|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-253 |
1.91e-103 |
|
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: 307.74 E-value: 1.91e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGK---------TTllhlltgtlPAKKGRVYLAGKLLADYKPKE 71
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKstllralagLL---------KPSSGEVLLDGRDLASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 72 LAQIMAVLPQKMDQAFTFTVEETVAFGRYPFQtGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQA 151
Cdd:COG1120 73 LARRIAYVPQEPPAPFGLTVRELVALGRYPHL-GLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGT---AGPkqkPEYAVTE 228
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRivaQGP---PEEVLTP 228
|
250 260
....*....|....*....|....*
gi 1238244423 229 QSIKAVYDTDVTALVHQSSPKPMIV 253
Cdd:COG1120 229 ELLEEVYGVEARVIEDPVTGRPLVL 253
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-255 |
7.74e-85 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 260.47 E-value: 7.74e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQK 82
Cdd:PRK13548 5 ARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 83 MDQAFTFTVEETVAFGRYPFQTGlfrqqTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ------QP 156
Cdd:PRK13548 85 SSLSFPFTVEEVVAMGRAPHGLS-----RAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGT---AGPkqkPEYAVTEQSIKA 233
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRlvaDGT---PAEVLTPETLRR 236
|
250 260
....*....|....*....|..
gi 1238244423 234 VYDTDVTALVHQSSPKPMIVIQ 255
Cdd:PRK13548 237 VYGADVLVQPHPETGAPLVLPR 258
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-256 |
4.72e-81 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 250.80 E-value: 4.72e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLP 80
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QKMDQAFTFTVEETVAFGRYPFQTGLFRQQtekgeAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ------ 154
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPHGSSAAQDR-----QIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 155 -QPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNG---TAGPkqkPEYAVTEQS 230
Cdd:COG4559 157 gGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGrlvAQGT---PEEVLTDEL 232
|
250 260
....*....|....*....|....*.
gi 1238244423 231 IKAVYDTDVTALVHQSSPKPMIVIQP 256
Cdd:COG4559 233 LERVYGADLRVLAHPEGGCPQVLPRA 258
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2-215 |
1.43e-75 |
|
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: 233.87 E-value: 1.43e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 kmdqaftftveetvafgrypfqtglfrqqtekgeaivqeAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:cd03214 81 ---------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1238244423 162 DEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-245 |
2.05e-65 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 209.95 E-value: 2.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKKGRVYLAGKLLADYKPKelaqiMAVLPQ 81
Cdd:COG1121 8 ELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKstllkailgllPPTSGTVRLFGKPPRRARRR-----IGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 K--MDQAFTFTVEETVAFGRYPfQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:COG1121 83 RaeVDWDFPITVRDVVLMGRYG-RRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 160 FLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNG--TAGPkqkPEYAVTEQSIKAVYDT 237
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGlvAHGP---PEEVLTPENLSRAYGG 237
|
....*...
gi 1238244423 238 DVTALVHQ 245
Cdd:COG1121 238 PVALLAHG 245
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-254 |
7.90e-64 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 206.40 E-value: 7.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLP 80
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QKMDQAFTFTVEETVAFGRYPFQTgLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGRSPWLS-LWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 161 LDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQKPEYAVTEQSIKAVYDTDvt 240
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVE-- 238
|
250
....*....|....*.
gi 1238244423 241 ALVHQS--SPKPMIVI 254
Cdd:PRK11231 239 AEIHPEpvSGTPMCVV 254
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-253 |
5.83e-60 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 196.07 E-value: 5.83e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLP 80
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QKMDQAFTFTVEETVAFGRYPFQTGlfrQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:COG4604 82 QENHINSRLTVRELVAFGRFPYSKG---RLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 161 LDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG---TAGPkqkPEYAVTEQSIKAVYDT 237
Cdd:COG4604 159 LDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGrvvAQGT---PEEIITPEVLSDIYDT 235
|
250
....*....|....*.
gi 1238244423 238 DVTalVHQSSPKPMIV 253
Cdd:COG4604 236 DIE--VEEIDGKRICV 249
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
2-214 |
9.38e-59 |
|
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: 191.59 E-value: 9.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKlladyKPKELAQIMAVLPQ 81
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 K--MDQAFTFTVEETVAFGRYPfQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:cd03235 76 RrsIDRDFPISVRDVVLMGLYG-HKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 160 FLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-236 |
5.81e-56 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 190.44 E-value: 5.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKMD 84
Cdd:PRK09536 8 DLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 85 QAFTFTVEETVAFGRYPfQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:PRK09536 88 LSFEFDVRQVVEMGRTP-HRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 165 TNFLDLAYQKDLLDLIKRLTrESGLAAVSVFHDLNTASLYCDGLMFMKNG---TAGPkqkPEYAVTEQSIKAVYD 236
Cdd:PRK09536 167 TASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGrvrAAGP---PADVLTADTLRAAFD 237
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
1-256 |
1.03e-51 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 174.62 E-value: 1.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLP 80
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QKMDQAFTFTVEETVAFGRYPFQtGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVALGRIPHR-SLWAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 161 LDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNG---TAGPkqkPEYAVTEQSIKAVYDT 237
Cdd:TIGR03873 161 LDEPTNHLDVRAQLETLALVRELAAT-GVTVVAALHDLNLAASYCDHVVVLDGGrvvAAGP---PREVLTPALIRAVYGV 236
|
250
....*....|....*....
gi 1238244423 238 DVTALVHQSSPKPMIVIQP 256
Cdd:TIGR03873 237 DATVLTHPDTGRPIIAFSP 255
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-253 |
4.52e-50 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 170.94 E-value: 4.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLP 80
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QKMDQAFTFTVEETVAFGRYPFQTgLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:PRK10253 88 QNATTPGDITVQELVARGRYPHQP-LFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 161 LDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQKPEYAVTEQSIKAVYDTDVT 240
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCM 246
|
250
....*....|...
gi 1238244423 241 ALVHQSSPKPMIV 253
Cdd:PRK10253 247 IIDDPVAGTPLVV 259
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-251 |
2.30e-49 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 168.81 E-value: 2.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKMDQAFTFTVEET 94
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 95 VAFGRYPFQTGLFRQQTEKGEAiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQK 174
Cdd:PRK10575 106 VAIGRYPWHGALGRFGAADREK-VEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 175 DLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQKPEYAVTEQSIKAVYDTDVTALVHQSSPKPM 251
Cdd:PRK10575 185 DVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGILPHPAGAAPV 261
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-215 |
7.47e-49 |
|
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: 165.72 E-value: 7.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSR--LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:cd03225 3 KNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 KMD-QAFTFTVEETVAFGryPFQTGLFRQQTEKgeaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:cd03225 83 NPDdQFFGPTVEEEVAFG--LENLGLPEEEIEE---RVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 161 LDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-215 |
1.86e-47 |
|
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: 162.50 E-value: 1.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSR-LINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKKGRVYLAGKLLADYKPKELAQIMAVLP 80
Cdd:COG1122 2 ELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKstllrllngllKPTSGEVLVDGKDITKKNLRELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QK-MDQAFTFTVEETVAFGryPFQTGLFRQQTEKgeaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:COG1122 82 QNpDDQLFAPTVEEDVAFG--PENLGLPREEIRE---RVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1238244423 160 FLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-214 |
1.76e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 147.13 E-value: 1.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADyKPKELAQIMAVLPQk 82
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 83 mDQAF--TFTVEETVAFgrypfQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:COG1131 81 -EPALypDLTVRENLRF-----FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 161 LDEPTNFLDLAYQKDLLDLIKRLtRESGlaaVSVF---HDLNTASLYCDGLMFMKNG 214
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLREL-AAEG---KTVLlstHYLEEAERLCDRVAIIDKG 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-214 |
2.10e-40 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 151.21 E-value: 2.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGY--GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK---KGRVYLAGKLLADYKPKELAQIMAV 78
Cdd:COG1123 8 RDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRIGM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 LPQK-MDQAFTFTVEETVAFGryPFQTGLFRQQTEkgeAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPR 157
Cdd:COG1123 88 VFQDpMTQLNPVTVGDQIAEA--LENLGLSRAEAR---ARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 158 ILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDG 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1-214 |
2.18e-40 |
|
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: 143.43 E-value: 2.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKlladykpkelaQIMAVLP 80
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR-----------DVTGVPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QKMDQAFTF---------TVEETVAFGrypfqtgLFRQQTEKGE--AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLA 149
Cdd:cd03259 70 ERRNIGMVFqdyalfphlTVAENIAFG-------LKLRGVPKAEirARVRELLELVGLEGLLNRYPHELSGGQQQRVALA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 150 QALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
9-203 |
1.35e-38 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 138.14 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 9 GYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGklladykpkelAQIMAVLPQK--MDQA 86
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRseVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 87 FTFTVEETVAFGRYPfQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:NF040873 70 LPLTVRDLVAMGRWA-RRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 1238244423 167 FLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASL 203
Cdd:NF040873 149 GLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-214 |
1.39e-38 |
|
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: 139.94 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYG----DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMA 77
Cdd:COG1124 3 EVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 78 VLPQkmdQAFT-----FTVEETVAfgrYPFQ-TGLFRQqtekgEAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQ 150
Cdd:COG1124 83 MVFQ---DPYAslhprHTVDRILA---EPLRiHGLPDR-----EERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238244423 151 ALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNG 215
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
14-253 |
6.33e-38 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 138.81 E-value: 6.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 14 RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK--------KGRVYLAGKLLADYKPKELAQIMAVLPQKMDQ 85
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 86 AFTFTVEETVAFGRYPFQTGLFRQQTEKGEaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ---------QP 156
Cdd:PRK13547 95 AFAFSAREIVLLGRYPHARRAGALTHRDGE-IAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQKPEYAVTEQSIKAVYD 236
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCYG 253
|
250
....*....|....*..
gi 1238244423 237 TDVTALVHQSSPKPMIV 253
Cdd:PRK13547 254 FAVRLVDAGDGVPPVIV 270
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-214 |
2.00e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 135.94 E-value: 2.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLS----GGYGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKKGRVYLAGKLLADYKPKELAQIM 76
Cdd:COG1136 5 LELRNLTksygTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKstllnilggldRPTSGEVLIDGQDISSLSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 77 A-----VLpqkmdQAF----TFTVEETVAFGRYpfqtgLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVY 147
Cdd:COG1136 85 RrhigfVF-----QFFnllpELTALENVALPLL-----LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 148 LAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASlYCDGLMFMKNG 214
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDG 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-234 |
2.44e-37 |
|
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: 142.73 E-value: 2.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGY-----GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI- 75
Cdd:COG1123 262 EVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELr 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 76 --MAVLPQKMDQAF--TFTVEETVAFGryPFQTGLFRQqtEKGEAIVQEAMEQTG-VADFAQKPIRELSGGEQQRVYLAQ 150
Cdd:COG1123 342 rrVQMVFQDPYSSLnpRMTVGDIIAEP--LRLHGLLSR--AERRERVAELLERVGlPPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 151 ALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGT---AGPKQK----PE 223
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRiveDGPTEEvfanPQ 497
|
250
....*....|.
gi 1238244423 224 YAVTEQSIKAV 234
Cdd:COG1123 498 HPYTRALLAAV 508
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-215 |
3.43e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 134.94 E-value: 3.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 kmdQAFTF--TVEETVAFgryPFQtglFRQQTEKGEAiVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRI 158
Cdd:COG4619 82 ---EPALWggTVRDNLPF---PFQ---LRERKFDRER-ALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 159 LFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-206 |
4.41e-37 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 135.95 E-value: 4.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLI-NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI---MAVL 79
Cdd:COG3638 6 RNLSKRYPGGTPAlDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrrIGMI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 80 PQKmdqaftF------TVEETV---AFGRYPFQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQ 150
Cdd:COG3638 86 FQQ------FnlvprlSVLTNVlagRLGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1238244423 151 ALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCD 206
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYAD 215
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
12-239 |
2.65e-36 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 133.81 E-value: 2.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 12 DSRLINnVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAkKGRVYLAGKLLADYKPKELAQIMAVLPQKMDQAFTFTV 91
Cdd:COG4138 9 AGRLGP-ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 92 EETVAFGRYPfqtglfRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ-------QPRILFLDEP 164
Cdd:COG4138 87 FQYLALHQPA------GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 165 TNFLDLAYQKDLLDLIKRLTrESGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQKPEYAVTEQSIKAVYDTDV 239
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKF 234
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-214 |
3.36e-36 |
|
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: 133.08 E-value: 3.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSR-LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI---MAVL 79
Cdd:cd03256 4 ENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 80 PQKMDQAFTFTVEETV---AFGRYPFQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:cd03256 84 FQQFNLIERLSVLENVlsgRLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1238244423 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-214 |
4.58e-36 |
|
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: 132.63 E-value: 4.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLS----GGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI-- 75
Cdd:cd03257 3 EVKNLSvsfpTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 76 -MAVLPQKMDQAF--TFTVEETVAFGrYPFQTGLFRQQTEKgEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQAL 152
Cdd:cd03257 83 eIQMVFQDPMSSLnpRMTIGEQIAEP-LRIHGKLSKKEARK-EAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238244423 153 AQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-236 |
6.73e-36 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 132.42 E-value: 6.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYG-DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI---M 76
Cdd:TIGR02315 2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLrrrI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 77 AVLPQKMDQAFTFTVEETV---AFGRYPFQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALA 153
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVlhgRLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 154 QQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQKPEyAVTEQSIKA 233
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPS-ELDDEVLRH 240
|
...
gi 1238244423 234 VYD 236
Cdd:TIGR02315 241 IYG 243
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
1.37e-35 |
|
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: 130.69 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLS----GGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMA 77
Cdd:cd03255 2 ELKNLSktygGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 78 vlpQKMD---QAF----TFTVEETVAFGryPFQTGLFRQQTEkgeAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQ 150
Cdd:cd03255 82 ---RHIGfvfQSFnllpDLTALENVELP--LLLAGVPKKERR---ERAEELLERVGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238244423 151 ALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASlYCDGLMFMKNG 214
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDG 216
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-214 |
1.91e-35 |
|
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: 131.08 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI---MAVLP 80
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QkmDQA-FT-FTVEETVAFgrypfqtgLFRQQTEKGE----AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ 154
Cdd:cd03261 84 Q--SGAlFDsLTVFENVAF--------PLREHTRLSEeeirEIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 155 QPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-215 |
2.49e-35 |
|
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: 130.87 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI---MAVLP 80
Cdd:COG1127 9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrIGMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QkmdQA--FT-FTVEETVAFgrypfqtGLfRQQTEKGEA----IVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALA 153
Cdd:COG1127 89 Q---GGalFDsLTVFENVAF-------PL-REHTDLSEAeireLVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238244423 154 QQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGK 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-214 |
2.45e-34 |
|
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: 125.97 E-value: 2.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADyKPKELAQIMAVLPQ 81
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 KMDQAFTFTVEETVafgrypfqtglfrqqtekgeaivqeameqtgvadfaqkpirELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:cd03230 81 EPSLYENLTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1238244423 162 DEPTNFLDLAYQKDLLDLIKRLTRESglaaVSVF---HDLNTASLYCDGLMFMKNG 214
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEG----KTILlssHILEEAERLCDRVAILNNG 171
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-215 |
7.24e-34 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 125.83 E-value: 7.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 3 AEGLSGGYGDSRLI-NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKllaDYKPKELAQIMAVLPQ 81
Cdd:cd03226 2 IENISFSYKKGTEIlDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 KMD-QAFTFTVEETVAFGRypfqtglfrQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:cd03226 79 DVDyQLFTDSVREELLLGL---------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 161 LDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-214 |
1.12e-33 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 127.16 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDS--RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADykPKELAQI---M 76
Cdd:TIGR04520 2 EVENVSFSYPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD--EENLWEIrkkV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 77 AVLPQKMDQAF-TFTVEETVAFGryPFQTGLfrqQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQ 155
Cdd:TIGR04520 80 GMVFQNPDNQFvGATVEDDVAFG--LENLGV---PREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1238244423 156 PRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTAsLYCDGLMFMKNG 214
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKG 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
4-197 |
1.25e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 129.06 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKKGRVYLAGKLLADykpkelaqimaVLPQKM 83
Cdd:COG3842 9 ENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKttllrmiagfeTPDSGRILLDGRDVTG-----------LPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 84 DQAFTF---------TVEETVAFgrypfqtGLFRQQTEKGE--AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQAL 152
Cdd:COG3842 78 NVGMVFqdyalfphlTVAENVAF-------GLRMRGVPKAEirARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1238244423 153 AQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHD 197
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHD 195
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-240 |
1.48e-33 |
|
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: 126.35 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhl-ltgtlPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKMDQAFT 88
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKstllslitgdlpPTYGNDVRLFGERRGGEDVWELRKRIGLVSPALQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 89 --FTVEETVAFGRYPfQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:COG1119 93 rdETVLDVVLSGFFD-SIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 167 FLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNtaslycDG------LMFMKNGT---AGPKqkpEYAVTEQSIKAVYDT 237
Cdd:COG1119 172 GLDLGARELLLALLDKLAAEGAPTLVLVTHHVE------EIppgithVLLLKDGRvvaAGPK---EEVLTSENLSEAFGL 242
|
...
