKVSELCGETACLyEAP---ADWKSLCEQFGIGSKIGNAVK-------SLSGGERQRLFI 141
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGL-ELPdelARMKAVITLKMVGFDEEKAEEildkypdELSEGERHRVAL 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1045868222 142 VLALIPNPELVFLDELTTGLDAKARRDVWK-ILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-217 |
1.87e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 86.64 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 28 KCGTVYGLLGANGAGKSTTIECILG--TKNADSGTVSILNCNPQKDRCrlFQKVGVQFQegdyQPEIKVSELCGETACLY 105
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALAFrsPKGVKGSGSVLLNGMPIDAKE--MRAISAYVQ----QDDLFIPTLTVREHLMF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 106 EA----PADW---------KSLCEQFGIGS----KIG--NAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKAR 166
Cdd:TIGR00955 123 QAhlrmPRRVtkkekrervDEVLQALGLRKcantRIGvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 167 RDVWKILQELKQGGLTIFITSHF-MDEVEILCDEICILKQGKAVFYGTVEQA 217
Cdd:TIGR00955 203 YSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-190 |
1.96e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.99 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGT--VSILNCN-PQKDRCRLFQKVGV 81
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDliVDGLKVNdPKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 82 QFQEGDYQPEIKVSE--LCGET----ACLYEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLD 155
Cdd:PRK09493 82 VFQQFYLFPHLTALEnvMFGPLrvrgASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1045868222 156 ELTTGLDAKARRDVWKILQELKQGGLTIFITSHFM 190
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEI 196
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-215 |
1.99e-19 |
|
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: 83.29 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDN----LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILN---CNPQKDRCRLFQ 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 78 K--------------VGVQFQEGDYQpeikvselcgetaclyEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVL 143
Cdd:cd03293 81 QdallpwltvldnvaLGLELQGVPKA----------------EARERAEELLELVGLSGFENAYPHQLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1045868222 144 ALIPNPELVFLDELTTGLDA----KARRDVWKILQELKQGglTIFITsHFMDEVEILCDEICILKQGKAVFYGTVE 215
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRETGKT--VLLVT-HDIDEAVFLADRVVVLSARPGRIVAEVE 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-213 |
2.44e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.40 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI-----LNCNPQKDRCRLFQKVGVQFQegdyQPEik 93
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvSSTSKQKEIKPVRKKVGVVFQ----FPE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 94 vSELCGETAClyeapADWKSLCEQFGIGSKIGNAVKS-------------------LSGGERQRLFIVLALIPNPELVFL 154
Cdd:PRK13643 95 -SQLFEETVL-----KDVAFGPQNFGIPKEKAEKIAAeklemvgladefwekspfeLSGGQMRRVAIAGILAMEPEVLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 155 DELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGT 213
Cdd:PRK13643 169 DEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-216 |
3.58e-19 |
|
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: 83.16 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN----PQKDRcrlfqKV 79
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDatdvPVQER-----NV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 GVQFQEGDYQPEIKVSELCGetACLYEAPAdwKSLCEQFGIGSKIGNAVK-------------SLSGGERQRLFIVLALI 146
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVA--FGLRVKPR--SERPPEAEIRAKVHELLKlvqldwladrypaQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 147 PNPELVFLDELTTGLDAKARRDVWKILQEL--KQGGLTIFITsHFMDEVEILCDEICILKQGKavfygtVEQ 216
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLhdELHVTTVFVT-HDQEEALEVADRVVVMNKGR------IEQ 217
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
3.88e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 83.63 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAY-DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCR-LFQK 78
Cdd:PRK13647 1 MDNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 79 VGVQFQEGDYQpeikvselcgetacLYEAPAdWKSLCeqFG----------IGSKIGNAVKS-------------LSGGE 135
Cdd:PRK13647 81 VGLVFQDPDDQ--------------VFSSTV-WDDVA--FGpvnmgldkdeVERRVEEALKAvrmwdfrdkppyhLSYGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 136 RQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVE 215
Cdd:PRK13647 144 KKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-213 |
4.16e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.60 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDN------LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI--LNCNPQKDR 72
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdgLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 73 CRLFQKVGVQFQEGDYQpeiKVSELCGETACLyeAPADWKSLCEQfgIGSKIGNAVKS-------------LSGGERQRL 139
Cdd:PRK13633 81 WDIRNKAGMVFQNPDNQ---IVATIVEEDVAF--GPENLGIPPEE--IRERVDESLKKvgmyeyrrhaphlLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1045868222 140 FIVLALIPNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVeILCDEICILKQGKAVFYGT 213
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-225 |
4.42e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.54 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN-PQKDRCRLFQKVGVQFQEGD-YQPEIKVSELCGE 100
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPlVQYDHHYLHRQVALVGQEPVlFSGSVRENIAYGL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 101 TACLYE--APADWKSLCEQF------GIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRdvwkI 172
Cdd:TIGR00958 580 TDTPDEeiMAAAKAANAHDFimefpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ----L 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1045868222 173 LQELK-QGGLTIFITSHFMDEVEiLCDEICILKQGKAVFYGTVEQAKAVSGCEK 225
Cdd:TIGR00958 656 LQESRsRASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-216 |
8.45e-19 |
|
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: 81.96 E-value: 8.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAY-DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN-PQKDRCRLFQKVGVQ 82
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDiREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 83 FQEGDYQPEIKVSE-------LCGETACLYEAPADwkSLCEQFGIGSK--IGNAVKSLSGGERQRLFIVLALIPNPELVF 153
Cdd:cd03295 81 IQQIGLFPHMTVEEnialvpkLLKWPKEKIRERAD--ELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1045868222 154 LDELTTGLDAKAR----RDVWKILQELkqgGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:cd03295 159 MDEPFGALDPITRdqlqEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDE 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-216 |
1.05e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 83.58 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 3 TAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNCNPQKDRcrlfqK 78
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIggrdVTDLPPKDR-----N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 79 VGVQFQegDY----------------------QPEIKvsELCGETAclyeapadwkslcEQFGIGSKIGNAVKSLSGGER 136
Cdd:COG3839 77 IAMVFQ--SYalyphmtvyeniafplklrkvpKAEID--RRVREAA-------------ELLGLEDLLDRKPKQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 137 QRLFIVLALIPNPELVFLDELTTGLDAK----ARRDVWKILQELkqgGLTIFITSHfmDEVEI--LCDEICILKQGKAVF 210
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLDAKlrveMRAEIKRLHRRL---GTTTIYVTH--DQVEAmtLADRIAVMNDGRIQQ 214
|
....*.
gi 1045868222 211 YGTVEQ 216
Cdd:COG3839 215 VGTPEE 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-214 |
1.14e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNcnpqKDRCRLFQK------ 78
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN----INYNKLDHKlaaqlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 79 VGVQFQEGDYQPEIKVSE-----------LCGETAclyeapADWKSLCEQ-------FGIGSKIGNAVKSLSGGERQRLF 140
Cdd:PRK09700 82 IGIIYQELSVIDELTVLEnlyigrhltkkVCGVNI------IDWREMRVRaammllrVGLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1045868222 141 IVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTV 214
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMV 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-212 |
1.22e-18 |
|
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: 81.16 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIECILG---TKNADSGTVSILNCNPQKDrcrLFQK-VGVQFQEGDYQPEIKVSELC 98
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPD---QFQKcVAYVRQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 99 GETACL---------YEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDV 169
Cdd:cd03234 103 TYTAILrlprkssdaIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1045868222 170 WKILQELKQGGLTIFITSHF-MDEVEILCDEICILKQGKAVFYG 212
Cdd:cd03234 183 VSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-210 |
2.31e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 80.95 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 3 TAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNC--------NPQKDRCR 74
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItidtarslSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 75 -LFQKVGVQFQEGDYQPEIKVSELCGETACLY------EAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIP 147
Cdd:PRK11264 82 qLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVkgepkeEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 148 NPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFM-------DEVeILCDEICILKQG--KAVF 210
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMsfardvaDRA-IFMDQGRIVEQGpaKALF 232
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-200 |
3.02e-18 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 80.17 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYD-------NLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRC 73
Cdd:COG4778 1 MTTLLEVENLSKTFTlhlqggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 74 RL--FQKVGVQFQEGDYqpeikVS--------------------ELCGETAclyEAPADWKSLCEQFGIGSKI-GNAVKS 130
Cdd:COG4778 81 QAspREILALRRRTIGY-----VSqflrviprvsaldvvaepllERGVDRE---EARARARELLARLNLPERLwDLPPAT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 131 LSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGG---LTIFitsHFMDEVEILCDEI 200
Cdd:COG4778 153 FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGtaiIGIF---HDEEVREAVADRV 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-212 |
3.14e-18 |
|
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: 79.28 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYD--NLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQKVGVQ 82
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 83 FQEgdyqpeikvselcgetACLYEAPadwkslceqfgIGSKIGnavKSLSGGERQRLFIVLALIPNPELVFLDELTTGLD 162
Cdd:cd03247 81 NQR----------------PYLFDTT-----------LRNNLG---RRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 163 AKARRDVWKILQELKQGGLTIFITSHF--MDEVeilcDEICILKQGKAVFYG 212
Cdd:cd03247 131 PITERQLLSLIFEVLKDKTLIWITHHLtgIEHM----DKILFLENGKIIMQG 178
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-216 |
3.53e-18 |
|
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: 80.35 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDN-LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQK-DRCRLFQKVGVQ 82
Cdd:cd03254 3 IEFENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 83 FQE---------------GDYQPEIKVSELCGETACLYEApadwKSLCEqfGIGSKIGNAVKSLSGGERQRLFIVLALIP 147
Cdd:cd03254 83 LQDtflfsgtimenirlgRPNATDEEVIEAAKEAGAHDFI----MKLPN--GYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 148 NPELVFLDELTTGLDAKARRDVWKILQELKQGGlTIFITSHFMDEVEiLCDEICILKQGKAVFYGTVEQ 216
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGR-TSIIIAHRLSTIK-NADKILVLDDGKIIEEGTHDE 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-213 |
4.84e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.94 E-value: 4.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV-----SILNCNPQKDRCRLFQKVGVQFQegdyQPEik 93
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddtLITSTSKNKDIKQIRKKVGLVFQ----FPE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 94 vSELCGETAClyeapADWKSLCEQFGIGSKIGNAVK-------------------SLSGGERQRLFIVLALIPNPELVFL 154
Cdd:PRK13649 96 -SQLFEETVL-----KDVAFGPQNFGVSQEEAEALAreklalvgiseslfeknpfELSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 155 DELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGT 213
Cdd:PRK13649 170 DEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
20-209 |
6.25e-18 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 80.23 E-value: 6.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 20 VDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVS-----ILNCNPqKDRCRLFQKVGVQFQE--GDYQPEI 92
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdLYQLDR-KQRRAFRRDVQLVFQDspSAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 93 KVSELCGETACLY------EAPADWKSLCEQFGIGSKIGNAV-KSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKA 165
Cdd:TIGR02769 106 TVRQIIGEPLRHLtsldesEQKARIAELLDMVGLRSEDADKLpRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1045868222 166 RRDVWKILQELKQ-GGLTIFITSHFMDEVEILCDEICILKQGKAV 209
Cdd:TIGR02769 186 QAVILELLRKLQQaFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
8-216 |
6.64e-18 |
|
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: 80.00 E-value: 6.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 8 EQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQK-DRCRLFQ----KVGVQ 82
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKELRElrrkKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 83 FQEGDYQPEIKVS-------ELCGETACLYEAPADwKSLcEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLD 155
Cdd:cd03294 108 FQSFALLPHRTVLenvafglEVQGVPRAEREERAA-EAL-ELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 156 ELTTGLDAKARRDVWKILQEL--KQGGLTIFITsHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLqaELQKTIVFIT-HDLDEALRLGDRIAIMKDGRLVQVGTPEE 247
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-215 |
8.91e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.03 E-value: 8.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAY-DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV---SILNCNPQKDRcRLFQKVG 80
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsGIDTGDFSKLQ-GIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQFQEGDYQPEIKVSE----LCGETACLyeAPADWKSLCE----QFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELV 152
Cdd:PRK13644 81 IVFQNPETQFVGRTVEedlaFGPENLCL--PPIEIRKRVDralaEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 153 FLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEIlCDEICILKQGKAVFYGTVE 215
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPE 220
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-231 |
1.77e-17 |
|
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: 78.95 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 26 SVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTvsiLNCNPQKD------RCRLFQKVGVQFQEGDYQPEIKV----- 94
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK---FDDPPDWDeildefRGSELQNYFTKLLEGDVKVIVKPqyvdl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 95 --SELCGETACLYEAPAD---WKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDV 169
Cdd:cd03236 99 ipKAVKGKVGELLKKKDErgkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 170 WKILQELKQGGLTIFITSHFMDEVEILCDEICILkQGKAVFYGTVEQAKAV-SGCEKFEDAYL 231
Cdd:cd03236 179 ARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL-YGEPGAYGVVTLPKSVrEGINEFLDGYL 240
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-212 |
6.27e-17 |
|
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: 76.80 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNcnpqKDRCRLFqkVGVQFQEgdyqpeikvsELC 98
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----RVSSLLG--LGGGFNP----------ELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 99 GE-------------TACLYEAPADWKSLCEqfgIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKA 165
Cdd:cd03220 101 GReniylngrllglsRKEIDEKIDEIIEFSE---LGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1045868222 166 RRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYG 212
Cdd:cd03220 178 QEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-216 |
6.28e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 77.46 E-value: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILN------CNPQKDRCR--LF 76
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawSPWELARRRavLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 QKVGVQFQegdyqpeIKVSE--LCGETACLYEAPADwKSLCEQ----FGIGSKIGNAVKSLSGGERQR--LFIVLALIPN 148
Cdd:COG4559 82 QHSSLAFP-------FTVEEvvALGRAPHGSSAAQD-RQIVREalalVGLAHLAGRSYQTLSGGEQQRvqLARVLAQLWE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 149 PE-----LVFLDELTTGLDAKARRDVWKILQELKQGGLTIFI-------TSHFmdeveilCDEICILKQGKAVFYGTVEQ 216
Cdd:COG4559 154 PVdggprWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAvlhdlnlAAQY-------ADRILLLHQGRLVAQGTPEE 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-208 |
7.42e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 77.05 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAY----DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNcnpqKDRCRLF 76
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 QKVGVQFQEgdyqpeikvselcgetACLYEapadWKSLCEQFGIGSKIGNAVKS-------------------------L 131
Cdd:COG1116 80 PDRGVVFQE----------------PALLP----WLTVLDNVALGLELRGVPKAerrerarellelvglagfedayphqL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 132 SGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTI-FITsHFMDEVEILCDEICILKQGKA 208
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVlFVT-HDVDEAVFLADRVVVLSARPG 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-222 |
