|
Name |
Accession |
Description |
Interval |
E-value |
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-244 |
8.27e-144 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 408.70 E-value: 8.27e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 1 MSY-IRVNNVGKAYRQYHSKTGRLIEWLSPLNTKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTT 79
Cdd:COG1134 1 MSSmIEVENVSKSYRLYHEPSRSLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 80 GEIEISGRVAALLELGMGFHSDFTGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVA 159
Cdd:COG1134 81 GRVEVNGRVSALLELGAGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 160 TAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMDYYNAL 239
Cdd:COG1134 161 TAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAYEAL 240
|
....*
gi 446042612 240 LADKQ 244
Cdd:COG1134 241 LAGRE 245
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-227 |
2.17e-105 |
|
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: 310.23 E-value: 2.17e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYRQYHSKTGRLIEWLSPLNTKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE 83
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 84 ISGRVAALLELGMGFHSDFTGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIR 163
Cdd:cd03220 81 VRGRVSSLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446042612 164 PDVLIIDEALSVGDAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEG 227
Cdd:cd03220 161 PDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1-258 |
6.72e-62 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 208.59 E-value: 6.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 1 MSY-IRVNNVGKAYRQYHSKTGRLIEWLspLNTKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTT 79
Cdd:PRK13545 1 MNYkVKFEHVTKKYKMYNKPFDKLKDLF--FRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 80 GEIEISGRvAALLELGMGFHSDFTGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVA 159
Cdd:PRK13545 79 GTVDIKGS-AALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 160 TAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMDYYNAL 239
Cdd:PRK13545 158 VHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEF 237
|
250
....*....|....*....
gi 446042612 240 LADKQNQSIKQVEHNGKTQ 258
Cdd:PRK13545 238 LKKYNQMSVEERKDFREEQ 256
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
4-253 |
1.58e-55 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 183.86 E-value: 1.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYRQYHSKTGRLIEWLSPLNtkRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE 83
Cdd:PRK13546 5 VNIKNVTKEYRIYRTNKERMKDALIPKH--KNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 84 ISGRVAaLLELGMGFHSDFTGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIR 163
Cdd:PRK13546 83 RNGEVS-VIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 164 PDVLIIDEALSVGDAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMDYYNALLADK 243
Cdd:PRK13546 162 PDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDF 241
|
250
....*....|
gi 446042612 244 QNQSIKQVEH 253
Cdd:PRK13546 242 KKKSKAEQKE 251
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
32-236 |
2.90e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 171.79 E-value: 2.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG------------RVAALLElGMGFH 99
Cdd:COG1131 7 TKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQ-EPALY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 100 SDFTGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSvG-DA 178
Cdd:COG1131 86 PDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS-GlDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446042612 179 YFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMDYY 236
Cdd:COG1131 165 EARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| Wzt_C-like |
cd10147 |
C-Terminal domain of O-antigenic polysaccharide transporter protein Wzt and related proteins; ... |
261-400 |
4.90e-43 |
|
C-Terminal domain of O-antigenic polysaccharide transporter protein Wzt and related proteins; The Escherichia coli ABC protein Wzt consists of 2 domains, a conventional ABC domain that binds ATP and utilizes its energy to transport molecules across membranes, and a C terminal domain which is responsible for its target molecule specificity. Wzt is part of the ATP-binding-cassette (ABC) transporter complex, responsible for the transport of the O-antigenic polysaccharide (O-PS) portion of lipopolysaccharide (LPS), a major component of the outer membrane of Gram-negative bacteria. This CD includes Wzt proteins from two Escherichia coli serotypes O8 and O9a, WztO8 and WztO9a; these proteins are specific for their cognate polysaccharides (O8 or O9a O-PS).
Pssm-ID: 199902 Cd Length: 144 Bit Score: 147.12 E-value: 4.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 261 SGTGEVTISEVHLLDEQGNVTEFVSVGHRVSLQVNVEVKDDIPELVVGYMIKDRLGQPIFGTNTYHLNQTLTSLKKGEKR 340
Cdd:cd10147 5 FGSGGARITDVELLDEDGEPVNTFRSGEPVTLRIEYEVNEDIEDPVVGFTIKDRDGQDVFGTNTLLLGGVLPSLKAGGEG 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 341 SFLFSFDARLGVGSYSVAVALHTSSTHLgKNYEWRDLAVVFNVVNTEQQEFVGVSWLPPE 400
Cdd:cd10147 85 EVEFTFPLPLNPGEYSLSVALADGDGHH-EVLDWIDDALSFEVESSSKSLFVGLVDLPHE 143
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
32-234 |
5.93e-43 |
|
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: 150.39 E-value: 5.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG------RVAALLELGM-----GFHS 100
Cdd:COG4555 8 SKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkePREARRQIGVlpderGLYD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 101 DFTGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYF 180
Cdd:COG4555 88 RLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446042612 181 QHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMD 234
Cdd:COG4555 168 RRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| Wzt_C |
pfam14524 |
Wzt C-terminal domain; This domain is found at the C-terminus of the Wzt protein. The crystal ... |
261-397 |
8.75e-41 |
|
Wzt C-terminal domain; This domain is found at the C-terminus of the Wzt protein. The crystal structure of C-Wzt(O9a) reveals a beta sandwich with an immunoglobulin-like topology that contains the O-antigenic polysaccharide binding pocket. This domain is often associated with the ABC-transporter domain.
Pssm-ID: 464200 Cd Length: 141 Bit Score: 141.31 E-value: 8.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 261 SGTGEVTISEVHLLDEQGNVTEFVSVGHRVSLQVNVEVKDDIPELVVGYMIKDRLGQPIFGTNTYHLNQTLTSLKKGEKR 340
Cdd:pfam14524 3 YGSGEAEIIDVELLDEDGKPTNTFESGEEVTLRIKVRFHEDVEDPIFGFTIKDRLGQEVFGTNTFLEGKSLGALKAGEVV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 446042612 341 SFLFSFDARLGVGSYSVAVALHTSS--THLGKNYEWRDLAVVFNVVNTEQQEFVGVSWL 397
Cdd:pfam14524 83 EVEFRFKLNLQPGEYLLSVAIEDADgeQHEHVVYDWLDDALVFEVGVSSKNVFVGLVDL 141
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
32-227 |
7.60e-39 |
|
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: 138.50 E-value: 7.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG-----------RVAALLElGMGFHS 100
Cdd:cd03268 7 TKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGksyqkniealrRIGALIE-APGFYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 101 DFTGRQNVYMSGQLLGLSSEKITElmpqIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYF 180
Cdd:cd03268 86 NLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446042612 181 QHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEG 227
Cdd:cd03268 162 IKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
32-223 |
1.55e-38 |
|
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: 136.37 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG------------RVAALLElGMGFH 99
Cdd:cd03230 7 SKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikkepeevkrRIGYLPE-EPSLY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 100 SDFTGRQNVYMSGqllglssekitelmpqieefaeigdyidqpvrvyssGMQVRLAFSVATAIRPDVLIIDEALSVGDAY 179
Cdd:cd03230 86 ENLTVRENLKLSG------------------------------------GMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446042612 180 FQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQI 223
Cdd:cd03230 130 SRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
38-239 |
7.28e-38 |
|
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: 136.31 E-value: 7.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRV---AALLEL----GMGFhsdftgrQNVYM 110
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDitkKNLRELrrkvGLVF-------QNPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 111 sgQL---------------LGLSSEKITElmpQIEEFAE---IGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEA 172
Cdd:COG1122 87 --QLfaptveedvafgpenLGLPREEIRE---RVEEALElvgLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446042612 173 LSVGDAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMDYYNAL 239
Cdd:COG1122 162 TAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-234 |
1.36e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 136.37 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 1 MSYIRVNNVGKAYRQyhsktgrliewlsplntkrhnlKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTG 80
Cdd:COG1121 4 MPAIELENLTVSYGG----------------------RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 81 EIEISGRVAALLELGMG-------FHSDF--TGRQNVYM-----SGQLLGLSS---EKITELMpqieEFAEIGDYIDQPV 143
Cdd:COG1121 62 TVRLFGKPPRRARRRIGyvpqraeVDWDFpiTVRDVVLMgrygrRGLFRRPSRadrEAVDEAL----ERVGLEDLADRPI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 144 RVYSSGMQ--VRLAFSVATaiRPDVLIIDEALSvG-DAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNK 220
Cdd:COG1121 138 GELSGGQQqrVLLARALAQ--DPDLLLLDEPFA-GvDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNR 214
|
250
....*....|....
gi 446042612 221 GQIEmEGEPEAVMD 234
Cdd:COG1121 215 GLVA-HGPPEEVLT 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
40-229 |
8.93e-37 |
|
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: 133.40 E-value: 8.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG------RVAALLELGMGFHSD-----FTGRQNV 108
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdRKAARQSLGYCPQFDalfdeLTVREHL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 109 YMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERI 188
Cdd:cd03263 97 RFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446042612 189 RKFRQeGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEP 229
Cdd:cd03263 177 LEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
41-233 |
1.86e-36 |
|
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: 132.95 E-value: 1.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEI-----EISG-RVAALLELGMG--------FHSdFTGRQ 106
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeDITGlPPHEIARLGIGrtfqiprlFPE-LTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 107 NVYMSGQ-------LLGLSSEKITELMPQIEEFAE---IGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDE---AL 173
Cdd:cd03219 95 NVMVAAQartgsglLLARARREEREARERAEELLErvgLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEpaaGL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 174 SVGDAyfqHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVM 233
Cdd:cd03219 175 NPEET---EELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-227 |
4.93e-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: 131.69 E-value: 4.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYRQyHSKTGRLIEWLSPLNTKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE 83
Cdd:cd03267 1 IEVSNLSKSYRV-YSKEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 84 ISGRV--------AALLELGMGFHS----DFTGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQ 151
Cdd:cd03267 80 VAGLVpwkrrkkfLRRIGVVFGQKTqlwwDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 152 VRLAFSVATAIRPDVLIIDEAlSVG-DAYFQHKsferIRKF-----RQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEM 225
Cdd:cd03267 160 MRAEIAAALLHEPEILFLDEP-TIGlDVVAQEN----IRNFlkeynRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
..
gi 446042612 226 EG 227
Cdd:cd03267 235 DG 236
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
40-221 |
5.17e-35 |
|
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: 128.42 E-value: 5.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLELGMGF---HSDF------TGRQNVYM 110
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYvpqRRSIdrdfpiSVRDVVLM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 111 -----SGQLLGLSSE---KITELMpqieEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQH 182
Cdd:cd03235 94 glyghKGLFRRLSKAdkaKVDEAL----ERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQE 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 446042612 183 KSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKG 221
Cdd:cd03235 170 DIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
32-230 |
2.42e-34 |
|
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: 126.72 E-value: 2.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG-----------RVAALLELGMGFHS 100
Cdd:cd03265 7 VKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrRRIGIVFQDLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 101 DFTGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEAlSVG-DAY 179
Cdd:cd03265 87 ELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP-TIGlDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446042612 180 FQHKSFERIRKF-RQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPE 230
Cdd:cd03265 166 TRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
32-234 |
2.58e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 129.95 E-value: 2.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG----RVAALLELGMG-------FHS 100
Cdd:PRK13536 48 SKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpARARLARARIGvvpqfdnLDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 101 DFTGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYF 180
Cdd:PRK13536 128 EFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446042612 181 QHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMD 234
Cdd:PRK13536 208 RHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
38-222 |
6.92e-34 |
|
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: 125.27 E-value: 6.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLELgmgfhsdFTGRQNVYMSGQ---- 113
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSL-------KELRRKVGLVFQnpdd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 114 ----------------LLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGD 177
Cdd:cd03225 87 qffgptveeevafgleNLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446042612 178 AYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQ 222
Cdd:cd03225 167 PAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
33-234 |
1.92e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 126.84 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 33 KRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG------------RVAALLELGmGFHS 100
Cdd:PRK13537 15 KRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsrarharqRVGVVPQFD-NLDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 101 DFTGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYF 180
Cdd:PRK13537 94 DFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446042612 181 QHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMD 234
Cdd:PRK13537 174 RHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
32-222 |
2.14e-33 |
|
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: 122.35 E-value: 2.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLELgmgfhsdFTGRQNVYMS 111
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL-------EELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 112 GQLlglssekitelmpqieefaeigdyidqpvrvySSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKF 191
Cdd:cd00267 79 PQL--------------------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL 126
|
170 180 190
....*....|....*....|....*....|.
gi 446042612 192 RQEGTTLLLVSHDKQAIQSICDRAILLNKGQ 222
Cdd:cd00267 127 AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
41-227 |
3.18e-33 |
|
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: 124.02 E-value: 3.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG----RVAALLELGMGFHSD-------FTGRQNVY 109
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvKEPAEARRRLGFVSDstglydrLTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 110 MSGQLLGLsseKITELMPQIEEFA---EIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFE 186
Cdd:cd03266 101 YFAGLYGL---KGDELTARLEELAdrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALRE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446042612 187 RIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEG 227
Cdd:cd03266 178 FIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
40-234 |
3.40e-33 |
|
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: 123.70 E-value: 3.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR-VAAL-----LELGMGF-------HSDFTGRQ 106
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRdITGLppherARAGIGYvpegrriFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 107 NVYMSGQLLGLSS-----EKITELMPQIEEFAeigdyiDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEAlSVGDA-YF 180
Cdd:cd03224 95 NLLLGAYARRRAKrkarlERVYELFPRLKERR------KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP-SEGLApKI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446042612 181 QHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMD 234
Cdd:cd03224 168 VEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
32-204 |
5.05e-33 |
|
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: 122.97 E-value: 5.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG------RVAALLELGM-----GFHS 100
Cdd:COG4133 9 SCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaREDYRRRLAYlghadGLKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 101 DFTGRQNVYMSGQLLGL--SSEKITELMpqieEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDE---ALSV 175
Cdd:COG4133 89 ELTVRENLRFWAALYGLraDREAIDEAL----EAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEpftALDA 164
|
170 180 190
....*....|....*....|....*....|
gi 446042612 176 -GDAYFQhksfERIRKFRQEGTTLLLVSHD 204
Cdd:COG4133 165 aGVALLA----ELIAAHLARGGAVLLTTHQ 190
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-223 |
7.95e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 125.58 E-value: 7.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYRQYHSKTGrLIEWLSPLNTKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE 83
Cdd:COG4586 2 IEVENLSKTYRVYEKEPG-LKGALKGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 84 ISG------RVAALLELG--MGFHS----DFTGRQNVYMSGQLLGLSSEKITELMpqiEEFAE---IGDYIDQPVRVYSS 148
Cdd:COG4586 81 VLGyvpfkrRKEFARRIGvvFGQRSqlwwDLPAIDSFRLLKAIYRIPDAEYKKRL---DELVElldLGELLDTPVRQLSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 149 GMQVRLAFSVATAIRPDVLIIDEA---LSVgdayfqhKSFERIRKF-----RQEGTTLLLVSHDKQAIQSICDRAILLNK 220
Cdd:COG4586 158 GQRMRCELAAALLHRPKILFLDEPtigLDV-------VSKEAIREFlkeynRERGTTILLTSHDMDDIEALCDRVIVIDH 230
|
...
gi 446042612 221 GQI 223
Cdd:COG4586 231 GRI 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
41-233 |
3.31e-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: 122.07 E-value: 3.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR------VAALLELGMG--------FhSDFTGRQ 106
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglpPHRIARLGIArtfqnprlF-PELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 107 NVYMSGQ----------LLGLSS---------EKITELMpqieEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVL 167
Cdd:COG0411 99 NVLVAAHarlgrgllaaLLRLPRarreerearERAEELL----ERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 168 IIDE--A-LSVGDAyfqHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVM 233
Cdd:COG0411 175 LLDEpaAgLNPEET---EELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVR 241
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
32-227 |
3.36e-32 |
|
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: 120.85 E-value: 3.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR-VAALLELGMGFHSDFTG------ 104
Cdd:cd03269 7 TKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpLDIAARNRIGYLPEERGlypkmk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 105 --RQNVYMsGQLLGLsseKITELMPQIEEFAE---IGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAY 179
Cdd:cd03269 87 viDQLVYL-AQLKGL---KKEEARRRIDEWLErleLSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446042612 180 FQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEG 227
Cdd:cd03269 163 NVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
40-224 |
4.80e-32 |
|
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: 120.32 E-value: 4.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALL-----ELGMGFHSD-----FTGRQNVY 109
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVpperrNIGMVFQDYalfphLTVAENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 110 MSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAyfqhKSFERIR 189
Cdd:cd03259 95 FGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDA----KLREELR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446042612 190 K-----FRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIE 224
Cdd:cd03259 171 EelkelQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
40-234 |
1.28e-31 |
|
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: 119.91 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR------VAALLEL----GMGFHS-----DFTG 104
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglsEAELYRLrrrmGMLFQSgalfdSLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 105 RQNV-YMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHK 183
Cdd:cd03261 95 FENVaFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446042612 184 SFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMD 234
Cdd:cd03261 175 IDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-241 |
2.05e-31 |
|
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: 119.91 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYRQyhsktgrliewlsplntkRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE 83
Cdd:COG1124 2 LEVRNLSVSYGQ------------------GGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVT 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 84 ISGRvaallELGMGFHSDFTGR-----QNVYMS-------GQLLG--LSSEKITELMPQIEEFAEI----GDYIDQPVRV 145
Cdd:COG1124 64 FDGR-----PVTRRRRKAFRRRvqmvfQDPYASlhprhtvDRILAepLRIHGLPDREERIAELLEQvglpPSFLDRYPHQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 146 YSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIE 224
Cdd:COG1124 139 LSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
250 260
....*....|....*....|..
gi 446042612 225 MEGEPEAV-----MDYYNALLA 241
Cdd:COG1124 219 EELTVADLlagpkHPYTRELLA 240
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
38-242 |
3.34e-31 |
|
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: 119.38 E-value: 3.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR---------VA---ALLELGMGFHSDFTGR 105
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaslsrreLArriAYVPQEPPAPFGLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 106 QNVYM-----SGQLLGLSSE---KITELMpqieEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDE---ALs 174
Cdd:COG1120 94 ELVALgryphLGLFGRPSAEdreAVEEAL----ERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEptsHL- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 175 vgDAYFQHKSFERIRKF-RQEGTTLLLVSHD-KQAIQsICDRAILLNKGQIEMEGEPEAVMDyyNALLAD 242
Cdd:COG1120 169 --DLAHQLEVLELLRRLaRERGRTVVMVLHDlNLAAR-YADRLVLLKDGRIVAQGPPEEVLT--PELLEE 233
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-232 |
1.31e-30 |
|
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: 117.30 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYRQYHSKTGrliewlsplntkrhnlkwILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE 83
Cdd:cd03258 2 IELKNVSKVFGDTGGKVT------------------ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 84 ISGRVAALL----------ELGMGFH-----SDFTGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSS 148
Cdd:cd03258 64 VDGTDLTLLsgkelrkarrRIGMIFQhfnllSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 149 GMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEG 227
Cdd:cd03258 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEG 223
|
....*
gi 446042612 228 EPEAV 232
Cdd:cd03258 224 TVEEV 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
34-227 |
3.30e-29 |
|
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: 111.76 E-value: 3.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 34 RHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR-VAAllelgmgfhsdftgrqnvyMSG 112
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdLAS-------------------LSP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 113 QLLglsSEKITeLMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKF- 191
Cdd:cd03214 69 KEL---ARKIA-YVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLa 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 446042612 192 RQEGTTLLLVSHD-KQAIQsICDRAILLNKGQIEMEG 227
Cdd:cd03214 145 RERGKTVVMVLHDlNLAAR-YADRVILLKDGRIVAQG 180
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-223 |
6.18e-29 |
|
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: 112.20 E-value: 6.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYRQyhsktgrliewlsplntkRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE 83
Cdd:cd03255 1 IELKNLSKTYGG------------------GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 84 ISGRVAALL-----------ELGMGFHS-----DFTGRQNVYMSGQLLGLSSEkitELMPQIEEFAE---IGDYIDQPVR 144
Cdd:cd03255 63 VDGTDISKLsekelaafrrrHIGFVFQSfnllpDLTALENVELPLLLAGVPKK---ERRERAEELLErvgLGDRLNHYPS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 145 VYSSGMQVRLAFSVATAIRPDVLIIDE---ALsvgDAYFQHKSFERIRKF-RQEGTTLLLVSHDKQaIQSICDRAILLNK 220
Cdd:cd03255 140 ELSGGQQQRVAIARALANDPKIILADEptgNL---DSETGKEVMELLRELnKEAGTTIVVVTHDPE-LAEYADRIIELRD 215
|
...