gi 1238244423 238 DVT 240
Cdd:COG1119 243 PVE 245
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-215 |
2.58e-33 |
|
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: 125.36 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQImAVLPQ 81
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-GVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 KMDQAFTFTVEETVA-FGRypfqtgLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:COG4555 82 ERGLYDRLTVRENIRyFAE------LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 161 LDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGK 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-197 |
3.70e-33 |
|
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: 124.66 E-value: 3.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE-----LAQIMAV 78
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKrpvntVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 LPQkmdqaftFTVEETVAFGrypfqtgLFRQQTEKGE--AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:cd03300 84 FPH-------LTVFENIAFG-------LRLKKLPKAEikERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1238244423 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHD 197
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHD 190
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-214 |
4.85e-33 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 124.47 E-value: 4.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELA-------- 73
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgigrtf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 74 QIMAVLPqkmdqafTFTVEETV-----AFGRYPFQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYL 148
Cdd:cd03219 82 QIPRLFP-------ELTVLENVmvaaqARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238244423 149 AQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-215 |
6.66e-32 |
|
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: 118.89 E-value: 6.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 kmdqaftftveetvafgrypfqtglfrqqtekgeaivqeameqtgvadfaqkpireLSGGEQQRVYLAQALAQQPRILFL 161
Cdd:cd00267 81 --------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1238244423 162 DEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:cd00267 105 DEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-215 |
1.04e-31 |
|
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: 119.21 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADY--KPKELAQIMAV 78
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 LPQKMDQAFTFTVEETVAFGrypfqtglfrqqtekgeaivqeameqtgvadfaqkpireLSGGEQQRVYLAQALAQQPRI 158
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 159 LFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1-214 |
7.70e-31 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 118.59 E-value: 7.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLiNNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPkELAQImAVLP 80
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP-EKRDI-SYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QkmDQAF--TFTVEETVAFGrypfqtglFRQQTEKGEAIVQEAMEQTGVADFA----QKPiRELSGGEQQRVYLAQALAQ 154
Cdd:cd03299 78 Q--NYALfpHMTVYKNIAYG--------LKKRKVDKKEIERKVLEIAEMLGIDhllnRKP-ETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 155 QPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNG 206
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
16-215 |
9.02e-30 |
|
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: 116.29 E-value: 9.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKttllhlltgTLPAKKGRVYLAGKLLADYKPKELA--------QIMAVLPQkmdqaf 87
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKttlfnlitgFYRPTSGRILFDGRDITGLPPHRIArlgiartfQNPRLFPE------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 88 tFTVEETVAFGRY----------PFQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPR 157
Cdd:COG0411 94 -LTVLENVLVAAHarlgrgllaaLLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1238244423 158 ILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:COG0411 173 LLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-214 |
1.46e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 116.27 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKMDQAFT-FTVEET 94
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPDNQFVgATVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 95 VAFGrypfqtgLFRQQTEKGEAI--VQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAY 172
Cdd:PRK13635 103 VAFG-------LENIGVPREEMVerVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1238244423 173 QKDLLDLIKRLTRESGLAAVSVFHDLNTAsLYCDGLMFMKNG 214
Cdd:PRK13635 176 RREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKG 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
12-214 |
2.28e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 115.56 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLaDYKPKELAQIMA----VLPQKMDQAF 87
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKtvgiVFQNPDDQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 88 TFTVEETVAFGryPFQTGLFRQQTEKGeaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNF 167
Cdd:PRK13639 93 APTVEEDVAFG--PLNLGLSKEEVEKR---VKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1238244423 168 LDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK13639 168 LDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1-198 |
1.62e-28 |
|
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: 111.79 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRL----INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKelaqiM 76
Cdd:cd03293 1 LEVRNVSKTYGGGGGavtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 77 AVLPQkmdQAFTF---TVEETVAFGryPFQTGLFRQQTEkgeAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALA 153
Cdd:cd03293 76 GYVFQ---QDALLpwlTVLDNVALG--LELQGVPKAEAR---ERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1238244423 154 QQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDL 198
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDI 192
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
1.84e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 113.40 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGD-SRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLaDYKPK---ELAQIM 76
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 77 AVLPQKMD-QAFTFTVEETVAFGryPFQTGLFRQQTEKGeaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQ 155
Cdd:PRK13636 85 GMVFQDPDnQLFSASVYQDVSFG--AVNLKLPEDEVRKR---VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238244423 156 PRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTA 216
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
16-166 |
2.41e-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: 109.27 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKMDQAFTFTVEETV 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 96 AFGRYpfqtgLFRQQTEKGEAIVQEAMEQTGVADFAQKPIR----ELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:pfam00005 81 RLGLL-----LKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
16-220 |
6.04e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 111.75 E-value: 6.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKMDQAFT-FTVEET 94
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPDNQFVgATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 95 VAFGRYpfQTGLFRQQTEKGeaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQK 174
Cdd:PRK13650 103 VAFGLE--NKGIPHEEMKER---VNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1238244423 175 DLLDLIKRLTRESGLAAVSVFHDLNTASLyCDGLMFMKNG----TAGPKQ 220
Cdd:PRK13650 178 ELIKTIKGIRDDYQMTVISITHDLDEVAL-SDRVLVMKNGqvesTSTPRE 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-214 |
1.67e-27 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 108.77 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKpKELAQIMavlpQ 81
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDK-KNINELR----Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 KMD---QAFTF----TVEETVAFGrypfQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ 154
Cdd:cd03262 77 KVGmvfQQFNLfphlTVLENITLA----PIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 155 QPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-214 |
4.06e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.44 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGD-SRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKEL-AQIMAVLPQ 81
Cdd:PRK13647 8 EDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 KMDQAFTFTVEETVAFGryPFQTGLFRQQTEKGeaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:PRK13647 88 PDDQVFSSTVWDDVAFG--PVNMGLDKDEVERR---VEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1238244423 162 DEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
12-248 |
6.06e-27 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 108.10 E-value: 6.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 12 DSRLINnVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAkKGRVYLAGKLLADYKPKELAQIMAVLPQKMDQAFTFTV 91
Cdd:PRK03695 9 STRLGP-LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 92 EETVAFGRYPfqtglfRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ-------QPRILFLDEP 164
Cdd:PRK03695 87 FQYLTLHQPD------KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 165 TNFLDLAYQKDLLDLIKRLTReSGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQKPEYAVTEQSIKAVYDTDVTALVH 244
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLDV 239
|
....
gi 1238244423 245 QSSP 248
Cdd:PRK03695 240 EGHP 243
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
7.08e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.54 E-value: 7.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSR--LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVL 79
Cdd:PRK13632 9 KVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 80 PQKMDQAFT-FTVEETVAFG----RYPFqtglfrqqtEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ 154
Cdd:PRK13632 89 FQNPDNQFIgATVEDDIAFGlenkKVPP---------KKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 155 QPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLyCDGLMFMKNGTAGPKQKPEYAVTEQSI 231
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-214 |
7.30e-27 |
|
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: 107.46 E-value: 7.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGkLLADYKPKELAQIMAVLPQK 82
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG-HDVVREPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 83 --MDQAFTFTvEETVAFGR-YPFQTGLFRQQTEkgeaivqEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:cd03265 82 lsVDDELTGW-ENLYIHARlYGVPGAERRERID-------ELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 160 FLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHG 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-194 |
1.28e-26 |
|
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: 106.97 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 14 RLINNVSLTVEKGEFLGILGPNGSGKTT---LLHLLTGTLPAKKGRVYLAGKLLadyKPKELAQIMAVLPQKMDQAFTFT 90
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNGQPR---KPDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 91 VEETVAFgrypfqTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRE-----LSGGEQQRVYLAQALAQQPRILFLDEPT 165
Cdd:cd03234 98 VRETLTY------TAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGnlvkgISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190
....*....|....*....|....*....|.
gi 1238244423 166 NFLD--LAYQkdLLDLIKRLTRESGLAAVSV 194
Cdd:cd03234 172 SGLDsfTALN--LVSTLSQLARRNRIVILTI 200
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-214 |
1.61e-26 |
|
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: 112.62 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSR--LINNVSLTVEKGEFLGILGPNGSGKTTLlhlltgtlpAK---------KGRVYLAGKLLADYKPKEL 72
Cdd:COG2274 477 ENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTL---------LKlllglyeptSGRILIDGIDLRQIDPASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 73 AQIMAVLPQkmdQAFTF--TVEETVAFGRypfqtglfrqqTEKGEAIVQEAMEQTGVADFAQK-------PIRE----LS 139
Cdd:COG2274 548 RRQIGVVLQ---DVFLFsgTIRENITLGD-----------PDATDEEIIEAARLAGLHDFIEAlpmgydtVVGEggsnLS 613
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 140 GGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSvfHDLNTASLyCDGLMFMKNG 214
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIA--HRLSTIRL-ADRIIVLDKG 685
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
11-198 |
2.14e-26 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 105.79 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQimavLPQKMDQAF--- 87
Cdd:TIGR02673 13 GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPL----LRRRIGVVFqdf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 88 ----TFTVEETVAFGrypfqtglFRQQTEKGEAI---VQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:TIGR02673 89 rllpDRTVYENVALP--------LEVRGKKEREIqrrVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1238244423 161 LDEPTNFLDLAYQKDLLDLIKRLTReSGLAAVSVFHDL 198
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDL 197
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
10-214 |
2.59e-26 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 107.86 E-value: 2.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGklladY----KPKELAQIMAVLPQK--M 83
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAG-----YdvvrEPRKVRRSIGIVPQYasV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 84 DQAFTFTvEETVAFGRYpfqTGLFRQQTEKGEAivqEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:TIGR01188 78 DEDLTGR-ENLEMMGRL---YGLPKDEAEERAE---ELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1238244423 164 PTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHG 200
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-214 |
2.65e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 109.27 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE-----LAQIMAVL 79
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENrhvntVFQSYALF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 80 PQkmdqaftFTVEETVAFGrypfqtgLFRQQTEKGE--AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPR 157
Cdd:PRK09452 99 PH-------MTVFENVAFG-------LRMQKTPAAEitPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 158 ILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-197 |
2.96e-26 |
|
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: 105.25 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtLPAKKGRVYLAGKLLADyKPKELAQIMAVLP 80
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKttllrilaglLPPSAGEVLWNGEPIRD-AREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QKMDQAFTFTVEETVAfgrypFQTGLFRQQTEKGEaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:COG4133 82 HADGLKPELTVRENLR-----FWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1238244423 161 LDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHD 197
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQ 190
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
11-198 |
4.31e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 106.33 E-value: 4.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 11 GDSRLINNVSLTVEKGEFLGILGPNGSGK----------TtllhlltgtlPAKKGRVYLAGKLLADYKPKelaqiMAVLP 80
Cdd:COG1116 22 GGVTALDDVSLTVAAGEFVALVGPSGCGKstllrliaglE----------KPTSGEVLVDGKPVTGPGPD-----RGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QKmdqaFT----FTVEETVAFGrypfqtgLFRQQTEKGEA--IVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ 154
Cdd:COG1116 87 QE----PAllpwLTVLDNVALG-------LELRGVPKAERreRARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1238244423 155 QPRILFLDEPtnF--LD----LAYQKDLLDLIkrltRESGLAAVSVFHDL 198
Cdd:COG1116 156 DPEVLLMDEP--FgaLDaltrERLQDELLRLW----QETGKTVLFVTHDV 199
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-214 |
4.36e-26 |
|
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: 104.97 E-value: 4.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGeFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYkPKELAQIMAVLPQ 81
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 KMDQAFTFTVEETVAFgrypfQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:cd03264 80 EFGVYPNFTVREFLDY-----IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1238244423 162 DEPTNFLDLAYQKDLLDLIKRLTrESGLAAVSVfHDLNTASLYCDGLMFMKNG 214
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELG-EDRIVILST-HIVEDVESLCNQVAVLNKG 205
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-215 |
4.61e-26 |
|
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: 105.85 E-value: 4.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSR-LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQK 82
Cdd:cd03295 4 ENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 83 MDQAFTFTVEETVAFgrYPfqtGLFRQQTEKGEAIVQEAMEQTGV--ADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:cd03295 84 IGLFPHMTVEENIAL--VP---KLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 161 LDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGE 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-214 |
8.21e-26 |
|
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: 105.80 E-value: 8.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI-----------MAVLPQKmd 84
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkismvfqsFALLPHR-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 85 qaftfTVEETVAFGrYPFQtGLFRQQTEkgeAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:cd03294 118 -----TVLENVAFG-LEVQ-GVPRAERE---ERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1238244423 165 TNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDG 237
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-245 |
1.14e-25 |
|
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: 104.34 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKElAQIMAV----- 78
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RNVGFVfqhya 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 LPQKMdqaftfTVEETVAFGrYPFQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRI 158
Cdd:cd03296 85 LFRHM------TVFDNVAFG-LRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 159 LFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGtagpkqkpeyaVTEQ--SIKAVYD 236
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKG-----------RIEQvgTPDEVYD 226
|
....*....
gi 1238244423 237 TDVTALVHQ 245
Cdd:cd03296 227 HPASPFVYS 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-186 |
1.16e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 103.98 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLI-NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELA----QIMAV 78
Cdd:COG2884 5 ENVSKRYPGGREAlSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrrRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 ------LPQKmdqaftfTVEETVAFgryPFQ-TGLFRQQTEKgeaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQA 151
Cdd:COG2884 85 fqdfrlLPDR-------TVYENVAL---PLRvTGKSRKEIRR---RVREVLDLVGLSDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190
....*....|....*....|....*....|....*
gi 1238244423 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRE 186
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINRR 186
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-214 |
1.87e-25 |
|
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: 108.69 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 3 AEGLSGGYGDSR-LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:COG4988 339 LEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 kmdQAFTF--TVEETVAFGRypfqtglfrqqTEKGEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYL 148
Cdd:COG4988 419 ---NPYLFagTIRENLRLGR-----------PDASDEELEAALEAAGLDEFVAAlpdgldtPLGEggrgLSGGQAQRLAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238244423 149 AQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTResGLAAVSVFHDLNTASLyCDGLMFMKNG 214
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDG 547
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-214 |
2.87e-25 |
|
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: 103.04 E-value: 2.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 6 LSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMavlpQKMDQ 85
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR----RRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 86 AF-------TFTVEETVAfgrYPFQtgLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRI 158
Cdd:cd03258 87 IFqhfnllsSRTVFENVA---LPLE--IAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1238244423 159 LFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKG 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-214 |
3.22e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 103.94 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKK---------GR-VYLAGKLLADYKpK 70
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRtVQREGRLARDIR-K 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 71 ELAQIMAVLpQKMDQAFTFTVEETV---AFGRYPFQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVY 147
Cdd:PRK09984 84 SRANTGYIF-QQFNLVNRLSVLENVligALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 148 LAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1-214 |
3.46e-25 |
|
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: 102.33 E-value: 3.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE--LA---QI 75
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDrdIAmvfQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 76 MAVLPQKmdqaftfTVEETVAFGrypfqtglFRQQTEKGEAI---VQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQAL 152
Cdd:cd03301 81 YALYPHM-------TVYDNIAFG--------LKLRKVPKDEIderVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238244423 153 AQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-215 |
3.82e-25 |
|
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: 102.58 E-value: 3.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLI--NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLAdYKPKELAQIMAV 78
Cdd:cd03263 1 LQIRNLTKTYKKGTKPavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 LPQKmDQAFT-FTVEETVAF-GRYpfqTGLFRQQtekGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:cd03263 80 CPQF-DALFDeLTVREHLRFyARL---KGLPKSE---IKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238244423 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTRESglaavSVF---HDLNTASLYCDGLMFMKNGT 215
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGR-----SIIlttHSMDEAEALCDRIAIMSDGK 209
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-214 |
5.99e-25 |
|
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: 103.35 E-value: 5.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQ---------- 74
Cdd:TIGR02769 16 GLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrdvqlvfq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 75 --IMAVLPQKmdqaftfTVEETVafgRYPFQTGLFRQQTEKgEAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQA 151
Cdd:TIGR02769 96 dsPSAVNPRM-------TVRQII---GEPLRHLTSLDESEQ-KARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238244423 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1-229 |
7.45e-25 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 101.87 E-value: 7.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTT------LLHLLTGTLPAKkGRVYLAGKLLA--DYKPKEL 72
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTllrllnRLNDLIPGAPDE-GEVLLDGKDIYdlDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 73 AQIMAVLPQKMDqAFTFTVEETVAFGrypfqtglFRQQTEKG----EAIVQEAMEQTG----VADFAQKpiRELSGGEQQ 144
Cdd:cd03260 80 RRRVGMVFQKPN-PFPGSIYDNVAYG--------LRLHGIKLkeelDERVEEALRKAAlwdeVKDRLHA--LGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 145 RVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSvfHDLNTASLYCDGLMFMKNGtagpkQKPEY 224
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVT--HNMQQAARVADRTAFLLNG-----RLVEF 221
|
....*
gi 1238244423 225 AVTEQ 229
Cdd:cd03260 222 GPTEQ 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
16-223 |
8.22e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 102.91 E-value: 8.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKMDQAFT-FTVEET 94
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQFVgSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 95 VAFGRYPFQTglfrqQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQK 174
Cdd:PRK13648 105 VAFGLENHAV-----PYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1238244423 175 DLLDLIKRLTRESGLAAVSVFHDLnTASLYCDGLMFMKNGTAGPKQKPE 223
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDL-SEAMEADHVIVMNKGTVYKEGTPT 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-214 |
1.07e-24 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 99.76 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDS--RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:cd03228 4 KNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 KMdQAFTFTVEETVafgrypfqtglfrqqtekgeaivqeameqtgvadfaqkpireLSGGEQQRVYLAQALAQQPRILFL 161
Cdd:cd03228 84 DP-FLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1238244423 162 DEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSvfHDLNTASLyCDGLMFMKNG 214
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIA--HRLSTIRD-ADRIIVLDDG 170
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
10-216 |
1.82e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 100.98 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRLinNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKElaQIMAVLPQKmDQAFT- 88
Cdd:COG3840 11 YGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLFQE-NNLFPh 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 89 FTVEETVAFGRYPfqtGLFRQQTEKgeAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFL 168
Cdd:COG3840 86 LTVAQNIGLGLRP---GLKLTAEQR--AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1238244423 169 DLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTA 216
Cdd:COG3840 161 DPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRI 208
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-214 |
2.03e-24 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 103.58 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKlladykpkelaQIMAVLP 80
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGR-----------DITRLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QKMDQAFTF---------TVEETVAFGRYPFQTGlfrqqTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQA 151
Cdd:TIGR03265 74 QKRDYGIVFqsyalfpnlTVADNIAYGLKNRGMG-----RAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238244423 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:TIGR03265 149 LATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHG 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
16-216 |
2.12e-24 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 100.62 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELA--QIMAVLPQKmdqaftfTVEE 93
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVvfQNYSLLPWL-------TVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 94 TVAFGrypFQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQ 173
Cdd:TIGR01184 74 NIALA---VDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1238244423 174 KDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTA 216
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPA 193
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-216 |
2.46e-24 |
|
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: 98.83 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSR--LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:cd03246 4 ENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 KmDQAFTFTVEETVafgrypfqtglfrqqtekgeaivqeameqtgvadfaqkpireLSGGEQQRVYLAQALAQQPRILFL 161
Cdd:cd03246 84 D-DELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 162 DEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLyCDGLMFMKNGTA 216
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-214 |
3.15e-24 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 101.06 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKllaDYKPKELAQI--------- 75
Cdd:TIGR02323 8 GLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMR---SGAELELYQLseaerrrlm 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 76 ---MAVLPQKMDQAFTFTVEETVAFGRYPFQTGL-----FRQQTEKGEAIVQeaMEQTGVADfaqKPiRELSGGEQQRVY 147
Cdd:TIGR02323 85 rteWGFVHQNPRDGLRMRVSAGANIGERLMAIGArhygnIRATAQDWLEEVE--IDPTRIDD---LP-RAFSGGMQQRLQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 148 LAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQG 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
19-214 |
3.88e-24 |
|
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: 100.20 E-value: 3.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 19 VSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAqimAVLPQKM---DQAF----TFTV 91
Cdd:COG4181 31 ISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARA---RLRARHVgfvFQSFqllpTLTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 92 EETVAfgrypfqTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLA 171
Cdd:COG4181 108 LENVM-------LPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1238244423 172 YQKDLLDLIKRLTRESGLAAVSVFHDLNTASLyCDGLMFMKNG 214
Cdd:COG4181 181 TGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAG 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-215 |
5.65e-24 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 104.46 E-value: 5.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSR--LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVL 79
Cdd:COG4987 335 ELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 80 PQkmdQAFTF--TVEETVAFGRyPfqtglfrqqtEKGEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRV 146
Cdd:COG4987 415 PQ---RPHLFdtTLRENLRLAR-P----------DATDEELWAALERVGLGDWLAAlpdgldtWLGEggrrLSGGERRRL 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238244423 147 YLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSvfHDLNTASLyCDGLMFMKNGT 215
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLIT--HRLAGLER-MDRILVLEDGR 546
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-214 |
5.89e-24 |
|
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: 99.36 E-value: 5.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 3 AEGLSGGYGDSRL----INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGkLLADYKPKELAQIMAV 78
Cdd:cd03266 4 ADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-FDVVKEPAEARRRLGF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 LPQKMDQAFTFTVEETVA-FGRYpfqTGLFRQQTEkgeAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPR 157
Cdd:cd03266 83 VSDSTGLYDRLTARENLEyFAGL---YGLKGDELT---ARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 158 ILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-216 |
7.67e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 98.51 E-value: 7.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTgtlpakkgRVYL--AGKLLADYKPKELA--QIM 76
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMIL--------GIILpdSGEVLFDGKPLDIAarNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 77 AVLP------QKMDqaftfTVEETVAFGRYpfqTGLFRQQTEKGeaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQ 150
Cdd:cd03269 73 GYLPeerglyPKMK-----VIDQLVYLAQL---KGLKKEEARRR---IDEWLERLELSEYANKRVEELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238244423 151 ALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNGTA 216
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-214 |
9.35e-24 |
|
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: 98.66 E-value: 9.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI-MAVLP 80
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QKMdQAF-TFTVEETvafgrypFQTGLFRQQTEKGEAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRI 158
Cdd:cd03224 82 EGR-RIFpELTVEEN-------LLLGAYARRRAKRKARLERVYELFPRlKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1238244423 159 LFLDEPTnfLDLA--YQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:cd03224 154 LLLDEPS--EGLApkIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERG 208
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-196 |
1.09e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.16 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPK-ELAQIMAVLPQKMDQAFTFT-VEE 93
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIRNKAGMVFQNPDNQIVATiVEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 94 TVAFGryPFQTGLfrqQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQ 173
Cdd:PRK13633 106 DVAFG--PENLGI---PPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180
....*....|....*....|...