7.54e-17 |
|
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: 76.76 E-value: 7.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 15 DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN-PQKDRCRLFQKVGVQFQE-------- 85
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlALADPAWLRRQVGVVLQEnvlfnrsi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 86 ------GDYQPE----IKVSELCGETACLYEAPADWKSLCEQFGIGskignavksLSGGERQRLFIVLALIPNPELVFLD 155
Cdd:cd03252 93 rdnialADPGMSmervIEAAKLAGAHDFISELPEGYDTIVGEQGAG---------LSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1045868222 156 ELTTGLDAKARRDVWKILQELKQgGLTIFITSHFMDEVEiLCDEICILKQGKAVFYGTVEQAKAVSG 222
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVK-NADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-216 |
8.74e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.84 E-value: 8.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILG--TKNADSGTVSILNCN-----PQKDRCRL-FQKVGVQFQE--GDY 88
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllAANGRIGGSATFNGReilnlPEKELNKLrAEQISMIFQDpmTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 89 QPEIKVSELCGETACLYEApadwKSLCEQFGIGSKIGNAVK-------------SLSGGERQRLFIVLALIPNPELVFLD 155
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLHKG----MSKAEAFEESVRMLDAVKmpearkrmkmyphEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 156 ELTTGLDAKARRDVWKILQELKQGGLT--IFITsHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTaiIMIT-HDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-222 |
1.36e-16 |
|
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: 76.04 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 24 NLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI-------LNCnpqkdrCRLFQKVGVQFQE----------- 85
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdgvdirdLNL------RWLRSQIGLVSQEpvlfdgtiaen 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 86 ---GDyqPEIKVSELcgETACLyeapadwKSLCEQF------GIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDE 156
Cdd:cd03249 97 iryGK--PDATDEEV--EEAAK-------KANIHDFimslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1045868222 157 LTTGLDAKARRDVWKILQELKQGGLTIFItSHFMDEVEiLCDEICILKQGKAVFYGTVEQAKAVSG 222
Cdd:cd03249 166 ATSALDAESEKLVQEALDRAMKGRTTIVI-AHRLSTIR-NADLIAVLQNGQVVEQGTHDELMAQKG 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-238 |
1.65e-16 |
|
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: 77.92 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKN--ADSG----------------------- 59
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGriiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 60 ------------TVSILNCNpQKDRCRLFQKVGVQFQE-----GDYQPEIKVSELCGETAclYEAPADWK---SLCEQFG 119
Cdd:TIGR03269 81 pcpvcggtlepeEVDFWNLS-DKLRRRIRKRIAIMLQRtfalyGDDTVLDNVLEALEEIG--YEGKEAVGravDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 120 IGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCD 198
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLSD 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1045868222 199 EICILKQGKAVFYGTVEQ--AKAVSGCEKFEDAYLMLSGEEV 238
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEvvAVFMEGVSEVEKECEVEVGEPI 279
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-207 |
2.14e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.38 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDN--LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN----PQKDRCRLFQ 77
Cdd:PRK13640 5 IVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDgitlTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 78 KVGVQFQEGDYQpeiKVSELCGETACL---------YEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPN 148
Cdd:PRK13640 85 KVGIVFQNPDNQ---FVGATVGDDVAFglenravprPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 149 PELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEiLCDEICILKQGK 207
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEAN-MADQVLVLDDGK 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-216 |
4.90e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.22 E-value: 4.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYD-NLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQK-VGVQ 82
Cdd:PRK13652 4 IETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKfVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 83 FQEGDYQ---PEIKVSELCGETAC-LYEAPADWK--SLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDE 156
Cdd:PRK13652 84 FQNPDDQifsPTVEQDIAFGPINLgLDEETVAHRvsSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1045868222 157 LTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEE 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-213 |
5.03e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 75.66 E-value: 5.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDN-----LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI---------------L 64
Cdd:PRK13631 22 LRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnheliT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 65 NCNPQK--DRCRLFQKVGVQFQEGDYQ---PEIKVSELCGETAC---LYEAPADWKSLCEQFGIGSK-IGNAVKSLSGGE 135
Cdd:PRK13631 102 NPYSKKikNFKELRRRVSMVFQFPEYQlfkDTIEKDIMFGPVALgvkKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQ 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1045868222 136 RQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGT 213
Cdd:PRK13631 182 KRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-216 |
5.69e-16 |
|
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: 74.19 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 15 DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI---------LNCnpqkdrcrLFQKVGVQFQE 85
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdvrdytLAS--------LRRQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 86 -----------------GDYQPEIkvsELCGETACLYEapadwksLCEQF--GIGSKIG-NAVKsLSGGERQRLFIVLAL 145
Cdd:cd03251 85 vflfndtvaeniaygrpGATREEV---EEAARAANAHE-------FIMELpeGYDTVIGeRGVK-LSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1045868222 146 IPNPELVFLDELTTGLDAKARRDVWKILQELKQgGLTIFITSHFMDEVEiLCDEICILKQGKAVFYGTVEQ 216
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIE-NADRIVVLEDGKIVERGTHEE 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-208 |
6.60e-16 |
|
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: 72.63 E-value: 6.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNL--LAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNcnpQKDRCRLFQK 78
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadIS---QWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 79 VGVQFQEgdyqpeikvSELcgetaclyeapadwkslceqFGiGSKIGNAvksLSGGERQRLFIVLALIPNPELVFLDELT 158
Cdd:cd03246 78 VGYLPQD---------DEL--------------------FS-GSIAENI---LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1045868222 159 TGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEiLCDEICILKQGKA 208
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-207 |
8.17e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 8.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDrcrlfqKVGVQFQEG-DYQPEIK-------- 93
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAL------STAQRLARGlVYLPEDRqssglyld 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 94 ------VSELCGETACLYEAPADWKSLCEQF--GIGSKIGNA---VKSLSGGERQRLFIVLALIPNPELVFLDELTTGLD 162
Cdd:PRK15439 356 aplawnVCALTHNRRGFWIKPARENAVLERYrrALNIKFNHAeqaARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1045868222 163 AKARRDVWKILQEL-KQGGLTIFITSHFmDEVEILCDEICILKQGK 207
Cdd:PRK15439 436 VSARNDIYQLIRSIaAQNVAVLFISSDL-EEIEQMADRVLVMHQGE 480
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-231 |
9.02e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 73.64 E-value: 9.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAvdKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN----PQKDRcrlfqKVG 80
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDltalPPAER-----PVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQFQEGD-------YQ-------PEIKVSElcGETACLYEApadwkslCEQFGIGSKIGNAVKSLSGGERQRLFIVLALI 146
Cdd:COG3840 75 MLFQENNlfphltvAQniglglrPGLKLTA--EQRAQVEQA-------LERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 147 PNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQAKAVSGCEK 225
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPA 225
|
....*.
gi 1045868222 226 FeDAYL 231
Cdd:COG3840 226 L-AAYL 230
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-209 |
1.00e-15 |
|
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: 73.39 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDN--LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN-PQKDRCRLFQKVG 80
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDiRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQFQE------------------GDYQPEIKVSELCGETACLYEAPAdwkslceqfGIGSKIGNAVKSLSGGERQRLFIV 142
Cdd:cd03245 82 YVPQDvtlfygtlrdnitlgaplADDERILRAAELAGVTDFVNKHPN---------GLDLQIGERGRGLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 143 LALIPNPELVFLDELTTGLDAKARRdvwKILQELKQ--GGLTIFITSHFMDEVEiLCDEICILKQGKAV 209
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEE---RLKERLRQllGDKTLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-222 |
1.01e-15 |
|
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: 75.91 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAY--DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVsILNCNPQKD---RC--RLFQ 77
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI-LLDGHDLADytlASlrRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 78 KVG-------------VQFQEGDYQPEIKVSELCgetaclyeAPADWKSLCEQF--GIGSKIG-NAVKsLSGGERQRLFI 141
Cdd:TIGR02203 410 LVSqdvvlfndtiannIAYGRTEQADRAEIERAL--------AAAYAQDFVDKLplGLDTPIGeNGVL-LSGGQRQRLAI 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 142 VLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFItSHFMDEVEiLCDEICILKQGKAVFYGTVEQAKAVS 221
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVI-AHRLSTIE-KADRIVVMDDGRIVERGTHNELLARN 558
|
.
gi 1045868222 222 G 222
Cdd:TIGR02203 559 G 559
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-209 |
1.19e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.51 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 2 QTAIKVEQLSKAYDN----LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNAD-----SGTV-----SILNCN 67
Cdd:PRK15134 3 QPLLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIrfhgeSLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 68 PQKDRCRLFQKVGVQFQEgdyqPEIKVSELCGETACLYE------------APADWKSLCEQFGI---GSKIGNAVKSLS 132
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQE----PMVSLNPLHTLEKQLYEvlslhrgmrreaARGEILNCLDRVGIrqaAKRLTDYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 133 GGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQG---GLtIFITsHFMDEVEILCDEICILKQGKAV 209
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElnmGL-LFIT-HNLSIVRKLADRVAVMQNGRCV 236
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
23-218 |
1.27e-15 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 73.45 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIECILGTKN--ADSGTVS-----ILNCNPQkDRCRL-----FQK----VGVQFQE- 85
Cdd:TIGR01978 19 VNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyeVTSGTILfkgqdLLELEPD-ERARAglflaFQYpeeiPGVSNLEf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 86 ----------GDYQPEIKVSE---LCGETACLYEAPADW--KSLCEQFgigskignavkslSGGERQRLFIVLALIPNPE 150
Cdd:TIGR01978 98 lrsalnarrsARGEEPLDLLDfekLLKEKLALLDMDEEFlnRSVNEGF-------------SGGEKKRNEILQMALLEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 151 LVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVE-ILCDEICILKQGKAVFYGTVEQAK 218
Cdd:TIGR01978 165 LAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNyIKPDYVHVLLDGRIVKSGDVELAK 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-216 |
1.55e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.09 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI-----LNCNPQKDrcrlfQKV 79
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIggnpcARLTPAKA-----HQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 GVQF--QEGDYQPEIKVSE-LCGETACLYEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDE 156
Cdd:PRK15439 87 GIYLvpQEPLLFPNLSVKEnILFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 157 LTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:PRK15439 167 PTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-212 |
1.56e-15 |
|
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: 72.53 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 25 LSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNCNPQKDRcrlfqKVGVQFQEGDYQPEIKVSE--LC 98
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIngvdVTAAPPADR-----PVSMLFQENNLFAHLTVEQnvGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 99 GETACLYEAPADW---KSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQE 175
Cdd:cd03298 94 GLSPGLKLTAEDRqaiEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1045868222 176 L-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYG 212
Cdd:cd03298 174 LhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-216 |
1.62e-15 |
|
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: 75.11 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTkNADSGTVSILNCN----PQKDRCRLFQKVGVQFQE--GDYQPEI 92
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDldglSRRALRPLRRRMQVVFQDpfGSLSPRM 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 93 KVSELCGETACLYEAPADwKSLCEQfgigsKIGNAVKS--------------LSGGERQRLFIVLALIPNPELVFLDELT 158
Cdd:COG4172 380 TVGQIIAEGLRVHGPGLS-AAERRA-----RVAEALEEvgldpaarhrypheFSGGQRQRIAIARALILEPKLLVLDEPT 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 159 TGLDAKARRDVWKILQEL-KQGGLT-IFItSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:COG4172 454 SALDVSVQAQILDLLRDLqREHGLAyLFI-SHDLAVVRALAHRVMVMKDGKVVEQGPTEQ 512
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-224 |
1.77e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 73.27 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 3 TAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN-----PQK-DRCR-- 74
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPladwsPAElARRRav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 75 LFQKVGVQFqegdyqPeIKVSE--------LCGETACLYEAPADWKSL--CEQFGigskiGNAVKSLSGGERQR--LFIV 142
Cdd:PRK13548 81 LPQHSSLSF------P-FTVEEvvamgrapHGLSRAEDDALVAAALAQvdLAHLA-----GRDYPQLSGGEQQRvqLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 143 LALI----PNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFI-------TSHFmdeveilCDEICILKQGKAVF 210
Cdd:PRK13548 149 LAQLwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVvlhdlnlAARY-------ADRIVLLHQGRLVA 221
|
250 260
....*....|....*....|
gi 1045868222 211 YGTVEQA------KAVSGCE 224
Cdd:PRK13548 222 DGTPAEVltpetlRRVYGAD 241
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-207 |
1.83e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 73.61 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYD---NLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRC-RLF 76
Cdd:PRK13650 1 MSNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 QKVGVQFQEGDYQpeikvseLCGETAclyeaPADWKSLCEQFGIG-----SKIGNAVK-------------SLSGGERQR 138
Cdd:PRK13650 81 HKIGMVFQNPDNQ-------FVGATV-----EDDVAFGLENKGIPheemkERVNEALElvgmqdfkerepaRLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 139 LFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQG-GLTIFITSHFMDEVEiLCDEICILKQGK 207
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQ 217
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
23-219 |
1.93e-15 |
|
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: 75.08 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNcnpQKDRCRLFQKVG-----VQFQEGDYQPEIK 93
Cdd:TIGR01842 337 ISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLdgadLK---QWDRETFGKHIGylpqdVELFPGTVAENIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 94 VSELCGETACLYEAP--ADWKSLCEQF--GIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDV 169
Cdd:TIGR01842 414 RFGENADPEKIIEAAklAGVHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQAL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1045868222 170 WKILQELKQGGLTIFITSHFMDEVEiLCDEICILKQGKAVFYGTVEQAKA 219
Cdd:TIGR01842 494 ANAIKALKARGITVVVITHRPSLLG-CVDKILVLQDGRIARFGERDEVLA 542
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-204 |
2.00e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDN-LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKD-RCRLFQK 78
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlQKNLVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 79 VGvQFQEGDYQPEIKVSELC-----GETACLYEAPADWKSLCE----QFGIGSKIGNAVKSLSGGERQRLFIVLALIPNP 149
Cdd:PRK15056 83 VP-QSEEVDWSFPVLVEDVVmmgryGHMGWLRRAKKRDRQIVTaalaRVDMVEFRHRQIGELSGGQKKRVFLARAIAQQG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1045868222 150 ELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILK 204
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-216 |
2.39e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.10 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVsILNCNP----------QK 70
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI-LLRGQHieglpghqiaRM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 71 DRCRLFQKVGVqFQE---------GDYQpEIKVSELCG----------ETACLYEApADWkslCEQFGIGSKIGNAVKSL 131
Cdd:PRK11300 81 GVVRTFQHVRL-FREmtvienllvAQHQ-QLKTGLFSGllktpafrraESEALDRA-ATW---LERVGLLEHANRQAGNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 132 SGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELK-QGGLTIFITSHFMDEVEILCDEICILKQGKAVF 210
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRnEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLA 234
|
....*.