gi 446042612 221 GQI 223
Cdd:cd03255 216 GKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
34-241 |
7.34e-29 |
|
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: 117.70 E-value: 7.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 34 RHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPT---TGEIEISGRVAALL-------ELGMGFHSDFT 103
Cdd:COG1123 15 PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELsealrgrRIGMVFQDPMT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 104 -------GRQnVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVG 176
Cdd:COG1123 95 qlnpvtvGDQ-IAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTAL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446042612 177 DAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMDYYNALLA 241
Cdd:COG1123 174 DVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAA 239
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-292 |
9.02e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 114.05 E-value: 9.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR---VAALLELG-M----GFHSDFT 103
Cdd:COG4152 8 TKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEpldPEDRRRIGyLpeerGLYPKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 104 -GRQNVYMsGQLLGLSS----EKITELMpqiEEFaEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSvG-D 177
Cdd:COG4152 88 vGEQLVYL-ARLKGLSKaeakRRADEWL---ERL-GLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS-GlD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 178 AYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMDYY----------NALLADKQNQS 247
Cdd:COG4152 162 PVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFgrntlrleadGDAGWLRALPG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446042612 248 IKQVEHNGKTQTVSGTGEVTISEV-HLLDEQGNVTEFVSVghRVSL 292
Cdd:COG4152 242 VTVVEEDGDGAELKLEDGADAQELlRALLARGPVREFEEV--RPSL 285
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-223 |
2.29e-28 |
|
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: 111.06 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYRqyhsktgrliewlsplnTKRHNLKwILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE 83
Cdd:cd03257 2 LEVKNLSVSFP-----------------TGGGSVK-ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSII 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 84 ISGRVaaLLELGMGFHSDFTGR-----QNVYMS-------GQLLG-------------LSSEKITELMPQIEEFAEIGD- 137
Cdd:cd03257 64 FDGKD--LLKLSRRLRKIRRKEiqmvfQDPMSSlnprmtiGEQIAeplrihgklskkeARKEAVLLLLVGVGLPEEVLNr 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 138 YIDQpvrvYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAI 216
Cdd:cd03257 142 YPHE----LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVA 217
|
....*..
gi 446042612 217 LLNKGQI 223
Cdd:cd03257 218 VMYAGKI 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
41-174 |
7.22e-28 |
|
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: 107.35 E-value: 7.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRV-------AALLELGMGFHSDF-----TGRQNV 108
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkSLRKEIGYVFQDPQlfprlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 109 YMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVY----SSGMQVRLAFSVATAIRPDVLIIDEALS 174
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERpgtlSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
40-234 |
1.83e-27 |
|
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: 108.92 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR------VAALLELGMG--------FhSDFTGR 105
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpPHRIARLGIGyvpegrriF-PSLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 106 QNVYMSGQLLGLSS------EKITELMPQIEEFAeigdyiDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEAlSVGDA- 178
Cdd:COG0410 97 ENLLLGAYARRDRAevradlERVYELFPRLKERR------RQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP-SLGLAp 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446042612 179 YFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMD 234
Cdd:COG0410 170 LIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
32-234 |
3.33e-27 |
|
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: 108.14 E-value: 3.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR------VAALLEL----GMGFH-- 99
Cdd:COG1127 12 TKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditglsEKELYELrrriGMLFQgg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 100 ---SDFTGRQNV--YMSgQLLGLSSEKITEL---------MPQIEEF--AEIgdyidqpvrvySSGMQVRLAFSVATAIR 163
Cdd:COG1127 92 alfDSLTVFENVafPLR-EHTDLSEAEIRELvleklelvgLPGAADKmpSEL-----------SGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446042612 164 PDVLIIDEALS----VGDAYFQhksfERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMD 234
Cdd:COG1127 160 PEILLYDEPTAgldpITSAVID----ELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
32-224 |
3.19e-26 |
|
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: 104.64 E-value: 3.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLE-----LGMGFHS-----D 101
Cdd:cd03301 7 TKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpkdrdIAMVFQNyalypH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 102 FTGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQ 181
Cdd:cd03301 87 MTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446042612 182 HKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIE 224
Cdd:cd03301 167 VQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-241 |
4.47e-26 |
|
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: 109.61 E-value: 4.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYRQYHSKTGRliewlsplntkrhnlkwILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE 83
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVR-----------------AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 84 ISGR-VAALL---------ELGMGFhsdftgrQNVYMS-------GQ-------LLGLSSEKitELMPQIEEFAEI---- 135
Cdd:COG1123 324 FDGKdLTKLSrrslrelrrRVQMVF-------QDPYSSlnprmtvGDiiaeplrLHGLLSRA--ERRERVAELLERvglp 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 136 GDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDR 214
Cdd:COG1123 395 PDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADR 474
|
250 260 270
....*....|....*....|....*....|..
gi 446042612 215 AILLNKGQIEMEGEPEAVMD-----YYNALLA 241
Cdd:COG1123 475 VAVMYDGRIVEDGPTEEVFAnpqhpYTRALLA 506
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
38-233 |
4.65e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.58 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR-VAAL--LEL-----------GMGFhsDFT 103
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRpLAAWspWELarrravlpqhsSLAF--PFT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 104 GRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQ--VRLAFSVA-----TAIRPDVLIIDEALSVG 176
Cdd:COG4559 92 VEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQqrVQLARVLAqlwepVDGGPRWLFLDEPTSAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446042612 177 DAYFQHKSFERIRKFRQEGTTLLLVSHD-KQAIQsICDRAILLNKGQIEMEGEPEAVM 233
Cdd:COG4559 172 DLAHQHAVLRLARQLARRGGGVVAVLHDlNLAAQ-YADRILLLHQGRLVAQGTPEEVL 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-223 |
7.92e-26 |
|
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: 105.27 E-value: 7.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 2 SYIRVNNVGKAYRqyhskTGRLIewlsplntKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGE 81
Cdd:TIGR02769 1 SLLEVRDVTHTYR-----TGGLF--------GAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 82 IEISG----------RVAALLELGMGFHsDFTGRQNVYMS-GQLLG-----LSS-------EKITELMPQIEEFAEIGDY 138
Cdd:TIGR02769 68 VSFRGqdlyqldrkqRRAFRRDVQLVFQ-DSPSAVNPRMTvRQIIGeplrhLTSldeseqkARIAELLDMVGLRSEDADK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 139 IDQPVrvySSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAIL 217
Cdd:TIGR02769 147 LPRQL---SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAV 223
|
....*.
gi 446042612 218 LNKGQI 223
Cdd:TIGR02769 224 MDKGQI 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
41-223 |
1.25e-25 |
|
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: 101.74 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAAllelgmgFHSDFTGRQN-VYMSGQLlglss 119
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS-------FASPRDARRAgIAMVYQL----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 120 ekitelmpqieefaeigdyidqpvrvySSGMQVRLAFSVATAIRPDVLIIDE---ALSVGDAyfqHKSFERIRKFRQEGT 196
Cdd:cd03216 84 ---------------------------SVGERQMVEIARALARNARLLILDEptaALTPAEV---ERLFKVIRRLRAQGV 133
|
170 180
....*....|....*....|....*..
gi 446042612 197 TLLLVSHDKQAIQSICDRAILLNKGQI 223
Cdd:cd03216 134 AVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
40-223 |
3.42e-25 |
|
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: 101.56 E-value: 3.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLEL--GMGFHSDFTGRQ--------NVY 109
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERrkSIGYVMQDVDYQlftdsvreELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 110 MSGQLLGLSSEKITELMPQIeefaEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIR 189
Cdd:cd03226 95 LGLKELDAGNEQAETVLKDL----DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIR 170
|
170 180 190
....*....|....*....|....*....|....
gi 446042612 190 KFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQI 223
Cdd:cd03226 171 ELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
41-241 |
5.27e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 103.17 E-value: 5.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVaaLLE---------LGMGFH---SDFTG---R 105
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV--LSEetvwdvrrqVGMVFQnpdNQFVGatvQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 106 QNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQ-PVRVySSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKS 184
Cdd:PRK13635 101 DDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNRePHRL-SGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446042612 185 FERIRKFRQEGT-TLLLVSHD-KQAIQSicDRAILLNKGQIEMEGEPEAVMDYYNALLA 241
Cdd:PRK13635 180 LETVRQLKEQKGiTVLSITHDlDEAAQA--DRVIVMNKGEILEEGTPEEIFKSGHMLQE 236
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
38-233 |
5.49e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.54 E-value: 5.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAA---LLEL-----------GMGFhsDFT 103
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwsPAELarrravlpqhsSLSF--PFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 104 GRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFS-V-----ATAIRPDVLIIDEALSVGD 177
Cdd:PRK13548 93 VEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArVlaqlwEPDGPPRWLLLDEPTSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446042612 178 AYFQHKSFERIRKF-RQEGTTLLLVSHD-KQAIQsICDRAILLNKGQIEMEGEPEAVM 233
Cdd:PRK13548 173 LAHQHHVLRLARQLaHERGLAVIVVLHDlNLAAR-YADRIVLLHQGRLVADGTPAEVL 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
38-224 |
6.11e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 6.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAallelgMGF----HSDFTGRQNVYmsgq 113
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVK------IGYfdqhQEELDPDKTVL---- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 114 llglssEKITELMPQIEE-----------FAeiGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDE----------- 171
Cdd:COG0488 398 ------DELRDGAPGGTEqevrgylgrflFS--GDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEptnhldietle 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446042612 172 ----ALsvgDAYfqhksferirkfrqEGTtLLLVSHDKQAIQSICDRAILLNKGQIE 224
Cdd:COG0488 470 aleeAL---DDF--------------PGT-VLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
32-227 |
8.04e-25 |
|
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: 100.73 E-value: 8.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGeAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG------RVAALLELG-----MGFHS 100
Cdd:cd03264 7 TKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqPQKLRRRIGylpqeFGVYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 101 DFTGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDE---ALSVGd 177
Cdd:cd03264 86 NFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEptaGLDPE- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446042612 178 ayfqhksfERIRkFRQ------EGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEG 227
Cdd:cd03264 165 --------ERIR-FRNllselgEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
38-239 |
3.22e-24 |
|
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: 104.92 E-value: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLELG-----MGFHSD----FTG--RQ 106
Cdd:COG2274 488 PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAslrrqIGVVLQdvflFSGtiRE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 107 NVYMSGQllGLSSEKITELMpqieEFAEIGDYI-------DQPV----RVYSSGMQVRLAfsVATAI--RPDVLIIDEAL 173
Cdd:COG2274 568 NITLGDP--DATDEEIIEAA----RLAGLHDFIealpmgyDTVVgeggSNLSGGQRQRLA--IARALlrNPRILILDEAT 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446042612 174 SVGDAYFQHKSFERIRKFRQeGTTLLLVSHDKQAIQsICDRAILLNKGQIEMEGEPEAVMD---YYNAL 239
Cdd:COG2274 640 SALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLArkgLYAEL 706
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
38-233 |
4.31e-24 |
|
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: 99.77 E-value: 4.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTG-EIEISGRvaallELG----------MGF-----HSD 101
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGE-----RRGgedvwelrkrIGLvspalQLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 102 FTGRQNVY---MSG--QLLGLSSE-------KITELMpqieEFAEIGDYIDQPVRVYSSGMQvRLAFsVATAI--RPDVL 167
Cdd:COG1119 91 FPRDETVLdvvLSGffDSIGLYREptdeqreRARELL----ELLGLAHLADRPFGTLSQGEQ-RRVL-IARALvkDPELL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446042612 168 IIDEALSVGDAYFQHKSFERIRKFRQEG-TTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVM 233
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-234 |
4.44e-24 |
|
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: 99.56 E-value: 4.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYRqyhsktgrliewlsplntkrhNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE 83
Cdd:cd03256 1 IEVENLSKTYP---------------------NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 84 ISG------RVAALLEL----GMGF-HSDFTGRQNVY---MSGQL---------LGLSSEKITELMPQIEEFAEIGDYID 140
Cdd:cd03256 60 IDGtdinklKGKALRQLrrqiGMIFqQFNLIERLSVLenvLSGRLgrrstwrslFGLFPKEEKQRALAALERVGLLDKAY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 141 QPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKF-RQEGTTLLLVSHDKQAIQSICDRAILLN 219
Cdd:cd03256 140 QRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLK 219
|
250
....*....|....*
gi 446042612 220 KGQIEMEGEPEAVMD 234
Cdd:cd03256 220 DGRIVFDGPPAELTD 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-204 |
1.44e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 98.62 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 1 MSYIRVNNVGKAYRqyhSKTGRLIewlsplntkrhnlkwILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTG 80
Cdd:COG1116 5 APALELRGVSKRFP---TGGGGVT---------------ALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 81 EIEISGRV--AALLELGMGFHSD-----FTGRQNVYMSGQLLGLSSEKITElmpQIEEFAEI---GDYIDQPVRVYSSGM 150
Cdd:COG1116 67 EVLVDGKPvtGPGPDRGVVFQEPallpwLTVLDNVALGLELRGVPKAERRE---RARELLELvglAGFEDAYPHQLSGGM 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446042612 151 QVRLAFSVATAIRPDVLIIDE---ALsvgDAyfQ-----HKSFERIrkFRQEGTTLLLVSHD 204
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEpfgAL---DA--LtrerlQDELLRL--WQETGKTVLFVTHD 198
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-224 |
3.50e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 96.65 E-value: 3.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYRQYHSKTgrliewlsplntkrhnlkWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE 83
Cdd:COG1136 5 LELRNLTKSYGTGEGEV------------------TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 84 ISGR-VAALLE----------LGM---GFH--SDFTGRQNVYMSGQLLGLSSEKITElmpQIEEFAE---IGDYIDQPVR 144
Cdd:COG1136 67 IDGQdISSLSErelarlrrrhIGFvfqFFNllPELTALENVALPLLLAGVSRKERRE---RARELLErvgLGDRLDHRPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 145 VYSSGMQVRLAfsVATAI--RPDVLIIDE---ALsvgDayfqHKS----FERIRKF-RQEGTTLLLVSHDkQAIQSICDR 214
Cdd:COG1136 144 QLSGGQQQRVA--IARALvnRPKLILADEptgNL---D----SKTgeevLELLRELnRELGTTIVMVTHD-PELAARADR 213
|
250
....*....|
gi 446042612 215 AILLNKGQIE 224
Cdd:COG1136 214 VIRLRDGRIV 223
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-220 |
5.73e-23 |
|
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: 96.00 E-value: 5.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYRqyhSKTGRLIewlsplntkrhnlkwILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE 83
Cdd:cd03293 1 LEVRNVSKTYG---GGGGAVT---------------ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 84 ISGR--VAALLELGMGFHSD-----FTGRQNVymsgqLLGLSSEKI--TELMPQIEEFAEI-------GDYIDQpvrvYS 147
Cdd:cd03293 63 VDGEpvTGPGPDRGYVFQQDallpwLTVLDNV-----ALGLELQGVpkAEARERAEELLELvglsgfeNAYPHQ----LS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446042612 148 SGMQVRLAFSVATAIRPDVLIIDEALSVGDAyfQ-----HKSFERIRkfRQEGTTLLLVSHD-KQAIqSICDRAILLNK 220
Cdd:cd03293 134 GGMRQRVALARALAVDPDVLLLDEPFSALDA--LtreqlQEELLDIW--RETGKTVLLVTHDiDEAV-FLADRVVVLSA 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-223 |
9.58e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 95.50 E-value: 9.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYRQYHsktgrliewlsplntkrhnlkWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE 83
Cdd:COG2884 2 IRFENVSKRYPGGR---------------------EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 84 ISGR---------VAAL-LELGMGFHsDF---TGR---QNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYS 147
Cdd:COG2884 61 VNGQdlsrlkrreIPYLrRRIGVVFQ-DFrllPDRtvyENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 148 SGMQVRLAfsVATAI--RPDVLIIDE-------ALSvgdayfqhksfERI----RKFRQEGTTLLLVSHDKQAIQSICDR 214
Cdd:COG2884 140 GGEQQRVA--IARALvnRPELLLADEptgnldpETS-----------WEImellEEINRRGTTVLIATHDLELVDRMPKR 206
|
....*....
gi 446042612 215 AILLNKGQI 223
Cdd:COG2884 207 VLELEDGRL 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
32-222 |
9.93e-23 |
|
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: 94.18 E-value: 9.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLELGMGFHsdftgRQNVYMS 111
Cdd:cd03229 7 SKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPL-----RRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 112 GQLLGLSS-----EKITELMpqieefaeigdyidqpvrvySSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFE 186
Cdd:cd03229 82 FQDFALFPhltvlENIALGL--------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRA 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 446042612 187 RIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQ 222
Cdd:cd03229 142 LLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
32-225 |
1.41e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRV-AALLELGMGFHSDFTGRQNVYM 110
Cdd:COG0488 5 SKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLrIGYLPQEPPLDDDLTVLDTVLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 111 S--------------GQLLGLSSEKITELMPQIEEFAEIGDY-------------------IDQPVRVYSSGMQVRLAFS 157
Cdd:COG0488 85 GdaelraleaeleelEAKLAEPDEDLERLAELQEEFEALGGWeaearaeeilsglgfpeedLDRPVSELSGGWRRRVALA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446042612 158 VATAIRPDVLIIDE------ALSVgdayfqhksfERIRKF-RQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEM 225
Cdd:COG0488 165 RALLSEPDLLLLDEptnhldLESI----------EWLEEFlKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTL 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
38-223 |
1.57e-22 |
|
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: 93.43 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGrvAALLELGMGFHSDFTGrqnvYmsgqllgl 117
Cdd:cd03246 15 PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG--ADISQWDPNELGDHVG----Y-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 118 ssekiteLMPQIEEFA-EIGDYIdqpvrvYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQEGT 196
Cdd:cd03246 81 -------LPQDDELFSgSIAENI------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGA 147
|
170 180
....*....|....*....|....*..
gi 446042612 197 TLLLVSHDKQAIQSiCDRAILLNKGQI 223
Cdd:cd03246 148 TRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-223 |
1.78e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 95.91 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 1 MSYIRVNNVGKAYRqYHSKTGRliewlsplntkrHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTG 80
Cdd:PRK10419 1 MTLLNVSGLSHHYA-HGGLSGK------------HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 81 EIEISGRvaALLELGMGFHSDFtgRQNVYMSGQ----------------------LLGLS----SEKITELMPQIEEFAE 134
Cdd:PRK10419 68 NVSWRGE--PLAKLNRAQRKAF--RRDIQMVFQdsisavnprktvreiireplrhLLSLDkaerLARASEMLRAVDLDDS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 135 IGDYIDQPVrvysSGMQV-RLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSIC 212
Cdd:PRK10419 144 VLDKRPPQL----SGGQLqRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFC 219
|
250
....*....|.