gi 1238244423 174 KDLLDLIKRLTRESGLAAVSVFH 196
Cdd:PRK13633 181 REVVNTIKELNKKYGITIILITH 203
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
6-223 |
1.66e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.49 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 6 LSGGYGDSR--LINNVSLTVEKGEFLGILGPNGSGKTTLLHLltgtlpakkgrvyLAGKLLADYKPKELAQI-------- 75
Cdd:PRK13640 11 VSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKL-------------INGLLLPDDNPNSKITVdgitltak 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 76 --------MAVLPQKMDQAFT-FTVEETVAFGRYpfQTGLFRQQTEKgeaIVQEAMEQTGVADFAQKPIRELSGGEQQRV 146
Cdd:PRK13640 78 tvwdirekVGIVFQNPDNQFVgATVGDDVAFGLE--NRAVPRPEMIK---IVRDVLADVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 147 YLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLyCDGLMFMKNGTAGPKQKPE 223
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPV 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-215 |
1.75e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 99.74 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYG-----DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPK--ELA 73
Cdd:PRK13637 3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 74 QIMAVLPQKMD-QAFTFTVEETVAFGryPFQTGLFRQQTEKGeaiVQEAMEQTGVA--DFAQKPIRELSGGEQQRVYLAQ 150
Cdd:PRK13637 83 KKVGLVFQYPEyQLFEETIEKDIAFG--PINLGLSEEEIENR---VKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 151 ALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-198 |
2.26e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 98.26 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELaqimavlpqKM 83
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKL---------YL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 84 DQAFTFTVEEtvaFGRypfqtglFRQQTEKGEaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PRK09544 79 DTTLPLTVNR---FLR-------LRPGTKKED--ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190
....*....|....*....|....*....|....*
gi 1238244423 164 PTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDL 198
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-220 |
3.22e-23 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 98.42 E-value: 3.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLAdykpKELAQ-IMAVLPQ--KMDQAFTFTVE 92
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKnLVAYVPQseEVDWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 93 ETVAFGRYPfQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAY 172
Cdd:PRK15056 99 DVVMMGRYG-HMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1238244423 173 QKDLLDLIKRLTRESGLAAVSVfHDLNTASLYCDGLMFMKnGT---AGPKQ 220
Cdd:PRK15056 178 EARIISLLRELRDEGKTMLVST-HNLGSVTEFCDYTVMVK-GTvlaSGPTE 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-215 |
3.40e-23 |
|
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: 97.40 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKMDQAFTF 89
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 90 TVEETVAFGR--YPFQTGLFRQQTEKgeaiVQEAMEqtgVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNF 167
Cdd:cd03267 111 PVIDSFYLLAaiYDLPPARFKKRLDE----LSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1238244423 168 LDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-214 |
3.59e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 99.84 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGK-----------TtllhlltgtlpAKKGRVYLAGKLLADYKPkel 72
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKttllriiagleT-----------PDSGRIVLNGRDLFTNLP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 73 aqimavlPQKMDQAFTF---------TVEETVAFGrypfqtglFRQQTEKGEAIVQEAMEQ------TGVADfaQKPiRE 137
Cdd:COG1118 72 -------PRERRVGFVFqhyalfphmTVAENIAFG--------LRVRPPSKAEIRARVEELlelvqlEGLAD--RYP-SQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238244423 138 LSGGEQQRVYLAQALAQQPRILFLDEPtnF--LDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:COG1118 134 LSGGQRQRVALARALAVEPEVLLLDEP--FgaLDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQG 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-206 |
4.15e-23 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 98.97 E-value: 4.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLlhlltgtlpAK------------KGRVYLAGKLLADYKPKELAQI--- 75
Cdd:COG0444 16 GVVKAVDGVSFDVRRGETLGLVGESGSGKSTL---------ARailgllpppgitSGEILFDGEDLLKLSEKELRKIrgr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 76 -MAVLPQkmDqAFT-----FTVEETVAfgrYPFQTglfRQQTEKGEAI--VQEAMEQTGVADfaqkPIR-------ELSG 140
Cdd:COG0444 87 eIQMIFQ--D-PMTslnpvMTVGDQIA---EPLRI---HGGLSKAEARerAIELLERVGLPD----PERrldryphELSG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238244423 141 GEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCD 206
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIAD 219
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1-198 |
4.17e-23 |
|
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: 101.67 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGY-GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVL 79
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 80 PQKMdQAFTFTVEETVAFGRypfqtglfrqqTEKGEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYL 148
Cdd:TIGR02868 415 AQDA-HLFDTTVRENLRLAR-----------PDATDEELWAALERVGLADWLRAlpdgldtVLGEggarLSGGERQRLAL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1238244423 149 AQALAQQPRILFLDEPTNFLDLAYQKDLLDLIkrLTRESGLAAVSVFHDL 198
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
11-214 |
1.11e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.18 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKMD-QAFTF 89
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDdQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 90 TVEETVAFGryPFQTGLfrqQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK13652 95 TVEQDIAFG--PINLGL---DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1238244423 170 LAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK13652 170 PQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKG 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-215 |
1.13e-22 |
|
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: 95.36 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKeLAQIMAVLpq 81
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA-LRRIGALI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 kmdqaftftveETVAFgrYPFQTG-----LFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:cd03268 79 -----------EAPGF--YPNLTArenlrLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238244423 157 RILFLDEPTNFLDLAYQKDLLDLIKRLtRESGlaaVSVF---HDLNTASLYCDGLMFMKNGT 215
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSL-RDQG---ITVLissHLLSEIQKVADRIGIINKGK 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-214 |
1.18e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 100.14 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 17 NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKkGRVYLAGKLLADYKPKELAQI---MAVLPQ--------KMdq 85
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRALRPLrrrMQVVFQdpfgslspRM-- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 86 aftfTVEETVAFGRYPFQTGLFRQQTEkgeAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:COG4172 380 ----TVGQIIAEGLRVHGPGLSAAERR---ARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1238244423 165 TNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:COG4172 453 TSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDG 502
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-199 |
1.19e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.94 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQkMDQAFTFT 90
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQ-TPTLFGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 91 VEETVAFgryPFQtglFRQQTEKGEAIVQEaMEQTGVAD-FAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK10247 97 VYDNLIF---PWQ---IRNQQPDPAIFLDD-LERFALPDtILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190
....*....|....*....|....*....|
gi 1238244423 170 LAYQKDLLDLIKRLTRESGLAAVSVFHDLN 199
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
1.35e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.98 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGD-SRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADY-KPKELAQIMAV 78
Cdd:PRK13644 2 IRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 LPQKMDQAFT-FTVEETVAFGryPFQTGLFRQQTEKgeaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPR 157
Cdd:PRK13644 82 VFQNPETQFVgRTVEEDLAFG--PENLCLPPIEIRK---RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 158 ILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLyCDGLMFMKNGTAGPKQKPEYAVTEQSIK 232
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-197 |
1.45e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 98.22 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKKGRVYLAGKLLADYKPKE--LAqiM----- 76
Cdd:COG3839 7 ENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKstllrmiagleDPTSGEILIGGRDVTDLPPKDrnIA--Mvfqsy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 77 AVLPQkMdqaftfTVEETVAFgrypfqtGLFRQQTEKGE--AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ 154
Cdd:COG3839 85 ALYPH-M------TVYENIAF-------PLKLRKVPKAEidRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1238244423 155 QPRILFLDEP-TNfLDLAYQKDLLDLIKRLTRESGLAAVSVFHD 197
Cdd:COG3839 151 EPKVFLLDEPlSN-LDAKLRVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-215 |
2.08e-22 |
|
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: 94.87 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 20 SLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKElaQIMAVLPQKMDQAFTFTVEETVAFGR 99
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 100 YPfqtGLfrQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDL 179
Cdd:cd03298 96 SP---GL--KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1238244423 180 IKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
10-201 |
2.51e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.47 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK---KGRVYLAGKLLADyKPKELAQImAVLPQkMDQA 86
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTA-LPAEQRRI-GILFQ-DDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 87 FT-FTVEETVAFGRYPFQTGLFRQQTekgeaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPT 165
Cdd:COG4136 88 FPhLSVGENLAFALPPTIGRAQRRAR------VEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1238244423 166 NFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTA 201
Cdd:COG4136 162 SKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA 197
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-201 |
3.19e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.15 E-value: 3.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE--LAQIMAV 78
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERgvVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 LPQKmdqaftfTVEETVAFGrypFQ-TGLFRQQTEkgeAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPR 157
Cdd:PRK11248 82 LPWR-------NVQDNVAFG---LQlAGVEKMQRL---EIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1238244423 158 ILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTA 201
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-198 |
3.25e-22 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 93.83 E-value: 3.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKllaDYKPKELAQIMAVLPQKM 83
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQ---ETPPLNSKKASKFRREKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 84 D---QAFTFTVEETVafgRYPFQTGLF---RQQTEKGEAIVqEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPR 157
Cdd:TIGR03608 79 GylfQNFALIENETV---EENLDLGLKykkLSKKEKREKKK-EALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1238244423 158 ILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDL 198
Cdd:TIGR03608 155 LILADEPTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDP 194
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-214 |
3.45e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 94.68 E-value: 3.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKKGRVYLAGKLLADyKPKELAQIMavlpQ 81
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKstllrcinlleEPDSGTITVDGEDLTD-SKKDINKLR----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 KMdqAFTF---------TVEETVAFGrypfQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQAL 152
Cdd:COG1126 78 KV--GMVFqqfnlfphlTVLENVTLA----PIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238244423 153 AQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGG 212
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-214 |
6.35e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 94.61 E-value: 6.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKllaDYKPKELAQIMAV-- 78
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR---DGQLRDLYALSEAer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 -LPQKMDQAFtftVEEtvafgrYPFQtGLfRQQTEKGEAIVQEAM----------EQTGVADFAQKPI---------REL 138
Cdd:PRK11701 84 rRLLRTEWGF---VHQ------HPRD-GL-RMQVSAGGNIGERLMavgarhygdiRATAGDWLERVEIdaariddlpTTF 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238244423 139 SGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-229 |
6.51e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.05 E-value: 6.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQImAVLPQ--K 82
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARI-GVVPQfdN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 83 MDQAFTFTvEETVAFGRYpfqtglFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:PRK13536 125 LDLEFTVR-ENLLVFGRY------FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238244423 163 EPTNFLD-----LAYQKdLLDLIKRltresGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQKPEYAVTEQ 229
Cdd:PRK13536 198 EPTTGLDpharhLIWER-LRSLLAR-----GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-204 |
1.12e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 97.36 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 3 AEGLSGGYGDSR-LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:TIGR02857 324 FSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 KmDQAFTFTVEETVAFGRypfqtglfrqqTEKGEAIVQEAMEQTGVADFAQ-------KPI----RELSGGEQQRVYLAQ 150
Cdd:TIGR02857 404 H-PFLFAGTIAENIRLAR-----------PDASDAEIREALERAGLDEFVAalpqgldTPIgeggAGLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1238244423 151 ALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTResGLAAVSVFHDLNTASLY 204
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA 523
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-214 |
1.16e-21 |
|
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: 92.74 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 18 NVSLTVEkGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKelaqiMAVLPQKMDQAFTF-------- 89
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKK-----INLPPQQRKIGLVFqqyalfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 90 -TVEETVAFGRYPFQTGLFRQQtekgeaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFL 168
Cdd:cd03297 90 lNVRENLAFGLKRKRNREDRIS-------VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1238244423 169 DLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:cd03297 163 DRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-214 |
2.10e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 92.46 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE---------LAQIMAVLP 80
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirqeagmVFQQFYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QkmdqaftFTVEETVAFGryPFQT-GLFRQQTEKgeaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:PRK09493 91 H-------LTALENVMFG--PLRVrGASKEEAEK---QARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 160 FLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
16-201 |
2.21e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 95.29 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE-----LAQIMAVLPQkmdqaftFT 90
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQrpinmMFQSYALFPH-------MT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 91 VEETVAFGrypfqtgLFRQQTEKGE--AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFL 168
Cdd:PRK11607 108 VEQNIAFG-------LKQDKLPKAEiaSRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 1238244423 169 DLA----YQKDLLDLIKRLtresGLAAVSVFHDLNTA 201
Cdd:PRK11607 181 DKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEA 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-190 |
2.24e-21 |
|
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: 92.35 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI-MAVLP 80
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QKMdQAF-TFTVEETVAFGRYPfqtglfRQQTEKGEAIVQEAMEQtgvadFaqkPI-RE--------LSGGEQQRVYLAQ 150
Cdd:COG0410 85 EGR-RIFpSLTVEENLLLGAYA------RRDRAEVRADLERVYEL-----F---PRlKErrrqragtLSGGEQQMLAIGR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1238244423 151 ALAQQPRILFLDEPTnfLDLA--YQKDLLDLIKRLtRESGLA 190
Cdd:COG0410 150 ALMSRPKLLLLDEPS--LGLAplIVEEIFEIIRRL-NREGVT 188
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-189 |
2.80e-21 |
|
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: 92.22 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI-MAVLP 80
Cdd:cd03218 2 RAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QkmdQAFTF---TVEETV-AFGRypFQTGLFRQQTEKGEAIVQEameqTGVADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:cd03218 82 Q---EASIFrklTVEENIlAVLE--IRGLSKKEREEKLEELLEE----FHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190
....*....|....*....|....*....|...