gi 1045868222 211 YGTVEQ 216
Cdd:PRK11300 235 NGTPEE 240
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-206 |
2.77e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.11 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCR-LFQKVGVQF 83
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARaASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 84 QEGDYQPEIKVSELC--GETACL----YEAPADWKSL---CEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFL 154
Cdd:PRK09536 84 QDTSLSFEFDVRQVVemGRTPHRsrfdTWTETDRAAVeraMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 155 DELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQG 206
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-213 |
3.29e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 74.23 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDNLL-AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQK-DRCRLFQKVGV 81
Cdd:PRK13657 334 AVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 82 QFQE--------GDyqpEIKVSELCGETACLYEAPA--------DWKSLCEQFGIGSKiGNavkSLSGGERQRLFIVLAL 145
Cdd:PRK13657 414 VFQDaglfnrsiED---NIRVGRPDATDEEMRAAAEraqahdfiERKPDGYDTVVGER-GR---QLSGGERQRLAIARAL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1045868222 146 IPNPELVFLDELTTGLDAKARRDVWKILQELKQgGLTIFITSHFMDEVEIlCDEICILKQGKAVFYGT 213
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGS 552
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-218 |
4.59e-15 |
|
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: 71.02 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIECILGTKN--ADSGTV-----SILNCNPQkDRCRLfqKVGVQFQegdYQPEIKvs 95
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEIlfkgeDITDLPPE-ERARL--GIFLAFQ---YPPEIP-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 96 elcgetaclyeapadwkslceqfgiGSKIGNAVKSL----SGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWK 171
Cdd:cd03217 91 -------------------------GVKNADFLRYVnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1045868222 172 ILQELKQGGLTIFITSHF---MDEVEIlcDEICILKQGKAVFYGTVEQAK 218
Cdd:cd03217 146 VINKLREEGKSVLIITHYqrlLDYIKP--DRVHVLYDGRIVKSGDKELAL 193
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-213 |
5.30e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 73.66 E-value: 5.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDN-LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN----PQKDrcrLFQK 78
Cdd:COG1132 339 EIEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDirdlTLES---LRRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 79 VGVQFQE--------------GDyqPEIKVSELcgETACLyeapadwKSLCEQF------GIGSKIGNAVKSLSGGERQR 138
Cdd:COG1132 416 IGVVPQDtflfsgtireniryGR--PDATDEEV--EEAAK-------AAQAHEFiealpdGYDTVVGERGVNLSGGQRQR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1045868222 139 LFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFIT---SHFMDeveilCDEICILKQGKAVFYGT 213
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAhrlSTIRN-----ADRILVLDDGRIVEQGT 557
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-216 |
7.65e-15 |
|
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: 71.11 E-value: 7.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYD-NLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQK-DRCRLFQKVGVQ 82
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 83 FQE--------------GDYQP-EIKVSELCgETACLYEAPADWKslceqFGIGSKIGNAVKSLSGGERQRLFIVLALIP 147
Cdd:cd03253 81 PQDtvlfndtigyniryGRPDAtDEEVIEAA-KAAQIHDKIMRFP-----DGYDTIVGERGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 148 NPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITsHFMDEVeILCDEICILKQGKAVFYGTVEQ 216
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLSTI-VNADKIIVLKDGRIVERGTHEE 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-207 |
1.12e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.40 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 20 VDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSIL--NCNPQ---KDRCRLFQKVGVQFQegdyQPEIKV 94
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyHITPEtgnKNLKKLRKKVSLVFQ----FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 95 SElcgET-------------ACLYEAPADWKSLCEQFGIGSKIGNavKS---LSGGERQRLFIVLALIPNPELVFLDELT 158
Cdd:PRK13641 99 FE---NTvlkdvefgpknfgFSEDEAKEKALKWLKKVGLSEDLIS--KSpfeLSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1045868222 159 TGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGK 222
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-212 |
1.16e-14 |
|
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: 69.96 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 21 DKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCrlFQK-VGVQFQEGDYQPEIKVSELCG 99
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRPLDKN--FQRsTGYVEQQDVHSPNLTVREALR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 100 ETACLyeapadwkslceqfgigskignavKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQG 179
Cdd:cd03232 102 FSALL------------------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1045868222 180 GLTIFITSH---------FmdeveilcDEICILKQ-GKAVFYG 212
Cdd:cd03232 158 GQAILCTIHqpsasifekF--------DRLLLLKRgGKTVYFG 192
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-209 |
1.22e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.65 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTknADSGTVS---ILNCNPQKDR-CRLF 76
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV--YPHGTYEgeiIFEGEELQASnIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 QKVGVQ--FQEGDYQPEIKVselcGETACLYEAPA-----DW-------KSLCEQFGIGSKIGNAVKSLSGGERQRLFIV 142
Cdd:PRK13549 80 ERAGIAiiHQELALVKELSV----LENIFLGNEITpggimDYdamylraQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1045868222 143 LALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLT-IFItSHFMDEVEILCDEICILKQGKAV 209
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIAcIYI-SHKLNEVKAISDTICVIRDGRHI 222
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-232 |
1.25e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.60 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 30 GTVYGLLGANGAGKSTTIECILGTKNADSGTVSILnCNPQKDRCRLFQKVGVQFQEGDYQPEIKVSE---LCG-----ET 101
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTIL-ANNRKPTKQILKRTGFVTQDDILYPHLTVREtlvFCSllrlpKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 102 ACLYEAPADWKSLCEQFGI----GSKIGNA-VKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQEL 176
Cdd:PLN03211 173 LTKQEKILVAESVISELGLtkceNTIIGNSfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1045868222 177 KQGGLTIFITSHF-MDEVEILCDEICILKQGKAVFYGTVEQAKAVSGCEKFEDAYLM 232
Cdd:PLN03211 253 AQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPM 309
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-207 |
1.51e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.77 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 2 QTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQ------------ 69
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 70 -KDRCRLFQ-KVGVQFQEGDYQPEIKVSElcgetaCLYEAPADWKSLCEQ------------FGI-GSKIGNAVKSLSGG 134
Cdd:PRK10619 83 dKNQLRLLRtRLTMVFQHFNLWSHMTVLE------NVMEAPIQVLGLSKQeareravkylakVGIdERAQGKYPVHLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 135 ERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-209 |
1.68e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.87 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 3 TAIKVEQLSKAY--DNLLA-------VDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI-------LNC 66
Cdd:PRK10419 2 TLLNVSGLSHHYahGGLSGkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWrgeplakLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 67 NPQKDRCRLFQKVgvqFQE--GDYQPEIKVSELCGET----ACLYEAP--ADWKSLCEQFGIGSKIGNAV-KSLSGGERQ 137
Cdd:PRK10419 82 AQRKAFRRDIQMV---FQDsiSAVNPRKTVREIIREPlrhlLSLDKAErlARASEMLRAVDLDDSVLDKRpPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1045868222 138 RLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLT--IFITsHFMDEVEILCDEICILKQGKAV 209
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFIT-HDLRLVERFCQRVMVMDNGQIV 231
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-207 |
1.74e-14 |
|
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: 70.19 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDN---LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVsILN--CNPQKDRCRLFQKV 79
Cdd:cd03248 12 VKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV-LLDgkPISQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 GVQFQE-----GDYQPEIKVSELCGETACLYEAPA-----DWKSLCEQfGIGSKIGNAVKSLSGGERQRLFIVLALIPNP 149
Cdd:cd03248 91 SLVGQEpvlfaRSLQDNIAYGLQSCSFECVKEAAQkahahSFISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1045868222 150 ELVFLDELTTGLDAKARRDVWKILQELKQGGlTIFITSHFMDEVEiLCDEICILKQGK 207
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERR-TVLVIAHRLSTVE-RADQILVLDGGR 225
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-231 |
2.09e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.91 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILN---CNPQKDRC---- 73
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkdiTDWQTAKImrea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 74 --------RLFQKVGVQ--------FQEGD-YQPEIK-VSELCGEtacLYEAPAdwkslceqfgigskigNAVKSLSGGE 135
Cdd:PRK11614 82 vaivpegrRVFSRMTVEenlamggfFAERDqFQERIKwVYELFPR---LHERRI----------------QRAGTMSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 136 RQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTve 215
Cdd:PRK11614 143 QQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDT-- 220
|
250
....*....|....*.
gi 1045868222 216 qAKAVSGCEKFEDAYL 231
Cdd:PRK11614 221 -GDALLANEAVRSAYL 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-216 |
2.83e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.07 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADS-----GTVSILNCNPQKDRC---RL 75
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVnlnRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 76 FQKVGVQFQEGD------------------YQPEIKVSELCgETAclYEAPADWKSlceqfgIGSKIGNAVKSLSGGERQ 137
Cdd:PRK14258 87 RRQVSMVHPKPNlfpmsvydnvaygvkivgWRPKLEIDDIV-ESA--LKDADLWDE------IKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 138 RLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELK-QGGLTIFITSHFMDEVEILCDEICILKQ-----GKAVFY 211
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEF 237
|
....*
gi 1045868222 212 GTVEQ 216
Cdd:PRK14258 238 GLTKK 242
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-216 |
2.92e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.43 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNL--LAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNCNPQKDRCR 74
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVggmvLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 75 lfqKVGVQFQEGDYQpeikvseLCGETAclyeaPADWKSLCEQFGIG-----SKIGNAVK-------------SLSGGER 136
Cdd:PRK13635 82 ---QVGMVFQNPDNQ-------FVGATV-----QDDVAFGLENIGVPreemvERVDQALRqvgmedflnrephRLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 137 QRLFI--VLALipNPELVFLDELTTGLDAKARRDVWKILQELK-QGGLTIFITSHFMDEVeILCDEICILKQGKAVFYGT 213
Cdd:PRK13635 147 QRVAIagVLAL--QPDIIILDEATSMLDPRGRREVLETVRQLKeQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGT 223
|
...
gi 1045868222 214 VEQ 216
Cdd:PRK13635 224 PEE 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-207 |
3.65e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQKVG 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQF--QEGDYQPEIKVSE---LCGETACLYEApADWK-------SLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPN 148
Cdd:PRK10762 81 IGIihQELNLIPQLTIAEnifLGREFVNRFGR-IDWKkmyaeadKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 149 PELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-216 |
6.15e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 70.25 E-value: 6.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNCNPQKDRcrlfqKVG 80
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLdgvdLSHVPPYQR-----PIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQFQEGDYQPEIKVselcgETACLYEAPADWKSLCEqfgIGSKIGNAVK-------------SLSGGERQRLFIVLALIP 147
Cdd:PRK11607 95 MMFQSYALFPHMTV-----EQNIAFGLKQDKLPKAE---IASRVNEMLGlvhmqefakrkphQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 148 NPELVFLDELTTGLDAKAR-RDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRdRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-216 |
7.04e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.90 E-value: 7.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 22 KINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSiLN-----------CNPQKDRcrlfqKVGVQFQEGDYQP 90
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIV-LNgrvlfdaekgiCLPPEKR-----RIGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 91 EIKV-SELCgeTACLYEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDV 169
Cdd:PRK11144 90 HYKVrGNLR--YGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1045868222 170 WKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:PRK11144 168 LPYLERLaREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-188 |
1.12e-13 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 69.70 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAY-DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQK-DRCRLFQKVGVQ 82
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 83 FQegdyQPEIKVSEL-------CGET--ACLYEAP-----ADW-KSLCEqfGIGSKIGNAVKSLSGGERQRLFIVLALIP 147
Cdd:TIGR02868 415 AQ----DAHLFDTTVrenlrlaRPDAtdEELWAALervglADWlRALPD--GLDTVLGEGGARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1045868222 148 NPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSH 188
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
5-213 |
1.58e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 68.24 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAY--DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILN-CNPQKDRCRLFQKVGV 81
Cdd:PRK13648 8 IVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 82 QFQEGDYQpeikvseLCGETACLYEA--------PAD-----WKSLCEQFGIGSKIGNAVKSLSGGERQRLFI--VLALi 146
Cdd:PRK13648 88 VFQNPDNQ-------FVGSIVKYDVAfglenhavPYDemhrrVSEALKQVDMLERADYEPNALSGGQKQRVAIagVLAL- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1045868222 147 pNPELVFLDELTTGLDAKARRDVWKILQELKQ-GGLTIFITSHFMDEVeILCDEICILKQGKAVFYGT 213
Cdd:PRK13648 160 -NPSVIILDEATSMLDPDARQNLLDLVRKVKSeHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGT 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-209 |
3.27e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.12 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 3 TAIKVEQLSKAYdnllAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI------LNcNPQK------ 70
Cdd:COG1129 255 VVLEVEGLSVGG----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLdgkpvrIR-SPRDairagi 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 71 -----DRCR--LFQKVGV----------QFQEG---DYQPEIKVSElcgetaclyeapadwkSLCEQFGI--GSkIGNAV 128
Cdd:COG1129 330 ayvpeDRKGegLVLDLSIrenitlasldRLSRGgllDRRRERALAE----------------EYIKRLRIktPS-PEQPV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 129 KSLSGGERQRlfIVLA--LIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTI-FITSHfMDEVEILCDEICILKQ 205
Cdd:COG1129 393 GNLSGGNQQK--VVLAkwLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAViVISSE-LPELLGLSDRILVMRE 469
|
....
gi 1045868222 206 GKAV 209
Cdd:COG1129 470 GRIV 473
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-216 |
3.40e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.19 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAY-----------DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNAdSGTVsILNCNP--QKD 71
Cdd:PRK15134 276 LDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEI-WFDGQPlhNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 72 RCRLF---QKVGVQFQE--GDYQPEIKVSELCGE---------TACLYEAPAdwKSLCEQFGIGSKIGNAVKS-LSGGER 136
Cdd:PRK15134 354 RRQLLpvrHRIQVVFQDpnSSLNPRLNVLQIIEEglrvhqptlSAAQREQQV--IAVMEEVGLDPETRHRYPAeFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 137 QRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQG-GLT-IFItSHFMDEVEILCDEICILKQGKAVFYGTV 214
Cdd:PRK15134 432 QRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAyLFI-SHDLHVVRALCHQVIVLRQGEVVEQGDC 510
|
..