gi 446042612 213 DRAILLNKGQI 223
Cdd:PRK10419 220 QRVMVMDNGQI 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
33-230 |
2.12e-22 |
|
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: 94.92 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 33 KRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLE------LGMGF----HSDF 102
Cdd:cd03218 8 KRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmhkrarLGIGYlpqeASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 103 ---TGRQNVYMSGQLLGLSSEKITELMPQ-IEEFaEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDE------A 172
Cdd:cd03218 88 rklTVEENILAVLEIRGLSKKEREEKLEElLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEpfagvdP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446042612 173 LSVGDayFQhksfERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPE 230
Cdd:cd03218 167 IAVQD--IQ----KIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPE 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
32-222 |
3.19e-22 |
|
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: 91.74 E-value: 3.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVaallelgmgfhsdftgrqnvyms 111
Cdd:cd03221 7 SKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 112 gqllglssekitelmpqieefaEIGdYIDQpvrvYSSGMQVRLAFSVATAIRPDVLIIDE-----------ALSvgdayf 180
Cdd:cd03221 64 ----------------------KIG-YFEQ----LSGGEKMRLALAKLLLENPNLLLLDEptnhldlesieALE------ 110
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446042612 181 qhksfERIRKFRQegtTLLLVSHDKQAIQSICDRAILLNKGQ 222
Cdd:cd03221 111 -----EALKEYPG---TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
41-234 |
3.22e-22 |
|
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: 94.33 E-value: 3.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALL---ELGMGF---------HsdFTGRQNV 108
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVpvqERNVGFvfqhyalfrH--MTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 109 ymsgqLLGLSSEKITELMPQieefAEIGDYIDQPVRV-------------YSSGMQVRLAFSVATAIRPDVLIIDEALSV 175
Cdd:cd03296 96 -----AFGLRVKPRSERPPE----AEIRAKVHELLKLvqldwladrypaqLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 176 GDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMD 234
Cdd:cd03296 167 LDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-232 |
3.36e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 94.33 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 1 MSYIRVNNVGKAYRQyhsktgrliewlsplntkrhnlKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTG 80
Cdd:COG1137 1 MMTLEAENLVKSYGK----------------------RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSG 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 81 EIEISGRVAALL------ELGMGF----HSDF---TGRQNVYMSGQLLGLSSEKITELMPQ-IEEFaEIGDYIDQPVRVY 146
Cdd:COG1137 59 RIFLDGEDITHLpmhkraRLGIGYlpqeASIFrklTVEDNILAVLELRKLSKKEREERLEElLEEF-GITHLRKSKAYSL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 147 SSGMQVRLAFSVATAIRPDVLIIDE--A----LSVGDAyfQhksfERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNK 220
Cdd:COG1137 138 SGGERRRVEIARALATNPKFILLDEpfAgvdpIAVADI--Q----KIIRHLKERGIGVLITDHNVRETLGICDRAYIISE 211
|
250
....*....|..
gi 446042612 221 GQIEMEGEPEAV 232
Cdd:COG1137 212 GKVLAEGTPEEI 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-231 |
3.85e-22 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 94.04 E-value: 3.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKayrQYHSKTGRLIewlsplntkrhnlkwILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE 83
Cdd:COG4181 9 IELRGLTK---TVGTGAGELT---------------ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 84 ISGR---------VAALLELGMGFhsdftgrqnVYMSGQLLG-LSS-EKIT---EL--MPQIEEFAE-------IGDYID 140
Cdd:COG4181 71 LAGQdlfaldedaRARLRARHVGF---------VFQSFQLLPtLTAlENVMlplELagRRDARARARallervgLGHRLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 141 QPVRVYSSGMQVRLAFSVATAIRPDVLIIDE---------ALSVGDAYFQHKsferirkfRQEGTTLLLVSHDkQAIQSI 211
Cdd:COG4181 142 HYPAQLSGGEQQRVALARAFATEPAILFADEptgnldaatGEQIIDLLFELN--------RERGTTLVLVTHD-PALAAR 212
|
250 260
....*....|....*....|
gi 446042612 212 CDRAILLNKGQIEMEGEPEA 231
Cdd:COG4181 213 CDRVLRLRAGRLVEDTAATA 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
40-233 |
6.75e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 6.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALL---ELGMGFHS---------DFTGRQN 107
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALsarAASRRVASvpqdtslsfEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 108 VYMsGQL-----LGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQH 182
Cdd:PRK09536 98 VEM-GRTphrsrFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446042612 183 KSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVM 233
Cdd:PRK09536 177 RTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
41-214 |
1.15e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.63 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAAL------LELGMGF-H------SDFTGRQN 107
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFrsprdaQAAGIAIiHqelnlvPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 108 VYMsGQLL---GLSSEKitELMPQIEE-FAEIGDYID--QPVRVYSSGMQVRLAFSVATAIRPDVLIIDE---ALSVGDA 178
Cdd:COG1129 100 IFL-GREPrrgGLIDWR--AMRRRARElLARLGLDIDpdTPVGDLSVAQQQLVEIARALSRDARVLILDEptaSLTEREV 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 446042612 179 yfqHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDR 214
Cdd:COG1129 177 ---ERLFRIIRRLKAQGVAIIYISHRLDEVFEIADR 209
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
38-233 |
1.30e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.52 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRV---AALLEL----GMGFhsdftgrQNVym 110
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITiskENLKEIrkkiGIIF-------QNP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 111 SGQLLGLSSE----------KIT--ELMPQIEEFAE---IGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSV 175
Cdd:PRK13632 93 DNQFIGATVEddiafglenkKVPpkKMKDIIDDLAKkvgMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 176 GDAYFQHKSFERIRKFRQEGT-TLLLVSHD-KQAIQsiCDRAILLNKGQIEMEGEPEAVM 233
Cdd:PRK13632 173 LDPKGKREIKKIMVDLRKTRKkTLISITHDmDEAIL--ADKVIVFSEGKLIAQGKPKEIL 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-232 |
1.58e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 94.75 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 1 MSYIRVNNVGKAYRQYHsktgrliewlsplntkrhnlkwILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTG 80
Cdd:COG3839 1 MASLELENVSKSYGGVE----------------------ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSG 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 81 EIEISGRVAALLE-----LGMGF-------HsdFTGRQNVYMSGQLLGLSSEKITElmpQIEEFAE---IGDYIDQPVRV 145
Cdd:COG3839 59 EILIGGRDVTDLPpkdrnIAMVFqsyalypH--MTVYENIAFPLKLRKVPKAEIDR---RVREAAEllgLEDLLDRKPKQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 146 YSSGMQVRLAfsVATAI--RPDVLIIDEALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQ 222
Cdd:COG3839 134 LSGGQRQRVA--LGRALvrEPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGR 211
|
250
....*....|
gi 446042612 223 IEMEGEPEAV 232
Cdd:COG3839 212 IQQVGTPEEL 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
36-222 |
1.96e-21 |
|
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: 90.52 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 36 NLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGrvaallelgmgfhsdftgrqnvymsgqlL 115
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG----------------------------V 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 116 GLSSEKITELMPQIEefaeigdYIDQPVRVYS--------SGMQV-RLAfsVATAI--RPDVLIIDEALSVGDAYFQHKS 184
Cdd:cd03228 65 DLRDLDLESLRKNIA-------YVPQDPFLFSgtirenilSGGQRqRIA--IARALlrDPPILILDEATSALDPETEALI 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 446042612 185 FERIRKFRQeGTTLLLVSHDKQAIQsICDRAILLNKGQ 222
Cdd:cd03228 136 LEALRALAK-GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
32-237 |
2.28e-21 |
|
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: 91.91 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR-VAALL----ELGMGFHS-----D 101
Cdd:cd03300 7 SKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKdITNLPphkrPVNTVFQNyalfpH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 102 FTGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYF- 180
Cdd:cd03300 87 LTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLr 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446042612 181 QHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEavmDYYN 237
Cdd:cd03300 167 KDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPE---EIYE 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
32-231 |
2.75e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.02 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG-----RVAALLELGMGFHS-----D 101
Cdd:PRK11432 13 TKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvthRSIQQRDICMVFQSyalfpH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 102 FTGRQNVYMSGQLLGLSSEKITElmpQIEEFAEIGD-------YIDQpvrvYSSGMQVRLAFSVATAIRPDVLIIDEALS 174
Cdd:PRK11432 93 MSLGENVGYGLKMLGVPKEERKQ---RVKEALELVDlagfedrYVDQ----ISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446042612 175 VGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEA 231
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-232 |
4.23e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 93.62 E-value: 4.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 1 MSYIRVNNVGKAYRQYHsktgrliewlsplntkrhnlkwILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTG 80
Cdd:COG3842 3 MPALELENVSKRYGDVT----------------------ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 81 EIEISGRVAALLE-----LGMGFHSD--F---TGRQNV-YmsG-QLLGLSSEKITElmpQIEEFAE---IGDYIDQPVRV 145
Cdd:COG3842 61 RILLDGRDVTGLPpekrnVGMVFQDYalFphlTVAENVaF--GlRMRGVPKAEIRA---RVAELLElvgLEGLADRYPHQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 146 YSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAyfqhKSFERIRK-----FRQEGTTLLLVSHDKQAIQSICDRAILLNK 220
Cdd:COG3842 136 LSGGQQQRVALARALAPEPRVLLLDEPLSALDA----KLREEMREelrrlQRELGITFIYVTHDQEEALALADRIAVMND 211
|
250
....*....|..
gi 446042612 221 GQIEMEGEPEAV 232
Cdd:COG3842 212 GRIEQVGTPEEI 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
41-233 |
4.25e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.36 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG-------RVAALLEL-GMGFH---SDFTGR---Q 106
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsKLQGIRKLvGIVFQnpeTQFVGRtveE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 107 NVYMSGQLLGLSSEKITELMPQieEFAEIG--DYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKS 184
Cdd:PRK13644 98 DLAFGPENLCLPPIEIRKRVDR--ALAEIGleKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446042612 185 FERIRKFRQEGTTLLLVSHDKQAIQsICDRAILLNKGQIEMEGEPEAVM 233
Cdd:PRK13644 176 LERIKKLHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
41-227 |
4.84e-21 |
|
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: 90.73 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLEL-----GMGF-HSD---FTG--RQNVY 109
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPadlrrNIGYvPQDvtlFYGtlRDNIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 110 MSGQLlgLSSEKITELMpqieEFAEIGDYIDQPVRVYS----------SGMQvRLAFSVATAI--RPDVLIIDEALSVGD 177
Cdd:cd03245 100 LGAPL--ADDERILRAA----ELAGVTDFVNKHPNGLDlqigergrglSGGQ-RQAVALARALlnDPPILLLDEPTSAMD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446042612 178 AYFQHKSFERIRKFRqEGTTLLLVSHdKQAIQSICDRAILLNKGQIEMEG 227
Cdd:cd03245 173 MNSEERLKERLRQLL-GDKTLIIITH-RPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-232 |
8.06e-21 |
|
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: 90.32 E-value: 8.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYRQYHsktgrliewlsplntkrhnlkwILSDINFEVAPGEAVGIIGINGAGKSTLLKLITG-----TSRPT 78
Cdd:cd03260 1 IELRDLNVYYGDKH----------------------ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPD 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 79 TGEIEISGR--------VAAL-LELGMGFHS----DFTGRQNVYMSGQLLGLSSEKIT-ELMPQIEEFAEIGDYIDQPVR 144
Cdd:cd03260 59 EGEVLLDGKdiydldvdVLELrRRVGMVFQKpnpfPGSIYDNVAYGLRLHGIKLKEELdERVEEALRKAALWDEVKDRLH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 145 VY--SSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQEgTTLLLVSHDKQAIQSICDRAILLNKGQ 222
Cdd:cd03260 139 ALglSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGR 217
|
250
....*....|
gi 446042612 223 IEMEGEPEAV 232
Cdd:cd03260 218 LVEFGPTEQI 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
41-232 |
8.95e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 91.65 E-value: 8.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEI-----EISGRVAALLEL----GMGF----HSDF--TGR 105
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvDITDKKVKLSDIrkkvGLVFqypeYQLFeeTIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 106 QNVYMSGQLLGLSSEKITELMpqIEEFAEIG----DYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQ 181
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRV--KRAMNIVGldyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446042612 182 HKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK13637 181 DEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
40-223 |
1.12e-20 |
|
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: 89.51 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRV-----AALLEL----GMGFHSdF------TG 104
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltddkKNINELrqkvGMVFQQ-FnlfphlTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 105 RQNVYMSG-QLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHK 183
Cdd:cd03262 94 LENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446042612 184 SFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQI 223
Cdd:cd03262 174 VLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
32-233 |
1.32e-20 |
|
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: 90.05 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKR-HNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR-VAAL--LEL---------GMGF 98
Cdd:cd03295 7 TKRyGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdIREQdpVELrrkigyviqQIGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 99 HSDFTGRQNVYMSGQLLGLSSEKI----TELMP----QIEEFAEigDYIDQpvrvYSSGMQVRLAFSVATAIRPDVLIID 170
Cdd:cd03295 87 FPHMTVEENIALVPKLLKWPKEKIreraDELLAlvglDPAEFAD--RYPHE----LSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446042612 171 EALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVM 233
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-230 |
2.04e-20 |
|
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: 90.01 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYrqyHSKTGRLIEWLSPLNTKRHNLKWI-----LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPT 78
Cdd:cd03294 1 IKIKGLYKIF---GKNPQKAFKLLAKGKSKEEILKKTgqtvgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 79 TGEIEISGR------VAALLEL-----GMGFHSdF------TGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQ 141
Cdd:cd03294 78 SGKVLIDGQdiaamsRKELRELrrkkiSMVFQS-FallphrTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 142 PVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYfqhksferIRKFRQE---------GTTLLLVSHD-KQAIQsI 211
Cdd:cd03294 157 YPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL--------IRREMQDellrlqaelQKTIVFITHDlDEALR-L 227
|
250
....*....|....*....
gi 446042612 212 CDRAILLNKGQIEMEGEPE 230
Cdd:cd03294 228 GDRIAIMKDGRLVQVGTPE 246
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-228 |
2.76e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 90.91 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKayrQYHSKTGRLIewlsplntkrhnlkwILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE 83
Cdd:COG1135 2 IELENLSK---TFPTKGGPVT---------------ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 84 ISGRV------AALLEL----GMGF-HsdF------TGRQNVYMSGQLLGLSSEKI----TELMpqieEFAEIGDYIDQp 142
Cdd:COG1135 64 VDGVDltalseRELRAArrkiGMIFqH--FnllssrTVAENVALPLEIAGVPKAEIrkrvAELL----ELVGLSDKADA- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 143 vrvY----SSGMQVRLAFSVATAIRPDVLIIDEALSVGDAyfqhKSFERI----RKFRQE-GTTLLLVSHDKQAIQSICD 213
Cdd:COG1135 137 ---YpsqlSGGQKQRVGIARALANNPKVLLCDEATSALDP----ETTRSIldllKDINRElGLTIVLITHEMDVVRRICD 209
|
250
....*....|....*
gi 446042612 214 RAILLNKGQIEMEGE 228
Cdd:COG1135 210 RVAVLENGRIVEQGP 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
41-223 |
4.20e-20 |
|
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: 87.85 E-value: 4.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG--------RVAALL--ELGMGFH-----SDFTGR 105
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgRAIPYLrrKIGVVFQdfrllPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 106 QNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSF 185
Cdd:cd03292 97 ENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 446042612 186 ERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQI 223
Cdd:cd03292 177 NLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
38-240 |
1.01e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 88.25 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRvaALLE---------LGMGFH---SDFTG- 104
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD--LLTEenvwdirhkIGMVFQnpdNQFVGa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 105 --RQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYID-QPVRVySSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQ 181
Cdd:PRK13650 98 tvEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKErEPARL-SGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 182 HKSFERIRKFRQE-GTTLLLVSHDKQAIqSICDRAILLNKGQIEMEGEPEAVMDYYNALL 240
Cdd:PRK13650 177 LELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGNDLL 235
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-223 |
1.09e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 89.47 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYRQYhsktGRLIEwlsplntkrhnlkwILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE 83
Cdd:PRK11153 2 IELKNISKVFPQG----GRTIH--------------ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 84 ISGR----------VAALLELGMGF-H----SDFTGRQNVYMSGQLLGLSSEKI----TELMpqieEFAEIGDYIDqpvr 144
Cdd:PRK11153 64 VDGQdltalsekelRKARRQIGMIFqHfnllSSRTVFDNVALPLELAGTPKAEIkarvTELL----ELVGLSDKAD---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 145 VY----SSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLN 219
Cdd:PRK11153 136 RYpaqlSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVID 215
|
....
gi 446042612 220 KGQI 223
Cdd:PRK11153 216 AGRL 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
41-223 |
3.46e-19 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 84.41 E-value: 3.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR------VAALLELGMGFHSDftGRQNvymSGQL 114
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsPRDAIRAGIAYVPE--DRKR---EGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 115 LGLSsekitelmpqIEEFAEIGDYIdqpvrvySSGMQVRLAFSVATAIRPDVLIIDE---ALSVGDAYFQHKsfeRIRKF 191
Cdd:cd03215 91 LDLS----------VAENIALSSLL-------SGGNQQKVVLARWLARDPRVLILDEptrGVDVGAKAEIYR---LIREL 150
|
170 180 190
....*....|....*....|....*....|..
gi 446042612 192 RQEGTTLLLVSHDKQAIQSICDRAILLNKGQI 223
Cdd:cd03215 151 ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
32-232 |
5.26e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 87.70 E-value: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALL-----ELGMGFHS-----D 101
Cdd:PRK09452 21 SKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaenrHVNTVFQSyalfpH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 102 FTGRQNVYMSGQLLGLSSEKITEL------MPQIEEFAeigdyiDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSV 175
Cdd:PRK09452 101 MTVFENVAFGLRMQKTPAAEITPRvmealrMVQLEEFA------QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446042612 176 GDAyfqhksfeRIRKF---------RQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK09452 175 LDY--------KLRKQmqnelkalqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
33-233 |
7.14e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 85.41 E-value: 7.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 33 KRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLE------------------- 93
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRdkdgqlkvadknqlrllrt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 94 -LGMGFH-----SDFTGRQNVYMSG-QLLGLSSEKITElmPQIEEFAEIGdyIDQ------PVRVySSGMQVRLAFSVAT 160
Cdd:PRK10619 93 rLTMVFQhfnlwSHMTVLENVMEAPiQVLGLSKQEARE--RAVKYLAKVG--IDEraqgkyPVHL-SGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446042612 161 AIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVM 233
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
41-222 |
2.12e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.00 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAAL------LELGMG--------FHSdFTGRQ 106
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIrsprdaIALGIGmvhqhfmlVPN-LTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 107 NVymsgqLLGLSSEK-----ITELMPQIEEFAEigDY-----IDQPVRVYSSGMQVRLafsvatAI------RPDVLIID 170
Cdd:COG3845 100 NI-----VLGLEPTKggrldRKAARARIRELSE--RYgldvdPDAKVEDLSVGEQQRV------EIlkalyrGARILILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446042612 171 EALSV-----GDAYFQHksferIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQ 222
Cdd:COG3845 167 EPTAVltpqeADELFEI-----LRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
48-227 |
6.39e-18 |
|
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: 86.22 E-value: 6.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 48 VAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR--VAALLEL--GMGFHSDF-------TGRQNVYMSGQLLG 116
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiLTNISDVhqNMGYCPQFdaiddllTGREHLYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 117 LSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQEGT 196
Cdd:TIGR01257 2042 VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR 2121
|
170 180 190
....*....|....*....|....*....|.
gi 446042612 197 TLLLVSHDKQAIQSICDRAILLNKGQIEMEG 227
Cdd:TIGR01257 2122 AVVLTSHSMEECEALCTRLAIMVKGAFQCLG 2152
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
32-234 |
8.06e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 82.06 E-value: 8.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGE-----IEISGRVAAL----LELGMGFHS-- 100
Cdd:PRK09493 8 SKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdgLKVNDPKVDErlirQEAGMVFQQfy 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 101 ---DFTGRQNVyMSG--QLLGLSSEKITELmpQIEEFAEIGdyIDQPVRVY----SSGMQVRLAFSVATAIRPDVLIIDE 171
Cdd:PRK09493 88 lfpHLTALENV-MFGplRVRGASKEEAEKQ--ARELLAKVG--LAERAHHYpselSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446042612 172 ALSVGDAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMD 234
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
32-250 |
8.61e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.11 E-value: 8.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEI--------------SGRVAALLE-LGM 96
Cdd:PRK11264 10 VKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqqKGLIRQLRQhVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 97 GFHSdF------TGRQNVyMSGQLL--GLSSEKITELMPQIeeFAEIG--DYIDQPVRVYSSGMQVRLAFSVATAIRPDV 166
Cdd:PRK11264 90 VFQN-FnlfphrTVLENI-IEGPVIvkGEPKEEATARAREL--LAKVGlaGKETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 167 LIIDEALSVGDAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEavmdyynALLADKQNQ 246
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK-------ALFADPQQP 238
|
....