gi 1238244423 157 RILFLDEPTNFLDLAYQKDLLDLIKRLtRESGL 189
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGI 184
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
14-215 |
9.71e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 92.01 E-value: 9.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 14 RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLL-ADYKPKELAqimaVLPQKMDQAFTF--- 89
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLK----PLRKKVGIVFQFpeh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 90 -----TVEETVAFGryPFQTGLFRqqtEKGEAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PRK13634 97 qlfeeTVEKDICFG--PMNFGVSE---EDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1238244423 164 PTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGT 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-214 |
1.28e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.45 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE-----LAQIMAv 78
Cdd:PRK10851 6 ANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDrkvgfVFQHYA- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 LPQKMdqaftfTVEETVAFGrypfQTGLFRQQTEKGEAIVQEAM---EQTGVADFAQKPIRELSGGEQQRVYLAQALAQQ 155
Cdd:PRK10851 85 LFRHM------TVFDNIAFG----LTVLPRRERPNAAAIKAKVTqllEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1238244423 156 PRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-169 |
1.86e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 93.69 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSR-LINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKKGRVYLAGKLLADYKPKELAQIMAVLPQK 82
Cdd:COG1132 343 ENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKstlvnlllrfyDPTSGRILIDGVDIRDLTLESLRRQIGVVPQD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 83 mdqAFTF--TVEETVAFGRypfqtglfrqqTEKGEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLA 149
Cdd:COG1132 423 ---TFLFsgTIRENIRYGR-----------PDATDEEVEEAAKAAQAHEFIEAlpdgydtVVGErgvnLSGGQRQRIAIA 488
|
170 180
....*....|....*....|
gi 1238244423 150 QALAQQPRILFLDEPTNFLD 169
Cdd:COG1132 489 RALLKDPPILILDEATSALD 508
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-214 |
1.99e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 90.52 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELA----------- 73
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafrrdiqmvfq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 74 -QIMAVLPQKmdqaftfTVEETVafgRYPFQTGLFRQQTEKgEAIVQEAMEQTGVAD-FAQKPIRELSGGEQQRVYLAQA 151
Cdd:PRK10419 97 dSISAVNPRK-------TVREII---REPLRHLLSLDKAER-LARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238244423 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNG 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-214 |
2.29e-20 |
|
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: 89.19 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 18 NVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKMdQAFTFTVEETVAF 97
Cdd:cd03245 22 NVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDV-TLFYGTLRDNITL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 98 GRyPFQTglfrqqtekgEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:cd03245 101 GA-PLAD----------DERILRAAELAGVTDFVNKhpngldlQIGErgrgLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1238244423 167 FLDLAYQKDLLDLIKRLTRESGLaaVSVFHDLNTASLyCDGLMFMKNG 214
Cdd:cd03245 170 AMDMNSEERLKERLRQLLGDKTL--IIITHRPSLLDL-VDRIIVMDSG 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-216 |
2.39e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.94 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLadyKPKELAQImAVLP- 80
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRI-GYLPe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 -----QKMdqaftfTVEET-VAFGRYpfqTGLfrqqtEKGEAI--VQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQAL 152
Cdd:COG4152 79 erglyPKM------KVGEQlVYLARL---KGL-----SKAEAKrrADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238244423 153 AQQPRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGlAAVsVF--HDLNTASLYCDGLMFMKNGTA 216
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIREL-AAKG-TTV-IFssHQMELVEELCDRIVIINKGRK 207
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-214 |
3.45e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 89.72 E-value: 3.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLadYKPKELAQIMAV-LPQKMDQAFT-- 88
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVL--YFGKDIFQIDAIkLRKEVGMVFQqp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 89 -----FTVEETVAfgrYPFQTGLFRQQTEKgEAIVQEAMEQTG----VADFAQKPIRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:PRK14246 100 npfphLSIYDNIA---YPLKSHGIKEKREI-KKIVEECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 160 FLDEPTNFLDLAYQKDLLDLIKRLTREsgLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
12-241 |
3.90e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.77 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKMDQAFT-FT 90
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFVgAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 91 VEETVAFGRYpfQTGLFRQQTEKGeaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDL 170
Cdd:PRK13642 99 VEDDVAFGME--NQGIPREEMIKR---VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238244423 171 AYQKDLLDLIKRLTRESGLAAVSVFHDLNTASlYCDGLMFMKNGTAGPKQKPE--YAVTEQSIKAVYDTDVTA 241
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIKEAAPSelFATSEDMVEIGLDVPFSS 245
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-215 |
4.40e-20 |
|
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: 87.61 E-value: 4.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 14 RLINNVSLTVEKGEFLGILGPNGSGKTT--LLHLLTGTLPAKKGRVYLAGKllaDYKPKELAQIMAVLPQKmDQAF-TFT 90
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTllNALAGRRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQD-DILHpTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 91 VEETVafgrypfqtglfrqqtekgeaivqeameqtgvaDFAQKpIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDL 170
Cdd:cd03213 99 VRETL---------------------------------MFAAK-LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1238244423 171 AYQKDLLDLIKRLtRESGLAAVSVFHDLnTASLY--CDGLMFMKNGT 215
Cdd:cd03213 145 SSALQVMSLLRRL-ADTGRTIICSIHQP-SSEIFelFDKLLLLSQGR 189
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
12-214 |
4.74e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.80 E-value: 4.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLL-ADYKPKELAQIMA----VLPQKMDQA 86
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQIRKkvglVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 87 FTFTVEETVAFGRYPFQTglfrqQTEKGEAIVQEAMEQTGVAD--FAQKPIrELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:PRK13649 99 FEETVLKDVAFGPQNFGV-----SQEEAEALAREKLALVGISEslFEKNPF-ELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1238244423 165 TNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKG 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
16-214 |
4.85e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.15 E-value: 4.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTT------------------LLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI-- 75
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTfiehlnalllpdtgtiewIFKDEKNKKKTKEKEKVLEKLVIQKTRFKKIKKIke 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 76 ----MAVLPQKMD-QAFTFTVEETVAFGryPFQTGLFRQQTEKgeaIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLA 149
Cdd:PRK13651 103 irrrVGVVFQFAEyQLFEQTIEKDIIFG--PVSMGVSKEEAKK---RAAKYIELVGLdESYLQRSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 150 QALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-214 |
6.01e-20 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 92.05 E-value: 6.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLS----GGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK----KGRVYLAGKLLADYKPKELAQI 75
Cdd:COG4172 10 EDLSvafgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSERELRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 76 ----MAVLPQK-MdqafT-----FTVE----ETVAFgrypfQTGLFRQQTEKgEAIvqEAMEQTGVADfAQKPIR----E 137
Cdd:COG4172 90 rgnrIAMIFQEpM----TslnplHTIGkqiaEVLRL-----HRGLSGAAARA-RAL--ELLERVGIPD-PERRLDayphQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 138 LSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQG 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
17-199 |
6.99e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 90.18 E-value: 6.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 17 NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKEL------AQIM-----AVLPQKMdq 85
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplrrrMQMVfqdpyASLNPRM-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 86 aftfTVEETVAFgryPFQtgLFRQQTEKG-EAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:COG4608 113 ----TVGDIIAE---PLR--IHGLASKAErRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 1238244423 164 PTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLN 199
Cdd:COG4608 184 PVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLS 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
6-214 |
7.11e-20 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 90.56 E-value: 7.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 6 LSGGYGDSRLinNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYkpkelAQIMAVLPQKmdQ 85
Cdd:TIGR02142 5 FSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDS-----RKGIFLPPEK--R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 86 AFTFTVEETVAFGRYPFQT----GLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:TIGR02142 76 RIGYVFQEARLFPHLSVRGnlryGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1238244423 162 DEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:TIGR02142 156 DEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDG 208
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
31-214 |
1.23e-19 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 89.48 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 31 ILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE-----LAQIMAVLPQkmdqaftFTVEETVAFGrypfqtg 105
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLrhinmVFQSYALFPH-------MTVEENVAFG------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 106 lFRQQTEKGEAI---VQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKR 182
Cdd:TIGR01187 67 -LKMRKVPRAEIkprVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKT 145
|
170 180 190
....*....|....*....|....*....|..
gi 1238244423 183 LTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:TIGR01187 146 IQEQLGITFVFVTHDQEEAMTMSDRIAIMRKG 177
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-170 |
1.63e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlpakkgRVyLAGKLLAD----YKPKELaqIMAV 78
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKst------------llKI-LAGELEPDsgevSIPKGL--RIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 LPQKMDQAFTFTVEETVAFG---------RYPFQTGLFRQQTEKGEAI--VQEAMEQTG-----------------VADF 130
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVLDGdaelraleaELEELEAKLAEPDEDLERLaeLQEEFEALGgweaearaeeilsglgfPEED 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1238244423 131 AQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDL 170
Cdd:COG0488 146 LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
16-181 |
1.98e-19 |
|
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: 86.31 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELA---QIMAVLPQKMDQAFTFTVE 92
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 93 ETVAFGrypfqtglFRQQTEKGEAI---VQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:cd03292 97 ENVAFA--------LEVTGVPPREIrkrVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170
....*....|..
gi 1238244423 170 LAYQKDLLDLIK 181
Cdd:cd03292 169 PDTTWEIMNLLK 180
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-199 |
2.06e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKKGRVYLAGKLLADYKPKElAQ---ImAV 78
Cdd:COG1129 6 EMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKstlmkilsgvyQPDSGEILLDGEPVRFRSPRD-AQaagI-AI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 LPQKMDQAFTFTVEETVAFGRYPFQTGLFRQQTEKGEAivQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRI 158
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRA--RELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1238244423 159 LFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLN 199
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLD 201
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-171 |
3.51e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTllhlltgtlpakkgrvyLAgKLLADykpkELAQimavlpqk 82
Cdd:COG0488 318 LEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKST-----------------LL-KLLAG----ELEP-------- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 83 mdQAFTFTVEETVAFGrYpfqtglFRQQTE--KGEAIVQEAMEQTG-----------VADF------AQKPIRELSGGEQ 143
Cdd:COG0488 368 --DSGTVKLGETVKIG-Y------FDQHQEelDPDKTVLDELRDGApggteqevrgyLGRFlfsgddAFKPVGVLSGGEK 438
|
170 180
....*....|....*....|....*...
gi 1238244423 144 QRVYLAQALAQQPRILFLDEPTNFLDLA 171
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDIE 466
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
1-229 |
3.54e-19 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 86.58 E-value: 3.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTL-----LHLLTGTLPAKKGRVYLAGKLLADYK--PKELA 73
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLlrslnRMNDLVPGVRIEGKVLFDGQDIYDKKidVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 74 QIMAVLPQKMDqAFTFTVEETVAFGryPFQTGLfrQQTEKGEAIVQEAMEQTG----VADFAQKPIRELSGGEQQRVYLA 149
Cdd:TIGR00972 82 RRVGMVFQKPN-PFPMSIYDNIAYG--PRLHGI--KDKKELDEIVEESLKKAAlwdeVKDRLHDSALGLSGGQQQRLCIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 150 QALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLtRESgLAAVSVFHDLNTASLYCDGLMFMKNGTAgpkqkPEYAVTEQ 229
Cdd:TIGR00972 157 RALAVEPEVLLLDEPTSALDPIATGKIEELIQEL-KKK-YTIVIVTHNMQQAARISDRTAFFYDGEL-----VEYGPTEQ 229
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1-235 |
3.83e-19 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 86.17 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI-MAVL 79
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 80 PQkmdQAFTF---TVEETVAfGRYPFQTGLFR-QQTEKGEAIvqeaMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQ 155
Cdd:TIGR04406 82 PQ---EASIFrklTVEENIM-AVLEIRKDLDRaEREERLEAL----LEEFQISHLRDNKAMSLSGGERRRVEIARALATN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 156 PRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQKPEYAVTEQSIKAVY 235
Cdd:TIGR04406 154 PKFILLDEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVY 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
2-201 |
6.04e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.07 E-value: 6.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLS---GGYGDSRLI-NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKlladykpkelaqimA 77
Cdd:COG4525 5 TVRHVSvryPGGGQPQPAlQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV--------------P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 78 VLPQKMDQAFTF---------TVEETVAFGrypFQ-TGLFRQQTEkgeAIVQEAMEQTGVADFAQKPIRELSGGEQQRVY 147
Cdd:COG4525 71 VTGPGADRGVVFqkdallpwlNVLDNVAFG---LRlRGVPKAERR---ARAEELLALVGLADFARRRIWQLSGGMRQRVG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1238244423 148 LAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTA 201
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-248 |
6.58e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.78 E-value: 6.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQImAVLPQKM 83
Cdd:PRK13537 11 RNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV-GVVPQFD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 84 DQAFTFTVEETV-AFGRYpfqtglFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:PRK13537 90 NLDPDFTVRENLlVFGRY------FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 163 EPTNFLDLAYQKDLLDLIKRLTrESGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQKPEYAVTEQ---SIKAVYDTDV 239
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEigcDVIEIYGPDP 242
|
....*....
gi 1238244423 240 TALVHQSSP 248
Cdd:PRK13537 243 VALRDELAP 251
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-235 |
8.43e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.33 E-value: 8.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGklladykpkelaQIMAVLP 80
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD------------EDISLLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 --QKMDQAFTFTVEETVAFGRYPFQTGLF-----RQQ--TEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQA 151
Cdd:PRK10895 72 lhARARRGIGYLPQEASIFRRLSVYDNLMavlqiRDDlsAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQKPEYAVTEQSI 231
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
....
gi 1238244423 232 KAVY 235
Cdd:PRK10895 231 KRVY 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-217 |
8.52e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.50 E-value: 8.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKkgrvylAGKLLADYKP----KELAQIM--- 76
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPS------AGELLAGTAPlaeaREDTRLMfqd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 77 -AVLPQKmdqaftfTVEETVAFGrypfQTGLFRQQTEkgeaivqEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQ 155
Cdd:PRK11247 90 aRLLPWK-------KVIDNVGLG----LKGQWRDAAL-------QALAAVGLADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238244423 156 PRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTAG 217
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIG 213
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
15-214 |
1.04e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.14 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAkkGRVYLAGKLLADYKPKELAQI----MAVLPQKMDQAFTfT 90
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDGKPVAPCALrgrkIATIMQNPRSAFN-P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 91 VEETVAFGRypfQTGLFRQQTEKgEAIVQEAMEQTGVADFAQKPIR---ELSGGEQQRVYLAQALAQQPRILFLDEPTNF 167
Cdd:PRK10418 95 LHTMHTHAR---ETCLALGKPAD-DATLTAALEAVGLENAARVLKLypfEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1238244423 168 LDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHG 217
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-214 |
1.71e-18 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 82.75 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 6 LSGGYGDSR--LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKpKELAQIMAVLPQKM 83
Cdd:cd03247 6 VSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQRP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 84 dqaftftveetvafgrYPFQTGLfrqqtekgeaivqeaMEQTGvadfaqkpiRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:cd03247 85 ----------------YLFDTTL---------------RNNLG---------RRFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1238244423 164 PTNFLDLAYQKDLLDLIKRLTRESGLAAVSvfHDLnTASLYCDGLMFMKNG 214
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLKDKTLIWIT--HHL-TGIEHMDKILFLENG 172
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-189 |
2.98e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 85.51 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 17 NNVSLTVEKGEFLGILGPNGSGKttllhlltgtlpakKGRVYLAGKLLADYKPKELAQI-----M-----AVLPQKmdqa 86
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKstlircinllerptSGSVLVDGVDLTALSERELRAArrkigMifqhfNLLSSR---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 87 ftfTVEETVAFgryPFQ-TGLFRQQTEKgeaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPT 165
Cdd:COG1135 98 ---TVAENVAL---PLEiAGVPKAEIRK---RVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180
....*....|....*....|....
gi 1238244423 166 NFLDLAYQKDLLDLIKRLTRESGL 189
Cdd:COG1135 169 SALDPETTRSILDLLKDINRELGL 192
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-214 |
4.53e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.30 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKkGRVYLAGKLLADYKPKELAQI---MAVLPQKMDQAF 87
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLLPVrhrIQVVFQDPNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 88 T--FTVEETVAFGRYPFQTGLFRQQTEkgeAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:PRK15134 376 NprLNVLQIIEEGLRVHQPTLSAAQRE---QQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1238244423 165 TNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
12-170 |
4.76e-18 |
|
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: 82.90 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKmDQAFTFTV 91
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQE-PVLFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 92 EETVAFgrypfqtGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRE-------LSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:cd03248 105 QDNIAY-------GLQSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEA 177
|
....*.
gi 1238244423 165 TNFLDL 170
Cdd:cd03248 178 TSALDA 183
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
7.56e-18 |
|
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: 80.55 E-value: 7.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKElaqimavlpq 81
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 kmdqaftftveetvafgrypfqtglfrqqtekgeaivqeaMEQTGVADFAQkpireLSGGEQQRVYLAQALAQQPRILFL 161
Cdd:cd03216 72 ----------------------------------------ARRAGIAMVYQ-----LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1238244423 162 DEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-220 |
1.14e-17 |
|
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: 85.18 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 3 AEGLSGGYGDSR--LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLP 80
Cdd:COG4618 333 VENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QkmD-QAFTFTVEETVAfgrypfqtglfRQQTEKGEAIVqEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYL 148
Cdd:COG4618 413 Q--DvELFDGTIAENIA-----------RFGDADPEKVV-AAAKLAGVHEMILRlpdgydtRIGEggarLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 149 AQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLyCDGLMFMKNGTA---GPKQ 220
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA-VDKLLVLRDGRVqafGPRD 551
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-222 |
1.74e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 82.36 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 14 RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVylagkLLADYK-PKELAQIMAV--LPQKMDQAFTF- 89
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-----IVGDYAiPANLKKIKEVkrLRKEIGLVFQFp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 90 -------TVEETVAFGryPFQTGLFRQQTEKGeaiVQEAMEQTGVA-DFAQKPIRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:PRK13645 100 eyqlfqeTIEKDIAFG--PVNLGENKQEAYKK---VPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238244423 162 DEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQKP 222
Cdd:PRK13645 175 DEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-215 |
2.02e-17 |
|
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: 78.64 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTllhlltgtlpakkgrvylagklladykpkeLAQIMAvlpq 81
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKST------------------------------LLKLIA---- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 kmdqaftftveetvafGRYPFQTGLFRQqtekgeaivqeaMEQTGVADFAQkpireLSGGEQQRVYLAQALAQQPRILFL 161
Cdd:cd03221 48 ----------------GELEPDEGIVTW------------GSTVKIGYFEQ-----LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 162 DEPTNFLDLAYQKDLLDLIKRLtrESGLAAVSvfHD---LNTAslyCDGLMFMKNGT 215
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEY--PGTVILVS--HDryfLDQV---ATKIIELEDGK 144
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
20-201 |
2.45e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.78 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 20 SLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKllaDYKPKELAQ-IMAVLPQKMDQAFTFTVEETVAFG 98
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ---DHTTTPPSRrPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 99 RYPfqtGL--FRQQTEKGEAIVQeameQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDL 176
Cdd:PRK10771 96 LNP---GLklNAAQREKLHAIAR----QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180
....*....|....*....|....*
gi 1238244423 177 LDLIKRLTRESGLAAVSVFHDLNTA 201
Cdd:PRK10771 169 LTLVSQVCQERQLTLLMVSHSLEDA 193
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
10-214 |
2.86e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 80.83 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLaDYKPKELAQIMAVLPQKMDQAFT- 88
Cdd:COG4161 12 YGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF-DFSQKPSEKAIRLLRQKVGMVFQq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 89 ------FTVEETVAfgRYPFQT-GLFRQQTeKGEAivQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:COG4161 91 ynlwphLTVMENLI--EAPCKVlGLSKEQA-REKA--MKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1238244423 162 DEPTNFLDLAYQKDLLDLIKRLTrESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:COG4161 166 DEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKG 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-214 |
3.22e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 81.80 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGK-LLADYKPKELAQIMA----VLPQKMDQAFTFT 90
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhITPETGNKNLKKLRKkvslVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 91 VEETVAFGryPFQTGlFRQQTEKGEAIvqEAMEQTGVA-DFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK13641 103 VLKDVEFG--PKNFG-FSEDEAKEKAL--KWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1238244423 170 LAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
17-209 |
3.40e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 83.70 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 17 NNVSLTVE-----KGEFLGILGPNGSGKTTLlhlltgtlpAKkgrvYLAGKLLADYKPKELAQIMAVLPQKMDQAFTFTV 91
Cdd:PRK13409 351 GDFSLEVEggeiyEGEVIGIVGPNGIGKTTF---------AK----LLAGVLKPDEGEVDPELKISYKPQYIKPDYDGTV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 92 EE-----TVAFGRYPFQTglfrqqtekgeaivqEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:PRK13409 418 EDllrsiTDDLGSSYYKS---------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1238244423 167 FLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLM 209
Cdd:PRK13409 483 HLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
10-214 |
4.08e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 80.44 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGK---LLADYKPKELAQimavLPQKMDQA 86
Cdd:PRK11124 12 YGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdFSKTPSDKAIRE----LRRNVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 87 FT-------FTVEETVAfgRYPFQT-GLFRQQTeKGEAIvqEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRI 158
Cdd:PRK11124 88 FQqynlwphLTVQQNLI--EAPCRVlGLSKDQA-LARAE--KLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1238244423 159 LFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENG 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-248 |
4.12e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.60 E-value: 4.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 14 RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK-----KGRVYLAGKLLADYKPKELAQI----MAVLPQKMD 84
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 85 QAFT--FTVE----ETVAFGRypfqtGLfRQQTEKGEAIvqEAMEQTGVADFAQK----PiRELSGGEQQRVYLAQALAQ 154
Cdd:PRK15134 103 VSLNplHTLEkqlyEVLSLHR-----GM-RREAARGEIL--NCLDRVGIRQAAKRltdyP-HQLSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 155 QPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQK-------PEYAVT 227
Cdd:PRK15134 174 RPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRaatlfsaPTHPYT 253
|
250 260
....*....|....*....|.