gi 1045868222 215 EQ 216
Cdd:PRK15134 511 ER 512
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-216 |
4.05e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSilnCNPQKDRCRLFQKVGVQ---------------- 82
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ---CDKMLLRRRSRQVIELSeqsaaqmrhvrgadma 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 83 --FQE--GDYQPEIKVSELCGETACLY------EAPADWKSLCEQFGI---GSKIGNAVKSLSGGERQRLFIVLALIPNP 149
Cdd:PRK10261 108 miFQEpmTSLNPVFTVGEQIAESIRLHqgasreEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1045868222 150 ELVFLDELTTGLDAKARRDVWKIL----QELKQGglTIFITsHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIkvlqKEMSMG--VIFIT-HDMGVVAEIADRVLVMYQGEAVETGSVEQ 255
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-205 |
4.46e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVS-----ILNCNPQKDR--- 72
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKrngklRIGYVPQKLYldt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 73 -----CRLFQKVGVQFQEGDYQPEIKVSelcgETACLYEAPadwkslceqfgigskignaVKSLSGGERQRLFIVLALIP 147
Cdd:PRK09544 81 tlpltVNRFLRLRPGTKKEDILPALKRV----QAGHLIDAP-------------------MQKLSGGETQRVLLARALLN 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 148 NPELVFLDELTTGLDAKARRDVWKILQELKQG-GLTIFITSHFMDEVEILCDEICILKQ 205
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
3-212 |
5.18e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.55 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 3 TAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCR-LFQKVGV 81
Cdd:PRK10253 6 ARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 82 QFQEGDYQPEIKVSELCGE---------TACLYEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELV 152
Cdd:PRK10253 86 LAQNATTPGDITVQELVARgryphqplfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1045868222 153 FLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYG 212
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-212 |
5.29e-13 |
|
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: 65.36 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 11 SKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECI---LGTKNADSGTVSiLNCNPQKDRCRLFQKVGVQFQEGD 87
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIH-YNGIPYKEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 88 -YQPEIKVSELCgETACLyeapadwkslCEqfgigskiGNA-VKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKA 165
Cdd:cd03233 93 vHFPTLTVRETL-DFALR----------CK--------GNEfVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1045868222 166 RRDVWKILQEL--KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYG 212
Cdd:cd03233 154 ALEILKCIRTMadVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-238 |
8.11e-13 |
|
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: 67.16 E-value: 8.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGT--KNADSGTVSILNCNPQKDRCRLFQKVGVQ 82
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 83 F--QEGDYQPEIKVSE---------LCGETACLYEAPADWKSLCEQFGI-GSKIGNAVKSLSGGERQRLFIVLALIPNPE 150
Cdd:TIGR02633 82 IihQELTLVPELSVAEniflgneitLPGGRMAYNAMYLRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 151 LVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVfyGTvEQAKAVSgcekFEDAY 230
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV--AT-KDMSTMS----EDDII 234
|
....*...
gi 1045868222 231 LMLSGEEV 238
Cdd:TIGR02633 235 TMMVGREI 242
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-192 |
8.84e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.96 E-value: 8.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 2 QTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIEC------ILGTKNADsGTVSILNCN---PQKDR 72
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRVE-GKVTFHGKNlyaPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 73 CRLFQKVGVQFQEGDYQPE---------IKVSELCGETACLYEAPADWKSLCEQfgIGSKIGNAVKSLSGGERQRLFIVL 143
Cdd:PRK14243 87 VEVRRRIGMVFQKPNPFPKsiydniaygARINGYKGDMDELVERSLRQAALWDE--VKDKLKQSGLSLSGGQQQRLCIAR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1045868222 144 ALIPNPELVFLDELTTGLDAKARRDVWKILQELKQgGLTIFITSHFMDE 192
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHNMQQ 212
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-216 |
1.02e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.72 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI---------LNCNPQKD 71
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdgqlrdLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 72 RCRLFQ-KVGVQFQEGDYQPEIKVS-------ELCGETACLY----EAPADWKSLCEqfgIG-SKIGNAVKSLSGGERQR 138
Cdd:PRK11701 83 RRRLLRtEWGFVHQHPRDGLRMQVSaggnigeRLMAVGARHYgdirATAGDWLERVE---IDaARIDDLPTTFSGGMQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 139 LFIVLALIPNPELVFLDELTTGLD--AKARrdvwkiLQELKQG-----GLTIFITSHFMDEVEILCDEICILKQGKAVFY 211
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDvsVQAR------LLDLLRGlvrelGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
....*
gi 1045868222 212 GTVEQ 216
Cdd:PRK11701 234 GLTDQ 238
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-216 |
1.24e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.58 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIEcILGTKNADSGTVSILNCNPQKD-RCRLF-QKVGVQFQEGDYQPEIKVSELcge 100
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPPSEGEILLDAQPLESwSSKAFaRKVAYLPQQLPAAEGMTVREL--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 101 tACLYEAPadWKSLCEQFGIG--SKIGNA-------------VKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKA 165
Cdd:PRK10575 106 -VAIGRYP--WHGALGRFGAAdrEKVEEAislvglkplahrlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 166 RRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:PRK10575 183 QVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-216 |
1.28e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.08 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKN------ADS---GTVSILNCNPQKDRCRLFQKVGVQFQE--GD 87
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhvtADRfrwNGIDLLKLSPRERRKIIGREIAMIFQEpsSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 88 YQPEIKVSELcgetacLYEAPADW-----------------KSLCEQFGIGS--KIGNAVK-SLSGGERQRLFIVLALIP 147
Cdd:COG4170 102 LDPSAKIGDQ------LIEAIPSWtfkgkwwqrfkwrkkraIELLHRVGIKDhkDIMNSYPhELTEGECQKVMIAMAIAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 148 NPELVFLDELTTGLDAKARRDVWKILQELKQ-GGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:COG4170 176 QPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQ 245
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-212 |
1.28e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.88 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQtaIKVEQLSKAYDN-----LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNP------- 68
Cdd:PRK13651 1 MQ--IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEknkkktk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 69 -----------QKDRCRLFQK-------VGVQFQEGDYQpeikVSELCGETACLYEAPADWKSLCEQFGIGSKIGNAV-- 128
Cdd:PRK13651 79 ekekvleklviQKTRFKKIKKikeirrrVGVVFQFAEYQ----LFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVgl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 129 ------KS---LSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDE 199
Cdd:PRK13651 155 desylqRSpfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKR 234
|
250
....*....|...
gi 1045868222 200 ICILKQGKAVFYG 212
Cdd:PRK13651 235 TIFFKDGKIIKDG 247
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-207 |
1.32e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.12 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN----PQKDRcrlfqKVG 80
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDithvPAENR-----HVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQFQEGDYQPEIKVSELCGETACLYEAPADwkslceqfGIGSKIGNAVK-------------SLSGGERQRLFIVLALIP 147
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGLRMQKTPAA--------EITPRVMEALRmvqleefaqrkphQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1045868222 148 NPELVFLDELTTGLDAKARrdvwKILQ-ELK----QGGLT-IFITsHFMDEVEILCDEICILKQGK 207
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLR----KQMQnELKalqrKLGITfVFVT-HDQEEALTMSDRIVVMRDGR 222
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-216 |
1.51e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 65.25 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECI--LGTKNADS---GTVSILNCN---PQKDR 72
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrLLELNEEArveGEVRLFGRNiysPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 73 CRLFQKVGVQFQegdyqpeikvselcgetaclYEAPADWKSLCEQFGIGSKIGNAVKS---------------------- 130
Cdd:PRK14267 81 IEVRREVGMVFQ--------------------YPNPFPHLTIYDNVAIGVKLNGLVKSkkeldervewalkkaalwdevk 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 131 ---------LSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQgGLTIFITSHFMDEVEILCDEIC 201
Cdd:PRK14267 141 drlndypsnLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPAQAARVSDYVA 219
|
250
....*....|....*
gi 1045868222 202 ILKQGKAVFYGTVEQ 216
Cdd:PRK14267 220 FLYLGKLIEVGPTRK 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-213 |
1.57e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 65.41 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI------LNCNPQKDRCRLFQKVGVQFQEGDYQ--- 89
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKKIKEVKRLRKEIGLVFQFPEYQlfq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 90 PEIKVSELCGETACLYEAPADWKSLCEQFGIGSKIGNAVK----SLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKA 165
Cdd:PRK13645 106 ETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1045868222 166 RRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGT 213
Cdd:PRK13645 186 EEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-216 |
1.81e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.80 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECI--LGTKNAD---SGTVSILNCN---PQKDR 72
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNiysPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 73 CRLFQKVGVQFQEGD------YQPEIKVSELCG--ETACLYEAPAdwKSLceqfgIGSKIGNAVK--------SLSGGER 136
Cdd:PRK14239 82 VDLRKEIGMVFQQPNpfpmsiYENVVYGLRLKGikDKQVLDEAVE--KSL-----KGASIWDEVKdrlhdsalGLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 137 QRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQgGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD-DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQ 233
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-207 |
1.87e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.51 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 10 LSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI------LNCNPQKDRCRLFQKV---- 79
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdgedvtHRSIQQRDICMVFQSYalfp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 ----------GVQFQeGDYQPEIK--VSELCgetaclyeAPADWKSLCEQFgigskignaVKSLSGGERQRLFIVLALIP 147
Cdd:PRK11432 92 hmslgenvgyGLKML-GVPKEERKqrVKEAL--------ELVDLAGFEDRY---------VDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1045868222 148 NPELVFLDELTTGLDAKARRDVWKILQELKQG-GLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-193 |
2.07e-12 |
|
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: 66.11 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI-----LNCNPQKdRCRLFQKV 79
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvkLAYVDQS-RDALDPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 GVqFQE-GDYQPEIKVSElcgetaclYEAPAdwKSLCEQFGI-GSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDEL 157
Cdd:TIGR03719 402 TV-WEEiSGGLDIIKLGK--------REIPS--RAYVGRFNFkGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
170 180 190
....*....|....*....|....*....|....*....
gi 1045868222 158 TTGLDAKARRDVWKILQELkqGGLTIFItSH---FMDEV 193
Cdd:TIGR03719 471 TNDLDVETLRALEEALLNF--AGCAVVI-SHdrwFLDRI 506
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-216 |
2.37e-12 |
|
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: 65.92 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAY--DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNcnpQKDRCRLFQK 78
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLdgadLS---QWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 79 VG-----VQ------------FQEGDyqPE--IKVSELCGetacLYEApadwkslceqfgIGS-------KIGNAVKSLS 132
Cdd:COG4618 408 IGylpqdVElfdgtiaeniarFGDAD--PEkvVAAAKLAG----VHEM------------ILRlpdgydtRIGEGGARLS 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 133 GGERQRlfIVLA--LIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHfmdEVEIL--CDEICILKQGKA 208
Cdd:COG4618 470 GGQRQR--IGLAraLYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITH---RPSLLaaVDKLLVLRDGRV 544
|
....*...
gi 1045868222 209 VFYGTVEQ 216
Cdd:COG4618 545 QAFGPRDE 552
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-188 |
2.50e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.82 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQKVGVQFQ 84
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 85 EGDYQPEIKVSELCGETACLYEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAK 164
Cdd:PRK13540 82 RSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....
gi 1045868222 165 ARRDVWKILQELKQGGLTIFITSH 188
Cdd:PRK13540 162 SLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-212 |
2.78e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.64 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV----SILNCNpQKDRCRLFQKVGVQFQEGDYQ--------- 89
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgKPLDYS-KRGLLALRQQVATVFQDPEQQifytdidsd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 90 ----------PEIKVSELCGETACLYEApadwKSLCEQfgigskignAVKSLSGGERQRLFIVLALIPNPELVFLDELTT 159
Cdd:PRK13638 99 iafslrnlgvPEAEITRRVDEALTLVDA----QHFRHQ---------PIQCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 160 GLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYG 212
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-230 |
2.79e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 64.32 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIECILGTKN--ADSGTV-----SILNCNPQkDRCR--LFqkvgVQFQegdYQPEIK 93
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSIlldgeDILELSPD-ERARagIF----LAFQ---YPVEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 94 -----------VSELCGETACLYEAPADWKSLCEQFGIGSKIGN-AV-KSLSGGERQRLFIVLALIPNPELVFLDELTTG 160
Cdd:COG0396 91 gvsvsnflrtaLNARRGEELSAREFLKLLKEKMKELGLDEDFLDrYVnEGFSGGEKKRNEILQMLLLEPKLAILDETDSG 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1045868222 161 LDAKARRDVWKILQELKQGGLTIFITSH---FMDEVEIlcDEICILKQGKAVFYGTVEQAKAV--SGCEKFEDAY 230
Cdd:COG0396 171 LDIDALRIVAEGVNKLRSPDRGILIITHyqrILDYIKP--DFVHVLVDGRIVKSGGKELALELeeEGYDWLKEEA 243
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-213 |
3.56e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.80 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIECILGTKNAdSGTVSILNCN----PQKD----RCRLFQKVGVQFQEGDYQ----- 89
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPleawSAAElarhRAYLSQQQTPPFAMPVFQyltlh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 90 -PEiKVSELCGETAcLYEapadwksLCEQFGIGSKIGNAVKSLSGGERQR-------LFIVLALIPNPELVFLDELTTGL 161
Cdd:PRK03695 94 qPD-KTRTEAVASA-LNE-------VAEALGLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 162 DAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGT 213
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGR 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-213 |
3.70e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.43 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYD--NLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCR-LFQKVGV 81
Cdd:PRK11176 342 IEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLAsLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 82 QFQE----GD-------YQPEIKVSELCGETACLYEAPADWKSLCEQfGIGSKIGNAVKSLSGGERQRLFIVLALIPNPE 150
Cdd:PRK11176 422 VSQNvhlfNDtianniaYARTEQYSREQIEEAARMAYAMDFINKMDN-GLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 151 LVFLDELTTGLDAKARRDVWKILQELkQGGLTIFITSHFMDEVEiLCDEICILKQGKAVFYGT 213
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIE-KADEILVVEDGEIVERGT 561
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-190 |
4.12e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.95 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAY-----DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN----PQKDRCRL 75
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtklPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 76 FQKVgvqFQegDYQ----PEIKVSELC------GETACLyeAPA-------DWKSLCEQFGIG--SKIGNAVKSLSGGER 136
Cdd:COG1101 82 IGRV---FQ--DPMmgtaPSMTIEENLalayrrGKRRGL--RRGltkkrreLFRELLATLGLGleNRLDTKVGLLSGGQR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1045868222 137 QRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLT-IFITsHFM 190
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTtLMVT-HNM 209
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-216 |
4.61e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.78 E-value: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 2 QTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECI-----LGTKNADSGTVSILNCNPQK-DRCRL 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIFKmDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 76 FQKVGVQFQEGDYQPEIKVSELCGETACLYEAPADWKSLCEQFG-----------IGSKIGNAVKSLSGGERQRLFIVLA 144
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELQERVRwalekaqlwdeVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 145 LIPNPELVFLDELTTGLDAKARRDVWKILQELKQgGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-219 |
5.46e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 64.66 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 3 TAIKVEQLS-KAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQKVGV 81
Cdd:COG3845 256 VVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 82 QFqegdyqpeikVSE------LCG-----ETACL--YEAPA-------DWK-------SLCEQFGI-GSKIGNAVKSLSG 133
Cdd:COG3845 336 AY----------IPEdrlgrgLVPdmsvaENLILgrYRRPPfsrggflDRKairafaeELIEEFDVrTPGPDTPARSLSG 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 134 GERQRLfiVLA--LIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVfy 211
Cdd:COG3845 406 GNQQKV--ILAreLSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV-- 481
|
....*...