gi 446042612 247 SIKQ 250
Cdd:PRK11264 239 RTRQ 242
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
36-234 |
2.10e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 80.57 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 36 NLKWILSD----INFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLELG-----MGFHSD--F-- 102
Cdd:COG3840 6 DLTYRYGDfplrFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAerpvsMLFQENnlFph 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 103 -TGRQNVYmsgqlLGLSSE-KITEL-MPQIEEFAE---IGDYIDQPVRVYSSGMQVRLAFsvATAI---RPdVLIIDEAL 173
Cdd:COG3840 86 lTVAQNIG-----LGLRPGlKLTAEqRAQVEQALErvgLAGLLDRLPGQLSGGQRQRVAL--ARCLvrkRP-ILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446042612 174 SVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMD 234
Cdd:COG3840 158 SALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLD 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
41-235 |
2.18e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.53 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR------VAALLELGMGF----------HSDFTG 104
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsPRDAIRAGIAYvpedrkgeglVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 105 RQNVYMS--GQL--LGLSSEKitelmpqiEEFAEIGDYI----------DQPVRVYSSGMQVRLAFSVATAIRPDVLIID 170
Cdd:COG1129 348 RENITLAslDRLsrGGLLDRR--------RERALAEEYIkrlriktpspEQPVGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446042612 171 E---ALSVGdAyfqhKS--FERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQI--EMEGE---PEAVMDY 235
Cdd:COG1129 420 EptrGIDVG-A----KAeiYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIvgELDREeatEEAIMAA 489
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
40-223 |
7.00e-17 |
|
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: 78.36 E-value: 7.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITG--TSRPTTGEIEISGRVAALLELG--MGF-------HSDFTGRQNV 108
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRkiIGYvpqddilHPTLTVRETL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 109 YMSGQLLGLssekitelmpqieefaeigdyidqpvrvySSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERI 188
Cdd:cd03213 104 MFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 446042612 189 RKFRQEGTTLLLVSHdkQAIQSI---CDRAILLNKGQI 223
Cdd:cd03213 155 RRLADTGRTIICSIH--QPSSEIfelFDKLLLLSQGRV 190
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
43-224 |
8.09e-17 |
|
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: 78.49 E-value: 8.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 43 DINFEVaPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRV-----------------------AAL-------- 91
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrkiglvfqqYALfphlnvre 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 92 -LELGMGFHSDFTGRQNVymsgqllglssEKITELMpQIEEFAeigdyiDQPVRVYSSGMQVRLAFSVATAIRPDVLIID 170
Cdd:cd03297 95 nLAFGLKRKRNREDRISV-----------DELLDLL-GLDHLL------NRYPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446042612 171 EALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIE 224
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
41-232 |
8.28e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.89 E-value: 8.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR-----VAALLEL----GMGF----HSDFTGR-- 105
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysRKGLMKLresvGMVFqdpdNQLFSASvy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 106 QNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSF 185
Cdd:PRK13636 102 QDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIM 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446042612 186 ERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK13636 182 KLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
43-232 |
9.83e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 80.66 E-value: 9.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 43 DINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLE-----LGMGF-------HsdFTGRQNVYM 110
Cdd:PRK11650 22 GIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEpadrdIAMVFqnyalypH--MSVRENMAY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 111 SGQLLGLSSEKITElmpQIEEFA---EIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQ-HKSFE 186
Cdd:PRK11650 100 GLKIRGMPKAEIEE---RVAEAArilELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRvQMRLE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446042612 187 rIRKF-RQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK11650 177 -IQRLhRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
40-233 |
1.09e-16 |
|
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: 81.72 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALL---ELG--MGFHSD----FTG--RQNV 108
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWdreELGrhIGYLPQdvelFDGtiAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 109 YMSGQllgLSSEKITE------------LMPQieefaeiGdY---IDQPVRVYSSGMQVRLAFsvATAI--RPDVLIIDE 171
Cdd:COG4618 427 ARFGD---ADPEKVVAaaklagvhemilRLPD-------G-YdtrIGEGGARLSGGQRQRIGL--ARALygDPRLVVLDE 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446042612 172 ALS----VGDAYFqhksFERIRKFRQEGTTLLLVSHDKQAIQsICDRAILLNKGQIEMEGEPEAVM 233
Cdd:COG4618 494 PNSnlddEGEAAL----AAAIRALKARGATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
36-223 |
1.42e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.97 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 36 NLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR-VAALLE------LG-------MGFHSD 101
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKLPEykrakyIGrvfqdpmMGTAPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 102 FTGRQNV---YMSGQLLGLSSEKITELMPQI-EEFAEIG----DYIDQPVRVYSSGmQvRLAFSV--ATAIRPDVLIIDE 171
Cdd:COG1101 97 MTIEENLalaYRRGKRRGLRRGLTKKRRELFrELLATLGlgleNRLDTKVGLLSGG-Q-RQALSLlmATLTKPKLLLLDE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446042612 172 ---ALsvgDAyfqhKSFERI----RKF-RQEGTTLLLVSHD-KQAIqSICDRAILLNKGQI 223
Cdd:COG1101 175 htaAL---DP----KTAALVleltEKIvEENNLTTLMVTHNmEQAL-DYGNRLIMMHEGRI 227
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
41-258 |
1.72e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.34 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSrPTTGEIEISGRvaALlelgmgfhSDFTG----RQNVYMS----- 111
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGR--PL--------SDWSAaelaRHRAYLSqqqsp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 112 ------GQLLGL------SSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQ--VRLA---FSVATAIRPD--VLIIDE- 171
Cdd:COG4138 81 pfampvFQYLALhqpagaSSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWqrVRLAavlLQVWPTINPEgqLLLLDEp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 172 --ALSVGdayfQHKSFER-IRKFRQEGTTLLLVSHD-----KQAiqsicDRAILLNKGQIEMEGEPEAVMDyyNALLADK 243
Cdd:COG4138 161 mnSLDVA----QQAALDRlLRELCQQGITVVMSSHDlnhtlRHA-----DRVWLLKQGKLVASGETAEVMT--PENLSEV 229
|
250
....*....|....*
gi 446042612 244 QNQSIKQVEHNGKTQ 258
Cdd:COG4138 230 FGVKFRRLEVEGHRW 244
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
41-223 |
1.79e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.84 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR------VAALLELGMGF-----HS-----DFTG 104
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsPRERRRLGVAYipedrLGrglvpDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 105 RQNVYMSGQLLGLSSEKITELMPQIEEFAE--IGDY------IDQPVRVYSSGMQVRLAfsVATAI--RPDVLIIDE--- 171
Cdd:COG3845 354 AENLILGRYRRPPFSRGGFLDRKAIRAFAEelIEEFdvrtpgPDTPARSLSGGNQQKVI--LARELsrDPKLLIAAQptr 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446042612 172 ALSVGDAYFQHKsfeRIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQI 223
Cdd:COG3845 432 GLDVGAIEFIHQ---RLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
35-227 |
3.75e-16 |
|
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: 75.81 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 35 HNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLElgmgfhsdftgrqnvymsgql 114
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 115 lGLSSEKITELMPQIEEFAE-IGDYIDQPvrvYSSGMQVRLAFSVATAIRPDVLIIDEAlSVG-DAYFQHKSFERIRKFr 192
Cdd:cd03247 71 -KALSSLISVLNQRPYLFDTtLRNNLGRR---FSGGERQRLALARILLQDAPIVLLDEP-TVGlDPITERQLLSLIFEV- 144
|
170 180 190
....*....|....*....|....*....|....*
gi 446042612 193 QEGTTLLLVSHDKQAIQSIcDRAILLNKGQIEMEG 227
Cdd:cd03247 145 LKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
40-244 |
3.88e-16 |
|
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: 77.14 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALL-------ELGMGFHSD--FTG--RQNV 108
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdpawlrrQVGVVLQENvlFNRsiRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 109 YMSGQllGLSSEKITElmpqIEEFAEIGDYIDQPVRVY-----------SSGMQVRLAFSVATAIRPDVLIIDEALSVGD 177
Cdd:cd03252 97 ALADP--GMSMERVIE----AAKLAGAHDFISELPEGYdtivgeqgaglSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446042612 178 AYFQHKSFERIRKFrQEGTTLLLVSHDKQAIQSiCDRAILLNKGQIEMEGEPEAVMD----YYNalLADKQ 244
Cdd:cd03252 171 YESEHAIMRNMHDI-CAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAenglYAY--LYQLQ 237
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
38-247 |
4.66e-16 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 79.83 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVaallELGMgfhsdFTGRQNVYMSGQLLGL 117
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGI----KLGY-----FAQHQLEFLRADESPL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 118 ssEKITELMPQIEE---------FAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERI 188
Cdd:PRK10636 396 --QHLARLAPQELEqklrdylggFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 189 RKFrqEGtTLLLVSHDKQAIQSICDRAILLNKGQIE-MEGEpeavMDYYNALLADKQNQS 247
Cdd:PRK10636 474 IDF--EG-ALVVVSHDRHLLRSTTDDLYLVHDGKVEpFDGD----LEDYQQWLSDVQKQE 526
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
41-222 |
4.87e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.57 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR------VAALLELGMG-----FH--SDFTGRQN 107
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasTTAALAAGVAiiyqeLHlvPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 108 VYMsGQL---LGLSSEKitELMPQI-EEFAEIGDYID--QPVRVYSSGMqvRLAFSVATAIRPDVLII--DEALSVGDAY 179
Cdd:PRK11288 100 LYL-GQLphkGGIVNRR--LLNYEArEQLEHLGVDIDpdTPLKYLSIGQ--RQMVEIAKALARNARVIafDEPTSSLSAR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446042612 180 FQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQ 222
Cdd:PRK11288 175 EIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
40-232 |
5.20e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 78.59 E-value: 5.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG----RVAAL-LELGMGFHSDFTGRQNVYMSGQL 114
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsRLHARdRKVGFVFQHYALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 115 LGLS-------------SEKITEL--MPQIEEFAEigDYIDQpvrvYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAY 179
Cdd:PRK10851 97 FGLTvlprrerpnaaaiKAKVTQLleMVQLAHLAD--RYPAQ----LSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446042612 180 FQhKSFER-IRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK10851 171 VR-KELRRwLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
41-232 |
5.21e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.43 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRV-----AALLE----LGMGFHSD----F--TGR 105
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikydkKSLLEvrktVGIVFQNPddqlFapTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 106 QNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSF 185
Cdd:PRK13639 98 EDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446042612 186 ERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK13639 178 KLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
38-233 |
1.17e-15 |
|
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: 78.65 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRvaallELgmgfhSDFTGR----------QN 107
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGV-----DL-----SDLDPAswrrqiawvpQN 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 108 VY-MSGQL---LGLSSEKIT-ELMPQIEEFAEIGDYIDQPVRVYS----------SGMQV-RLAfsVATAI--RPDVLII 169
Cdd:COG4988 420 PYlFAGTIrenLRLGRPDASdEELEAALEAAGLDEFVAALPDGLDtplgeggrglSGGQAqRLA--LARALlrDAPLLLL 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446042612 170 DEALSVGDAYFQHKSFERIRKFRQeGTTLLLVSHDKQAIQsICDRAILLNKGQIEMEGEPEAVM 233
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLA-QADRILVLDDGRIVEQGTHEELL 559
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
41-240 |
1.19e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 76.33 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAA---LLEL----GMGFHS---DFTG---RQN 107
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITddnFEKLrkhiGIVFQNpdnQFVGsivKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 108 VYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFER 187
Cdd:PRK13648 105 VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446042612 188 IRKFRQE-GTTLLLVSHD-KQAIQSicDRAILLNKGQIEMEGEPEAVMDYYNALL 240
Cdd:PRK13648 185 VRKVKSEhNITIISITHDlSEAMEA--DHVIVMNKGTVYKEGTPTEIFDHAEELT 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
32-237 |
1.33e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.57 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALL-----ELGMGFHS-----D 101
Cdd:PRK11607 26 TKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVppyqrPINMMFQSyalfpH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 102 FTGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQ 181
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446042612 182 HK-SFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMDYYN 237
Cdd:PRK11607 186 DRmQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPT 242
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
41-223 |
1.34e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.30 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALL----------ELGMGFHS-----DFTGR 105
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevpflrrQIGMIFQDhhllmDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 106 QNVYMSGQLLGLSSEKI-TELMPQIEEFAEIGDYIDQPVRVySSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKS 184
Cdd:PRK10908 98 DNVAIPLIIAGASGDDIrRRVSAALDKVGLLDKAKNFPIQL-SGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 446042612 185 FERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQI 223
Cdd:PRK10908 177 LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
44-233 |
1.59e-15 |
|
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: 78.31 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 44 INFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEI----------------SGRVA----------------AL 91
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpdgRGRAKryigilhqeydlyphrTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 92 LE-----LGMGFHSDFTGRQNVYMSgQLLGLSSEKITELMPQieefaeigdYIDQpvrvYSSGMQVRLAFSVATAIRPDV 166
Cdd:TIGR03269 383 LDnlteaIGLELPDELARMKAVITL-KMVGFDEEKAEEILDK---------YPDE----LSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446042612 167 LIIDEALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVM 233
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
38-233 |
1.69e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.82 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG------------RVAALLELGMGFHSDFTGR 105
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlaRRLALLPQHHLTPEGITVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 106 QNV------YMS--GQLLGLSSEKITELMP--QIEEFAeigdyiDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSV 175
Cdd:PRK11231 95 ELVaygrspWLSlwGRLSAEDNARVNQAMEqtRINHLA------DRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446042612 176 GDAYFQHKSFERIRKFRQEGTTLLLVSHD-KQAIQsICDRAILLNKGQIEMEGEPEAVM 233
Cdd:PRK11231 169 LDINHQVELMRLMRELNTQGKTVVTVLHDlNQASR-YCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
31-232 |
1.92e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.89 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 31 NTKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR----------------------- 87
Cdd:PRK13633 16 SNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdtsdeenlwdirnkagmvfqnpd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 88 ---VAALLELGMGFhsdftGRQNvymsgqlLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRP 164
Cdd:PRK13633 96 nqiVATIVEEDVAF-----GPEN-------LGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 165 DVLIIDEALSVGDAYFQHKSFERIRKF-RQEGTTLLLVSH-DKQAIQSicDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHyMEEAVEA--DRIIVMDSGKVVMEGTPKEI 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
32-236 |
2.51e-15 |
|
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: 77.54 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTS--RPTTGEI--------------------------- 82
Cdd:TIGR03269 7 TKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpskvgepcpvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 83 -------------------EISGRVAALLELGMGFHSDFTGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPV 143
Cdd:TIGR03269 87 gtlepeevdfwnlsdklrrRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 144 RVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGD---AYFQHKSFERIRKfrQEGTTLLLVSHDKQAIQSICDRAILLNK 220
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVHNALEEAVK--ASGISMVLTSHWPEVIEDLSDKAIWLEN 244
|
250
....*....|....*.
gi 446042612 221 GQIEMEGEPEAVMDYY 236
Cdd:TIGR03269 245 GEIKEEGTPDEVVAVF 260
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
38-234 |
2.73e-15 |
|
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: 74.57 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR------VAALLE-LGMGFHSDF----TGRQ 106
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisRKSLRSmIGVVLQDTFlfsgTIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 107 NVYMSGQLLGLSSEKITELMPQIEEFAE--IGDYIDQPV---RVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQ 181
Cdd:cd03254 96 NIRLGRPNATDEEVIEAAKEAGAHDFIMklPNGYDTVLGengGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446042612 182 HKSFERIRKFRqEGTTLLLVSHDKQAIQSiCDRAILLNKGQIEMEGEPEAVMD 234
Cdd:cd03254 176 KLIQEALEKLM-KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
41-226 |
3.22e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.97 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALlelgmgfHSDFTGRQN--VYMS------G 112
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT-------RSPQDGLANgiVYISedrkrdG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 113 QLLGLSS---------EKITELMPQI---EEFAEIGDYI----------DQPVRVYSSGMQVRLAFSVATAIRPDVLIID 170
Cdd:PRK10762 341 LVLGMSVkenmsltalRYFSRAGGSLkhaDEQQAVSDFIrlfniktpsmEQAIGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446042612 171 EALSVGDAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEME 226
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGE 476
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
34-232 |
3.53e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.04 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 34 RHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRV-----AALLELGMG----------- 97
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldyskRGLLALRQQvatvfqdpeqq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 98 -FHSDFTgrQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVG 176
Cdd:PRK13638 90 iFYTDID--SDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446042612 177 DAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
38-233 |
5.72e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 76.36 E-value: 5.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR------VAALLE-LGMGFHsD---FTG--R 105
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdirdltLESLRRqIGVVPQ-DtflFSGtiR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 106 QNvymsgqlLGLSSEKITElmPQIEE---FAEIGDYI-------DQPVR---VYSSGMQV-RLAFsvATAI--RPDVLII 169
Cdd:COG1132 432 EN-------IRYGRPDATD--EEVEEaakAAQAHEFIealpdgyDTVVGergVNLSGGQRqRIAI--ARALlkDPPILIL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446042612 170 DEALSVGDAYFQHKSFERIRKFRQeGTTLLLVSHDKQAIQSiCDRAILLNKGQIEMEGEPEAVM 233
Cdd:COG1132 501 DEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELL 562
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
40-203 |
7.78e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.78 E-value: 7.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAA---------LLELGM--GFHSDFTGRQNV 108
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAeqrdephenILYLGHlpGLKPELSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 109 YMSGQLLGLSSEKITELMpqieefAEIG--DYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDE---ALSV-GDAYFQH 182
Cdd:TIGR01189 95 HFWAAIHGGAQRTIEDAL------AAVGltGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEpttALDKaGVALLAG 168
|
170 180
....*....|....*....|.