gi 1238244423 228 EQSIKAVYDTDVTALVHQSSP 248
Cdd:PRK15134 254 QKLLNSEPSGDPVPLPEPASP 274
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-214 |
6.03e-17 |
|
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: 82.95 E-value: 6.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLP--AKKGRVYLAGKLL--ADYKPKELAQIm 76
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLkaSNIRDTERAGI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 77 AVLPQKMDQAFTFTVEETVAFGR---YPFQTGLFRQQTEKGEAIVQEAMEQtgvADFAQKPIRELSGGEQQRVYLAQALA 153
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNeitLPGGRMAYNAMYLRAKNLLRELQLD---ADNVTRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238244423 154 QQPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
15-202 |
6.59e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.47 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLL--------ADYKPKELA---QIMAVLPQkm 83
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssaakAELRNQKLGfiyQFHHLLPD-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 84 dqaftFTVEETVAFgryPFQTGLFRQQTEKGEAivQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PRK11629 102 -----FTALENVAM---PLLIGKKKPAEINSRA--LEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1238244423 164 PTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTAS 202
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAK 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-214 |
6.69e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.55 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 13 SRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLL-ADYKPKELA----QIMAVLPQKMDQAF 87
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsSTSKQKEIKpvrkKVGVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 88 TFTVEETVAFGryPFQTGLFRQQTEKgeaIVQEAMEQTGVA-DFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:PRK13643 99 EETVLKDVAFG--PQNFGIPKEKAEK---IAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1238244423 167 FLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK13643 174 GLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
20-209 |
7.57e-17 |
|
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: 82.91 E-value: 7.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 20 SLTVE-----KGEFLGILGPNGSGKTTLlhlltgtlpAKkgrvYLAGKLLADYKPKELAQIMAVLPQKMDQAFTFTVEE- 93
Cdd:COG1245 355 SLEVEggeirEGEVLGIVGPNGIGKTTF---------AK----ILAGVLKPDEGEVDEDLKISYKPQYISPDYDGTVEEf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 94 -----TVAFGRYPFQTglfrqqtekgeaivqEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFL 168
Cdd:COG1245 422 lrsanTDDFGSSYYKT---------------EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1238244423 169 DLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLM 209
Cdd:COG1245 487 DVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-200 |
9.04e-17 |
|
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: 79.20 E-value: 9.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQkmdQAFTF--TVEE 93
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQ---DVFLFndTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 94 TVAFGRypfqtglfrqqTEKGEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:cd03251 95 NIAYGR-----------PGATREEVEEAARAANAHEFIMElpegydtVIGErgvkLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1238244423 163 EPTNFLDLAYQKDLLDLIKRLTResGLAAVSVFHDLNT 200
Cdd:cd03251 164 EATSALDTESERLVQAALERLMK--NRTTFVIAHRLST 199
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-231 |
9.31e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.14 E-value: 9.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE-LAQIMA-VLPQKMDQAF-- 87
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDaVKKGMAyITESRRDNGFfp 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 88 TFTVEETVAF------GRYPFQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKpIRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:PRK09700 355 NFSIAQNMAIsrslkdGGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQN-ITELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 162 DEPTNFLDLAYQKDLLDLIKRLTrESGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQKPEYAVTEQSI 231
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEI 502
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-164 |
9.32e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 79.30 E-value: 9.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI-MAVLP 80
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 Q------KMdqaftfTVEETVAfgrypfqtgLFRQQTEKG----EAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQ 150
Cdd:COG1137 85 QeasifrKL------TVEDNIL---------AVLELRKLSkkerEERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170
....*....|....
gi 1238244423 151 ALAQQPRILFLDEP 164
Cdd:COG1137 150 ALATNPKFILLDEP 163
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-206 |
1.56e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.51 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLP--AKKGRVYLAGKLL--ADYKPKELAQImAVLPQKMDQ 85
Cdd:PRK13549 15 FGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELqaSNIRDTERAGI-AIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 86 AFTFTVEETVAFGRYPFQTGLFRQQTEKGEAivQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPT 165
Cdd:PRK13549 94 VKELSVLENIFLGNEITPGGIMDYDAMYLRA--QKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1238244423 166 NFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCD 206
Cdd:PRK13549 172 ASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISD 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
9-215 |
1.85e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.28 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 9 GYGDSRL--INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKMDQA 86
Cdd:PRK10584 17 GQGEHELsiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 87 F----TFTVEETVAFgrypfqTGLFRQQTEK-GEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:PRK10584 97 FmlipTLNALENVEL------PALLRGESSRqSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1238244423 162 DEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASlYCDGLMFMKNGT 215
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAA-RCDRRLRLVNGQ 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-214 |
2.23e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 81.25 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 18 NVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE-LAQIMAVLPQK-------MDQAFTF 89
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDrqssglyLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 90 TVEeTVAFGRYPFQtglfrQQTEKGEAIVQEAMEQTGVA-DFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFL 168
Cdd:PRK15439 361 NVC-ALTHNRRGFW-----IKPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1238244423 169 DLAYQKDLLDLIKRLTrESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK15439 435 DVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-190 |
2.75e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.83 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGygdsRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE-LAQIMAVL 79
Cdd:COG1129 257 LEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 80 PQ--KMDQAF-TFTVEETVAFGRYPFQT--GLFRQQTEKgeAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALA 153
Cdd:COG1129 333 PEdrKGEGLVlDLSIRENITLASLDRLSrgGLLDRRRER--ALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLA 410
|
170 180 190
....*....|....*....|....*....|....*..
gi 1238244423 154 QQPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsGLA 190
Cdd:COG1129 411 TDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKA 446
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1-201 |
3.13e-16 |
|
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: 76.76 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPkELAQIMAVLP 80
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QKMDQAFTFTVEETVAFGRypfqtglfrqqTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:cd03231 80 HAPGIKTTLSVLENLRFWH-----------ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1238244423 161 LDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTA 201
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-214 |
3.29e-16 |
|
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: 77.66 E-value: 3.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 9 GYGDSR-LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKMdQAF 87
Cdd:cd03253 9 AYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDT-VLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 88 TFTVEETVAFGRypfqtglfrqqTEKGEAIVQEAMEQTGVADFAQK-P------IRE----LSGGEQQRVYLAQALAQQP 156
Cdd:cd03253 88 NDTIGYNIRYGR-----------PDATDEEVIEAAKAAQIHDKIMRfPdgydtiVGErglkLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1238244423 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTResGLAAVSVFHDLNTASlYCDGLMFMKNG 214
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIV-NADKIIVLKDG 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-215 |
4.26e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 79.38 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE-----LAQIMAVLPQkmd 84
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQrdicmVFQSYALFPH--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 85 qaftFTVEETVAFGrypfqtgLFRQQTEKGE--AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:PRK11432 93 ----MSLGENVGYG-------LKMLGVPKEErkQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1238244423 163 EPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-223 |
4.37e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.72 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAV-- 78
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVrt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 -----LPQKMdqaftfTVEET--VAFGRYpFQTGLFR--------QQTEKgEAIVQEA--MEQTGVADFAQKPIRELSGG 141
Cdd:PRK11300 86 fqhvrLFREM------TVIENllVAQHQQ-LKTGLFSgllktpafRRAES-EALDRAAtwLERVGLLEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 142 EQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQK 221
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
..
gi 1238244423 222 PE 223
Cdd:PRK11300 238 PE 239
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-180 |
5.75e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.87 E-value: 5.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRL--INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:PRK11160 342 NNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 KMDqAFTFTVEETVAFGrypfqtglfrqQTEKGEAIVQEAMEQTGVADFAQ--KPI--------RELSGGEQQRVYLAQA 151
Cdd:PRK11160 422 RVH-LFSATLRDNLLLA-----------APNASDEALIEVLQQVGLEKLLEddKGLnawlgeggRQLSGGEQRRLGIARA 489
|
170 180
....*....|....*....|....*....
gi 1238244423 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLI 180
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELL 518
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-214 |
8.75e-16 |
|
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: 75.16 E-value: 8.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGygdsRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI-MAVL 79
Cdd:cd03215 5 LEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 80 PqkmdqaftftvEEtvafgryPFQTGLFRQQTekgeaivqeAMEQTGVADFaqkpireLSGGEQQRVYLAQALAQQPRIL 159
Cdd:cd03215 81 P-----------ED-------RKREGLVLDLS---------VAENIALSSL-------LSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 160 FLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-214 |
9.77e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.46 E-value: 9.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 6 LSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYkpkELAQIM----AVLPQ 81
Cdd:PRK11614 11 VSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QTAKIMreavAIVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 KMDQAFTFTVEETVAFGRYPFQTGLFRQQTEKGEAIVQEAMEQTgvadfAQKPiRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:PRK11614 88 GRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERR-----IQRA-GTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1238244423 162 DEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-228 |
1.09e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.97 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLaDYKPK---ELAQIMAVLPQKMDQA 86
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 87 FTFT-VEETVAFGRYpfQTGLFRQQTEKGeaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPT 165
Cdd:PRK13638 90 IFYTdIDSDIAFSLR--NLGVPEAEITRR---VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 166 NFLDLAYQKDLLDLIKRLTRESGLAAVSVfHDLNTASLYCDGLMFMKNGTAGPKQKPE--YAVTE 228
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIISS-HDIDLIYEISDAVYVLRQGQILTHGAPGevFACTE 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-199 |
1.42e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 17 NNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKKGRVYLAGKLLADYKPKElaqimAvlpqkMD-------QAF-- 87
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKstlmkilyglyQPDSGEILIDGKPVRIRSPRD-----A-----IAlgigmvhQHFml 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 88 --TFTVEETVAFGRYPfqTGLFRQQTEKGEAIVQEAMEQTGVA-DfAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:COG3845 92 vpNLTVAENIVLGLEP--TKGGRLDRKAARARIRELSERYGLDvD-PDAKVEDLSVGEQQRVEILKALYRGARILILDEP 168
|
170 180 190
....*....|....*....|....*....|....*
gi 1238244423 165 TNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLN 199
Cdd:COG3845 169 TAVLTPQEADELFEILRRLAAE-GKSIIFITHKLR 202
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-200 |
1.42e-15 |
|
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: 75.99 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 11 GDSRLI-NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKEL-AQIMAVLPQKMdqAFT 88
Cdd:cd03252 12 PDGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLrRQVGVVLQENV--LFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 89 FTVEETVAFGRypfqTGLFRQQtekgeaiVQEAMEQTGVADFAQKpIRE------------LSGGEQQRVYLAQALAQQP 156
Cdd:cd03252 90 RSIRDNIALAD----PGMSMER-------VIEAAKLAGAHDFISE-LPEgydtivgeqgagLSGGQRQRIAIARALIHNP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1238244423 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTreSGLAAVSVFHDLNT 200
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLST 199
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-201 |
1.53e-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: 74.70 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPkELAQIMAVLPQK 82
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 83 MDQAFTFTVEETVAFGRYPFQTglfRQQTekgeaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:TIGR01189 82 PGLKPELSALENLHFWAAIHGG---AQRT------IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1238244423 163 EPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTA 201
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-216 |
1.56e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.44 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI-----------MAVLPQKMd 84
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdiqmifqdpLASLNPRM- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 85 qaftfTVEETVAFGRYPFQTGLFRQQTEKGeaiVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PRK15079 116 -----TIGEIIAEPLRTYHPKLSRQEVKDR---VKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1238244423 164 PTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTA 216
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 240
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-237 |
1.60e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.23 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK-----KGRVYLAGKLLADYK---PKEL 72
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRvnlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 73 AQIMAVLPQKmdQAFTFTVEETVAFGrypFQTGLFRQQTEKgEAIVQEAMEQTGVADFAQKPIR----ELSGGEQQRVYL 148
Cdd:PRK14258 88 RQVSMVHPKP--NLFPMSVYDNVAYG---VKIVGWRPKLEI-DDIVESALKDADLWDEIKHKIHksalDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 149 AQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQKPEYAVTE 228
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEFGLTK 241
|
....*....
gi 1238244423 229 QSIKAVYDT 237
Cdd:PRK14258 242 KIFNSPHDS 250
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
16-215 |
2.48e-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: 74.78 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLhlltgtlpakKG--RVYLA--GKLL--ADYKPKELA-----QIMA------- 77
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLL----------KCiyGNYLPdsGSILvrHDGGWVDLAqasprEILAlrrrtig 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 78 -------VLPQKmdqaftfTVEETVAfgrypfqTGLFRQQTEKGEAI--VQEAMEQTGV---------ADFaqkpirelS 139
Cdd:COG4778 97 yvsqflrVIPRV-------SALDVVA-------EPLLERGVDREEARarARELLARLNLperlwdlppATF--------S 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238244423 140 GGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-259 |
2.77e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 76.28 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLhlltgtlpaK---------KGRVYLAGklladYKP----KELA-QIMAVLPQ 81
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTI---------KmltgilvptSGEVRVLG-----YVPfkrrKEFArRIGVVFGQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 K---------MDqafTFTVEETVafgrYPFQTGLFRQQTEkgeaivqEAMEQTGVADFAQKPIRELSGGEQQRVYLAQAL 152
Cdd:COG4586 104 RsqlwwdlpaID---SFRLLKAI----YRIPDAEYKKRLD-------ELVELLDLGELLDTPVRQLSLGQRMRCELAAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 153 AQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGlaaVSVF---HDLN-TASLyCDGLMFMKNGtagpkqkpeyavte 228
Cdd:COG4586 170 LHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERG---TTILltsHDMDdIEAL-CDRVIVIDHG-------------- 231
|
250 260 270
....*....|....*....|....*....|.
gi 1238244423 229 qsiKAVYDTDVTALVHQSSPKPMIVIQPEKD 259
Cdd:COG4586 232 ---RIIYDGSLEELKERFGPYKTIVLELAEP 259
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
11-214 |
4.00e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 76.61 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI----MAVLPQKMDQA 86
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 87 FTFTVEETVAFGrypfqTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:PRK10070 119 PHMTVLDNTAFG-----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1238244423 167 FLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-165 |
4.02e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 74.77 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELA--------QI 75
Cdd:COG4674 14 EDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIArlgigrkfQK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 76 MAVLPQkmdqaftFTVEE----TVAFGRYPFQTgLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQA 151
Cdd:COG4674 94 PTVFEE-------LTVFEnlelALKGDRGVFAS-LFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGML 165
|
170
....*....|....
gi 1238244423 152 LAQQPRILFLDEPT 165
Cdd:COG4674 166 LAQDPKLLLLDEPV 179
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
12-196 |
4.20e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.15 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 12 DSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKKGRVYLagklladykPkELAQIMaVLPQK--MDQAftf 89
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKstllraiaglwPYGSGRIAR---------P-AGARVL-FLPQRpyLPLG--- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 90 TVEETVAfgrYPFQTGLFrqqtekGEAIVQEAMEQTGVADFAQKP------IRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:COG4178 441 TLREALL---YPATAEAF------SDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|...