gi 1045868222 212 GTVEQAKA 219
Cdd:COG3845 482 GEVPAAEA 489
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-167 |
6.19e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.81 E-value: 6.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSIlncnPQKDRCRLFQKVGVQFQ 84
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----AKGIKLGYFAQHQLEFL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 85 EGDYQPEIKVSELCGEtaclyEAPADWKSLCEQFGI-GSKIGNAVKSLSGGERQRLfiVLALI--PNPELVFLDELTTGL 161
Cdd:PRK10636 389 RADESPLQHLARLAPQ-----ELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARL--VLALIvwQRPNLLLLDEPTNHL 461
|
....*.
gi 1045868222 162 DAKARR 167
Cdd:PRK10636 462 DLDMRQ 467
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-231 |
6.43e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 27 VKCGTVYGLLGANGAGKSTTIEcILgtknadSGTVsILN-CNPQK--------DRCR---LFQ----------KVGVQFQ 84
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVK-IL------SGEL-IPNlGDYEEepswdevlKRFRgteLQNyfkklyngeiKVVHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 85 EGDYQPEI---KVSELCGETaclyeapaD----WKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDEL 157
Cdd:PRK13409 168 YVDLIPKVfkgKVRELLKKV--------DergkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1045868222 158 TTGLDAKARRDVWKILQELKQGGlTIFITSHFMDEVEILCDEICILkQGKAVFYGTVEQAKAV-SGCEKFEDAYL 231
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAEGK-YVLVVEHDLAVLDYLADNVHIA-YGEPGAYGVVSKPKGVrVGINEYLKGYL 312
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
131-216 |
7.13e-12 |
|
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: 64.32 E-value: 7.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 131 LSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQ-GGLTI-FITsHFMDEVEILCDEICILKQGKA 208
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQReLGMALlLIT-HDLGVVRRFADRVAVMRQGEI 235
|
....*...
gi 1045868222 209 VFYGTVEQ 216
Cdd:COG4172 236 VEQGPTAE 243
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-213 |
9.13e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.14 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 2 QTAIKVEQLSKAY---DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIEC------ILGTKNADSGTVSILNCNP-QKD 71
Cdd:PRK14246 5 KSAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDIfQID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 72 RCRLFQKVGVQFQEGDYQPEI----------------------KVSELCGETACLyeapadWKSlceqfgIGSKIGNAVK 129
Cdd:PRK14246 85 AIKLRKEVGMVFQQPNPFPHLsiydniayplkshgikekreikKIVEECLRKVGL------WKE------VYDRLNSPAS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 130 SLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQgGLTIFITSHFMDEVEILCDEICILKQGKAV 209
Cdd:PRK14246 153 QLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
....
gi 1045868222 210 FYGT 213
Cdd:PRK14246 232 EWGS 235
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-207 |
1.07e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.20 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAY-DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCR----LFQKV 79
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 GVQFQEGDYQPEIKVSELCGETACLYEAPAD-----WKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFL 154
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDdirrrVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 155 DELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-192 |
1.39e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 62.57 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 3 TAIKVEQLSKAYDN----LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSiLNCN----PQKDRcr 74
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEIT-LDGVpvtgPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 75 lfqkvGVQFQEGDYQPEIKVSE-------LCGETACLYEAPADwkSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIP 147
Cdd:COG4525 79 -----GVVFQKDALLPWLNVLDnvafglrLRGVPKAERRARAE--ELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1045868222 148 NPELVFLDELTTGLDAKARRDvwkiLQEL-----KQGGLTIFITSHFMDE 192
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQ----MQELlldvwQRTGKGVFLITHSVEE 197
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-237 |
1.51e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.61 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRlfqkvgvqf 83
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHR--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 84 qegdyqpeikvSELCGETAC--------LYeaPAdwKSLCE-------QFGIGS-----KIGNAVKS------------- 130
Cdd:NF033858 72 -----------RAVCPRIAYmpqglgknLY--PT--LSVFEnldffgrLFGQDAaerrrRIDELLRAtglapfadrpagk 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 131 LSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQG--GLTIFITSHFMDEVEiLCDEICILKQGKA 208
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAE-RFDWLVAMDAGRV 215
|
250 260
....*....|....*....|....*....
gi 1045868222 209 VFYGTVEQAKAVSGCEKFEDAYLMLSGEE 237
Cdd:NF033858 216 LATGTPAELLARTGADTLEAAFIALLPEE 244
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-216 |
1.68e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.31 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 2 QTAIKVEQLSKAYDN--LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQK-DRCRLFQK 78
Cdd:PRK11160 336 QVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 79 VGVQFQEGDY------------QPEIKVSELCG-----ETACLYEAPAdwkslceqfGIGSKIGNAVKSLSGGERQRLFI 141
Cdd:PRK11160 416 ISVVSQRVHLfsatlrdnlllaAPNASDEALIEvlqqvGLEKLLEDDK---------GLNAWLGEGGRQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1045868222 142 VLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITsHFMDEVEILcDEICILKQGKAVFYGTVEQ 216
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMIT-HRLTGLEQF-DRICVMDNGQIIEQGTHQE 559
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-231 |
2.31e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.88 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 30 GTVYGLLGANGAGKSTTIEcILgtknadSGTVS----ILNCNPQKDRC-RLFQkvGVQFQ---EGDYQPEIKVSE----- 96
Cdd:COG1245 99 GKVTGILGPNGIGKSTALK-IL------SGELKpnlgDYDEEPSWDEVlKRFR--GTELQdyfKKLANGEIKVAHkpqyv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 97 ------LCGETACLYEApAD----WKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKAR 166
Cdd:COG1245 170 dlipkvFKGTVRELLEK-VDergkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQR 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1045868222 167 RDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILkQGKAVFYGTVEQAKAV-SGCEKFEDAYL 231
Cdd:COG1245 249 LNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHIL-YGEPGVYGVVSKPKSVrVGINQYLDGYL 313
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-213 |
2.32e-11 |
|
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: 61.27 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLL--AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQK-DRCRLFQKVGV 81
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 82 QFQEgdyqPEIkvseLCGeTACLYEAPADWKSLCEQFGiGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGL 161
Cdd:cd03369 87 IPQD----PTL----FSG-TIRSNLDPFDEYSDEEIYG-ALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 162 DAKARRDVWKILQELKQGGlTIFITSHFMDEVeILCDEICILKQGKAVFYGT 213
Cdd:cd03369 157 DYATDALIQKTIREEFTNS-TILTIAHRLRTI-IDYDKILVMDAGEVKEYDH 206
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-207 |
2.72e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 61.33 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN----PQKDRCRL-FQKVGVQFQEGDYQPEIKVSE- 96
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlhqmDEEARAKLrAKHVGFVFQSFMLIPTLNALEn 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 97 ------LCGETAclYEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVW 170
Cdd:PRK10584 109 velpalLRGESS--RQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 1045868222 171 KILQELKQGGLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:PRK10584 187 DLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQ 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-214 |
2.77e-11 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 61.33 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 20 VDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILN---CNPQKDRCrlfqkvgVQFQEGDYQPEIKVSE 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqiTEPGPDRM-------VVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 97 ---LCGETACLYEAPADWKSLCEQ----FGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDV 169
Cdd:TIGR01184 74 niaLAVDRVLPDLSKSERRAIVEEhialVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1045868222 170 W-KILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTV 214
Cdd:TIGR01184 154 QeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-207 |
4.21e-11 |
|
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: 62.15 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 20 VDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDR-CRLFQKVGVQFQEGDYQPEIKVSEL- 97
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDIRnPAQAIRAGIAMVPEDRKRHGIVPILg 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 98 CGETACLyeapADWKSLC---------EQFGIGSKIGN----------AVKSLSGGERQRLFIVLALIPNPELVFLDELT 158
Cdd:TIGR02633 356 VGKNITL----SVLKSFCfkmridaaaELQIIGSAIQRlkvktaspflPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1045868222 159 TGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
20-216 |
4.66e-11 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 62.21 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 20 VDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQK-DRCRLFQKVGVQFQEG-----DYQPEIK 93
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTvTRESLRKSIATVFQDAglfnrSIRENIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 94 VSELCGETACLYEAPADWKS----LCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDV 169
Cdd:TIGR01192 431 LGREGATDEEVYEAAKAAAAhdfiLKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARV 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1045868222 170 WKILQELKQgGLTIFITSHFMDEVEIlCDEICILKQGKAVFYGTVEQ 216
Cdd:TIGR01192 511 KNAIDALRK-NRTTFIIAHRLSTVRN-ADLVLFLDQGRLIEKGSFQE 555
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-216 |
5.44e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 61.26 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 16 NLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSIL--NCNPQKDRCRLFQKVGVQ--FQE--GDYQ 89
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLgkDLLGMKDDEWRAVRSDIQmiFQDplASLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 90 PEIKVSELCGETACLYEAPADWKSLCEQF-GIGSKIG---NAVK----SLSGGERQRLFIVLALIPNPELVFLDELTTGL 161
Cdd:PRK15079 113 PRMTIGEIIAEPLRTYHPKLSRQEVKDRVkAMMLKVGllpNLINryphEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1045868222 162 DAKARRDVWKILQEL-KQGGLT-IFItSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:PRK15079 193 DVSIQAQVVNLLQQLqREMGLSlIFI-AHDLAVVKHISDRVLVMYLGHAVELGTYDE 248
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-218 |
6.00e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.97 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 21 DKINLSVKCGTVYGLLGANGAGKSTTIECILG--TKNADSGTVSILNcNPQKDRCRLFQKVGvqfQEGDYQPEIKVSELC 98
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPD-NQFGREASLIDAIG---RKGDFKDAVELLNAV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 99 G-ETACLYEAPadwkslceqfgigskignaVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQEL- 176
Cdd:COG2401 123 GlSDAVLWLRR-------------------FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLa 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1045868222 177 KQGGLTIFITSHFMDEVEILCDEICILKQgkavfYGTVEQAK 218
Cdd:COG2401 184 RRAGITLVVATHHYDVIDDLQPDLLIFVG-----YGGVPEEK 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-207 |
9.02e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.08 E-value: 9.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 3 TAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNC--NPQKDRCRLFqkvg 80
Cdd:PRK11247 11 TPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAplAEAREDTRLM---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 vqFQEGDYQPEIKVSE-----LCGetaclyeapaDWKSLCEQ----FGIGSKIGNAVKSLSGGERQRLFIVLALIPNPEL 151
Cdd:PRK11247 87 --FQDARLLPWKKVIDnvglgLKG----------QWRDAALQalaaVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1045868222 152 VFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
23-207 |
1.31e-10 |
|
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: 59.02 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV----SILNCnPQKDRCR--------LFqkvGVQFQEGDYQp 90
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVsvpgSIAYV-SQEPWIQngtireniLF---GKPFDEERYE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 91 eiKVSELCgetaCLYEapaDWKSLCE--QFGIGSKiGNavkSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRD 168
Cdd:cd03250 99 --KVIKAC----ALEP---DLEILPDgdLTEIGEK-GI---NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRH 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1045868222 169 VWK--ILQELKQGGLTIFITSHfmdeVEIL--CDEICILKQGK 207
Cdd:cd03250 166 IFEncILGLLLNNKTRILVTHQ----LQLLphADQIVVLDNGR 204
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-209 |
1.34e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 59.72 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLAVDKIN---LSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRC-RLF 76
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 QKVGVQFQEGDYQ-------------------PEIKVSELCGEtACLYEAPADWKSlceqfgigskigNAVKSLSGGERQ 137
Cdd:PRK13642 81 RKIGMVFQNPDNQfvgatveddvafgmenqgiPREEMIKRVDE-ALLAVNMLDFKT------------REPARLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 138 RLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELK-QGGLTIFITSHFMDEVEIlCDEICILKQGKAV 209
Cdd:PRK13642 148 RVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEII 219
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-237 |
1.42e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.71 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLaVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTK----NADSGTVSI--LNCNPQKDRCR 74
Cdd:PRK10418 1 MPQQIELRNIALQAAQPL-VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLdgKPVAPCALRGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 75 LFQKVgVQFQEGDYQPEIKVSELCGETACLYEAPADWKSLCEQF-GIGSKIGNAVKSL-----SGGERQRLFIVLALIPN 148
Cdd:PRK10418 80 KIATI-MQNPRSAFNPLHTMHTHARETCLALGKPADDATLTAALeAVGLENAARVLKLypfemSGGMLQRMMIALALLCE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 149 PELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVE---QAKAVSGCE 224
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVEtlfNAPKHAVTR 238
|
250
....*....|...
gi 1045868222 225 KFEDAYLMLSGEE 237
Cdd:PRK10418 239 SLVSAHLALYGME 251
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-206 |
2.21e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.94 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNC---NPQKDRcrlfqkvG 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpveGPGAER-------G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQFQEGDYQPEIKVS-------ELCGETACLYEAPAdwKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVF 153
Cdd:PRK11248 74 VVFQNEGLLPWRNVQdnvafglQLAGVEKMQRLEIA--HQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1045868222 154 LDELTTGLDAKARRDVWKILQELKQG-GLTIFITSHFMDEVEILCDEICILKQG 206
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-207 |
2.31e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 2 QTAIKVEQLSKAydnllAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVS-----ILNCNPQ------- 69
Cdd:PRK10762 255 EVRLKVDNLSGP-----GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTldgheVVTRSPQdglangi 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 70 ----KDR-------------------CRLFQKVGVQFQEGDYQpeikvselcgetaclyEAPADWKSLceqFGI-----G 121
Cdd:PRK10762 330 vyisEDRkrdglvlgmsvkenmsltaLRYFSRAGGSLKHADEQ----------------QAVSDFIRL---FNIktpsmE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 122 SKIGNavksLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEIC 201
Cdd:PRK10762 391 QAIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRIL 466
|
....*.