gi 446042612 183 ksfeRIRKFRQEGTTLLLVSH 203
Cdd:TIGR01189 169 ----LLRAHLARGGIVLLTTH 185
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
41-222 |
9.14e-15 |
|
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: 72.85 E-value: 9.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG-------------RVAALLELGMGFHSDF----- 102
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwvdlaqasprEILALRRRTIGYVSQFlrvip 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 103 --TGRQNVYMSGQLLGLSSEKitelmpQIEEFAEIGDYIDQPVRV-------YSSGMQVRLAFSVATAIRPDVLIIDEAL 173
Cdd:COG4778 107 rvSALDVVAEPLLERGVDREE------ARARARELLARLNLPERLwdlppatFSGGEQQRVNIARGFIADPPLLLLDEPT 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446042612 174 SVGDAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQ 222
Cdd:COG4778 181 ASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
44-224 |
1.35e-14 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 75.22 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 44 INFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRV------AALLELgmgF---HSDFtgrqnvYMSGQL 114
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPvtadnrEAYRQL---FsavFSDF------HLFDRL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 115 LGLSS----EKITELMPQIEefaeigdyIDQPVRV---------YSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQ 181
Cdd:COG4615 422 LGLDGeadpARARELLERLE--------LDHKVSVedgrfsttdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFR 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446042612 182 HKSFERI-RKFRQEGTTLLLVSHDKQAIqSICDRAILLNKGQIE 224
Cdd:COG4615 494 RVFYTELlPELKARGKTVIAISHDDRYF-DLADRVLKMDYGKLV 536
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
40-222 |
1.53e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 71.73 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVA-----ALLELGmgfhsdfTGRQNVymsgqL 114
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAyvsqePWIQNG-------TIRENI-----L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 115 LGLS-----SEKITE---LMPQIEEFA-----EIGDyidqpvR-VYSSGMQ-VRLafSVATAI--RPDVLIIDEALSVGD 177
Cdd:cd03250 88 FGKPfdeerYEKVIKacaLEPDLEILPdgdltEIGE------KgINLSGGQkQRI--SLARAVysDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446042612 178 AYFQHKSFER-IRKFRQEGTTLLLVSHDKQAIqSICDRAILLNKGQ 222
Cdd:cd03250 160 AHVGRHIFENcILGLLLNNKTRILVTHQLQLL-PHADQIVVLDNGR 204
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
32-223 |
2.80e-14 |
|
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: 71.53 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRP---TTGEIEISG----------RVAALLELGMgF 98
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGqprkpdqfqkCVAYVRQDDI-L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 99 HSDFTGRQNVYMSGQLLG--LSSEKITElmpQIEEFAEIGDYIDQPVRVY-----SSGMQVRLAFSVATAIRPDVLIIDE 171
Cdd:cd03234 93 LPGLTVRETLTYTAILRLprKSSDAIRK---KRVEDVLLRDLALTRIGGNlvkgiSGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446042612 172 ALSVGDAYFQHKSFERIRKFRQEGTTLLLVSHDKQA-IQSICDRAILLNKGQI 223
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSdLFRLFDRILLLSSGEI 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
45-234 |
3.55e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.54 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 45 NFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR-----VAALLELGMGFH-----SDFTGRQNVYmsgql 114
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttPPSRRPVSMLFQennlfSHLTVAQNIG----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 115 LGLS-----SEKITELMPQIEEFAEIGDYIDQ-PVRVySSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERI 188
Cdd:PRK10771 94 LGLNpglklNAAQREKLHAIARQMGIEDLLARlPGQL-SGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446042612 189 RKF-RQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMD 234
Cdd:PRK10771 173 SQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-205 |
4.20e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.14 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 2 SYIRVNNVGKAYRQYHSKTGRLIEWLSPLNTKRHNLKW-ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITG--TSRPT 78
Cdd:COG2401 6 PFFVLMRVTKVYSSVLDLSERVAIVLEAFGVELRVVERyVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 79 TGEIEI----SGRVAALLElgmgfhsDFTGRQNVYMSGQLL---GLSSekitelmPQIeefaeigdYIdQPVRVYSSGMQ 151
Cdd:COG2401 86 AGCVDVpdnqFGREASLID-------AIGRKGDFKDAVELLnavGLSD-------AVL--------WL-RRFKELSTGQK 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446042612 152 VRLAFSVATAIRPDVLIIDEALSVGD---AYFQHKSFERIrkFRQEGTTLLLVSHDK 205
Cdd:COG2401 143 FRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKL--ARRAGITLVVATHHY 197
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
41-244 |
4.79e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 71.69 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR-VAALLE------LGMGFHS------DFTGRQN 107
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGReVNAENEkwvrskVGLVFQDpddqvfSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 108 VYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFER 187
Cdd:PRK13647 101 VAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446042612 188 IRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEavmdyynaLLADKQ 244
Cdd:PRK13647 181 LDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS--------LLTDED 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
41-233 |
5.03e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.06 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR-------------VAALLELGMGFHSDFTGRQN 107
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqtakimreAVAIVPEGRRVFSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 108 VYMSG-----QLLGLSSEKITELMPQIEEFAEigdyidQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEAlSVGDA-YFQ 181
Cdd:PRK11614 101 LAMGGffaerDQFQERIKWVYELFPRLHERRI------QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP-SLGLApIII 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446042612 182 HKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVM 233
Cdd:PRK11614 174 QQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-235 |
5.51e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.75 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 1 MSYIRVNNVGKAYRQYHsktgrliewlsplntkrhnlkwILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTG 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVV----------------------ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSG 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 81 EIEISGRVAALLE-----LGMGFHS-DFTGRQNVY--MS-GqlLGLSSEKITELMPQIEEFAEI---GDYIDQPVRVYSS 148
Cdd:PRK11000 59 DLFIGEKRMNDVPpaergVGMVFQSyALYPHLSVAenMSfG--LKLAGAKKEEINQRVNQVAEVlqlAHLLDRKPKALSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 149 GMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKF-RQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEG 227
Cdd:PRK11000 137 GQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
....*...
gi 446042612 228 EPEAVMDY 235
Cdd:PRK11000 217 KPLELYHY 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
40-226 |
9.67e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.19 E-value: 9.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRV---------AALL--ELGMGFHS-----DFT 103
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlhqmdeearAKLRakHVGFVFQSfmlipTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 104 GRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDayfqHK 183
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD----RQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446042612 184 SFERIRKF-----RQEGTTLLLVSHDKQaIQSICDRAILLNKGQIEME 226
Cdd:PRK10584 181 TGDKIADLlfslnREHGTTLILVTHDLQ-LAARCDRRLRLVNGQLQEE 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
40-226 |
1.12e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.84 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALL-----------ELGM--GFH---SDFT 103
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaelrnqKLGFiyQFHhllPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 104 GRQNVYMSGQLLGLSSEKITElmPQIEEFAEIGdyIDQpvRVY------SSGMQVRLAFSVATAIRPDVLIIDEALSVGD 177
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINS--RALEMLAAVG--LEH--RANhrpselSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446042612 178 AYFQHKSFERIRKF-RQEGTTLLLVSHDKQAIQSIcDRAILLNKGQIEME 226
Cdd:PRK11629 178 ARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
41-218 |
1.73e-13 |
|
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: 71.93 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAAllelgmGFHSDFTGRQNVYMSGQ------- 113
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA------DADADSWRDQIAWVPQHpflfagt 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 114 -----LLGLSSEKITELMPQIE-----EF-AEIGDYIDQPV----RVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDA 178
Cdd:TIGR02857 412 iaeniRLARPDASDAEIREALEragldEFvAALPQGLDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446042612 179 YFQHKSFERIRKFRQeGTTLLLVSHDKqAIQSICDRAILL 218
Cdd:TIGR02857 492 ETEAEVLEALRALAQ-GRTVLLVTHRL-ALAALADRIVVL 529
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
40-223 |
2.30e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 69.27 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRvaallelgmgfHSDFTG----------RQNVY 109
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN-----------HFDFSKtpsdkairelRRNVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 110 MSGQ--------------------LLGLSSEKITELMPQIEEFAEIGDYIDQ-PVRVySSGMQVRLAFSVATAIRPDVLI 168
Cdd:PRK11124 86 MVFQqynlwphltvqqnlieapcrVLGLSKDQALARAEKLLERLRLKPYADRfPLHL-SGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446042612 169 IDEALSVGDAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQI 223
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
41-255 |
2.41e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSrPTTGEIEISGRvaALLELGmgfHSDFtGRQNVYMSGQ------- 113
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQ--PLEAWS---AAEL-ARHRAYLSQQqtppfam 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 114 ----LLGLS------SEKITELMPQIEEFAEIGDYIDQPVRVYSSG--MQVRLA---FSVATAIRPD--VLIIDE---AL 173
Cdd:PRK03695 85 pvfqYLTLHqpdktrTEAVASALNEVAEALGLDDKLGRSVNQLSGGewQRVRLAavvLQVWPDINPAgqLLLLDEpmnSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 174 SVGdayfQHKSFER-IRKFRQEGTTLLLVSHD-----KQAiqsicDRAILLNKGQIEMEGEPEAVMDYYNalLADKQNQS 247
Cdd:PRK03695 165 DVA----QQAALDRlLSELCQQGIAVVMSSHDlnhtlRHA-----DRVWLLKQGKLLASGRRDEVLTPEN--LAQVFGVN 233
|
....*...
gi 446042612 248 IKQVEHNG 255
Cdd:PRK03695 234 FRRLDVEG 241
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
40-232 |
4.24e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRvaalLELG---MGFHSDFTgrqnvymsgqlLG 116
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK----LRIGyvpQKLYLDTT-----------LP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 117 LSSEKITELMPQIE--------EFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERI 188
Cdd:PRK09544 84 LTVNRFLRLRPGTKkedilpalKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446042612 189 RKFRQE-GTTLLLVSHDKQAIQSICDRAILLNkGQIEMEGEPEAV 232
Cdd:PRK09544 164 DQLRRElDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVV 207
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
41-234 |
4.28e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.06 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG-----------RVAALLELGMGFHS-----DFTG 104
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelREVRRKKIAMVFQSfalmpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 105 RQNVYMSGQLLGLSSEKITElmPQIEEFAEIG--DYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQH 182
Cdd:PRK10070 124 LDNTAFGMELAGINAEERRE--KALDALRQVGleNYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446042612 183 KSFERIRKFR-QEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMD 234
Cdd:PRK10070 202 EMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
38-235 |
7.06e-13 |
|
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: 67.64 E-value: 7.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLELG-----MGFHSdftgrQNVYM-S 111
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAslrrqIGLVS-----QDVFLfN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 112 GQLlglsSEKIT-----ELMPQIEEFAEIG---DYIDQPVRVY-----------SSGMQVRLAFSVATAIRPDVLIIDEA 172
Cdd:cd03251 90 DTV----AENIAygrpgATREEVEEAARAAnahEFIMELPEGYdtvigergvklSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446042612 173 LSVGDAYFQH---KSFERIrkfrQEGTTLLLVSHDKQAIQSIcDRAILLNKGQIEMEGEPEAVMDY 235
Cdd:cd03251 166 TSALDTESERlvqAALERL----MKNRTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELLAQ 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
32-223 |
9.45e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.78 E-value: 9.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIeISGRV---------------AALL---- 92
Cdd:PRK11247 19 SKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAplaearedtrlmfqdARLLpwkk 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 93 ---ELGMGFHSDFtgRQNVYMSGQLLGLSSEKitelmpqieefaeigdyIDQPVRVySSGMQVRLAFSVATAIRPDVLII 169
Cdd:PRK11247 98 vidNVGLGLKGQW--RDAALQALAAVGLADRA-----------------NEWPAAL-SGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446042612 170 DEALSVGDAyfqhksFERI-------RKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQI 223
Cdd:PRK11247 158 DEPLGALDA------LTRIemqdlieSLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
40-218 |
1.06e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 66.36 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRvaallelGMGFHSDFTGRQNVYMsGQLLGLSS 119
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-------PLDFQRDSIARGLLYL-GHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 120 -----EKITELMP-----QIEE-FAEIG--DYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFE 186
Cdd:cd03231 87 tlsvlENLRFWHAdhsdeQVEEaLARVGlnGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
170 180 190
....*....|....*....|....*....|..
gi 446042612 187 RIRKFRQEGTTLLLVSHDKQAIQSICDRAILL 218
Cdd:cd03231 167 AMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
40-234 |
1.08e-12 |
|
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: 67.26 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLELgmgfHSdftGRQNVYMSGQLLGLSS 119
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTL----DS---LRRAIGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 120 EKI-----------TElmPQIEEFAEIGDYIDQPVRV---Y-----------SSGMQVRLAFSVATAIRPDVLIIDEALS 174
Cdd:cd03253 89 DTIgynirygrpdaTD--EEVIEAAKAAQIHDKIMRFpdgYdtivgerglklSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 175 VGDAYFQHKSFERIRKFRQeGTTLLLVSHDKQAIQSiCDRAILLNKGQIEMEGEPEAVMD 234
Cdd:cd03253 167 ALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
38-232 |
1.27e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 67.90 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRP---TTGEIEISG------RVAALLE-LGMGFHS---DFTG 104
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGitltakTVWDIREkVGIVFQNpdnQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 105 ---RQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQ 181
Cdd:PRK13640 100 atvGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446042612 182 HKSFERIRKFRQE-GTTLLLVSHD-KQAIQSicDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK13640 180 EQILKLIRKLKKKnNLTVISITHDiDEANMA--DQVLVLDDGKLLAQGSPVEI 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
43-227 |
1.35e-12 |
|
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: 66.36 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 43 DINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLE-----LGMGFH-----SDFTGRQNVYmsg 112
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPpadrpVSMLFQennlfAHLTVEQNVG--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 113 qlLGLS-SEKITELMPQIEEFAE----IGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFER 187
Cdd:cd03298 93 --LGLSpGLKLTAEDRQAIEVALarvgLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446042612 188 IRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEG 227
Cdd:cd03298 171 VLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
36-229 |
1.42e-12 |
|
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: 66.28 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 36 NLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLELGmgfhsdfTGRQNVYMSGQLL 115
Cdd:cd03369 19 DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE-------DLRSSLTIIPQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 116 GLSSEKITELMPQIEEFAEigDYIDQPVRVYSSGMQV----RLAFSVATAI--RPDVLIIDEALSVGDAYFQHKSFERIR 189
Cdd:cd03369 92 TLFSGTIRSNLDPFDEYSD--EEIYGALRVSEGGLNLsqgqRQLLCLARALlkRPRVLVLDEATASIDYATDALIQKTIR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446042612 190 KFRQeGTTLLLVSHDKQAIQSiCDRAILLNKGQIEMEGEP 229
Cdd:cd03369 170 EEFT-NSTILTIAHRLRTIID-YDKILVMDAGEVKEYDHP 207
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
40-228 |
1.61e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.92 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALL------ELG--------MGFhSDFTGR 105
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtpakahQLGiylvpqepLLF-PNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 106 QNVymsgqLLGL-----SSEKITELMPQIeefaeigdyidqpvrvyssGMQVRLAFSVATAIRPD--------------- 165
Cdd:PRK15439 105 ENI-----LFGLpkrqaSMQKMKQLLAAL-------------------GCQLDLDSSAGSLEVADrqiveilrglmrdsr 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446042612 166 VLIIDE---ALSVGDAyfqHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGE 228
Cdd:PRK15439 161 ILILDEptaSLTPAET---ERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
44-232 |
1.84e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.94 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 44 INFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLE----LGMGFHSDFtgrQNVYM--------- 110
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPghqiARMGVVRTF---QHVRLfremtvien 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 111 ----------SGQLLGL--------SSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEA 172
Cdd:PRK11300 101 llvaqhqqlkTGLFSGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446042612 173 LSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
40-205 |
2.06e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.74 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG------RVAALLELGM-----GFHSDFTGRQNV 108
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdLCTYQKQLCFvghrsGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 109 YMSgqlLGLSSE--KITELMpqieEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFE 186
Cdd:PRK13540 96 LYD---IHFSPGavGITELC----RLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168
|
170
....*....|....*....
gi 446042612 187 RIRKFRQEGTTLLLVSHDK 205
Cdd:PRK13540 169 KIQEHRAKGGAVLLTSHQD 187
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
41-241 |
2.34e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.07 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG-----------------RVAALLELGMGFHSDFT 103
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqkeikpvrkKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 104 GRQNVYMSGQLLGLSSEKITELMPQIEEFAEIG-DYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQH 182
Cdd:PRK13643 102 VLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446042612 183 KSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMDYYNALLA 241
Cdd:PRK13643 182 EMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKA 240
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
40-234 |
2.56e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.60 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRvaALLELGMGF---HSDFTGRQNVYMSGQL-- 114
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV--PLVQYDHHYlhrQVALVGQEPVLFSGSVre 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 115 ---LGLSSEKITELMPQIEEfAEIGDYIDQPVRVY-----------SSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYF 180
Cdd:TIGR00958 574 niaYGLTDTPDEEIMAAAKA-ANAHDFIMEFPNGYdtevgekgsqlSGGQKQRIAIARALVRKPRVLILDEATSALDAEC 652
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446042612 181 QHkSFERIRKFrqEGTTLLLVSHDKQAIQSiCDRAILLNKGQIEMEGEPEAVMD 234
Cdd:TIGR00958 653 EQ-LLQESRSR--ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLME 702
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
41-232 |
3.13e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.78 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG-----------------RVAALLELGMGFHSDFT 103
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 104 GRQNVYMSGQLLGLSSEKITElmPQIEEFAEIG---DYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYF 180
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKE--KALKWLKKVGlseDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446042612 181 QHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
41-221 |
3.73e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALL------ELGMGF-------HSDFTGRQN 107
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLdhklaaQLGIGIiyqelsvIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 108 VYM----SGQLLGLSSEKITELMPQIEEFA-EIGDYIDQPVRV----YSSGMQVRLAFSVATAIRpdVLIIDEALSVGDA 178
Cdd:PRK09700 101 LYIgrhlTKKVCGVNIIDWREMRVRAAMMLlRVGLKVDLDEKVanlsISHKQMLEIAKTLMLDAK--VIIMDEPTSSLTN 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446042612 179 YFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKG 221
Cdd:PRK09700 179 KEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
40-171 |
3.85e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.90 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLELGMGF----HSDF-----TGRQNVYM 110
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAChylgHRNAmkpalTVAENLEF 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446042612 111 SGQLLGLSSEKITELMpqieEFAEIGDYIDQPVRVYSSGMQVRLAFS-VATAIRPdVLIIDE 171
Cdd:PRK13539 97 WAAFLGGEELDIAAAL----EAVGLAPLAHLPFGYLSAGQKRRVALArLLVSNRP-IWILDE 153
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
40-226 |
4.94e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.12 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLelgmgfhSDFTGRQNVYMSGQLLGLSS 119
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTL-------KPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 120 E----------KITELMPQIEEFA------EIGDYI-DQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQH 182
Cdd:PRK10247 95 DtvydnlifpwQIRNQQPDPAIFLddlerfALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446042612 183 KSFERIRKF-RQEGTTLLLVSHDKQAIQSiCDRAILLNKGQIEME 226
Cdd:PRK10247 175 NVNEIIHRYvREQNIAVLWVTHDKDEINH-ADKVITLQPHAGEMQ 218
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
41-270 |
5.38e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.69 E-value: 5.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPT-TGEIEISGRVAALLELGMGFHSdfTGRQNVYMSGQllgLSS 119
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSVAYVPQVSWIFNA--TVRENILFGSD---FES 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 120 EK------ITELMPQIEEFA-----EIGdyiDQPVRVySSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERI 188
Cdd:PLN03232 708 ERywraidVTALQHDLDLLPgrdltEIG---ERGVNI-SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSC 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 189 RKFRQEGTTLLLVSHDKQAIQSIcDRAILLNKGQIEMEGEPEAVM---DYYNALL--ADKQNQSIKQVEHNGKTQTVSGT 263
Cdd:PLN03232 784 MKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSksgSLFKKLMenAGKMDATQEVNTNDENILKLGPT 862
|
....*..
gi 446042612 264 GEVTISE 270
Cdd:PLN03232 863 VTIDVSE 869
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-223 |
5.44e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.45 E-value: 5.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 36 NLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAAL-------------LELGMGFHS-- 100
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFgkdifqidaiklrKEVGMVFQQpn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 101 ---DFTGRQNVYMSGQLLGLSSEK-----ITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEA 172
Cdd:PRK14246 101 pfpHLSIYDNIAYPLKSHGIKEKReikkiVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446042612 173 LSVGDAYFQHKSFERIRKFRQEgTTLLLVSHDKQAIQSICDRAILLNKGQI 223
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
44-229 |
6.90e-12 |
|
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: 67.73 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 44 INFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR------VAALLELGMG------FHSdFTGRQNVYMS 111
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnlDAVRQSLGMCpqhnilFHH-LTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 112 GQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKF 191
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY 1107
|
170 180 190
....*....|....*....|....*....|....*...