gi 1238244423 164 PTNFLDLAYQKDLLDLIKRLTRESGLaaVSVFH 196
Cdd:COG4178 512 ATSALDEENEAALYQLLREELPGTTV--ISVGH 542
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-201 |
4.73e-15 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 75.51 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRL-INNVSLTVEKGEFLGILGPNGSGKTTLLhlltgtlpaK---------KGRVYLAGKLLADYKPKEL- 72
Cdd:COG1125 5 ENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTL---------RminrlieptSGRILIDGEDIRDLDPVELr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 73 -------AQImAVLPqkmdqafTFTVEETVAfgrypfqT--GLFRQQTEKGEAIVQEAMEQTG--VADFAQKPIRELSGG 141
Cdd:COG1125 76 rrigyviQQI-GLFP-------HMTVAENIA-------TvpRLLGWDKERIRARVDELLELVGldPEEYRDRYPHELSGG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238244423 142 EQQRVYLAQALAQQPRILFLDEPtnF--LDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTA 201
Cdd:COG1125 141 QQQRVGVARALAADPPILLMDEP--FgaLDPITREQLQDELLRLQRELGKTIVFVTHDIDEA 200
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-198 |
1.02e-14 |
|
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: 76.02 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK-KGRVYLAGKLLADYKP-KELAQIMAVLPQKMDQ---AFTFT 90
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPaQAIRAGIAMVPEDRKRhgiVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 91 VEETVAFGRYPFQTGLFRQQTEKGEAIVQEAMEQTGVADFAQK-PIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:TIGR02633 356 VGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFlPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180
....*....|....*....|....*....
gi 1238244423 170 LAYQKDLLDLIKRLTREsGLAAVSVFHDL 198
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQE-GVAIIVVSSEL 463
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
5-219 |
1.47e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 74.23 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQimavLPQKMD 84
Cdd:PRK11308 20 GLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKL----LRQKIQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 85 QAFT-------------FTVEETVAFgrypfQTGLFRQQ-TEKgeaiVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLA 149
Cdd:PRK11308 96 IVFQnpygslnprkkvgQILEEPLLI-----NTSLSAAErREK----ALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238244423 150 QALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTA---GPK 219
Cdd:PRK11308 167 RALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCvekGTK 239
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-231 |
1.48e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.02 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHL-----LTGTLPAKKGRVYLAGKLLADYKPKELAQI 75
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrliELYPEARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 76 MAVLPQKMDQAFTFTVEETVAFGryPFQTGLFRQQTEKgEAIVQEAMEQTG----VADFAQKPIRELSGGEQQRVYLAQA 151
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALG--LKLNRLVKSKKEL-QERVRWALEKAQlwdeVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsgLAAVSVFHDLNTASLYCDGLMFMKNGT---AGPKQ----KPEY 224
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQiveWGPTRevftNPRH 238
|
....*..
gi 1238244423 225 AVTEQSI 231
Cdd:PRK14247 239 ELTEKYV 245
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
6-214 |
2.06e-14 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 73.98 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 6 LSGGYGDSRLinNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYkpkelAQIMAVLPQKMDQ 85
Cdd:COG4148 7 FRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDS-----ARGIFLPPHRRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 86 AFTF---------TVEETVAFGRypfqtglfrQQTEKGEAIVQ--EAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ 154
Cdd:COG4148 80 GYVFqearlfphlSVRGNLLYGR---------KRAPRAERRISfdEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 155 QPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:COG4148 151 SPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQG 210
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-214 |
2.49e-14 |
|
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: 71.79 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 8 GGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLAdykPKELAqiMAVLPQkmdqaf 87
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS---LLGLG--GGFNPE------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 88 tFTVEETVAF-GRypfqtgLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:cd03220 99 -LTGRENIYLnGR------LLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1238244423 167 FLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:cd03220 172 VGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKG 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-202 |
2.52e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIM----AV 78
Cdd:PRK13539 5 GEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLghrnAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 LPqkmdqafTFTVEETVAFGRypfqtGLFRQqtekGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRI 158
Cdd:PRK13539 85 KP-------ALTVAENLEFWA-----AFLGG----EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1238244423 159 LFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTAS 202
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHIPLGLPG 192
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-214 |
2.85e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 75.14 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 18 NVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKmDQAFTFTVEETVAF 97
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQE-PVLFSGSVRENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 98 GRypfqtglfrQQTEKGEaiVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:TIGR00958 578 GL---------TDTPDEE--IMAAAKAANAHDFIMEfpngydtEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1238244423 167 FLDLAYQKDLLDLIKRltreSGLAAVSVFHDLNTASlYCDGLMFMKNG 214
Cdd:TIGR00958 647 ALDAECEQLLQESRSR----ASRTVLLIAHRLSTVE-RADQILVLKKG 689
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-194 |
3.52e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSG-GygdsrlINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE-LAQIMAV 78
Cdd:PRK10762 258 LKVDNLSGpG------VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 LPQ--KMDQ-AFTFTVEETVAFgrypfqTGLfRQQTEKGEAIvQEAMEQTGVADFAQ----------KPIRELSGGEQQR 145
Cdd:PRK10762 332 ISEdrKRDGlVLGMSVKENMSL------TAL-RYFSRAGGSL-KHADEQQAVSDFIRlfniktpsmeQAIGLLSGGNQQK 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1238244423 146 VYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSV 194
Cdd:PRK10762 404 VAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILV 451
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-228 |
4.18e-14 |
|
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: 74.07 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 14 RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVY-LAGKLLADY-KPKEL-----AQIMAVLPQKMDQA 86
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEWVDMtKPGPDgrgraKRYIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 87 FTFTVEE--TVAFG-RYPFQTGLFRqqtekgeaivqeAMEQTGVADFAQKPIR--------ELSGGEQQRVYLAQALAQQ 155
Cdd:TIGR03269 378 PHRTVLDnlTEAIGlELPDELARMK------------AVITLKMVGFDEEKAEeildkypdELSEGERHRVALAQVLIKE 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238244423 156 PRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQKPEYAVTE 228
Cdd:TIGR03269 446 PRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
17-196 |
4.21e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 72.91 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 17 NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQimavLPQKMD---QAFTF---- 89
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRK----ARRQIGmifQHFNLlssr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 90 TVEETVAFgryPFQtgLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK11153 98 TVFDNVAL---PLE--LAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
170 180
....*....|....*....|....*..
gi 1238244423 170 LAYQKDLLDLIKRLTRESGLAAVSVFH 196
Cdd:PRK11153 173 PATTRSILELLKDINRELGLTIVLITH 199
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
12-214 |
4.38e-14 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 71.42 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKmDQAFTFTV 91
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQE-PVLFDGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 92 EETVAFGRYPfqtglfRQQTEkgeaiVQEAMEQTGVADFAQK-PIR----------ELSGGEQQRVYLAQALAQQPRILF 160
Cdd:cd03249 94 AENIRYGKPD------ATDEE-----VEEAAKKANIHDFIMSlPDGydtlvgergsQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1238244423 161 LDEPTNFLDLAYQKDLLDLIKRLTResGLAAVSVFHDLNTASlYCDGLMFMKNG 214
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIR-NADLIAVLQNG 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-214 |
4.46e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 71.70 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLaGKLLADyKPKELAQIMAVLPQKM 83
Cdd:PRK11264 7 KNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITID-TARSLSQQKGLIRQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 84 DQA-FTFTveetvAFGRYPFQTGL--------FRQQTEKGEAIV--QEAMEQTGVADFAQKPIRELSGGEQQRVYLAQAL 152
Cdd:PRK11264 85 QHVgFVFQ-----NFNLFPHRTVLeniiegpvIVKGEPKEEATAraRELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238244423 153 AQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESgLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-198 |
5.20e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.47 E-value: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDS----RLINNVSLTVEKGEFLGILGPNGSGKTTLLHlltgtlpAKKGRVYLAGKLLAD---------- 66
Cdd:PRK11022 4 LNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSL-------AIMGLIDYPGRVMAEklefngqdlq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 67 -YKPKELAQI----MAVLPQ----KMDQAFT--FTVEETVAFgrypFQTGlfRQQTEKGEAIvqEAMEQTGVADFAQK-- 133
Cdd:PRK11022 77 rISEKERRNLvgaeVAMIFQdpmtSLNPCYTvgFQIMEAIKV----HQGG--NKKTRRQRAI--DLLNQVGIPDPASRld 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 134 --PiRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDL 198
Cdd:PRK11022 149 vyP-HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDL 214
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-215 |
7.03e-14 |
|
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: 70.72 E-value: 7.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQkmdQAFTF--TVEE 93
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQ---DTFLFsgTIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 94 TVAFGRypfqtglfrqqTEKGEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:cd03254 96 NIRLGR-----------PNATDEEVIEAAKEAGAHDFIMKlpngydtVLGEnggnLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1238244423 163 EPTNFLDLAYQKDLLDLIKRLTResGLAAVSVFHDLNTAsLYCDGLMFMKNGT 215
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTI-KNADKILVLDDGK 214
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
13-214 |
7.95e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.54 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 13 SRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPA---KKGRVYLAGKLLadyKPKELAQIMAVLPQkmDQAF-- 87
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI---DAKEMRAISAYVQQ--DDLFip 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 88 TFTVEETVAFG---RYPfqtglfRQQTEKGE-AIVQEAMEQTGVADFAQKPI------RELSGGEQQRVYLAQALAQQPR 157
Cdd:TIGR00955 113 TLTVREHLMFQahlRMP------RRVTKKEKrERVDEVLQALGLRKCANTRIgvpgrvKGLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238244423 158 ILFLDEPTNFLD--LAYQkdLLDLIKRLTrESGLAAVSVFHDlNTASLYC--DGLMFMKNG 214
Cdd:TIGR00955 187 LLFCDEPTSGLDsfMAYS--VVQVLKGLA-QKGKTIICTIHQ-PSSELFElfDKIILMAEG 243
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-220 |
9.62e-14 |
|
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: 70.51 E-value: 9.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 20 SLTVEKGEF-----LGILGPNGSGKTTLLHLltgtlpakkgrvyLAGKLLADY--KPKELAQImAVLPQKMDQAFTFTVE 92
Cdd:cd03237 14 TLEVEGGSIsesevIGILGPNGIGKTTFIKM-------------LAGVLKPDEgdIEIELDTV-SYKPQYIKADYEGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 93 E-----TVAFGRYP-FQTglfrqqtekgeaivqEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:cd03237 80 DllssiTKDFYTHPyFKT---------------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1238244423 167 FLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFM-----KNGTAGPKQ 220
Cdd:cd03237 145 YLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFegepsVNGVANPPQ 203
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
10-223 |
1.14e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.77 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLL------------ADYKPKELAQI-M 76
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvADKNQLRLLRTrL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 77 AVLPQKMDQAFTFTVEETVAfgRYPFQTGLFRQQTEKGEAIvqEAMEQTGVADFAQ-KPIRELSGGEQQRVYLAQALAQQ 155
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVM--EAPIQVLGLSKQEARERAV--KYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238244423 156 PRILFLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNGTAGPKQKPE 223
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPE 237
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-169 |
1.71e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 70.07 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGK---------------TtllhlltgtlpAK-KGRVYLAGK-- 62
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKstllrclnrmndlipG-----------ARvEGEILLDGEdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 63 LLADYKPKEL-AQIMAVlPQKmDQAFTFTVEETVAFG-RYpfqtglfRQQTEKGE--AIVQEAMEQTG----VADFAQKP 134
Cdd:COG1117 81 YDPDVDVVELrRRVGMV-FQK-PNPFPKSIYDNVAYGlRL-------HGIKSKSEldEIVEESLRKAAlwdeVKDRLKKS 151
|
170 180 190
....*....|....*....|....*....|....*
gi 1238244423 135 IRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
11-207 |
1.80e-13 |
|
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: 68.71 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK--KGRVYLAGKLLADYKPKELAQiMAVlpqkmdqaft 88
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPEERAR-LGI---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 89 ftveeTVAFgrypfqtglfrqqtekgeaivQEAMEQTGV--ADFaqkpIREL----SGGEQQRVYLAQALAQQPRILFLD 162
Cdd:cd03217 80 -----FLAF---------------------QYPPEIPGVknADF----LRYVnegfSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1238244423 163 EPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFH-----DL---NTASLYCDG 207
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKL-REEGKSVLIITHyqrllDYikpDRVHVLYDG 181
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-215 |
1.94e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.58 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAG-KLLADYKPKELAQIMA----VLPQKMDQAFTFT 90
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKYIRPVRKrigmVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 91 VEETVAFGRYPFQTGLfrqqtEKGEAIVQEAMEQTGVA-DFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK13646 103 VEREIIFGPKNFKMNL-----DEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1238244423 170 LAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGS 223
|
|
| CbiZ |
COG1865 |
Adenosylcobinamide amidohydrolase [Coenzyme transport and metabolism]; |
276-440 |
2.28e-13 |
|
Adenosylcobinamide amidohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 441470 Cd Length: 224 Bit Score: 69.13 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 276 RDDILLQTEIPLRTLSSTPIGAGFSWSRTLIHKRLP---DQPDPIEGLTACLSESGFQLQETCAMASSERLDRFVYRTYE 352
Cdd:COG1865 11 DGVLVVRFPGPRRVLSTAVLNGGLREARAVFNHQVPedyDRTDPEEYLAEVLARLGLPPGDTVGLLTAADMENAAIAEES 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 353 DGELSVFICVQTGFS------------------------IWILINGYAADQFFIKALM-AAEAeRTKVLGDGG------- 400
Cdd:COG1865 91 FGGLSVTAVVTAGVSnavragadpasyyeprppppgtinIIVLINAPLSDGALVNAVItATEA-KTAALQELGigsrysg 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1238244423 401 ----GTG-D-ILIAATqtqQSENIEQ------RLNQLIKKGTAECIKEAAEL 440
Cdd:COG1865 170 glatGTGtDaIAVAAP---PDGEPLTyagkhtKLGELIGRAVYEAVREALRR 218
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-214 |
3.11e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.34 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 14 RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQ--KMDQAFTFTV 91
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQdpMMGTAPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 92 EE--TVAFGRyPFQTGLFRQQTEKGEAIVQEAMEQT--GVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNF 167
Cdd:COG1101 100 EEnlALAYRR-GKRRGLRRGLTKKRRELFRELLATLglGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1238244423 168 LDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:COG1101 179 LDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-289 |
3.19e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLL-------ADYKPKELAQIMAVLPQKMDQAF- 87
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrsrqvIELSEQSAAQMRHVRGADMAMIFq 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 88 --------TFTVEETVAfgrypfQTGLFRQQTEKGEAIVQ--EAMEQTGVAD----FAQKPiRELSGGEQQRVYLAQALA 153
Cdd:PRK10261 112 epmtslnpVFTVGEQIA------ESIRLHQGASREEAMVEakRMLDQVRIPEaqtiLSRYP-HQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 154 QQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTA---GPKQK----PEYAV 226
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAvetGSVEQifhaPQHPY 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238244423 227 TEQSIKAVydTDVTALVHQSSPK--PMIVI-QPEKDSVKRQS---IPFEALLQAgRDdilLQTEIPLRT 289
Cdd:PRK10261 265 TRALLAAV--PQLGAMKGLDYPRrfPLISLeHPAKQEPPIEQdtvVDGEPILQV-RN---LVTRFPLRS 327
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-214 |
4.61e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 68.65 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKgRVYLAGKLLAD----YKPK----EL 72
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNP-EVTITGSIVYNghniYSPRtdtvDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 73 -AQIMAVLPQKmdQAFTFTVEETVAFGrypfqtglFRQQTEKGEAIVQEAMEQT--------GVADFAQKPIRELSGGEQ 143
Cdd:PRK14239 85 rKEIGMVFQQP--NPFPMSIYENVVYG--------LRLKGIKDKQVLDEAVEKSlkgasiwdEVKDRLHDSALGLSGGQQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238244423 144 QRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSvfHDLNTASLYCDGLMFMKNG 214
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT--RSMQQASRISDRTGFFLDG 223
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-170 |
5.43e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 70.69 E-value: 5.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVylagklladyKPKELAQImAVLPQk 82
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------KWSENANI-GYYAQ- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 83 mDQAFTFTVEETVafgrypFQ-TGLFRQQTEKGEAIvqeameqTGV-------ADFAQKPIRELSGGEQQRVYLAQALAQ 154
Cdd:PRK15064 390 -DHAYDFENDLTL------FDwMSQWRQEGDDEQAV-------RGTlgrllfsQDDIKKSVKVLSGGEKGRMLFGKLMMQ 455
|
170
....*....|....*.
gi 1238244423 155 QPRILFLDEPTNFLDL 170
Cdd:PRK15064 456 KPNVLVMDEPTNHMDM 471
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-198 |
6.04e-13 |
|
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: 68.55 E-value: 6.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 22 TVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRV-----------YLAGKLLADYKPKELAQIM--AVLPQKMDQ--- 85
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNYFTKLLEGDVkvIVKPQYVDLipk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 86 AFTFTVEEtvafgrypfqtgLFRQQTEKGEaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPT 165
Cdd:cd03236 102 AVKGKVGE------------LLKKKDERGK--LDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|...