gi 1045868222 202 ILKQGK 207
Cdd:PRK10762 467 VMHEGR 472
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-216 |
2.36e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 59.66 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 18 LAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV-----SILNCNPQKDRCRLFQKVGVQFQEGDYQPEI 92
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvDIAKISDAELREVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 93 KV---SELCGETACLYEAPADWKSL--CEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARR 167
Cdd:PRK10070 122 TVldnTAFGMELAGINAEERREKALdaLRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1045868222 168 DVWKILQELK-QGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:PRK10070 202 EMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDE 251
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-190 |
2.38e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 58.89 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECI-----LgTKNAD-SGTVSILNCN---PQKD 71
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndL-IPGARvEGEILLDGEDiydPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 72 RCRLFQKVGVQFQegdyQP------------------EIKV-SELCG--ETAcLYEApADWkslceqfgigskigNAVK- 129
Cdd:COG1117 87 VVELRRRVGMVFQ----KPnpfpksiydnvayglrlhGIKSkSELDEivEES-LRKA-ALW--------------DEVKd 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1045868222 130 -------SLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRdvwKI---LQELKQgGLTIFITSHFM 190
Cdd:COG1117 147 rlkksalGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTA---KIeelILELKK-DYTIVIVTHNM 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-209 |
2.76e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 59.36 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV-----SILNCNPQKDRcRLFQKVGVQFQE--GDYQPE 91
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEIlfdgqDITGLSGRELR-PLRRRMQMVFQDpyASLNPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 92 IKVSELCGEtaclyeaPAdwkslcEQFGIGSK--IGNAVKSL------------------SGGERQRLFIVLALIPNPEL 151
Cdd:COG4608 112 MTVGDIIAE-------PL------RIHGLASKaeRRERVAELlelvglrpehadryphefSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 152 VFLDELTTGLDAKARRDVWKILQEL-KQGGLT-IFItSHFMDEVEILCDEICILKQGKAV 209
Cdd:COG4608 179 IVCDEPVSALDVSIQAQVLNLLEDLqDELGLTyLFI-SHDLSVVRHISDRVAVMYLGKIV 237
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-207 |
2.80e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 59.27 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 11 SKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI----LNCNPQKDRcrlfqKVGVQFQEG 86
Cdd:PRK11000 10 TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIgekrMNDVPPAER-----GVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 87 DYQPEIKVSE-------LCGetACLYEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTT 159
Cdd:PRK11000 85 ALYPHLSVAEnmsfglkLAG--AKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1045868222 160 GLDAKARRDVWKILQEL-KQGGLTIFITSHfmDEVE--ILCDEICILKQGK 207
Cdd:PRK11000 163 NLDAALRVQMRIEISRLhKRLGRTMIYVTH--DQVEamTLADKIVVLDAGR 211
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-207 |
7.15e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.26 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 20 VDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSiLNCNPQKDRCRLFQ-KVGVQF--------------- 83
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR-LNGKDISPRSPLDAvKKGMAYitesrrdngffpnfs 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 84 --QEGDYQPEIKVSELCGETACLYEApaDWKSLCEQ----FGIG-SKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDE 156
Cdd:PRK09700 358 iaQNMAISRSLKDGGYKGAMGLFHEV--DEQRTAENqrelLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1045868222 157 LTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGK 207
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
30-230 |
7.37e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.70 E-value: 7.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 30 GTVYGLLGANGAGKSTTIECILGTKNAD--SGTVSIlNCNPQKDRCrlFQKVGVQFQEGD-YQPEIKVSELCGETACLY- 105
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRI-SGFPKKQET--FARISGYCEQNDiHSPQVTVRESLIYSAFLRl 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 106 --EAPADWK--------SLCEQFGIGSKIGN--AVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKIL 173
Cdd:PLN03140 983 pkEVSKEEKmmfvdevmELVELDNLKDAIVGlpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1062
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1045868222 174 QELKQGGLTIFITSH--FMDEVEILcDEICILKQGKAVFYG---------TVEQAKAVSGCEKFEDAY 230
Cdd:PLN03140 1063 RNTVDTGRTVVCTIHqpSIDIFEAF-DELLLMKRGGQVIYSgplgrnshkIIEYFEAIPGVPKIKEKY 1129
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-216 |
9.27e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.79 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNcnpqKDRCRLF---QKVG 80
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG----TDVSRLHardRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQFQEGDYQPEIKVSELCG---------ETACLYEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPEL 151
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAfgltvlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 152 VFLDELTTGLDAKARRDV--W--KILQELKQGGltIFITsHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELrrWlrQLHEELKFTS--VFVT-HDQEEAMEVADRVVVMSQGNIEQAGTPDQ 223
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-218 |
1.01e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.96 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILG--TKNADSGTV-----SILNCNPQkDRCRL-- 75
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDIlfkgeSILDLEPE-ERAHLgi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 76 ---FQK----VGV---QFQEGDYQPEIKVSELcgetaclyeapaDWKSLCEQFGIGSKIGNAVK------------SLSG 133
Cdd:CHL00131 87 flaFQYpieiPGVsnaDFLRLAYNSKRKFQGL------------PELDPLEFLEIINEKLKLVGmdpsflsrnvneGFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 134 GERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVE-ILCDEICILKQGKAVFYG 212
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDyIKPDYVHVMQNGKIIKTG 234
|
....*.
gi 1045868222 213 TVEQAK 218
Cdd:CHL00131 235 DAELAK 240
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
119-222 |
1.15e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.93 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 119 GIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITsHFMDEVEiLCD 198
Cdd:PRK11174 474 GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQLEDLA-QWD 551
|
90 100
....*....|....*....|....
gi 1045868222 199 EICILKQGKAVFYGTVEQAKAVSG 222
Cdd:PRK11174 552 QIWVMQDGQIVQQGDYAELSQAGG 575
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-162 |
1.44e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI-------------LNCNPQKD 71
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgetvklayvdqsrDALDPNKT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 72 rcrLFQKVgvqfqeGDYQPEIKVSElcgetaclYEAPAdwKSLCEQFGI-GSKIGNAVKSLSGGERQRLFIVLALIPNPE 150
Cdd:PRK11819 405 ---VWEEI------SGGLDIIKVGN--------REIPS--RAYVGRFNFkGGDQQKKVGVLSGGERNRLHLAKTLKQGGN 465
|
170
....*....|..
gi 1045868222 151 LVFLDELTTGLD 162
Cdd:PRK11819 466 VLLLDEPTNDLD 477
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-188 |
1.57e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.43 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 21 DKINLSVKCGTVYGLLGANGAGKSTTIEcILGT-KNADSGT-------VSILNcNPQKDRCRLfQKVGVQFQEGDYQPEI 92
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMN-ILGClDKPTSGTyrvagqdVATLD-ADALAQLRR-EHFGFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 93 KVSELCgETACLY------EAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKAR 166
Cdd:PRK10535 102 TAAQNV-EVPAVYaglerkQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG 180
|
170 180
....*....|....*....|..
gi 1045868222 167 RDVWKILQELKQGGLTIFITSH 188
Cdd:PRK10535 181 EEVMAILHQLRDRGHTVIIVTH 202
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-191 |
1.59e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 2 QTAIKVEQLSKAYDNLlavdkiNLSVKCGTVY-----GLLGANGAGKSTTIECILGTKNADSGTVSIlncnpqkdrcrlf 76
Cdd:PRK13409 338 ETLVEYPDLTKKLGDF------SLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP------------- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 qKVGV----QFQEGDYqpEIKVSELcgetacLYEAPADWKS------LCEQFGIGSKIGNAVKSLSGGERQRLFIVLALI 146
Cdd:PRK13409 399 -ELKIsykpQYIKPDY--DGTVEDL------LRSITDDLGSsyykseIIKPLQLERLLDKNVKDLSGGELQRVAIAACLS 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1045868222 147 PNPELVFLDELTTGLDAKARRDVWKILQELKQG-GLTIFITSH---FMD 191
Cdd:PRK13409 470 RDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHdiyMID 518
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
127-207 |
1.84e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 127 AVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQG 206
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
.
gi 1045868222 207 K 207
Cdd:PRK13549 482 K 482
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-162 |
1.89e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSIL-NCNpqkdrcrlfqkVGVQ 82
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSeNAN-----------IGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 83 FQEGDYQPEIKVSelcgetacLYEAPADWKSLC--EQ----------FGiGSKIGNAVKSLSGGERQR-LFIVLALIpNP 149
Cdd:PRK15064 388 AQDHAYDFENDLT--------LFDWMSQWRQEGddEQavrgtlgrllFS-QDDIKKSVKVLSGGEKGRmLFGKLMMQ-KP 457
|
170
....*....|...
gi 1045868222 150 ELVFLDELTTGLD 162
Cdd:PRK15064 458 NVLVMDEPTNHMD 470
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
89-203 |
2.22e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 89 QPEIKVSELCGEtaclyeapadwksLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRD 168
Cdd:PRK10938 107 QDEVKDPARCEQ-------------LAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
90 100 110
....*....|....*....|....*....|....*
gi 1045868222 169 VWKILQELKQGGLTIFITSHFMDEVEILCDEICIL 203
Cdd:PRK10938 174 LAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
130-218 |
2.56e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 130 SLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAV 209
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
....*....
gi 1045868222 210 fyGTVEQAK 218
Cdd:PRK10982 471 --GIVDTKT 477
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-213 |
3.84e-09 |
|
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: 56.29 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAY---DNLLavDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQK-DRCRLFQKVG 80
Cdd:TIGR01193 474 IVINDVSYSYgygSNIL--SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQFQEgdyqPEI---------------KVSELCGETAC-LYEAPADWKSLceQFGIGSKIGNAVKSLSGGERQRLFIVLA 144
Cdd:TIGR01193 552 YLPQE----PYIfsgsilenlllgakeNVSQDEIWAACeIAEIKDDIENM--PLGYQTELSEEGSSISGGQKQRIALARA 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 145 LIPNPELVFLDELTTGLDAKARRDVWKILQELKQGglTIFITSHFMdEVEILCDEICILKQGKAVFYGT 213
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRL-SVAKQSDKIIVLDHGKIIEQGS 691
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-178 |
4.71e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.52 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDN----LLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNAdSGTVSI---------LNCNPQKD 71
Cdd:PRK11022 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMAeklefngqdLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 72 RCRL--------FQ----------KVGVQFQEGdyqpeIKVSElCGETACLYEAPADwksLCEQFGI---GSKIGNAVKS 130
Cdd:PRK11022 83 RRNLvgaevamiFQdpmtslnpcyTVGFQIMEA-----IKVHQ-GGNKKTRRQRAID---LLNQVGIpdpASRLDVYPHQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1045868222 131 LSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQ 178
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQ 201
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-217 |
5.36e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.58 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILG-TKN-----ADS---GTVSILNCNPQKDRCRLFQKVGVQFQEGdyQ 89
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvTKDnwrvtADRmrfDDIDLLRLSPRERRKLVGHNVSMIFQEP--Q 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 90 PEIKVSELCGETacLYEAPADWK-----------------SLCEQFGIGSK---IGNAVKSLSGGERQRLFIVLALIPNP 149
Cdd:PRK15093 100 SCLDPSERVGRQ--LMQNIPGWTykgrwwqrfgwrkrraiELLHRVGIKDHkdaMRSFPYELTEGECQKVMIAIALANQP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 150 ELVFLDELTTGLDAKARRDVWKILQELKQ-GGLTIFITSHFMDEVEILCDEICILKQGKavfygTVEQA 217
Cdd:PRK15093 178 RLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQ-----TVETA 241
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-237 |
6.32e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.49 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAY-DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVsILNCNP-------------- 68
Cdd:PRK10790 340 RIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI-RLDGRPlsslshsvlrqgva 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 69 --QKDRCRLFQKVGVQFQEGDYQPEIKVSELCgETACLyeapADW-KSLCEqfGIGSKIGNAVKSLSGGERQRLFIVLAL 145
Cdd:PRK10790 419 mvQQDPVVLADTFLANVTLGRDISEEQVWQAL-ETVQL----AELaRSLPD--GLYTPLGEQGNNLSVGQKQLLALARVL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 146 IPNPELVFLDELTTGLDAKARRDVWKILQELKQgGLTIFITSHFMDEVeILCDEICILKQGKAVFYGTVEQAKAVSGceK 225
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALAAVRE-HTTLVVIAHRLSTI-VEADTILVLHRGQAVEQGTHQQLLAAQG--R 567
|
250
....*....|...
gi 1045868222 226 FEDAY-LMLSGEE 237
Cdd:PRK10790 568 YWQMYqLQLAGEE 580
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-185 |
7.84e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.44 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 9 QLSKAY-DNLLAVD---KINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV----SILNCNPQKDRCRLF-QKV 79
Cdd:PRK11629 10 NLCKRYqEGSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngQPMSKLSSAAKAELRnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 GVQFQEGDYQPEIKVSE------LCGETAcLYEAPADWKSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVF 153
Cdd:PRK11629 90 GFIYQFHHLLPDFTALEnvamplLIGKKK-PAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190
....*....|....*....|....*....|..