gi 446042612 192 RQeGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEP 229
Cdd:TIGR01257 1108 RS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
40-232 |
6.91e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.17 E-value: 6.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR----------VAALLELGMGFHSD--FTG--- 104
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamsrsrlYTVRKRMSMLFQSGalFTDmnv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 105 -------------------RQNVYMSGQLLGLSSEkiTELMPqieefAEIgdyidqpvrvySSGMQVRLAFSVATAIRPD 165
Cdd:PRK11831 102 fdnvayplrehtqlpapllHSTVMMKLEAVGLRGA--AKLMP-----SEL-----------SGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446042612 166 VLIIDEALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
41-232 |
7.75e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.57 E-value: 7.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGrvaalLELGMGFHSDF--TGRQNVYM-----SGQ 113
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDD-----ITITHKTKDKYirPVRKRIGMvfqfpESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 114 LLGLSSEKITELMP--------QIEEFA-----EIG---DYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGD 177
Cdd:PRK13646 98 LFEDTVEREIIFGPknfkmnldEVKNYAhrllmDLGfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446042612 178 AYFQHKSFERIRKFR-QEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK13646 178 PQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
42-155 |
9.34e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.67 E-value: 9.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 42 SDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRV---------AALLELG--MGFHSDFTGRQNVYM 110
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPirrqrdeyhQDLLYLGhqPGIKTELTALENLRF 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446042612 111 SGQLLGLSSEkitELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLA 155
Cdd:PRK13538 98 YQRLHGPGDD---EALWEALAQVGLAGFEDVPVRQLSAGQQRRVA 139
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
34-209 |
1.02e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 63.65 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 34 RHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRP---TTGEIEISGRVAALL-----ELGMGFHSD---- 101
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALpaeqrRIGILFQDDllfp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 102 -FTGRQNVymsgqLLGLS-----SEKITELMPQIEEfAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSV 175
Cdd:COG4136 90 hLSVGENL-----AFALPptigrAQRRARVEQALEE-AGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 446042612 176 GDA----YFQHKSFERIrkfRQEGTTLLLVSHDKQAIQ 209
Cdd:COG4136 164 LDAalraQFREFVFEQI---RQRGIPALLVTHDEEDAP 198
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
40-223 |
1.15e-11 |
|
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: 64.03 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLELGMgFHSDFT--GRQNVYMSGQ---- 113
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY-LHSKVSlvGQEPVLFARSlqdn 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 114 ----LLGLSSEKITELMPQ------IEEFA-EIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQH 182
Cdd:cd03248 108 iaygLQSCSFECVKEAAQKahahsfISELAsGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446042612 183 KSFERIRKFrQEGTTLLLVSHDKQAIQSiCDRAILLNKGQI 223
Cdd:cd03248 188 QVQQALYDW-PERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
31-223 |
1.16e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 31 NTKRHNLKWIlSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAAL------LELGM-------- 96
Cdd:PRK09700 270 NVTSRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPrspldaVKKGMayitesrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 97 --GFHSDFTGRQNVYMSGQL--------LGLSSE----KITElmPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAI 162
Cdd:PRK09700 349 dnGFFPNFSIAQNMAISRSLkdggykgaMGLFHEvdeqRTAE--NQRELLALKCHSVNQNITELSGGNQQKVLISKWLCC 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446042612 163 RPDVLIIDEALSVGDAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQI 223
Cdd:PRK09700 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
38-237 |
1.40e-11 |
|
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: 63.31 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTS--RPTTGEIEISGRVaaLLELGMgfhsDFTGRQNVYMSGQll 115
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGED--ITDLPP----EERARLGIFLAFQ-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 116 glSSEKITELmpqieefaEIGDYIdQPVRV-YSSGMQVRLAFSVATAIRPDVLIIDE--------ALSVgdayfqhkSFE 186
Cdd:cd03217 85 --YPPEIPGV--------KNADFL-RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEpdsgldidALRL--------VAE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446042612 187 RIRKFRQEGTTLLLVSHDKQAIQSI-CDRAILLNKGQIEMEGEPEAVMDYYN 237
Cdd:cd03217 146 VINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALEIEK 197
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
41-229 |
1.49e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 64.34 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG-RVAA------LLELGMGFH---SDFTG---RQN 107
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGeLLTAenvwnlRRKIGMVFQnpdNQFVGatvEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 108 VYMSGQLLGLSSEkitELMPQIEEFAEIGDYID----QPVRVySSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHK 183
Cdd:PRK13642 103 VAFGMENQGIPRE---EMIKRVDEALLAVNMLDfktrEPARL-SGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446042612 184 SFERIRKFRQE-GTTLLLVSHDKQAIQSiCDRAILLNKGQIEMEGEP 229
Cdd:PRK13642 179 IMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAP 224
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
32-243 |
1.73e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.68 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAallelgMGF----HS-DFTGRQ 106
Cdd:PRK15064 326 TKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENAN------IGYyaqdHAyDFENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 107 NVY--MS----------------GQLLglssekitelmpqieeFAeiGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLI 168
Cdd:PRK15064 400 TLFdwMSqwrqegddeqavrgtlGRLL----------------FS--QDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 169 IDEALSvgdayfqHKSFERI-------RKFrqEGtTLLLVSHDKQAIQSICDRAIllnkgqiemEGEPEAVMDY---YNA 238
Cdd:PRK15064 462 MDEPTN-------HMDMESIeslnmalEKY--EG-TLIFVSHDREFVSSLATRII---------EITPDGVVDFsgtYEE 522
|
....*
gi 446042612 239 LLADK 243
Cdd:PRK15064 523 YLRSQ 527
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-84 |
1.89e-11 |
|
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: 65.73 E-value: 1.89e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEI 84
Cdd:TIGR03719 329 TKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
32-256 |
2.41e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.56 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG------------RVAALLELGMGFH 99
Cdd:COG4604 8 SKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvattpsrelaKRLAILRQENHIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 100 SDFTGRQNV------YMSGQLLGLSSEKITELMpqieEFAEIGD----YIDQpvrvySSGMQVRLAFsVATAI--RPDVL 167
Cdd:COG4604 88 SRLTVRELVafgrfpYSKGRLTAEDREIIDEAI----AYLDLEDladrYLDE-----LSGGQRQRAF-IAMVLaqDTDYV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 168 IIDEALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMDyyNALLADKQNQ 246
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIIT--PEVLSDIYDT 235
|
250
....*....|
gi 446042612 247 SIKQVEHNGK 256
Cdd:COG4604 236 DIEVEEIDGK 245
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
41-232 |
2.51e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 63.67 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR---VAALLEL----GMGFHS------DFTGRQN 107
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitKENIREVrkfvGLVFQNpddqifSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 108 VYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFER 187
Cdd:PRK13652 100 IAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDF 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446042612 188 IRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK13652 180 LNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
31-234 |
2.53e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.10 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 31 NTKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISgrvaallELGMGFHSDFTGRQNVYM 110
Cdd:PRK13631 32 DEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG-------DIYIGDKKNNHELITNPY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 111 SGQLLGLSS-EKITELMPQIEEFAEIGDYIDQ-----PVRV-------------------------------YSSGMQVR 153
Cdd:PRK13631 105 SKKIKNFKElRRRVSMVFQFPEYQLFKDTIEKdimfgPVALgvkkseakklakfylnkmglddsylerspfgLSGGQKRR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 154 LAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEP-EAV 232
Cdd:PRK13631 185 VAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPyEIF 264
|
..
gi 446042612 233 MD 234
Cdd:PRK13631 265 TD 266
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
40-233 |
3.63e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.99 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLEL------GMGF---HSDFTGRQNVYm 110
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhararrGIGYlpqEASIFRRLSVY- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 111 sGQLLG-------LSSE----KITELMpqiEEF--AEIGDYIDQPVrvySSGMQVRLAFSVATAIRPDVLIIDEALSVGD 177
Cdd:PRK10895 97 -DNLMAvlqirddLSAEqredRANELM---EEFhiEHLRDSMGQSL---SGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446042612 178 AYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVM 233
Cdd:PRK10895 170 PISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
34-229 |
4.33e-11 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 62.13 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 34 RHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR---VAALLELgmgfhsdftgRQN--- 107
Cdd:cd03244 13 RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdisKIGLHDL----------RSRisi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 108 -----VYMSGQL------LGLSSE----KITELMPQIEEFAEIGDYIDQPV----RVYSSGmQVRLaFSVATAI--RPDV 166
Cdd:cd03244 83 ipqdpVLFSGTIrsnldpFGEYSDeelwQALERVGLKEFVESLPGGLDTVVeeggENLSVG-QRQL-LCLARALlrKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446042612 167 LIIDEALSVGDayfqHKSFERIRK-FRQE--GTTLLLVSHdkqAIQSI--CDRAILLNKGQIEMEGEP 229
Cdd:cd03244 161 LVLDEATASVD----PETDALIQKtIREAfkDCTVLTIAH---RLDTIidSDRILVLDKGRVVEFDSP 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
43-241 |
5.23e-11 |
|
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: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 43 DINFEVAPGEAVGIIGINGAGKSTL----LKLItgtsrPTTGEIEISGR------------------------------- 87
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQdldglsrralrplrrrmqvvfqdpfgslspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 88 --VAALLELGMGFHSDftgrqnvymsgqllGLSSEKITELMpqIEEFAEIG---DYIDQPVRVYSSGMQVRLAFSVATAI 162
Cdd:COG4172 379 mtVGQIIAEGLRVHGP--------------GLSAAERRARV--AEALEEVGldpAARHRYPHEFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 163 RPDVLIIDEALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVM-----DYY 236
Cdd:COG4172 443 EPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFdapqhPYT 522
|
....*
gi 446042612 237 NALLA 241
Cdd:COG4172 523 RALLA 527
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-233 |
5.39e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.50 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYRQyhsKTGrlieWLsplntKRHNLKWIlSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE 83
Cdd:PRK15112 5 LEVRNLSKTFRY---RTG----WF-----RRQTVEAV-KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 84 ISGRVaalLELG----------MGFHSDFTG---RQNVymsGQLLGLSSEKITELMPQ------IEEFAEIG---DYIDQ 141
Cdd:PRK15112 72 IDDHP---LHFGdysyrsqrirMIFQDPSTSlnpRQRI---SQILDFPLRLNTDLEPEqrekqiIETLRQVGllpDHASY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 142 PVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNK 220
Cdd:PRK15112 146 YPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQ 225
|
250
....*....|...
gi 446042612 221 GQIEMEGEPEAVM 233
Cdd:PRK15112 226 GEVVERGSTADVL 238
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-84 |
5.70e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 4 IRVNNVGKAYRqyhsktGR-LIEwlsplntkrhnlkwilsDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEI 82
Cdd:PRK11819 325 IEAENLSKSFG------DRlLID-----------------DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
..
gi 446042612 83 EI 84
Cdd:PRK11819 382 KI 383
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
31-233 |
5.75e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.50 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 31 NTKRHNLKWILSDINFEVA-------------PGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAAllelgmG 97
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE------S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 98 FHSDFTGRQNVYMSGQLLGLSSEKITELMP-------------QIEEFAEIGDYID----QP-----VRVYSSGMQVR-- 153
Cdd:PRK10575 78 WSSKAFARKVAYLPQQLPAAEGMTVRELVAigrypwhgalgrfGAADREKVEEAISlvglKPlahrlVDSLSGGERQRaw 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 154 LAFSVATAIRpdVLIIDEALSVGDAYFQHKSFERIRKF-RQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK10575 158 IAMLVAQDSR--CLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
.
gi 446042612 233 M 233
Cdd:PRK10575 236 M 236
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
32-234 |
5.77e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.25 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLEL-GMG-------FHSDFt 103
Cdd:PRK11701 13 TKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyALSeaerrrlLRTEW- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 104 G--RQNVyMSGQLLGLSS-EKITE-LMP-------QIEEFA-------EIG-DYIDQPVRVYSSGMQVRLAFSVATAIRP 164
Cdd:PRK11701 92 GfvHQHP-RDGLRMQVSAgGNIGErLMAvgarhygDIRATAgdwlervEIDaARIDDLPTTFSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446042612 165 DVLIIDEALSVGDAYFQHKSFERIRKF-RQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMD 234
Cdd:PRK11701 171 RLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLD 241
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
41-233 |
1.06e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.60 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTT-GEIEISGRVAALLELGMGFHSdfTGRQNVymsgqLLGLSS 119
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQVSWIFNA--TVRDNI-----LFGSPF 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 120 E--------KITELMPQIE-----EFAEIGdyiDQPVRVySSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFE 186
Cdd:PLN03130 706 DperyeraiDVTALQHDLDllpggDLTEIG---ERGVNI-SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD 781
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446042612 187 RIRKFRQEGTTLLLVSHDKQAIQSIcDRAILLNKGQIEMEGEPEAVM 233
Cdd:PLN03130 782 KCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELS 827
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
33-233 |
1.12e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.77 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 33 KRHNLkwILSDINFEVAPGEAVGIIGINGAGKSTLLKL----ITGTSRP----TTGEIEISG------------RVAALL 92
Cdd:PRK13547 11 RRHRA--ILRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPrgarVTGDVTLNGeplaaidaprlaRLRAVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 93 ----ELGMGFHSD---FTGRqnvYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAF--------- 156
Cdd:PRK13547 89 pqaaQPAFAFSAReivLLGR---YPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFarvlaqlwp 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446042612 157 SVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKF-RQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVM 233
Cdd:PRK13547 166 PHDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
44-228 |
1.19e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.07 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 44 INFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR------VAALLELgmgFHSDFTgrqNVYMSGQLLG- 116
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpvtaeqPEDYRKL---FSAVFT---DFHLFDQLLGp 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 117 LSSEKITELMPQIEEFAEIGDYID-QPVRV----YSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQhKSFER--IR 189
Cdd:PRK10522 416 EGKPANPALVEKWLERLKMAHKLElEDGRIsnlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFR-REFYQvlLP 494
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446042612 190 KFRQEGTTLLLVSHDKQAIQSiCDRAILLNKGQI-EMEGE 228
Cdd:PRK10522 495 LLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLsELTGE 533
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
35-231 |
1.48e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.81 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 35 HNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLELgmgfhSDFTGRQNVYmsGQL 114
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQL-----DSWRSRLAVV--SQT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 115 LGLSSEKITELMP---------QIEEFAEIGDYIDQPVRV--------------YSSGMQVRLAFSVATAIRPDVLIIDE 171
Cdd:PRK10789 398 PFLFSDTVANNIAlgrpdatqqEIEHVARLASVHDDILRLpqgydtevgergvmLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 172 ALSVGDAYFQHKSFERIRKFRQeGTTLLLVSHDKQAIQSiCDRAILLNKGQIEMEGEPEA 231
Cdd:PRK10789 478 ALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQ 535
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
44-228 |
1.55e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.06 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 44 INFEVAPGEAVGIIGINGAG--KSTLLKLITGTS---RPTTGEIEISGRVAALLELGM------GFHSDFTGRQNVYMSG 112
Cdd:NF000106 32 VDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDagrRPWRF*TWCANRRALRRTIG*hrpvr*GRRESFSGRENLYMIG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 113 QLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKFR 192
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV 191
|
170 180 190
....*....|....*....|....*....|....*.
gi 446042612 193 QEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGE 228
Cdd:NF000106 192 RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
40-223 |
1.87e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.43 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR---------VAALLELGMGF-----H--SDFT 103
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvatldadaLAQLRREHFGFifqryHllSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 104 GRQNVYMSGQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHK 183
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446042612 184 SFERIRKFRQEGTTLLLVSHDKQ-AIQSicDRAILLNKGQI 223
Cdd:PRK10535 183 VMAILHQLRDRGHTVIIVTHDPQvAAQA--ERVIEIRDGEI 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
40-204 |
2.67e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.48 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR--VAALLELGMGFHSD-----FTGRQNVYMSG 112
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpvEGPGAERGVVFQNEgllpwRNVQDNVAFGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 113 QLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKFR 192
Cdd:PRK11248 96 QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLW 175
|
170
....*....|...
gi 446042612 193 QE-GTTLLLVSHD 204
Cdd:PRK11248 176 QEtGKQVLLITHD 188
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
43-171 |
3.56e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.06 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 43 DINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR-VAAllelgmgfhSDFTGRQNV-YMS--------- 111
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpVDA---------GDIATRRRVgYMSqafslygel 354
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446042612 112 ---------GQLLGLSSEKITelmPQIEEFAE---IGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDE 171
Cdd:NF033858 355 tvrqnlelhARLFHLPAAEIA---ARVAEMLErfdLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
38-241 |
3.77e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.64 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKST----LLKLItgtsrPTTGEIEISGRVAALL----------ELGMGF---HS 100
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLnrrqllpvrhRIQVVFqdpNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 101 DFTGRQNVYmsgQLL---------GLSSEKITELMpqIEEFAEIGdyIDQPVR-----VYSSGMQVRLAFSVATAIRPDV 166
Cdd:PRK15134 374 SLNPRLNVL---QIIeeglrvhqpTLSAAQREQQV--IAVMEEVG--LDPETRhrypaEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 167 LIIDEALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVM-----DYYNALL 240
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFaapqqEYTRQLL 526
|
.
gi 446042612 241 A 241
Cdd:PRK15134 527 A 527
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
41-232 |
4.85e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.03 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAA-------LLEL----GMGF----HSDF--T 103
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkkLKPLrkkvGIVFqfpeHQLFeeT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 104 GRQNVYMSGQLLGLSSEKITELMPqiEEFAEIG---DYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYF 180
Cdd:PRK13634 103 VEKDICFGPMNFGVSEEDAKQKAR--EMIELVGlpeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446042612 181 QHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK13634 181 RKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
41-232 |
5.17e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 59.76 E-value: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRV-----------AALLELGMGFH------SDFT 103
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikQIRKKVGLVFQfpesqlFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 104 GRQNVYMSGQLLGLSSEKITELmpQIEEFAEIG---DYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYF 180
Cdd:PRK13649 103 VLKDVAFGPQNFGVSQEEAEAL--AREKLALVGiseSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446042612 181 QHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
42-223 |
5.19e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 42 SDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEI-----EISGR-VAALLELGM----------GFHSDFTGR 105
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRImlngkEINALsTAQRLARGLvylpedrqssGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 106 QNV--YMSGQL---LGLSSEKITelmpqIEEF-AEIG---DYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVG 176
Cdd:PRK15439 360 WNVcaLTHNRRgfwIKPARENAV-----LERYrRALNikfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446042612 177 DAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQI 223
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
41-241 |
5.77e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.51 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR-------------VAALLELGMGFHSDFtgrQN 107
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlvayVPQSEEVDWSFPVLV---ED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 108 VYMSGQ-----LLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQH 182
Cdd:PRK15056 100 VVMMGRyghmgWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446042612 183 KSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLnKGQIEMEGEPEAVMDYYNALLA 241
Cdd:PRK15056 180 RIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFTAENLELA 237
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
40-223 |
9.13e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.64 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAallelgMGFHS-------DFTGRQNVYMSG 112
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVR------MAVFSqhhvdglDLSSNPLLYMMR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 113 QLLGLSSEKiteLMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIID-----------EALSVGDAYFQ 181
Cdd:PLN03073 598 CFPGVPEQK---LRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDepsnhldldavEALIQGLVLFQ 674
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446042612 182 hksferirkfrqegTTLLLVSHDKQAIQSICDRAILLNKGQI 223
Cdd:PLN03073 675 --------------GGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
40-225 |
1.39e-09 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 57.76 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGeiEISGRVAALLELGMG--FHSDFTGRQNVYMSGQLLGL 117
Cdd:PRK15177 2 VLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEG--DFIGLRGDALPLGANsfILPGLTGEENARMMASLYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 118 SSEKITELMPQIEEFAEIgdYIDQpVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIR-KFRQEGt 196
Cdd:PRK15177 80 DGDEFSHFCYQLTQLEQC--YTDR-VSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAALAcQLQQKG- 155
|
170 180
....*....|....*....|....*....
gi 446042612 197 tLLLVSHDKQAIQSICDRAILLNKGQIEM 225
Cdd:PRK15177 156 -LIVLTHNPRLIKEHCHAFGVLLHGKITM 183
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
40-157 |
1.46e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR----------VAALLELGmGFHSDFTGRQNVY 109
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHLP-GLKADLSTLENLH 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446042612 110 MSGQLLGLSSEKitelMPQiEEFAEIG--DYIDQPVRVYSSGMQVRLAFS 157
Cdd:PRK13543 105 FLCGLHGRRAKQ----MPG-SALAIVGlaGYEDTLVRQLSAGQKKRLALA 149
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
40-203 |
2.00e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.44 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEI--SGRVAAL-----LELGmgfhsdfTGRQNVYMSG 112
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLpqrpyLPLG-------TLREALLYPA 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 113 QLLGLSSEKITELMpqieEFAEIGDYI---DQPV---RVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFE 186
Cdd:COG4178 451 TAEAFSDAELREAL----EAVGLGHLAerlDEEAdwdQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ 526
|
170
....*....|....*..