gi 1238244423 166 NFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDL 198
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAED-DNYVLVVEHDL 199
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
11-214 |
6.26e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 69.37 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLpAKKGRV----YLAGKLLADYKPKEL-------------- 72
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIggsaTFNGREILNLPEKELnklraeqismifqd 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 73 ------------AQIMAVLP--QKMDQAFTFtvEETVAFGrypfqtglfrqqtekgEAIvqeAMEQtgvadfAQKPIR-- 136
Cdd:PRK09473 106 pmtslnpymrvgEQLMEVLMlhKGMSKAEAF--EESVRML----------------DAV---KMPE------ARKRMKmy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 137 --ELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK09473 159 phEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-197 |
7.29e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.67 E-value: 7.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE-----LAQIMAVLPQkmd 84
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAErgvgmVFQSYALYPH--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 85 qaftFTVEETVAFgrypfqtGLFRQQTEKGEaiVQEAMEQtgVADFAQ-------KPiRELSGGEQQRVYLAQALAQQPR 157
Cdd:PRK11000 90 ----LSVAENMSF-------GLKLAGAKKEE--INQRVNQ--VAEVLQlahlldrKP-KALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1238244423 158 ILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHD 197
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHD 193
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-210 |
8.49e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 68.27 E-value: 8.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLH---LLTGTLPAKK--GRVYLAGKLL--ADYKPKELA 73
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPGFRveGKVTFHGKNLyaPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 74 QIMAVLPQKMDqAFTFTVEETVAFGRypfqtglfRQQTEKG--EAIVQEAMEQTGVADFAQKPIRE----LSGGEQQRVY 147
Cdd:PRK14243 91 RRIGMVFQKPN-PFPKSIYDNIAYGA--------RINGYKGdmDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLC 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238244423 148 LAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLaaVSVFHDLNTASLYCDGLMF 210
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSDMTAF 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-198 |
1.00e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.84 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 22 TVEKGEFLGILGPNGSGKTTLLHLL---------TGTLPAKKGRV--YLAGKLLADYKpKELA--QIMAVL-PQKMDQ-- 85
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILsgelipnlgDYEEEPSWDEVlkRFRGTELQNYF-KKLYngEIKVVHkPQYVDLip 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 86 -AFTFTVEEtvafgrypfqtgLFRQQTEKGeaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:PRK13409 174 kVFKGKVRE------------LLKKVDERG--KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....*
gi 1238244423 165 TNFLDLaYQK-DLLDLIKRLTRESglAAVSVFHDL 198
Cdd:PRK13409 240 TSYLDI-RQRlNVARLIRELAEGK--YVLVVEHDL 271
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-229 |
1.41e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 67.17 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHL----LTGTLPAK-KGRVYLAGKLL--ADYKPKELAQIMAVLPQK 82
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrlLELNEEARvEGEVRLFGRNIysPDVDPIEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 83 MDQAFTFTVEETVAFG-RYpfqTGLFRQQTEKGEaIVQEAMEQTGVADFAQKPIRE----LSGGEQQRVYLAQALAQQPR 157
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGvKL---NGLVKSKKELDE-RVEWALKKAALWDEVKDRLNDypsnLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238244423 158 ILFLDEPTNFLDLAYQKDLLDLIKRLTREsgLAAVSVFHDLNTASLYCDGLMFMKNGT---AGPKQK----PEYAVTEQ 229
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKlieVGPTRKvfenPEHELTEK 246
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-296 |
1.57e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 68.39 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 14 RLINNVSLTVEKGEFLGILGPNGSGKTTLlhlltgtlpAK-------------KGRVYLAGKLLADYKPKELAQIM---- 76
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLI---------AKaicgitkdnwhvtADRFRWNGIDLLKLSPRERRKIIgrei 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 77 AVLPQK-----------MDQaftftVEETVAFGRYpfqTGLF--RQQTEKGEAIvqEAMEQTGVADfaQKPIR-----EL 138
Cdd:COG4170 92 AMIFQEpsscldpsakiGDQ-----LIEAIPSWTF---KGKWwqRFKWRKKRAI--ELLHRVGIKD--HKDIMnsyphEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 139 SGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGtagp 218
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCG---- 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238244423 219 kQKPEYAVTEQSIKAVYDTDVTALVHqSSPKpmiviqpekdsvKRQSIPFEALLQAgrddilLQTEIPlrTLSSTPIG 296
Cdd:COG4170 236 -QTVESGPTEQILKSPHHPYTKALLR-SMPD------------FRQPLPHKSRLNT------LPGSIP--PLQHLPIG 291
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-194 |
1.98e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 14 RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLP-AKKGRVYLAGKLLADYKPKE-LAQIMAVLPQK--------- 82
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQaIAQGIAMVPEDrkrdgivpv 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 83 MDQAFTFTVeetVAFGRYpfqTGLFRQQTEKGEAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:PRK13549 356 MGVGKNITL---AALDRF---TGGSRIDDAAELKTILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190
....*....|....*....|....*....|...
gi 1238244423 162 DEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSV 194
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVI 461
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
11-202 |
2.35e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.60 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPkELAQIMAVLPQ----KMDqa 86
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLGHqpgiKTE-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 87 ftFTVEETVAFgrypfqtgLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:PRK13538 89 --LTALENLRF--------YQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1238244423 167 FLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTAS 202
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVAS 194
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
10-214 |
2.57e-12 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 66.75 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLL------------ADykPKELAQIMA 77
Cdd:COG4598 18 FGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgelvpAD--RRQLQRIRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 78 VLpqkmdqAFTF---------TVEETVAFGryPFQT-GLFRQQ-TEKGEAIvqeaMEQTGVADFAQKPIRELSGGEQQRV 146
Cdd:COG4598 96 RL------GMVFqsfnlwshmTVLENVIEA--PVHVlGRPKAEaIERAEAL----LAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238244423 147 YLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQG 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-169 |
3.00e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 68.42 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTllhlltgtlpakkgrvylagklladykpkeLAQIMAvlP 80
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKST------------------------------LFRMIT--G 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QKMDQAFTFTVEETVAFGrYPFQT--GLFRQQT-----EKGEAIVQ----EAMEQTGVADFA------QKPIRELSGGEQ 143
Cdd:TIGR03719 371 QEQPDSGTIEIGETVKLA-YVDQSrdALDPNKTvweeiSGGLDIIKlgkrEIPSRAYVGRFNfkgsdqQKKVGQLSGGER 449
|
170 180
....*....|....*....|....*.
gi 1238244423 144 QRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-185 |
3.08e-12 |
|
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: 68.31 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLI-NNVSLTVEKGEFLGILGPNGSGKTTLlhlltgtlpAK---------KGRVYLAGKLLADYKPKELA 73
Cdd:COG5265 361 ENVSFGYDPERPIlKGVSFEVPAGKTVAIVGPSGAGKSTL---------ARllfrfydvtSGRILIDGQDIRDVTQASLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 74 QIMAVLPQkmDQA-FTFTVEETVAFGRypfqtglfrqqTEKGEAIVQEAMEQTGVADFaqkpIRE--------------- 137
Cdd:COG5265 432 AAIGIVPQ--DTVlFNDTIAYNIAYGR-----------PDASEEEVEAAARAAQIHDF----IESlpdgydtrvgerglk 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1238244423 138 LSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTR 185
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR 542
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-198 |
4.23e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 67.89 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 22 TVEKGEFLGILGPNGSGKTTLLHLL---------TGTLPAKKGRV--YLAGKLLADYKpKELA--QIMAVL-PQKMDQ-- 85
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILsgelkpnlgDYDEEPSWDEVlkRFRGTELQDYF-KKLAngEIKVAHkPQYVDLip 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 86 -AFTFTVEEtvafgrypfqtgLFRQQTEKGeaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:COG1245 174 kVFKGTVRE------------LLEKVDERG--KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....*
gi 1238244423 165 TNFLDLaYQK-DLLDLIKRLTREsGLAAVSVFHDL 198
Cdd:COG1245 240 SSYLDI-YQRlNVARLIRELAEE-GKYVLVVEHDL 272
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-277 |
4.49e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI-MAVL 79
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 80 PQKMDQAFTFTVEETVAFGRYPFQT--GLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPR 157
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKKvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 158 ILFLDEPTNFLDLAyQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTagpkqkpeyAVTEQSIKAVYDT 237
Cdd:PRK09700 166 VIIMDEPTSSLTNK-EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGS---------SVCSGMVSDVSND 235
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1238244423 238 D-VTALVHQSSPKPMIVIQPEKDSVKRQSIpFEALLQAGRD 277
Cdd:PRK09700 236 DiVRLMVGRELQNRFNAMKENVSNLAHETV-FEVRNVTSRD 275
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-196 |
4.72e-12 |
|
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: 67.91 E-value: 4.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLL--TGTLPAKKGRVY----LAGKLLADYKPKELAQ 74
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvaLCEKCGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 75 IMAVLPQKM----------DQAFTFTVEETVA------FGRYPFQTGL------FRQQTEKGEAIVQEA---MEQTGVAD 129
Cdd:TIGR03269 81 PCPVCGGTLepeevdfwnlSDKLRRRIRKRIAimlqrtFALYGDDTVLdnvleaLEEIGYEGKEAVGRAvdlIEMVQLSH 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 130 FAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFH 196
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-181 |
5.63e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 66.41 E-value: 5.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLaGKLLADYKPKELAQIMAVLPQKMD----------- 84
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV-GDIYIGDKKNNHELITNPYSKKIKnfkelrrrvsm 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 85 -------QAFTFTVEETVAFGryPFQTGLFRQQTEKGEAIVQEAMeqtGV-ADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:PRK13631 121 vfqfpeyQLFKDTIEKDIMFG--PVALGVKKSEAKKLAKFYLNKM---GLdDSYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180
....*....|....*....|....*
gi 1238244423 157 RILFLDEPTNFLDLAYQKDLLDLIK 181
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLIL 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-192 |
5.75e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.36 E-value: 5.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 2 KAEGLS--GGYGDSRLiNNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI-MAV 78
Cdd:COG3845 259 EVENLSvrDDRGVPAL-KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 LP---QKMDQAFTFTVEETVAFGRY---PFQTGLFRQQtEKGEAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQA 151
Cdd:COG3845 338 IPedrLGRGLVPDMSVAENLILGRYrrpPFSRGGFLDR-KAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILARE 416
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1238244423 152 LAQQPRILFLDEPTNFLDLA-----YQKdLLDLikrltRESGlAAV 192
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGaiefiHQR-LLEL-----RDAG-AAV 455
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
137-246 |
9.97e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 65.98 E-value: 9.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 137 ELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG-- 214
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGqt 237
|
90 100 110
....*....|....*....|....*....|....*..
gi 1238244423 215 --TAGPKQ---KPEYAVTEQSIKAVYDTDvTALVHQS 246
Cdd:PRK15093 238 veTAPSKElvtTPHHPYTQALIRAIPDFG-SAMPHKS 273
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
11-200 |
1.18e-11 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 66.66 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 11 GDSR-LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQkmdQAFTF 89
Cdd:TIGR02203 342 GRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQ---DVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 90 --TVEETVAFGRypfqtglfrqQTEKGEAIVQEAMEQTGVADFA-------QKPIRE----LSGGEQQRVYLAQALAQQP 156
Cdd:TIGR02203 419 ndTIANNIAYGR----------TEQADRAEIERALAAAYAQDFVdklplglDTPIGEngvlLSGGQRQRLAIARALLKDA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1238244423 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTResGLAAVSVFHDLNT 200
Cdd:TIGR02203 489 PILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLST 530
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-198 |
1.25e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.79 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI---MAVLPQ 81
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVrkrMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 KmDQAFT-FTVEETVAfgrYPfqtglFRQQTEKGEAIVQEA----MEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:PRK11831 92 S-GALFTdMNVFDNVA---YP-----LREHTQLPAPLLHSTvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1238244423 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDL 198
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDV 204
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
9-202 |
1.79e-11 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 66.30 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 9 GYGdSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKmDQAFT 88
Cdd:TIGR01193 484 GYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQE-PYIFS 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 89 FTVEETVAFGRYPfqtGLFRQQTEKGEAIVQ-----EAMEQTGVADFAQKPiRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:TIGR01193 562 GSILENLLLGAKE---NVSQDEIWAACEIAEikddiENMPLGYQTELSEEG-SSISGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190
....*....|....*....|....*....|....*....
gi 1238244423 164 PTNFLDLAYQKDLLDLIKRLTRESglaAVSVFHDLNTAS 202
Cdd:TIGR01193 638 STSNLDTITEKKIVNNLLNLQDKT---IIFVAHRLSVAK 673
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1-214 |
2.11e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 63.20 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGD--SRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAV 78
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 LPQKmDQAFTFTVEETV-AFGRYpfqtglfrqqtekGEAIVQEAMEQTGVADfaqkpirELSGGEQQRVYLAQALAQQPR 157
Cdd:cd03369 87 IPQD-PTLFSGTIRSNLdPFDEY-------------SDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1238244423 158 ILFLDEPTNFLDlaYQKDLldLIKRLTRE--SGLAAVSVFHDLNTAsLYCDGLMFMKNG 214
Cdd:cd03369 146 VLVLDEATASID--YATDA--LIQKTIREefTNSTILTIAHRLRTI-IDYDKILVMDAG 199
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
9-197 |
2.22e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.90 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 9 GYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAvlpqkmdQAFT 88
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRR-------EHFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 89 FTveetvaFGRYPFQTGLFRQQ------------TEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:PRK10535 90 FI------FQRYHLLSHLTAAQnvevpavyagleRKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1238244423 157 RILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHD 197
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHD 203
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-215 |
2.87e-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: 62.90 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKmdqAFTFtvEETV 95
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQD---PVLF--SGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 96 AFGRYPFQtglfrqqtEKGEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:cd03244 95 RSNLDPFG--------EYSDEELWQALERVGLKEFVESlpggldtVVEEggenLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1238244423 165 TNFLDlaYQKDllDLIKRLTRESgLAAVSVF---HDLNTAsLYCDGLMFMKNGT 215
Cdd:cd03244 167 TASVD--PETD--ALIQKTIREA-FKDCTVLtiaHRLDTI-IDSDRILVLDKGR 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-211 |
2.87e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.53 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLAdykPKELAQIMAVlpQK 82
Cdd:NF033858 269 ARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDIATRRRV--GY 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 83 MDQAFTFTVEETV-------AfgRypfqtgLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQ 155
Cdd:NF033858 344 MSQAFSLYGELTVrqnlelhA--R------LFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHK 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1238244423 156 PRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGlaaVSVF---HDLNTAsLYCDGLMFM 211
Cdd:NF033858 416 PELLILDEPTSGVDPVARDMFWRLLIELSREDG---VTIFistHFMNEA-ERCDRISLM 470
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-234 |
4.08e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.19 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVY-----LAGKLLADYKPK-ELAQ 74
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIFNYRDVlEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 75 IMAVLPQKMDqAFTFTVEETVAFGRYPFQtgLFRQQTEKGeaIVQEAMEQTGVAD-----FAQKPIReLSGGEQQRVYLA 149
Cdd:PRK14271 102 RVGMLFQRPN-PFPMSIMDNVLAGVRAHK--LVPRKEFRG--VAQARLTEVGLWDavkdrLSDSPFR-LSGGQQQLLCLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 150 QALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsgLAAVSVFHDL-------NTASLYCDGLMFMKNGTAGPKQKP 222
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLaqaarisDRAALFFDGRLVEEGPTEQLFSSP 253
|
250
....*....|..
gi 1238244423 223 EYAVTEQSIKAV 234
Cdd:PRK14271 254 KHAETARYVAGL 265
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-214 |
4.87e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.55 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE-LAQIMAVLPQKM 83
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 84 DQAFTFTVEETVAFGRYPFQTGLFRQQTEKGEAivQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PRK11288 89 HLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEA--REQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1238244423 164 PTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-196 |
5.06e-11 |
|
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: 61.02 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYlagklladyKPkELAQIMaVLPQK--MDQAftfTVE 92
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG---------MP-EGEDLL-FLPQRpyLPLG---TLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 93 ETVAfgrYPFQtglfrqqtekgeaivqeameqtgvadfaqkpiRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAY 172
Cdd:cd03223 82 EQLI---YPWD--------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180
....*....|....*....|....
gi 1238244423 173 QKDLLDLIKrltrESGLAAVSVFH 196
Cdd:cd03223 127 EDRLYQLLK----ELGITVISVGH 146
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-231 |
1.32e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGygdsRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE-LAQIMAVL 79
Cdd:PRK11288 258 LRLDGLKGP----GLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaIRAGIMLC 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 80 PQ--KMDQAF-TFTVEETVAFG--RYPFQTGLF---RQQTEKGEAIVQEAMEQTGVADfaqKPIRELSGGEQQRVYLAQA 151
Cdd:PRK11288 334 PEdrKAEGIIpVHSVADNINISarRHHLRAGCLinnRWEAENADRFIRSLNIKTPSRE---QLIMNLSGGNQQKAILGRW 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTrESGLAAVSVFHDLNTASLYCDGLMFMKNG-TAGPKQKPEyaVTEQS 230
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGrIAGELAREQ--ATERQ 487
|
.
gi 1238244423 231 I 231
Cdd:PRK11288 488 A 488
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-169 |
3.54e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYkpkeLAQIMAVL-PQ 81
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAY----FDQHRAELdPE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 KmdqaftfTVEETVAFGRypfqtglfrqqtekgeaivQEAMeQTGVA--------DF------AQKPIRELSGGEQQRVY 147
Cdd:PRK11147 398 K-------TVMDNLAEGK-------------------QEVM-VNGRPrhvlgylqDFlfhpkrAMTPVKALSGGERNRLL 450
|
170 180
....*....|....*....|..
gi 1238244423 148 LAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLD 472
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-198 |
4.06e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.50 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGY-GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE---LAQIM 76
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 77 AVLPQKMDQAFTFTVEETVAFgryPFQTGlfrqqTEKGEAI---VQEAMEQTGVADFAQK-PIrELSGGEQQRVYLAQAL 152
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAI---PLIIA-----GASGDDIrrrVSAALDKVGLLDKAKNfPI-QLSGGEQQRVGIARAV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1238244423 153 AQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTReSGLAAVSVFHDL 198
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDI 197
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-213 |
4.71e-10 |
|
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: 61.95 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLaDYKPKELAQIMAVLPQKMDQAFTFTVEETV 95
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 96 AFgrYPFQTGlfrQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKD 175
Cdd:TIGR01257 1025 LF--YAQLKG---RSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1238244423 176 LLDLIkrLTRESGLAAVSVFHDLNTAS-------------LYCDGL-MFMKN 213
Cdd:TIGR01257 1100 IWDLL--LKYRSGRTIIMSTHHMDEADllgdriaiisqgrLYCSGTpLFLKN 1149
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-169 |
7.27e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 6 LSGGY---GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLladykpkelaqIMAVLPQK 82
Cdd:PRK11147 6 IHGAWlsfSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDL-----------IVARLQQD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 83 MDQAFTFTVEETVAFG---------RYpfQTGLFRQQTEKGE------AIVQEAMEQTGVADF--------------AQK 133
Cdd:PRK11147 75 PPRNVEGTVYDFVAEGieeqaeylkRY--HDISHLVETDPSEknlnelAKLQEQLDHHNLWQLenrinevlaqlgldPDA 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 1238244423 134 PIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK11147 153 ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-184 |
1.03e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.42 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKMdQAFTFTVEETV 95
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNV-HLFNDTIANNI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 96 AFGRYPFQTglfRQQTEKGeAIVQEAMeqtgvaDFAQK-------PIRE----LSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:PRK11176 438 AYARTEQYS---REQIEEA-ARMAYAM------DFINKmdngldtVIGEngvlLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180
....*....|....*....|....