gi 1045868222 154 LDELTTGLDAKARRDVWKILQELKQGGLTIFI 185
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFL 200
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
5-192 |
1.07e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 53.82 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAvdKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN-----PQKdrcrlfQKV 79
Cdd:PRK10771 2 LKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhtttpPSR------RPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 80 GVQFQEGDYQPEIKVSE-----------LCGETACLYEAPAdwkslcEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPN 148
Cdd:PRK10771 74 SMLFQENNLFSHLTVAQniglglnpglkLNAAQREKLHAIA------RQMGIEDLLARLPGQLSGGQRQRVALARCLVRE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1045868222 149 PELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDE 192
Cdd:PRK10771 148 QPILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLED 192
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-213 |
1.32e-08 |
|
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: 54.79 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 3 TAIKVEQLSKAYDNLlavdkiNLSVKCGTVY-----GLLGANGAGKSTTIECILGTKNADSGTVSilncnpqkdrcrlfQ 77
Cdd:COG1245 340 TLVEYPDLTKSYGGF------SLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVD--------------E 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 78 KVGV----QFQEGDYqpEIKVSELcgetacLYEAPAD------WKS-LCEQFGIGSKIGNAVKSLSGGERQRLFIVLALI 146
Cdd:COG1245 400 DLKIsykpQYISPDY--DGTVEEF------LRSANTDdfgssyYKTeIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLS 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1045868222 147 PNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSH---FMDeveILCDEIcilkqgkAVFYGT 213
Cdd:COG1245 472 RDADLYLLDEPSAHLDVEQRLAVAKAIRRFaENRGKTAMVVDHdiyLID---YISDRL-------MVFEGE 532
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-215 |
1.35e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.05 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGT------VSILNCNPQKDRcrlfQKVGVQFQE------G 86
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKvdrngeVSVIAISAGLSG----QLTGIENIEfkmlcmG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 87 DYQPEIKvsELCGETACLYEapadwkslceqfgIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDE-LTTGLDAKA 165
Cdd:PRK13546 115 FKRKEIK--AMTPKIIEFSE-------------LGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEaLSVGDQTFA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1045868222 166 RRDVWKIlQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVE 215
Cdd:PRK13546 180 QKCLDKI-YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELD 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-216 |
1.55e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.95 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSG----------TVSILNcnpQKDRC 73
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllgGRSIFN---YRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 74 RLFQKVGVQFQEGDYQP-EIKVSELCGETACLYEAPADWKSLCEQFGIGSKIGNAVKS--------LSGGERQRLFIVLA 144
Cdd:PRK14271 98 EFRRRVGMLFQRPNPFPmSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDrlsdspfrLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 145 LIPNPELVFLDELTTGLDAKARRDVWKILQELKQgGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQ 216
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAD-RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQ 248
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-188 |
1.58e-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: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 30 GTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQKVGVqfqegdyqpeikvselcgetaclyeapa 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 110 dwkslceqfgigskIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKI------LQELKQGGLTI 183
Cdd:smart00382 54 --------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrllLLLKSEKNLTV 119
|
....*
gi 1045868222 184 FITSH 188
Cdd:smart00382 120 ILTTN 124
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-212 |
1.72e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 27 VKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKdRCRLFQKVGVQFQEGD-YQPEIKVSELCGETACL- 104
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRP-LDSSFQRSIGYVQQQDlHLPTSTVRESLRFSAYLr 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 105 -------YEAPADWKSLCEQFGIGSK----IGNAVKSLSGGERQRLFIVLALIPNPE-LVFLDELTTGLDAKARRDVWKI 172
Cdd:TIGR00956 865 qpksvskSEKMEYVEEVIKLLEMESYadavVGVPGEGLNVEQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSICKL 944
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1045868222 173 LQELKQGGLTIFITSH-----FMDEVeilcDEICILKQG-KAVFYG 212
Cdd:TIGR00956 945 MRKLADHGQAILCTIHqpsaiLFEEF----DRLLLLQKGgQTVYFG 986
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-237 |
4.03e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.36 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSIlncnpqKDRCRLF--------QKVGVQFQE----- 85
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI------KGSAALIaissglngQLTGIENIElkglm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 86 -GDYQPEIKvsELCGEtaclyeapadwksLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAK 164
Cdd:PRK13545 113 mGLTKEKIK--EIIPE-------------IIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQT 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 165 ARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQakAVSGCEKFEDAYLMLSGEE 237
Cdd:PRK13545 178 FTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKE--VVDHYDEFLKKYNQMSVEE 248
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
131-188 |
4.47e-08 |
|
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: 51.00 E-value: 4.47e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 131 LSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELkqggLTIFIT-SH 188
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL----GITVISvGH 146
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
131-213 |
5.55e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 52.90 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 131 LSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFIT---SHFMDeveilCDEICILKQGK 207
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAhrlSTIVD-----ADEILVLEAGR 569
|
....*.
gi 1045868222 208 AVFYGT 213
Cdd:COG5265 570 IVERGT 575
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-174 |
7.26e-08 |
|
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: 51.64 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 25 LSVKCGT-----VYGLLGANGAGKSTTIECILGTKNADSGTVSILNcnpqkdrcrlfQKVGV--QFQEGDYqpEIKVSE- 96
Cdd:cd03237 15 LEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL-----------DTVSYkpQYIKADY--EGTVRDl 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 97 LCGETACLYEAPAdWKS-LCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQ 174
Cdd:cd03237 82 LSSITKDFYTHPY-FKTeIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
122-219 |
7.57e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 122 SKIGNA-VKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELkqggLTIFITSHFM------DEVE 194
Cdd:TIGR00956 200 TKVGNDfVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTS----ANILDTTPLVaiyqcsQDAY 275
|
90 100
....*....|....*....|....*
gi 1045868222 195 ILCDEICILKQGKAVFYGTVEQAKA 219
Cdd:TIGR00956 276 ELFDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
131-188 |
8.17e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.12 E-value: 8.17e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 131 LSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGglTIFIT-SH 188
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG--TTVISvGH 542
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
130-188 |
9.60e-08 |
|
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: 51.62 E-value: 9.60e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 130 SLSGGERQRLFIVLALI---PNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSH 188
Cdd:pfam13304 236 ELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
132-216 |
1.06e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.50 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 132 SGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQG-GLT-IFItSHFMDEVEILCDEICILKQGKAV 209
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSyVFI-SHDLSVVEHIADEVMVMYLGRCV 234
|
....*..
gi 1045868222 210 FYGTVEQ 216
Cdd:PRK11308 235 EKGTKEQ 241
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-219 |
1.22e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.30 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN-PQKDRCRLFQ---KVG 80
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENiPAMSRSRLYTvrkRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 81 VQFQEGDYQPEIKVSELCG----ETACLYEAPADWKSLCEQFGIGSKiGNA---VKSLSGGERQRLFIVLALIPNPELVF 153
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAyplrEHTQLPAPLLHSTVMMKLEAVGLR-GAAklmPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1045868222 154 LDELTTGLDAKARRDVWKILQELKQG-GLTIFITSHFMDEVEILCDEICILKQGKAVFYGTVEQAKA 219
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
124-200 |
1.36e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.75 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 124 IGNAVKSLSGGERQRL---FIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEIlCDEI 200
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLklaYELLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKV-ADYV 881
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
124-185 |
1.50e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 1.50e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1045868222 124 IGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELK--QGGLTIFI 185
Cdd:PTZ00265 573 VGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIII 636
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-203 |
1.52e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 50.48 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 20 VDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV-----SILNCNPQKDRcrlfQKVGVQFQegdyqpeikV 94
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegeDISTLKPEIYR----QQVSYCAQ---------T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 95 SELCGETacLYE-------------APADWKSLCEQFGIGSKIGN-AVKSLSGGERQRlfivLALIPN----PELVFLDE 156
Cdd:PRK10247 90 PTLFGDT--VYDnlifpwqirnqqpDPAIFLDDLERFALPDTILTkNIAELSGGEKQR----ISLIRNlqfmPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1045868222 157 LTTGLDAKARRDVWKILQEL-KQGGLTIFITSHFMDEVEiLCDEICIL 203
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEIN-HADKVITL 210
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-222 |
2.21e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.87 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV---SILNCNPQKD--RCRLFQKVGVQFQEGDY----- 88
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhDIPLTKLQLDswRSRLAVVSQTPFLFSDTvanni 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 89 ---QPEIKVSELcGETACLYEAPADWKSLCEqfGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKA 165
Cdd:PRK10789 410 algRPDATQQEI-EHVARLASVHDDILRLPQ--GYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRT 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 166 RRdvwKILQELKQGG--LTIFITSHFMDEVeILCDEICILKQGKAVFYGTVEQAKAVSG 222
Cdd:PRK10789 487 EH---QILHNLRQWGegRTVIISAHRLSAL-TEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-227 |
3.62e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.68 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIECILGT------KNADSGTVSIlncNPQ---------KDRCrLFqkvGVQFQEGD 87
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGElepsegKIKHSGRISF---SPQtswimpgtiKDNI-IF---GLSYDEYR 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 88 YQPEIKVSELCGETACLyeaPADWKSLCEQFGIgskignavkSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARR 167
Cdd:TIGR01271 518 YTSVIKACQLEEDIALF---PEKDKTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1045868222 168 DVW-KILQELKQGGLTIFITShfmdEVEIL--CDEICILKQGKAVFYGTVEQAKAVS--------GCEKFE 227
Cdd:TIGR01271 586 EIFeSCLCKLMSNKTRILVTS----KLEHLkkADKILLLHEGVCYFYGTFSELQAKRpdfsslllGLEAFD 652
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-188 |
3.91e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.36 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAY-DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV-----SILNCNPQKDRcRLFQK 78
Cdd:PRK10522 323 LELRNVTFAYqDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIlldgkPVTAEQPEDYR-KLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 79 VGVQFQEGDY--QPEikvselcGETAclyeAPADWKSLCEQFGIGSKI---GNAVK--SLSGGERQRLFIVLALIPNPEL 151
Cdd:PRK10522 402 VFTDFHLFDQllGPE-------GKPA----NPALVEKWLERLKMAHKLeleDGRISnlKLSKGQKKRLALLLALAEERDI 470
|
170 180 190
....*....|....*....|....*....|....*...
gi 1045868222 152 VFLDELTTGLDAKARRDVW-KILQELKQGGLTIFITSH 188
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYqVLLPLLQEMGKTIFAISH 508
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
119-209 |
3.91e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.17 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 119 GIGSKIGNavksLSGGERQRlfIVLA--LIPNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFITSHfMDEVEI 195
Cdd:NF040905 397 SVFQKVGN----LSGGNQQK--VVLSkwLFTDPDVLILDEPTRGIDVGAKYEIYTIINELaAEGKGVIVISSE-LPELLG 469
|
90
....*....|....
gi 1045868222 196 LCDEICILKQGKAV 209
Cdd:NF040905 470 MCDRIYVMNEGRIT 483
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-216 |
6.05e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCN----PQ---------KDRCrLFqkvGVQFQEGDYQ 89
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTvayvPQvswifnatvRDNI-LF---GSPFDPERYE 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 90 PEIKVSELCGETACLyeaPAdwkslceqfGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDV 169
Cdd:PLN03130 712 RAIDVTALQHDLDLL---PG---------GDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQV 779
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1045868222 170 W-KILQELKQGGLTIFITS--HFMDEVeilcDEICILKQGKAVFYGTVEQ 216
Cdd:PLN03130 780 FdKCIKDELRGKTRVLVTNqlHFLSQV----DRIILVHEGMIKEEGTYEE 825
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-212 |
7.44e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.47 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSIlncnpqkdrcrlfqkvgvQFQEGDYQPEIKVSELC 98
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIF------------------NGQRIDTLSPGKLQALR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 99 GETACLYEAPadWKSLCEQFGIGSKI-----------GNAVKS----------------------LSGGERQRLFIVLAL 145
Cdd:PRK10261 401 RDIQFIFQDP--YASLDPRQTVGDSImeplrvhgllpGKAAAArvawllervgllpehawrypheFSGGQRQRICIARAL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1045868222 146 IPNPELVFLDELTTGLDAKARRDVWKILQELKQG-GLTIFITSHFMDEVEILCDEICILKQGKAVFYG 212
Cdd:PRK10261 479 ALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
122-188 |
7.46e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 7.46e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1045868222 122 SKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELK-QGGLTIFITSH 188
Cdd:PTZ00265 1350 TNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAH 1417
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-193 |
7.58e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.55 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 10 LSKAYD-NLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSilncnPQKDRcrlfqKVGVQFQEGDY 88
Cdd:TIGR03719 10 VSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR-----PQPGI-----KVGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 89 QPEIKVSEL----CGET-----------ACLYEAPADWKSLCEQFG-------------IGSKIGNA------------V 128
Cdd:TIGR03719 80 DPTKTVRENveegVAEIkdaldrfneisAKYAEPDADFDKLAAEQAelqeiidaadawdLDSQLEIAmdalrcppwdadV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1045868222 129 KSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKqgGLTIFIT--SHFMDEV 193
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP--GTVVAVThdRYFLDNV 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
34-216 |
9.14e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.59 E-value: 9.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 34 GLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQK----DRCRLFQKV---------GVQFQEGDYQPEikvselcgE 100
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgltDLRRVLSIIpqspvlfsgTVRFNIDPFSEH--------N 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 101 TACLYEA--PADWKSLCEQ--FGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWK-ILQE 175
Cdd:PLN03232 1338 DADLWEAleRAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRtIREE 1417
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1045868222 176 LKQggLTIFITSHFMDEVeILCDEICILKQGKAVFYGTVEQ 216
Cdd:PLN03232 1418 FKS--CTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQE 1455
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-213 |