gi 446042612 187 RIRKfRQEGTTLLLVSH 203
Cdd:COG4178 527 LLRE-ELPGTTVISVGH 542
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
43-226 |
2.52e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.20 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 43 DINFEVAPGEAVGIIGINGAGKS----TLLKLITGTSRpTTGEIEISGRVAALL-----------ELGMGFHSDFTGrQN 107
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREILNLpekelnklraeQISMIFQDPMTS-LN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 108 VYMSgqllglSSEKITEL------MPQIEEFAE---IGDYIDQP-----VRVY----SSGMQVRLAFSVATAIRPDVLII 169
Cdd:PRK09473 112 PYMR------VGEQLMEVlmlhkgMSKAEAFEEsvrMLDAVKMPearkrMKMYphefSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446042612 170 DEALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIeME 226
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRT-ME 242
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
51-229 |
4.61e-09 |
|
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: 56.65 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 51 GEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAAL----LElgmgfhSDFTGRQNVYMSGQL--LGLSSEKITE 124
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYkpqyIK------ADYEGTVRDLLSSITkdFYTHPYFKTE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 125 LM-P-QIEefaeigDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKF-RQEGTTLLLV 201
Cdd:cd03237 99 IAkPlQIE------QILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaENNEKTAFVV 172
|
170 180
....*....|....*....|....*...
gi 446042612 202 SHDKQAIQSICDRAILLnkgqiemEGEP 229
Cdd:cd03237 173 EHDIIMIDYLADRLIVF-------EGEP 193
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
34-223 |
5.59e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 34 RHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGT-------------SRPTTGEI--EIS---GRVAALLelg 95
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpqgysndltlfgRRRGSGETiwDIKkhiGYVSSSL--- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 96 mgfHSDF---TGRQNVYMSGQL--LGL---SSEKITELMPQIEEFAEIGDYI-DQPVRVYSSGMQvRLAFSV-ATAIRPD 165
Cdd:PRK10938 346 ---HLDYrvsTSVRNVILSGFFdsIGIyqaVSDRQQKLAQQWLDILGIDKRTaDAPFHSLSWGQQ-RLALIVrALVKHPT 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446042612 166 VLIIDEALSVGDAyfqhksFER--IRKF-----RQEGTTLLLVSH-DKQAIQSICDRAILLNKGQI 223
Cdd:PRK10938 422 LLILDEPLQGLDP------LNRqlVRRFvdvliSEGETQLLFVSHhAEDAPACITHRLEFVPDGDI 481
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
50-217 |
6.07e-09 |
|
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: 54.30 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 50 PGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIeisgrvaallelgmgfhsdftgrqnVYMSGqllglssekitELMPQI 129
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-------------------------IYIDG-----------EDILEE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 130 EEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIR------KFRQEGTTLLLVSH 203
Cdd:smart00382 45 VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllllLKSEKNLTVILTTN 124
|
170
....*....|....
gi 446042612 204 DKQAIQSICDRAIL 217
Cdd:smart00382 125 DEKDLGPALLRRRF 138
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
35-234 |
8.33e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.94 E-value: 8.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 35 HNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLIT--GTSRP---TTGEIEISGR---------VAALLELGMGFHS 100
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHniysprtdtVDLRKEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 101 ----DFTGRQNVYMSgqlLGLSSEKITELMPQIEEFAEIGDYIDQPV--RVYSS------GMQVRLAFSVATAIRPDVLI 168
Cdd:PRK14239 95 pnpfPMSIYENVVYG---LRLKGIKDKQVLDEAVEKSLKGASIWDEVkdRLHDSalglsgGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446042612 169 IDEALSVGDAYFQHKSFERIRKFRQEgTTLLLVSHDKQAIQSICDR-AILLNKGQIEMEGEPEAVMD 234
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRtGFFLDGDLIEYNDTKQMFMN 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-227 |
1.01e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 55.69 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLK----LITGTSRP-TTGEIEISGR---VAALLELgmgfhsdftgRQNVYMS 111
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEArVSGEVYLDGQdifKMDVIEL----------RRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 112 GQL--------------LGLS-----------SEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDV 166
Cdd:PRK14247 88 FQIpnpipnlsifenvaLGLKlnrlvkskkelQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446042612 167 LIIDEALSVGDAYFQHKSFERIRKFRQEgTTLLLVSHDKQAIQSICDRAILLNKGQIEMEG 227
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
29-203 |
1.11e-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: 54.08 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 29 PLNTKRHNLkwILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEIsgrvaallelgmgfhsdfTGRQNV 108
Cdd:cd03223 7 SLATPDGRV--LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM------------------PEGEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 109 YMsgqllglssekitelMPQIEEFAeIGDYIDQPV----RVYSSGMQVRLAFsvATAI--RPDVLIIDEALSVGDayfqH 182
Cdd:cd03223 67 LF---------------LPQRPYLP-LGTLREQLIypwdDVLSGGEQQRLAF--ARLLlhKPKFVFLDEATSALD----E 124
|
170 180
....*....|....*....|..
gi 446042612 183 KSFERI-RKFRQEGTTLLLVSH 203
Cdd:cd03223 125 ESEDRLyQLLKELGITVISVGH 146
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
38-237 |
1.20e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.04 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLElgmgfHSDFtgRQNVYMSGQ---- 113
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-----HSVL--RQGVAMVQQdpvv 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 114 ---------LLG--LSSEKITELMPQIeEFAEIgdyidqpVRVYSSGMQVRLA-----FSV------ATA----IRPDVL 167
Cdd:PRK10790 427 ladtflanvTLGrdISEEQVWQALETV-QLAEL-------ARSLPDGLYTPLGeqgnnLSVgqkqllALArvlvQTPQIL 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446042612 168 IIDEALSVGDAYFQHKSFERIRKFRQEgTTLLLVSHDKQAIQSiCDRAILLNKGQIEMEGEPEAVMD----YYN 237
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAaqgrYWQ 570
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
40-243 |
1.48e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 56.37 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR-VAAL----LELGMGFHSdftgrQNVYM-SGQ 113
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpIADYseaaLRQAISVVS-----QRVHLfSAT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 114 L---LGLSSEKITElmpqiEEFAEI------GDYIDQPV----------RVYSSGMQVRLAfsVATAIRPD--VLIIDEA 172
Cdd:PRK11160 430 LrdnLLLAAPNASD-----EALIEVlqqvglEKLLEDDKglnawlgeggRQLSGGEQRRLG--IARALLHDapLLLLDEP 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446042612 173 LSVGDAYFQHKSFERIRKFRQeGTTLLLVSHDKQAIQSIcDRAILLNKGQIEMEGEpeavmdyYNALLADK 243
Cdd:PRK11160 503 TEGLDAETERQILELLAEHAQ-NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGT-------HQELLAQQ 564
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
40-204 |
1.53e-08 |
|
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: 56.60 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEI-------------EISGRVAALLELGMGFHSdfTGRQ 106
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvssldqdEVRRRVSVCAQDAHLFDT--TVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 107 NVymsgqLLG---LSSEKITELMPQI---EEFAEIGDYIDQPV----RVYSSGMQVRLAFSVATAIRPDVLIIDE---AL 173
Cdd:TIGR02868 428 NL-----RLArpdATDEELWAALERVglaDWLRALPDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEpteHL 502
|
170 180 190
....*....|....*....|....*....|...
gi 446042612 174 SVGDAYfqhksfERIRKFRQ--EGTTLLLVSHD 204
Cdd:TIGR02868 503 DAETAD------ELLEDLLAalSGRTVVLITHH 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
44-246 |
1.59e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 56.39 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 44 INFEVAPGEAVGIIGINGAGKSTLLKLITGTSrPTTGEIEISGRvaALLELGMG---------------FHSdfTGRQNV 108
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGI--ELRELDPEswrkhlswvgqnpqlPHG--TLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 109 ymsgqLLG---LSSEKITELMPQ--IEEF-AEIGDYIDQPVRVYSSGMQV----RLAFSVATAIRPDVLIIDEALSVGDA 178
Cdd:PRK11174 444 -----LLGnpdASDEQLQQALENawVSEFlPLLPQGLDTPIGDQAAGLSVgqaqRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446042612 179 YFQHKSFERIRKFRQeGTTLLLVSHDKQAIQSiCDRAILLNKGQIEMEGEPEAVMD---YYNALLADKQNQ 246
Cdd:PRK11174 519 HSEQLVMQALNAASR-RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQaggLFATLLAHRQEE 587
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
40-233 |
2.30e-08 |
|
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: 54.47 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLELG-----MGFHS------DFTGRQNV 108
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwlrsqIGLVSqepvlfDGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 109 ymsgqLLGLSSEKITELMpQIEEFAEIGDYI-------DQPVRVY----SSGMQVRLAfsVATAI--RPDVLIIDEALSV 175
Cdd:cd03249 98 -----RYGKPDATDEEVE-EAAKKANIHDFImslpdgyDTLVGERgsqlSGGQKQRIA--IARALlrNPKILLLDEATSA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446042612 176 GDAYFQHKSFERIRKFRqEGTTLLLVSHDKQAIQSiCDRAILLNKGQIEMEGEPEAVM 233
Cdd:cd03249 170 LDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELM 225
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
44-240 |
2.72e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.13 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 44 INFEVAPGEAVGIIGINGAGKS----TLLKLITGTSRPTTGEIEISGR-------------VAAllELGMGFHSDFTGRQ 106
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQdlqrisekerrnlVGA--EVAMIFQDPMTSLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 107 NVYMSG-QLLGL-----SSEKITELMPQIEEFAEIGdyIDQP---VRVY----SSGMQVRLAFSVATAIRPDVLIIDEAL 173
Cdd:PRK11022 104 PCYTVGfQIMEAikvhqGGNKKTRRQRAIDLLNQVG--IPDPasrLDVYphqlSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446042612 174 SVGDAYFQHKSFERIRKF-RQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMD-----YYNALL 240
Cdd:PRK11022 182 TALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRaprhpYTQALL 254
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
40-241 |
3.05e-08 |
|
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: 55.46 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKS----TLLKLITGTSRPTTGEIEISGRvaALLEL-------------GMGF---- 98
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQ--DLLGLserelrrirgnriAMIFqepm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 99 ------HSdfTGRQnVYMSGQL-LGLSSEKITELMpqIEEFAEIGdyIDQPVRVYSS-------GMQVRLAFSVATAIRP 164
Cdd:COG4172 103 tslnplHT--IGKQ-IAEVLRLhRGLSGAAARARA--LELLERVG--IPDPERRLDAyphqlsgGQRQRVMIAMALANEP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 165 DVLIIDE---ALsvgDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVM-----DY 235
Cdd:COG4172 176 DLLIADEpttAL---DVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFaapqhPY 252
|
....*.
gi 446042612 236 YNALLA 241
Cdd:COG4172 253 TRKLLA 258
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
41-229 |
4.78e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.94 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLELgmgfhsdfTGRQNVYMSGQLLGLSS- 119
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKK--------TKEKEKVLEKLVIQKTRf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 120 ---EKITELMPQIE---EFAE------------------------------------IG---DYIDQPVRVYSSGMQVRL 154
Cdd:PRK13651 95 kkiKKIKEIRRRVGvvfQFAEyqlfeqtiekdiifgpvsmgvskeeakkraakyielVGldeSYLQRSPFELSGGQKRRV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446042612 155 AFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEP 229
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDT 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
43-241 |
5.39e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 43 DINFEVAPGEAVGIIGINGAGKS----TLLKLITGTS-----------RPTTGEIEISGRVAALL------ELGMGFHSD 101
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGglvqcdkmllrRRSRQVIELSEQSAAQMrhvrgaDMAMIFQEP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 102 FTGRQNVYMSGQLLGlSSEKITELMPQIEEFAEIGDYIDQpVRV-------------YSSGMQVRLAFSVATAIRPDVLI 168
Cdd:PRK10261 114 MTSLNPVFTVGEQIA-ESIRLHQGASREEAMVEAKRMLDQ-VRIpeaqtilsryphqLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446042612 169 IDEALSVGDAYFQHKSFERIRKFRQEGTT-LLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMD-----YYNALLA 241
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHapqhpYTRALLA 270
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
40-86 |
5.76e-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: 54.83 E-value: 5.76e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG 86
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDG 419
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
32-236 |
6.93e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 54.67 E-value: 6.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTT---GEIEISGRVAAL--------------LEL 94
Cdd:TIGR00955 32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPIDAkemraisayvqqddLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 95 GMgfhsdFTGRQNVYMSGQLlglsseKITELMPQIEEFAEIGDYIDQ---------------PVRVYSSGMQVRLAFSVA 159
Cdd:TIGR00955 112 PT-----LTVREHLMFQAHL------RMPRRVTKKEKRERVDEVLQAlglrkcantrigvpgRVKGLSGGERKRLAFASE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446042612 160 TAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQEGTTLLLVSHDKQA-IQSICDRAILLNKGQIEMEGEPEAVMDYY 236
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSeLFELFDKIILMAEGRVAYLGSPDQAVPFF 258
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
40-222 |
1.03e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 52.94 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAallelgmgFHSDF------TGRQNVymsgq 113
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRIS--------FSSQFswimpgTIKENI----- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 114 LLGLSSE--------KITELMPQIEEFAEiGDYI--DQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHK 183
Cdd:cd03291 119 IFGVSYDeyryksvvKACQLEEDITKFPE-KDNTvlGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446042612 184 SFER-IRKFRQEGTTLLLVS---HDKQAiqsicDRAILLNKGQ 222
Cdd:cd03291 198 IFEScVCKLMANKTRILVTSkmeHLKKA-----DKILILHEGS 235
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
32-241 |
1.52e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.79 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 32 TKRHNLKWIlSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAalleLGMGFHSDFTGRQNVYMS 111
Cdd:PRK15079 29 QPPKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL----LGMKDDEWRAVRSDIQMI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 112 GQllglssEKITELMPQIeefaEIGDYIDQPVRVY----------------------------------SSGMQVRLAFS 157
Cdd:PRK15079 104 FQ------DPLASLNPRM----TIGEIIAEPLRTYhpklsrqevkdrvkammlkvgllpnlinryphefSGGQCQRIGIA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 158 VATAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQiEME-GEPEAVMD- 234
Cdd:PRK15079 174 RALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH-AVElGTYDEVYHn 252
|
250
....*....|.
gi 446042612 235 ----YYNALLA 241
Cdd:PRK15079 253 plhpYTKALMS 263
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
38-81 |
1.62e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.40 E-value: 1.62e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGE 81
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE 61
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
41-223 |
1.76e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 53.04 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG---RVAALLELgmgfhsdftgRQNVYMSGQLLGL 117
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVTRASL----------RRNIAVVFQDAGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 118 SSEKIT------------ELMPQIEEFAEIGDYIDQPVRVY-----------SSGMQVRLAFSVATAIRPDVLIIDEALS 174
Cdd:PRK13657 421 FNRSIEdnirvgrpdatdEEMRAAAERAQAHDFIERKPDGYdtvvgergrqlSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446042612 175 VGDAYFQHKSFERIRKFRQEGTTlLLVSHDKQAIQSiCDRAILLNKGQI 223
Cdd:PRK13657 501 ALDVETEAKVKAALDELMKGRTT-FIIAHRLSTVRN-ADRILVFDNGRV 547
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
41-222 |
1.95e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAAL------LELGMGF-HSDFTG-RQNVYMSG 112
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFksskeaLENGISMvHQELNLvLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 113 QLLG--------LSSEKITELMPQIeeFAEIGDYIDQPVRVYS---SGMQ---VRLAFSVATAIrpdvLIIDEAL-SVGD 177
Cdd:PRK10982 94 MWLGryptkgmfVDQDKMYRDTKAI--FDELDIDIDPRAKVATlsvSQMQmieIAKAFSYNAKI----VIMDEPTsSLTE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446042612 178 AYFQHkSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQ 222
Cdd:PRK10982 168 KEVNH-LFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
42-87 |
3.82e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 3.82e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446042612 42 SDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR 87
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK 315
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
47-229 |
4.59e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 47 EVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVA---ALLElgmgfhSDFTGRQNVYMSGQLLGLSSEKI- 122
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISykpQYIK------PDYDGTVEDLLRSITDDLGSSYYk 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 123 TELM-P-QIEEFaeigdyIDQPVRVYSSG-MQvRLAFSVATAIRPDVLIIDEA---------LSVGDAyfqhksferIRK 190
Cdd:PRK13409 435 SEIIkPlQLERL------LDKNVKDLSGGeLQ-RVAIAACLSRDADLYLLDEPsahldveqrLAVAKA---------IRR 498
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446042612 191 F-RQEGTTLLLVSHDKQAIQSICDRAILLnkgqiemEGEP 229
Cdd:PRK13409 499 IaEEREATALVVDHDIYMIDYISDRLMVF-------EGEP 531
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
41-256 |
4.80e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 50.78 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLK----LITGTSRPTT------GEIEISGRVA-----ALLELGMGFHS-DFTG 104
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGShiellgRTVQREGRLArdirkSRANTGYIFQQfNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 105 RQNVyMSGQLLG-LSSEKI--------TELMPQ--IEEFAEIG--DYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDE 171
Cdd:PRK09984 100 RLSV-LENVLIGaLGSTPFwrtcfswfTREQKQraLQALTRVGmvHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 172 ALSVGDAYFQHKSFERIRKFRQ-EGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAvmdyYNALLADKQNQSIKQ 250
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ----FDNERFDHLYRSINR 254
|
....*.
gi 446042612 251 VEHNGK 256
Cdd:PRK09984 255 VEENAK 260
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-81 |
5.40e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 5.40e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446042612 32 TKRHNL-KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGE 81
Cdd:PRK11819 13 SKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE 63
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
41-222 |
7.33e-07 |
|
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: 50.98 E-value: 7.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTT--GEIEISGR--VA-----------ALLELGMGFHSDFTGR 105
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSplKAsnirdteragiVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 106 QNVYMSGQLL--------GLSSEKITELMPQIEEFAeigDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGD 177
Cdd:TIGR02633 97 ENIFLGNEITlpggrmayNAMYLRAKNLLRELQLDA---DNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446042612 178 AYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQ 222
Cdd:TIGR02633 174 EKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
41-234 |
7.54e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.48 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLElgMGFHSDFTGRQNVYMSGQLLGLSSE 120
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQ--QAWIQNDSLRENILFGKALNEKYYQ 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 121 KITE---LMPQIE-----EFAEIGdyiDQPVRVySSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERI--RK 190
Cdd:TIGR00957 732 QVLEacaLLPDLEilpsgDRTEIG---EKGVNL-SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigPE 807
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446042612 191 FRQEGTTLLLVSHDKQAIQSIcDRAILLNKGQIEMEGEPEAVMD 234
Cdd:TIGR00957 808 GVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
40-221 |
7.58e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.45 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAallelgmgFHSDF------TGRQNVymsgq 113
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRIS--------FSPQTswimpgTIKDNI----- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 114 LLGLSSE--------KITELMPQIEEFAEIGDYI--DQPVRVySSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHK 183
Cdd:TIGR01271 508 IFGLSYDeyrytsviKACQLEEDIALFPEKDKTVlgEGGITL-SGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446042612 184 SFER-IRKFRQEGTTLLLVS---HDKQAiqsicDRAILLNKG 221
Cdd:TIGR01271 587 IFEScLCKLMSNKTRILVTSkleHLKKA-----DKILLLHEG 623
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
47-229 |
1.11e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.55 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 47 EVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIE----IS-----------GRVAALLElgMGFHSDFTGrqNVYMS 111
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkISykpqyispdydGTVEEFLR--SANTDDFGS--SYYKT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 112 GQLLGLSSEKItelmpqieefaeigdyIDQPVRVYSSG-MQvRLAFSVATAIRPDVLIIDEA---------LSVGDAyfq 181
Cdd:COG1245 438 EIIKPLGLEKL----------------LDKNVKDLSGGeLQ-RVAIAACLSRDADLYLLDEPsahldveqrLAVAKA--- 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446042612 182 hksferIRKF-RQEGTTLLLVSHDKQAIQSICDRAILLnkgqiemEGEP 229
Cdd:COG1245 498 ------IRRFaENRGKTAMVVDHDIYLIDYISDRLMVF-------EGEP 533
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
41-229 |
1.38e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.62 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKL-----ITGTSRPTTGEIEISGRVAAL-------LELGMGF----HSDF-- 102
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliISETGQTIVGDYAIPANLKKIkevkrlrKEIGLVFqfpeYQLFqe 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 103 TGRQNVYMSGQLLGLSSEKITELMPQIEEFAEIG-DYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALS----VGD 177
Cdd:PRK13645 107 TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGgldpKGE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446042612 178 AYFQHkSFERIRKfrQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEP 229
Cdd:PRK13645 187 EDFIN-LFERLNK--EYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
41-171 |
1.63e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG--------------RVAALLE-LGMGFHSDFTGR 105
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdmadarhrravcpRIAYMPQgLGKNLYPTLSVF 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446042612 106 QNVYMSGQLLGLSSE----KITELM------PqieeFAeigdyiDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDE 171
Cdd:NF033858 97 ENLDFFGRLFGQDAAerrrRIDELLratglaP----FA------DRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 162
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
35-171 |
2.02e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.94 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 35 HNLKW-----ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEI--------EISGRVAALLELGMGFHSD 101
Cdd:PRK13541 5 HQLQFnieqkNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyykncninNIAKPYCTYIGHNLGLKLE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 102 FTGRQNVYMSGQLLglsseKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDE 171
Cdd:PRK13541 85 MTVFENLKFWSEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
50-230 |
2.05e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.94 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 50 PGEAV-GIIGINGAGKSTLLKLITGTSRPTTG-----EIEISGR----VAALLE----LGMGFHsdftgRQNVY----MS 111
Cdd:PRK14271 45 PARAVtSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRsifnYRDVLEfrrrVGMLFQ-----RPNPFpmsiMD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 112 GQLLGLSSEKiteLMPQIE-------EFAEIG--DYI-----DQPVRVySSGMQVRLAFSVATAIRPDVLIIDEALSVGD 177
Cdd:PRK14271 120 NVLAGVRAHK---LVPRKEfrgvaqaRLTEVGlwDAVkdrlsDSPFRL-SGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446042612 178 AYFQHKSFERIRKFrQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPE 230
Cdd:PRK14271 196 PTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTE 247
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
34-108 |
2.43e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.78 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 34 RHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR-VAA--LLELGMGFHS--------DF 102
Cdd:PTZ00243 1319 REGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGReIGAygLRELRRQFSMipqdpvlfDG 1398
|
....*.
gi 446042612 103 TGRQNV 108
Cdd:PTZ00243 1399 TVRQNV 1404
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
50-204 |
2.49e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.40 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 50 PGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLEL--GMGFHSDFT----GR-------QNVYM------ 110
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDEVLKRfrGTELQDYFKklanGEikvahkpQYVDLipkvfk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 111 --SGQLLglssEKITELMpQIEEFAE---IGDYIDQPVRVYSSG-MQvRLAFSVATAIRPDVLIIDEALSVGDAYfqhks 184
Cdd:COG1245 178 gtVRELL----EKVDERG-KLDELAEklgLENILDRDISELSGGeLQ-RVAIAAALLRDADFYFFDEPSSYLDIY----- 246
|
170 180
....*....|....*....|....*.
gi 446042612 185 fER------IRKFRQEGTTLLLVSHD 204
Cdd:COG1245 247 -QRlnvarlIRELAEEGKYVLVVEHD 271
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
33-223 |
2.68e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 47.64 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 33 KRHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTsrpTTGEIEISGRVAALLELGMGFHSDFTGrQNVYMSG 112
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDIHYNGIPYKEFAEKYPG-EIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 113 QLLGLSSEKITELMpqieEFAE--IGdyiDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERIRK 190
Cdd:cd03233 91 EDVHFPTLTVRETL----DFALrcKG---NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRT 163
|
170 180 190
....*....|....*....|....*....|....*
gi 446042612 191 FRQE--GTTLLLVSHDKQAIQSICDRAILLNKGQI 223
Cdd:cd03233 164 MADVlkTTTFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
34-229 |
3.82e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.17 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 34 RHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLEL-GMGFHSDFTGRQNVYMSG 112
Cdd:TIGR00957 1295 REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLhDLRFKITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 113 QL---LGLSSEKITELMPQIEEFAEIGDYID-QPVRV----------YSSGMQVRLAFSVATAIRPDVLIIDEALSVGDA 178
Cdd:TIGR00957 1375 SLrmnLDPFSQYSDEEVWWALELAHLKTFVSaLPDKLdhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446042612 179 YFQHKSFERIRKfRQEGTTLLLVSHdkqAIQSICD--RAILLNKGQIEMEGEP 229
Cdd:TIGR00957 1455 ETDNLIQSTIRT-QFEDCTVLTIAH---RLNTIMDytRVIVLDKGEVAEFGAP 1503
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
38-221 |
4.31e-06 |
|
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: 46.85 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITG--TSRPTTGEIEISGRvaallELGMGF------------HSDF- 102
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGR-----PLDKNFqrstgyveqqdvHSPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 103 TGRQNVYMSGQLLGLSSEKitelmpqieefaeigdyidqpvrvyssgmQVRLAFSVATAIRPDVLIIDEALSVGDAYFQH 182
Cdd:cd03232 95 TVREALRFSALLRGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446042612 183 KSFERIRKFRQEGTTLLLVSHdkQAIQSIC---DRAILLNKG 221
Cdd:cd03232 146 NIVRFLKKLADSGQAILCTIH--QPSASIFekfDRLLLLKRG 185
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-232 |
4.42e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.33 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 36 NLKWILSDINFEVA---PGEAV-GIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAallelgmgfhsdFTGRQNVYMS 111
Cdd:PRK11144 5 NFKQQLGDLCLTVNltlPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL------------FDAEKGICLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 112 ----------------------GQLLGLSSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLII 169
Cdd:PRK11144 73 pekrrigyvfqdarlfphykvrGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446042612 170 DEALSVGD--------AYFQHKSferirkfRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAV 232
Cdd:PRK11144 153 DEPLASLDlprkrellPYLERLA-------REINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
34-233 |
4.51e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.20 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 34 RHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG-RVAALLELGMGFHSDFTGRQNVYMSG 112
Cdd:PLN03232 1245 RPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcDVAKFGLTDLRRVLSIIPQSPVLFSG 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 113 ----QLLGLSSEKITELMPQIEEfAEIGDYIDQ-PVRV----------YSSGMQVRLAFSVATAIRPDVLIIDEALSVGD 177
Cdd:PLN03232 1325 tvrfNIDPFSEHNDADLWEALER-AHIKDVIDRnPFGLdaevseggenFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446042612 178 AYFQHKSFERIR-KFRQegTTLLLVSHDKQAIQSiCDRAILLNKGQIEMEGEPEAVM 233
Cdd:PLN03232 1404 VRTDSLIQRTIReEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
41-86 |
6.41e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 6.41e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTT--GEIEISG 86
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEG 68
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
41-90 |
7.86e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 7.86e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTsRPT---TGEIEISGRVAA 90
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCR 68
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
40-221 |
1.08e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGtsRPTTGEIEISGRVAALLELGMGF------------HS-DFTGRQ 106
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRPLDSSFqrsigyvqqqdlHLpTSTVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 107 NVYMSGQLLGLSSEKITELMPQIEE---FAEIGDYIDQPVRVYSSGMQV----RLAFSVATAIRPDVLI-IDEALSVGDA 178
Cdd:TIGR00956 856 SLRFSAYLRQPKSVSKSEKMEYVEEvikLLEMESYADAVVGVPGEGLNVeqrkRLTIGVELVAKPKLLLfLDEPTSGLDS 935
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446042612 179 YFQHKSFERIRKFRQEGTTLLLVSHDKQA-IQSICDRAILLNKG 221
Cdd:TIGR00956 936 QTAWSICKLMRKLADHGQAILCTIHQPSAiLFEEFDRLLLLQKG 979
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
41-87 |
1.31e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 1.31e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR 87
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGK 66
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
29-235 |
1.64e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 29 PLNTKRHnlkwILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTS--RPTTGEIEISGR------VAALLELGM---- 96
Cdd:NF040905 268 PLHPERK----VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKevdvstVSDAIDAGLayvt 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 97 ------GFHSDFTGRQNVYMSGqLLGLSSEKITElmpQIEEFAEIGDY----------IDQPVRVYSSGMQ--VRLA--- 155
Cdd:NF040905 344 edrkgyGLNLIDDIKRNITLAN-LGKVSRRGVID---ENEEIKVAEEYrkkmniktpsVFQKVGNLSGGNQqkVVLSkwl 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 156 FSvataiRPDVLIIDE---ALSVGDAYfqhKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQI--EMEGE-- 228
Cdd:NF040905 420 FT-----DPDVLILDEptrGIDVGAKY---EIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRItgELPREea 491
|
....*...
gi 446042612 229 -PEAVMDY 235
Cdd:NF040905 492 sQERIMRL 499
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
43-234 |
1.82e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.77 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 43 DINFEVAPGEAVGIIGINGAGKST----LLKLITGTSrpttGEIEISGRVAALLELG--------MGF-----HSDFTGR 105
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTtgraLLRLVESQG----GEIIFNGQRIDTLSPGklqalrrdIQFifqdpYASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 106 QNVYMS--------GQLLG-LSSEKITELMPQIEEFAEigdYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVG 176
Cdd:PRK10261 418 QTVGDSimeplrvhGLLPGkAAAARVAWLLERVGLLPE---HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446042612 177 DAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMD 234
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
40-86 |
1.95e-05 |
|
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: 46.83 E-value: 1.95e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRpTTGEIEISG 86
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG 1279
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-224 |
2.13e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 46.36 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 29 PLNTKRHNLkwilSDINFEVAPGEAVGIIGINGAGKSTLLKLITGtSRPTT--GEIEISGRVAAL------LELGMGFHS 100
Cdd:TIGR02633 268 VINPHRKRV----DDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKfeGNVFINGKPVDIrnpaqaIRAGIAMVP 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 101 DFTGRQNVYMS---GQLLGLSSEKITELMPQIEEFAE---IGDYIDQ----------PVRVYSSGMQVRLAFSVATAIRP 164
Cdd:TIGR02633 343 EDRKRHGIVPIlgvGKNITLSVLKSFCFKMRIDAAAElqiIGSAIQRlkvktaspflPIGRLSGGNQQKAVLAKMLLTNP 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 165 DVLIIDEALSVGDAYFQHKSFERIRKFRQEGTTLLLVSHDKQAIQSICDRAILLNKGQIE 224
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-234 |
3.89e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.83 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLK-----LITGTSRPTTGEIEISGR---------VAALLELGMGFH-----S 100
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRniyspdvdpIEVRREVGMVFQypnpfP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 101 DFTGRQNVYMSGQLLGLSSEKitELMPQIEEFA--------EIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEA 172
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGLVKSK--KELDERVEWAlkkaalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446042612 173 LSVGDAYFQHKSFERIRKFRQEgTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVMD 234
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
48-204 |
3.97e-05 |
|
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: 44.66 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 48 VAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLEL--GMGFHSDFT----GRQNVYMSGQLLGLSSE- 120
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEfrGSELQNYFTklleGDVKVIVKPQYVDLIPKa 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 121 ---KITELMPQIEEFAEIGDYIDQ---------PVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAYFQHKSFERI 188
Cdd:cd03236 103 vkgKVGELLKKKDERGKLDELVDQlelrhvldrNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
|
170
....*....|....*.
gi 446042612 189 RKFRQEGTTLLLVSHD 204
Cdd:cd03236 183 RELAEDDNYVLVVEHD 198
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
40-171 |
4.51e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 44.64 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLK-------LITGTSrpTTGEIEISGR--------VAAL-LELGMGF----- 98
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEdiydpdvdVVELrRRVGMVFqkpnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 99 --HSDFtgrQNVYMSGQLLGLSSEKItelMPQIEEFA--------EIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLI 168
Cdd:COG1117 104 fpKSIY---DNVAYGLRLHGIKSKSE---LDEIVEESlrkaalwdEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLL 177
|
...
gi 446042612 169 IDE 171
Cdd:COG1117 178 MDE 180
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
38-82 |
4.79e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 4.79e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEI 82
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
38-236 |
6.36e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 45.26 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITG--TSRPTTGEIEISGRVAA---LLELGMGFHSD-----FTGRQN 107
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNRKPTkqiLKRTGFVTQDDilyphLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 108 VYMSGQL-----------LGLSSEKITELMPQIEEFAEIGDYIdqpVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVG 176
Cdd:PLN03211 161 LVFCSLLrlpksltkqekILVAESVISELGLTKCENTIIGNSF---IRGISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446042612 177 DAYFQHKSFERIRKFRQEGTTLLLVSHDKQA-IQSICDRAILLNKGQIEMEGEPEAVMDYY 236
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFGKGSDAMAYF 298
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
34-230 |
6.72e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 34 RHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGrvAALLELGMgfhSDFtgRQN------ 107
Cdd:PLN03130 1248 RPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG--CDISKFGL---MDL--RKVlgiipq 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 108 --VYMSG----QLLGLSSEKITELMPQIEEfAEIGDYIdqpvRVYSSGMQVRLA-----FSV--------ATAI--RPDV 166
Cdd:PLN03130 1321 apVLFSGtvrfNLDPFNEHNDADLWESLER-AHLKDVI----RRNSLGLDAEVSeagenFSVgqrqllslARALlrRSKI 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446042612 167 LIIDEA---LSVG-DAYFQhksfERIR-KFRQegTTLLLVSHDKQAIQSiCDRAILLNKGQIEMEGEPE 230
Cdd:PLN03130 1396 LVLDEAtaaVDVRtDALIQ----KTIReEFKS--CTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPE 1457
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
182-270 |
1.17e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 182 HKSFERIRKFRQEGTTLLLVSHDKQAIqSICDRAILLNK------GQIEMEGEPEAVMDYYNALLAD--KQNQSIKQVEH 253
Cdd:PRK00635 515 HKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIIDIGPgagifgGEVLFNGSPREFLAKSDSLTAKylRQELTIPIPEK 593
|
90
....*....|....*..
gi 446042612 254 NGKTqtvsgTGEVTISE 270
Cdd:PRK00635 594 RTNS-----LGTLTLSK 605
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
40-73 |
1.99e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 42.71 E-value: 1.99e-04
10 20 30
....*....|....*....|....*....|....
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITG 73
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
43-210 |
2.43e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 41.87 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 43 DINFEVAPGEAV-GIIGINGAGKSTLLKLIT----GTSrPTTGEIEISGRVAALLELGMGFHSDFTGRQNVYMSGQLLGL 117
Cdd:cd03279 19 VIDFTGLDNNGLfLICGPTGAGKSTILDAITyalyGKT-PRYGRQENLRSVFAPGEDTAEVSFTFQLGGKKYRVERSRGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 118 SSEKITE--LMPQiEEFAEigdYIDQPVRVYSSGMQVRLAFSVATA----------IRPDVLIIDEALSVGDAYFQHKSF 185
Cdd:cd03279 98 DYDQFTRivLLPQ-GEFDR---FLARPVSTLSGGETFLASLSLALAlsevlqnrggARLEALFIDEGFGTLDPEALEAVA 173
|
170 180
....*....|....*....|....*...
gi 446042612 186 ERIRKFRQEGTTLLLVSHD---KQAIQS 210
Cdd:cd03279 174 TALELIRTENRMVGVISHVeelKERIPQ 201
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
40-86 |
2.53e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 42.53 E-value: 2.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTL----LKLITgtsrpTTGEIEISG 86
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDG 64
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-223 |
3.67e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.63 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 1 MSYIRVNNVgkayrqyhsktgrlieWLS----PLntkrhnlkwiLSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSR 76
Cdd:PRK11147 1 MSLISIHGA----------------WLSfsdaPL----------LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 77 PTTGEIE-------------------------ISGRVAALLELGMGFHsdftgrqnvYMSGQLLGLSSEKITELMPQIEE 131
Cdd:PRK11147 55 LDDGRIIyeqdlivarlqqdpprnvegtvydfVAEGIEEQAEYLKRYH---------DISHLVETDPSEKNLNELAKLQE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 132 FAE----------IGDYI-------DQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSvgdayfqHKSFERI---RKF 191
Cdd:PRK11147 126 QLDhhnlwqlenrINEVLaqlgldpDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTN-------HLDIETIewlEGF 198
|
250 260 270
....*....|....*....|....*....|...
gi 446042612 192 RQE-GTTLLLVSHDKQAIQSICDRAILLNKGQI 223
Cdd:PRK11147 199 LKTfQGSIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
38-94 |
4.03e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.70 E-value: 4.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446042612 38 KWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTS--RPTTGEIEISGRvaALLEL 94
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGK--DLLEL 70
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
34-216 |
4.97e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 34 RHNLKWILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGR--------------VAAL-------- 91
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqetpalpQPALeyvidgdr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 92 ----LELGMGFHSDFT-GRQNVYMSGQL------------------LGLSSEKITelmpqieefaeigdyidQPVRVYSS 148
Cdd:PRK10636 90 eyrqLEAQLHDANERNdGHAIATIHGKLdaidawtirsraasllhgLGFSNEQLE-----------------RPVSDFSG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446042612 149 GMQVRLAFSVATAIRPDVLIIDEALSvgdayfqHKSFERI----RKFRQEGTTLLLVSHDKQAIQSICDRAI 216
Cdd:PRK10636 153 GWRMRLNLAQALICRSDLLLLDEPTN-------HLDLDAViwleKWLKSYQGTLILISHDRDFLDPIVDKII 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
40-85 |
5.49e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 5.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446042612 40 ILSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEIS 85
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN 445
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
41-223 |
1.04e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 41.16 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISG------RVAALlelgmgfhsdftgRQNVYMSGQL 114
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdyTLASL-------------RNQVALVSQN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 115 LGLSSEKITELMP----------QIEEFAEIG---DYIDQPVR-----------VYSSGMQVRLAfsVATAIRPD--VLI 168
Cdd:PRK11176 426 VHLFNDTIANNIAyarteqysreQIEEAARMAyamDFINKMDNgldtvigengvLLSGGQRQRIA--IARALLRDspILI 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446042612 169 IDEALSVGDAYFQ---HKSFERIRKFRqegtTLLLVSHDKQAIQSiCDRAILLNKGQI 223
Cdd:PRK11176 504 LDEATSALDTESEraiQAALDELQKNR----TSLVIAHRLSTIEK-ADEILVVEDGEI 556
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
41-219 |
1.34e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.15 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 41 LSDINFEVAPGEAVGIIGINGAGKSTLLK-------LITGTSrpTTGEIEISGR---------VAALLELGMGFHSDFTG 104
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKnlyapdvdpVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 105 RQNVY-----------MSGQLlglsSEKITELMPQIEEFAEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEAL 173
Cdd:PRK14243 104 PKSIYdniaygaringYKGDM----DELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446042612 174 SVGDAYFQHKSFERIRKFRQEgTTLLLVSHDKQAIQSICDRAILLN 219
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFN 224
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
157-233 |
1.49e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.17 E-value: 1.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446042612 157 SVATAIRPDVLIIDEALSVGDAYFQHKSFERIRKFRQE-GTTLLLVSHDKQAIQSICDRAILLNKGQIEMEGEPEAVM 233
Cdd:PRK15093 170 AIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELV 247
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
50-204 |
2.68e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.79 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 50 PGEAVGIIGINGAGKSTLLKLITGTSRPTTGEIEISGRVAALLELGMGfhsdfTGRQNvYMSgqllGLSSEKIT------ 123
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVLKRFRG-----TELQN-YFK----KLYNGEIKvvhkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446042612 124 --ELMPQ----------------------IEEFaEIGDYIDQPVRVYSSGMQVRLAFSVATAIRPDVLIIDEALSVGDAY 179
Cdd:PRK13409 168 yvDLIPKvfkgkvrellkkvdergkldevVERL-GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180 190
....*....|....*....|....*....|
gi 446042612 180 fqhksfERIRKFR-----QEGTTLLLVSHD 204
Cdd:PRK13409 247 ------QRLNVARlirelAEGKYVLVVEHD 270
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
43-71 |
5.18e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.44 E-value: 5.18e-03
10 20
....*....|....*....|....*....
gi 446042612 43 DINFEVAPGEAVgIIGINGAGKSTLLKLI 71
Cdd:COG3950 18 EIDFDNPPRLTV-LVGENGSGKTTLLEAI 45
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
55-85 |
6.48e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.72 E-value: 6.48e-03
10 20 30
....*....|....*....|....*....|.
gi 446042612 55 GIIGINGAGKSTLLKLITGTSRPTTGEIEIS 85
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVSLD 61
|
|
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