1.22e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 48.25 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 1 MQTAIKVEQLSKAY---------DNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSIlNCNPQK- 70
Cdd:PRK15112 1 VETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI-DDHPLHf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 71 -DRCRLFQKVGVQFQE--GDYQPEIKVSELCGETACL---YEAPADWKSLCE---QFGIGSKIGNAV-KSLSGGERQRLF 140
Cdd:PRK15112 80 gDYSYRSQRIRMIFQDpsTSLNPRQRISQILDFPLRLntdLEPEQREKQIIEtlrQVGLLPDHASYYpHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1045868222 141 IVLALIPNPELVFLDELTTGLDAKARRDVWKILQEL--KQGGLTIFITSHF--MDEVEilcDEICILKQGKAVFYGT 213
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLgmMKHIS---DQVLVMHQGEVVERGS 233
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-206 |
1.22e-06 |
|
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: 47.71 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 16 NLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV---SILNCNPQKDRCRLFQKVGVQFqeGDYQPEI 92
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNKNESEPSFEATRSRNRYSVAY--AAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 93 KVSELcgETACLYEAPAD---WKSLCEQ-----------FGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELT 158
Cdd:cd03290 91 LNATV--EENITFGSPFNkqrYKAVTDAcslqpdidllpFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1045868222 159 TGLDAK-----ARRDVWKILQELKQgglTIFITSHFMDEVeILCDEICILKQG 206
Cdd:cd03290 169 SALDIHlsdhlMQEGILKFLQDDKR---TLVLVTHKLQYL-PHADWIIAMKDG 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
24-193 |
2.04e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 24 NLSVKC--GTVYGLLGANGAGKSTTIECILGTKNADSGTVSIlncNPQKDRCRLFQKvgvQF------------------ 83
Cdd:PRK15064 19 NISVKFggGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL---DPNERLGKLRQD---QFafeeftvldtvimghtel 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 84 ----QEGD--Y-QPE------IKVSELCGETACL--YEAPADWKSLCEQFGIGSKIGNAVKS-LSGGERQRLFIVLALIP 147
Cdd:PRK15064 93 wevkQERDriYaLPEmseedgMKVADLEVKFAEMdgYTAEARAGELLLGVGIPEEQHYGLMSeVAPGWKLRVLLAQALFS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1045868222 148 NPELVFLDELTTGLDAKARRdvWkILQELKQGGLTIFITSH---FMDEV 193
Cdd:PRK15064 173 NPDILLLDEPTNNLDINTIR--W-LEDVLNERNSTMIIISHdrhFLNSV 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-194 |
2.05e-06 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 47.09 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 6 KVEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNAD---SGTVSI----LNCNPQKDRcrlfqK 78
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLngrrLTALPAEQR-----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 79 VGVQFQEGDYQPEIKVSE-LCgetaclYEAPADWK----------SLcEQFGIGSKIGNAVKSLSGGERQRLFIVLALIP 147
Cdd:COG4136 78 IGILFQDDLLFPHLSVGEnLA------FALPPTIGraqrrarveqAL-EEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1045868222 148 NPELVFLDELTTGLDAKARRDV--WkILQELKQGGLTIFITSHFMDEVE 194
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFreF-VFEQIRQRGIPALLVTHDEEDAP 198
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-213 |
2.12e-06 |
|
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: 47.10 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 5 IKVEQLSKAY-DNL-LAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQK-DRCRLFQKVGV 81
Cdd:cd03244 3 IEFKNVSLRYrPNLpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 82 QFQE---------------GDYQPE--IKVSELCGetaclyeapadWKSLCEQF--GIGSKIGNAVKSLSGGERQRLFIV 142
Cdd:cd03244 83 IPQDpvlfsgtirsnldpfGEYSDEelWQALERVG-----------LKEFVESLpgGLDTVVEEGGENLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1045868222 143 LALIPNPELVFLDELTTGLDAKARRDVWKILQElKQGGLTIFITSHFMDEVeILCDEICILKQGKAVFYGT 213
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTI-IDSDRILVLDKGRVVEFDS 220
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-209 |
2.95e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 19 AVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILncnpqkdrcrlFQKVGVQFQEgdyqpeIKVSELC 98
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEIL-----------FDGEVCRFKD------IRDSEAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 99 G-----------------ETACLYEAPA-----DW-------KSLCEQFGIGSKIGNAVKSLSGGERQRLFIVLALIPNP 149
Cdd:NF040905 79 GiviihqelalipylsiaENIFLGNERAkrgviDWnetnrraRELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 150 ELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICILKQGKAV 209
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-232 |
3.12e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.03 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 27 VKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSIlncnpqkDRCRLfqkvgvqfqegDYQPEikvselcgetaclye 106
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-------DGITP-----------VYKPQ--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 107 apadwkslceqfgigsKIgnavkSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQEL-KQGGLTIFI 185
Cdd:cd03222 69 ----------------YI-----DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLsEEGKKTALV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1045868222 186 TSHFMDEVEILCDEICILkQGKAVFYGTVEQAKAV-SGCEKFEDAYLM 232
Cdd:cd03222 128 VEHDLAVLDYLSDRIHVF-EGEPGVYGIASQPKGTrEGINRFLRGYLI 174
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
23-218 |
4.27e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.32 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIECILGTKN--ADSGTVS-----ILNCNPQkDRC-------------------RLF 76
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEfkgkdLLELSPE-DRAgegifmafqypveipgvsnQFF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 77 QKVGV----QFQEGDYQPEIKVSELCGETACLYEAPADWksLCEQFGIGskignavksLSGGERQRLFIVLALIPNPELV 152
Cdd:PRK09580 99 LQTALnavrSYRGQEPLDRFDFQDLMEEKIALLKMPEDL--LTRSVNVG---------FSGGEKKRNDILQMAVLEPELC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1045868222 153 FLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVE-ILCDEICILKQGKAVFYGTVEQAK 218
Cdd:PRK09580 168 ILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDyIKPDYVHVLYQGRIVKSGDFTLVK 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
123-207 |
5.01e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 123 KIGNavksLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILCDEICI 202
Cdd:PRK11288 393 LIMN----LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVV 468
|
....*
gi 1045868222 203 LKQGK 207
Cdd:PRK11288 469 MREGR 473
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-213 |
6.10e-06 |
|
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: 46.00 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTV---SILNCNPQ---------KDRCrLFqkvGVQFQEGDYQP 90
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkhsGRISFSSQfswimpgtiKENI-IF---GVSYDEYRYKS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 91 EIKVSELCGETACLYEApaDWKSLCEQfGIgskignavkSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVW 170
Cdd:cd03291 132 VVKACQLEEDITKFPEK--DNTVLGEG-GI---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIF 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1045868222 171 -KILQELKQGGLTIFITSHfMDEVEIlCDEICILKQGKAVFYGT 213
Cdd:cd03291 200 eSCVCKLMANKTRILVTSK-MEHLKK-ADKILILHEGSSYFYGT 241
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
35-189 |
6.36e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.04 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 35 LLGANGAGKSTTIECI-LGTKNADSGTVSilncnpqkdrcrlfqkvGVQFQEGDYQPEIKVsELCGetaclyeapadwks 113
Cdd:cd03227 26 ITGPNGSGKSTILDAIgLALGGAQSATRR-----------------RSGVKAGCIVAAVSA-ELIF-------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 114 lceqfgigskignAVKSLSGGERQR--LFIVLAL---IPNPeLVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSH 188
Cdd:cd03227 74 -------------TRLQLSGGEKELsaLALILALaslKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
.
gi 1045868222 189 F 189
Cdd:cd03227 140 L 140
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-206 |
1.67e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.74 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 4 AIKVEQLSKAYDNLLA---VDKINLSVKCGTVYGLLGANGAGKSTTIECILG------TKNAD-SGTVS-------ILNC 66
Cdd:PLN03232 614 AISIKNGYFSWDSKTSkptLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGelshaeTSSVViRGSVAyvpqvswIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 67 NPQKDRcrLFqkvGVQFQEGDYQPEIKVSELCGETACLyeaPAdwKSLCEqfgigskIGNAVKSLSGGERQRLFIVLALI 146
Cdd:PLN03232 694 TVRENI--LF---GSDFESERYWRAIDVTALQHDLDLL---PG--RDLTE-------IGERGVNISGGQKQRVSMARAVY 756
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1045868222 147 PNPELVFLDELTTGLDAKARRDVW-KILQELKQGGLTIFITS--HFMDEVE--ILCDEICILKQG 206
Cdd:PLN03232 757 SNSDIYIFDDPLSALDAHVAHQVFdSCMKDELKGKTRVLVTNqlHFLPLMDriILVSEGMIKEEG 821
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-188 |
2.23e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 44.02 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 21 DKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILNCNPQKDRCRLFQK---VGvqfqegdYQPEIKvSEL 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllyLG-------HQPGIK-TEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 98 CGE--------TACLYEAPADWKSLcEQFGIGSKIGNAVKSLSGGERQRlfIVLA--LIPNPELVFLDELTTGLDAKARR 167
Cdd:PRK13538 90 TALenlrfyqrLHGPGDDEALWEAL-AQVGLAGFEDVPVRQLSAGQQRR--VALArlWLTRAPLWILDEPFTAIDKQGVA 166
|
170 180
....*....|....*....|..
gi 1045868222 168 DVWKILQE-LKQGGLTIFiTSH 188
Cdd:PRK13538 167 RLEALLAQhAEQGGMVIL-TTH 187
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
119-200 |
3.58e-05 |
|
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: 43.08 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 119 GIGS-KIGNAVKSLSGGERQRLFIV--LALIPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHfmdEVEI 195
Cdd:cd03238 75 GLGYlTLGQKLSTLSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEH---NLDV 151
|
....*..
gi 1045868222 196 LC--DEI 200
Cdd:cd03238 152 LSsaDWI 158
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-163 |
4.93e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 44.17 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 23 INLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSI---LNCNPQK---DRCRLFQKV--GVQFQEGDYQpeiKV 94
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMkgsVAYVPQQawiQNDSLRENIlfGKALNEKYYQ---QV 733
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1045868222 95 SELCGETACLYEAPAdwkslceqfGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDA 163
Cdd:TIGR00957 734 LEACALLPDLEILPS---------GDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-191 |
5.06e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.79 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 7 VEQLSKAYDNLLAVDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVsilncnpqkdRCRlfQKVGV----Q 82
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----------HCG--TKLEVayfdQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 83 FQEgDYQPEIKVSElcgetaclyeAPADWKSLCEQFGIGSKI--------------GNAVKSLSGGERQRLFIV-LALIP 147
Cdd:PRK11147 390 HRA-ELDPEKTVMD----------NLAEGKQEVMVNGRPRHVlgylqdflfhpkraMTPVKALSGGERNRLLLArLFLKP 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1045868222 148 NpELVFLDELTTGLDAkarrDVWKILQEL---KQGglTIFITSH---FMD 191
Cdd:PRK11147 459 S-NLLILDEPTNDLDV----ETLELLEELldsYQG--TVLLVSHdrqFVD 501
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
123-191 |
9.09e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.08 E-value: 9.09e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 123 KIGNAVKSLSGGERQRLFIVLAL---IPNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMD 191
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLD 893
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
128-175 |
2.02e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 39.14 E-value: 2.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1045868222 128 VKSLSGGERQRLF---IVLALI----------PNPELVFLDELTTGLDAKARRDVWKILQE 175
Cdd:pfam13558 30 SGGLSGGEKQLLAylpLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
128-208 |
2.36e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.53 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 128 VKSLSGGERQRLFIVLALI-------PNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSH---FMDEVEIlc 197
Cdd:COG3593 160 LDRLGSGFQRLILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHsphLLSEVPL-- 237
|
90
....*....|.
gi 1045868222 198 DEICILKQGKA 208
Cdd:COG3593 238 ENIRRLRRDSG 248
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
118-215 |
3.91e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 118 FGIGSKIGNAVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWK-ILQELKqgGLTIFITSHFMDEVeIL 196
Cdd:PLN03130 1362 LGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKtIREEFK--SCTMLIIAHRLNTI-ID 1438
|
90
....*....|....*....
gi 1045868222 197 CDEICILKQGKAVFYGTVE 215
Cdd:PLN03130 1439 CDRILVLDAGRVVEFDTPE 1457
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
123-200 |
4.33e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 40.29 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 123 KIGNAVKSLSGGERQRLFIVLALI---PNPELVFLDELTTGL---DAKARRDVwkiLQELKQGGLTIFITSHFMDEVEIl 196
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLhfhDVKKLLEV---LQRLVDKGNTVVVIEHNLDVIKC- 237
|
....
gi 1045868222 197 CDEI 200
Cdd:cd03271 238 ADWI 241
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-205 |
5.59e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.54 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 20 VDKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSGTVSILN------CNPQK------------DRCRLFQKVGV 81
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawVNQETpalpqpaleyviDGDREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 82 QFQEGDYQPE-IKVSELCGEtaclYEAPADW------KSLCEQFGIGS-KIGNAVKSLSGGERQRLFIVLALIPNPELVF 153
Cdd:PRK10636 97 QLHDANERNDgHAIATIHGK----LDAIDAWtirsraASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQALICRSDLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 154 LDELTTGLDAKARrdVWkILQELKQGGLTIFITSHFMDEVEILCDEICILKQ 205
Cdd:PRK10636 173 LDEPTNHLDLDAV--IW-LEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-163 |
7.24e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.10 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 10 LSKAYDNLLAV-DKINLSVKCGTVYGLLGANGAGKSTTIECILGTKNADSG--------TVSILNCNPQ----------- 69
Cdd:PRK11819 12 VSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGearpapgiKVGYLPQEPQldpektvrenv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 70 -------KDRCRLFQKVGVQFQEgdyqPEIKVSELCGETACLYEA-----------------------PADWKslceqfg 119
Cdd:PRK11819 92 eegvaevKAALDRFNEIYAAYAE----PDADFDALAAEQGELQEIidaadawdldsqleiamdalrcpPWDAK------- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1045868222 120 igskignaVKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDA 163
Cdd:PRK11819 161 --------VTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
128-206 |
2.85e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 38.80 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 128 VKSLSGGERQRLFIVLALI----------PNPELVFLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHFMDEVEILC 197
Cdd:TIGR00618 948 SATLSGGETFLASLSLALAladllstsggTVLDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERIP 1027
|
....*....
gi 1045868222 198 DEICILKQG 206
Cdd:TIGR00618 1028 HRILVKKTN 1036
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
127-214 |
3.58e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 127 AVKSLSGGERQRlfIVLALIPNPELV----FLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHfmDEVEI-LCDEIC 201
Cdd:PRK00635 473 ALATLSGGEQER--TALAKHLGAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEH--DEQMIsLADRII 548
|
90
....*....|...
gi 1045868222 202 ILKQGKAVFYGTV 214
Cdd:PRK00635 549 DIGPGAGIFGGEV 561
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
130-196 |
6.37e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 36.85 E-value: 6.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1045868222 130 SLSGGERQRLFIVLALipNPELV----FLDELTTGLDAKARRDVWKILQELKQGGLTIFITSHfmDEVEIL 196
Cdd:cd03270 137 TLSGGEAQRIRLATQI--GSGLTgvlyVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEH--DEDTIR 203
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
104-191 |
7.63e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 36.92 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045868222 104 LYEAPAD--------WKSLceqFGIGSKIGNA-VKSLSGGERQRLFIVLALIPNPELVFLDELTTGLDAKARRDVWKILQ 174
Cdd:PRK10938 369 IYQAVSDrqqklaqqWLDI---LGIDKRTADApFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVD 445
|
90
....*....|....*....
gi 1045868222 175 ELKQGGLT--IFITSHFMD 191
Cdd:PRK10938 446 VLISEGETqlLFVSHHAED 464
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
128-192 |
9.26e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 36.47 E-value: 9.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1045868222 128 VKSLSGGerQRLFIVLALI-------PNPeLVFLDELTTGLDAKARRDVWKILQELKQGglTIFITSHFMDE 192
Cdd:cd03272 156 MQQLSGG--QKSLVALALIfaiqkcdPAP-FYLFDEIDAALDAQYRTAVANMIKELSDG--AQFITTTFRPE 222
|
|
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