gi 1238244423 165 TNFLD----LAYQKDLLDLIKRLT 184
Cdd:PRK11176 508 TSALDteseRAIQAALDELQKNRT 531
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-215 |
1.05e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 58.11 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI----MAVLPQKmDQAFTFTV 91
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQK-PWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 92 EETVAFGRyPFQTGLFRQQTEKGEaiVQEAMEQTGVADfaQKPIRE----LSGGEQQRVYLAQALAQQPRILFLDEPTNF 167
Cdd:cd03290 96 EENITFGS-PFNKQRYKAVTDACS--LQPDIDLLPFGD--QTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1238244423 168 LDLAYQKDLLDL-IKRLTRESGLAAVSVFHDLNTASlYCDGLMFMKNGT 215
Cdd:cd03290 171 LDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLP-HADWIIAMKDGS 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-215 |
1.44e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.17 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 17 NNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKKGRVYLAGK---LLadykpkELAqiMAVLPQkmdqaftFTVEE 93
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKstllkliagilEPTSGRVEVNGRvsaLL------ELG--AGFHPE-------LTGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 94 TVAF-GRYpfqTGLFRQQTekgEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAY 172
Cdd:COG1134 108 NIYLnGRL---LGLSRKEI---DEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAF 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1238244423 173 QKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:COG1134 182 QKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-169 |
1.45e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLlhlltgtlpakkgrvylagklladYKpkelaqiMAVLPQK 82
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTL------------------------FK-------MITGQEQ 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 83 MDQAfTFTVEETVAFGrYPFQT--GLFRQQT-----EKGEAIVQ----EAMEQTGVADFA------QKPIRELSGGEQQR 145
Cdd:PRK11819 376 PDSG-TIKIGETVKLA-YVDQSrdALDPNKTvweeiSGGLDIIKvgnrEIPSRAYVGRFNfkggdqQKKVGVLSGGERNR 453
|
170 180
....*....|....*....|....
gi 1238244423 146 VYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-248 |
1.46e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKmdqafTFTVEET 94
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQS-----PVLFSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 95 VAFGRYPFqtglfrqqTEKGEAIVQEAMEQTGVAD-FAQKPI----------RELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PLN03232 1326 VRFNIDPF--------SEHNDADLWEALERAHIKDvIDRNPFgldaevseggENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 164 PTNFLDLAYQKdlldLIKRLTRES--GLAAVSVFHDLNTAsLYCDGLMFMKNGTAGPKQKPEYAVTEQSikavydTDVTA 241
Cdd:PLN03232 1398 ATASVDVRTDS----LIQRTIREEfkSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSRDT------SAFFR 1466
|
....*..
gi 1238244423 242 LVHQSSP 248
Cdd:PLN03232 1467 MVHSTGP 1473
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-197 |
1.60e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.80 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGK-------------LLADY 67
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGiklgyfaqhqlefLRADE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 68 KPkeLAQIMAVLPQKMDQAFTFTVeetvafGRYPFQtglfrqqtekgeaivqeameqtgvADFAQKPIRELSGGEQQRVY 147
Cdd:PRK10636 393 SP--LQHLARLAPQELEQKLRDYL------GGFGFQ------------------------GDKVTEETRRFSGGEKARLV 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1238244423 148 LAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIkrLTRESGLAAVSvfHD 197
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL--IDFEGALVVVS--HD 486
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-215 |
2.56e-09 |
|
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: 59.64 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 13 SRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADyKPKELAQIMAVLPQkmdqaftFTVE 92
Cdd:TIGR01257 1952 SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQ-------FDAI 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 93 ETVAFGR-----YPFQTGLFRQQTEKgeaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNF 167
Cdd:TIGR01257 2024 DDLLTGRehlylYARLRGVPAEEIEK---VANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1238244423 168 LDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:TIGR01257 2101 MDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
11-164 |
3.38e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 57.00 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLlhlltgtlpAK-----------KGRVYLAGKLLADYKPKELAQ----- 74
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTL---------AKvlmghpkyevtSGSILLDGEDILELSPDERARagifl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 75 --------------------IMAVLPQKMDqAFTFtveetvafgrypfqtglfrqqtekgEAIVQEAMEQTGV-ADFAQK 133
Cdd:COG0396 82 afqypveipgvsvsnflrtaLNARRGEELS-AREF-------------------------LKLLKEKMKELGLdEDFLDR 135
|
170 180 190
....*....|....*....|....*....|..
gi 1238244423 134 PIRE-LSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:COG0396 136 YVNEgFSGGEKKRNEILQMLLLEPKLAILDET 167
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-169 |
3.92e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.74 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHlltgtlpAKKGRVY---LAGKLLA-DYKP-KELAQIMAVLPQKMDQAFTF 89
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLN-------ALAGRIQgnnFTGTILAnNRKPtKQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 90 TVEETVAFG---RYPfqTGLFRQ-QTEKGEAIVQE-AMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:PLN03211 156 TVRETLVFCsllRLP--KSLTKQeKILVAESVISElGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
....*
gi 1238244423 165 TNFLD 169
Cdd:PLN03211 234 TSGLD 238
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
11-214 |
4.51e-09 |
|
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: 55.71 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTgtlpAKKGRVYLAGKLLADYKPKelaqimavlpqkmdqaftft 90
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA----GRKTAGVITGEILINGRPL-------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 91 veeTVAFGRYpfqTGLFRQQ-TEKGEAIVQEAMEqtgvadFAQKpIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:cd03232 74 ---DKNFQRS---TGYVEQQdVHSPNLTVREALR------FSAL-LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1238244423 170 LAYQKDLLDLIKRLTrESGLAAVSVFHDLNTASL-YCDGLMFMKNG 214
Cdd:cd03232 141 SQAAYNIVRFLKKLA-DSGQAILCTIHQPSASIFeKFDRLLLLKRG 185
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-169 |
4.80e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 58.32 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKkGRVYLAGKLLADYKPKELAQIMAVLPQKmDQAFTFTV 91
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKHLSWVGQN-PQLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 92 EETVAFGRypfqtglfrqqTEKGEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLAQALAQQPRILF 160
Cdd:PRK11174 440 RDNVLLGN-----------PDASDEQLQQALENAWVSEFLPLlpqgldtPIGDqaagLSVGQAQRLALARALLQPCQLLL 508
|
....*....
gi 1238244423 161 LDEPTNFLD 169
Cdd:PRK11174 509 LDEPTASLD 517
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-198 |
5.17e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.10 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQKMDQAFTFTV 91
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNNTDMLSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 92 EETvaFGRYPFQTglfRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLA 171
Cdd:PRK10938 95 EDD--TGRTTAEI---IQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190
....*....|....*....|....*....|
gi 1238244423 172 YQKDLLDLIKRLTREsGLAAVSV---FHDL 198
Cdd:PRK10938 170 SRQQLAELLASLHQS-GITLVLVlnrFDEI 198
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-216 |
6.55e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.16 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE--LA---QIMAVLPQkMdq 85
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADrdIAmvfQNYALYPH-M-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 86 aftfTVEETVAFGrypfqtgLFRQQTEKGE--AIVQEAMEQTGVADFAQ-KPiRELSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:PRK11650 92 ----SVRENMAYG-------LKIRGMPKAEieERVAEAARILELEPLLDrKP-RELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1238244423 163 EPTNFLD--LAYQKDLldLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNGTA 216
Cdd:PRK11650 160 EPLSNLDakLRVQMRL--EIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-164 |
7.55e-09 |
|
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: 55.55 E-value: 7.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 7 SGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKlladykpkelaqiMAVLPQkmdQA 86
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-------------IAYVSQ---EP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 87 FTF--TVEETVAFGrYPFQTGLFRQ------------------QTEKGEaivqeameqTGVAdfaqkpireLSGGEQQRV 146
Cdd:cd03250 76 WIQngTIRENILFG-KPFDEERYEKvikacalepdleilpdgdLTEIGE---------KGIN---------LSGGQKQRI 136
|
170
....*....|....*...
gi 1238244423 147 YLAQALAQQPRILFLDEP 164
Cdd:cd03250 137 SLARAVYSDADIYLLDDP 154
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-169 |
8.86e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.42 E-value: 8.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLI-NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQK 82
Cdd:PRK10790 344 DNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQD 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 83 -MDQAFTFTVeeTVAFGRypfqtglfrqqtEKGEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLAQ 150
Cdd:PRK10790 424 pVVLADTFLA--NVTLGR------------DISEEQVWQALETVQLAELARSlpdglytPLGEqgnnLSVGQKQLLALAR 489
|
170
....*....|....*....
gi 1238244423 151 ALAQQPRILFLDEPTNFLD 169
Cdd:PRK10790 490 VLVQTPQILILDEATANID 508
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1-220 |
9.96e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.50 E-value: 9.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLinNVSL-TVEKGEFLGILGPNGSGKTTLLHLltgtlpakkgrvyLAGKLLADYKPKELAQI-MAV 78
Cdd:cd03222 1 QLYPDCVKRYGVFFL--LVELgVVKEGEVIGIVGPNGTGKTTAVKI-------------LAGQLIPNGDNDEWDGItPVY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 LPQKMDqaftftveetvafgrypfqtglfrqqtekgeaivqeameqtgvadfaqkpireLSGGEQQRVYLAQALAQQPRI 158
Cdd:cd03222 66 KPQYID-----------------------------------------------------LSGGELQRVAIAAALLRNATF 92
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 159 LFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFM-----KNGTAGPKQ 220
Cdd:cd03222 93 YLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFegepgVYGIASQPK 159
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-198 |
1.06e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGK---LLADYKPKELAQIMAVLPQkmDQAFTFTVE 92
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQ--DPYASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 93 ETVAFG-RYPFQT-GLFrqQTEKGEAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK10261 418 QTVGDSiMEPLRVhGLL--PGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180
....*....|....*....|....*....
gi 1238244423 170 LAYQKDLLDLIKRLTRESGLAAVSVFHDL 198
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDM 524
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1-186 |
1.18e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.67 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKElAQIMAVLP 80
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRRALR-RTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QKMDQAFTFTVEETVafgrypFQTGLFRQQTEK-GEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:NF000106 93 VR*GRRESFSGRENL------YMIGR*LDLSRKdARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180
....*....|....*....|....*..
gi 1238244423 160 FLDEPTNFLDLAYQKDLLDLIKRLTRE 186
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRD 193
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-169 |
1.53e-08 |
|
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: 56.87 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 5 GLSGGYGDSRLI-NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE------------ 71
Cdd:TIGR03719 9 RVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEpqldptktvren 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 72 ----LAQIMAVLpQKMDQAFTFTVEETVAFgrypfqTGLFRQQTEkgeaiVQEAMEQTGVADFAQK-------------- 133
Cdd:TIGR03719 89 veegVAEIKDAL-DRFNEISAKYAEPDADF------DKLAAEQAE-----LQEIIDAADAWDLDSQleiamdalrcppwd 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1238244423 134 -PIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:TIGR03719 157 aDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-207 |
1.96e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 56.68 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVylagklladYKPKElaQIMAVLPQK--MDQAftfTVE 92
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL---------TKPAK--GKLFYVPQRpyMTLG---TLR 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 93 ETVAfgrYP------FQTGLFRQQTEKG------EAIVQEAMEQTGVADFAQkpirELSGGEQQRVYLAQALAQQPRILF 160
Cdd:TIGR00954 533 DQII---YPdssedmKRRGLSDKDLEQIldnvqlTHILEREGGWSAVQDWMD----VLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1238244423 161 LDEPTNfldlAYQKDLLDLIKRLTRESGLAAVSVFH-----DLNTASLYCDG 207
Cdd:TIGR00954 606 LDECTS----AVSVDVEGYMYRLCREFGITLFSVSHrkslwKYHEYLLYMDG 653
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-214 |
2.27e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.80 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLA----DYKPKELAQIM-----AVLP-QKMDQ 85
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySYRSQRIRMIFqdpstSLNPrQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 86 AFTFTVEetvafgrypFQTGLFRQQTEKgeAIVQeAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:PRK15112 109 ILDFPLR---------LNTDLEPEQREK--QIIE-TLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1238244423 165 TNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-165 |
3.46e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGtlpAKK---GRVYLAGKLLADYKPKElaqimAVLP 80
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG---ARKiqqGRVEVLGGDMADARHRR-----AVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 Q--KMDQAF------TFTVEETVAF-GRypfqtgLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQA 151
Cdd:NF033858 77 RiaYMPQGLgknlypTLSVFENLDFfGR------LFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCA 150
|
170
....*....|....
gi 1238244423 152 LAQQPRILFLDEPT 165
Cdd:NF033858 151 LIHDPDLLILDEPT 164
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-174 |
3.98e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 55 GRVYLAGKLLADYKPKELAQIMAVLPQKmDQAFTFTVEETVAFGRypfqTGLFRQQTEKGE--AIVQEAMEQ------TG 126
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQE-PMLFNMSIYENIKFGK----EDATREDVKRACkfAAIDEFIESlpnkydTN 1351
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1238244423 127 VADFAqkpiRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQK 174
Cdd:PTZ00265 1352 VGPYG----KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1395
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-186 |
4.02e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKElaqimavlpqKMDQAFTFTVEETV 95
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANE----------AINHGFALVTEERR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 96 AFGRYPF-----------------QTGLFrqQTEKGEAIVQEAMEQTGVADFAQK-PIRELSGGEQQRVYLAQALAQQPR 157
Cdd:PRK10982 334 STGIYAYldigfnslisnirnyknKVGLL--DNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPE 411
|
170 180
....*....|....*....|....*....
gi 1238244423 158 ILFLDEPTNFLDLAYQKDLLDLIKRLTRE 186
Cdd:PRK10982 412 ILMLDEPTRGIDVGAKFEIYQLIAELAKK 440
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
138-214 |
6.51e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.11 E-value: 6.51e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 138 LSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQG 205
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-169 |
8.92e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 8.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKK-------GRVYLAGKLLADYKPKelaqIMAVLPQ- 81
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYsndltlfGRRRGSGETIWDIKKH----IGYVSSSl 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 82 KMDQAFTFTVEETVAFGrYPFQTGLFRQQTEKGEAIVQEAMEQTGVAD-FAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:PRK10938 346 HLDYRVSTSVRNVILSG-FFDSIGIYQAVSDRQQKLAQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPTLLI 424
|
....*....
gi 1238244423 161 LDEPTNFLD 169
Cdd:PRK10938 425 LDEPLQGLD 433
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-192 |
1.15e-07 |
|
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: 51.88 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPakkGRVYLAGKLLAD-YKPKELAQIM---AVLPQKMDQAF-TF 89
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---GNVSVEGDIHYNgIPYKEFAEKYpgeIIYVSEEDVHFpTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 90 TVEETVAFGRypfqtglfrqqTEKGEAIVqeameqtgvadfaqkpiRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:cd03233 99 TVRETLDFAL-----------RCKGNEFV-----------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180
....*....|....*....|...
gi 1238244423 170 LAYQKDLLDLIKRLTRESGLAAV 192
Cdd:cd03233 151 SSTALEILKCIRTMADVLKTTTF 173
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
134-169 |
1.19e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 1.19e-07
10 20 30
....*....|....*....|....*....|....*.
gi 1238244423 134 PIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK11819 160 KVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-171 |
1.22e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 53.81 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQkmdQAFTF- 89
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQ---DAGLFn 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 90 -TVEETVAFGRypfqtglfrqqTEKGEAIVQEAMEQTGVADF-AQKPI----------RELSGGEQQRVYLAQALAQQPR 157
Cdd:PRK13657 423 rSIEDNIRVGR-----------PDATDEEMRAAAERAQAHDFiERKPDgydtvvgergRQLSGGERQRLAIARALLKDPP 491
|
170
....*....|....
gi 1238244423 158 ILFLDEPTNFLDLA 171
Cdd:PRK13657 492 ILILDEATSALDVE 505
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-196 |
3.59e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 50.73 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLlhlltgtlpakkgrvylaGKLLADYKPKELAQIMAVLP 80
Cdd:COG2401 31 LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTL------------------LRLLAGALKGTPVAGCVDVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QKmdqafTFTVEETV--AFGRypfqtglfrqQTEKGEAIvqEAMEQTGVAD--FAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:COG2401 93 DN-----QFGREASLidAIGR----------KGDFKDAV--ELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1238244423 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFH 196
Cdd:COG2401 156 KLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-178 |
3.79e-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: 51.40 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLlaDYKPkelaQIMAVLPQkmdqaftfTVEET 94
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRI--SFSS----QFSWIMPG--------TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 95 VAFG------RYpfqtglfrqqtekgEAIVQEAMEQTGVADFAQK---PIRE----LSGGEQQRVYLAQALAQQPRILFL 161
Cdd:cd03291 118 IIFGvsydeyRY--------------KSVVKACQLEEDITKFPEKdntVLGEggitLSGGQRARISLARAVYKDADLYLL 183
|
170
....*....|....*..
gi 1238244423 162 DEPTNFLDLAYQKDLLD 178
Cdd:cd03291 184 DSPFGYLDVFTEKEIFE 200
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-214 |
4.36e-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: 52.61 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLlaDYKPkelaQIMAVLPQkmdqaftfTVEET 94
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRI--SFSP----QTSWIMPG--------TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 95 VAFG------RYpfqtglfrqqtekgEAIVQEAMEQTGVADFAQK---PIRE----LSGGEQQRVYLAQALAQQPRILFL 161
Cdd:TIGR01271 507 IIFGlsydeyRY--------------TSVIKACQLEEDIALFPEKdktVLGEggitLSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1238244423 162 DEPTNFLDLAYQKDLLD--LIKRLTRESGLAAVSVFHDLNTAslycDGLMFMKNG 214
Cdd:TIGR01271 573 DSPFTHLDVVTEKEIFEscLCKLMSNKTRILVTSKLEHLKKA----DKILLLHEG 623
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-199 |
4.86e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.71 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 17 NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK--KGRVYLAGKLLA--DYKPKELAQI------MAVLPQkmdqa 86
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRfkDIRDSEALGIviihqeLALIPY----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 87 ftFTVEETVAFGRYPFQTGLF-RQQTEKgEAivQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPT 165
Cdd:NF040905 93 --LSIAENIFLGNERAKRGVIdWNETNR-RA--RELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190
....*....|....*....|....*....|....
gi 1238244423 166 NFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLN 199
Cdd:NF040905 168 AALNEEDSAALLDLLLEL-KAQGITSIIISHKLN 200
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-200 |
7.49e-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: 51.87 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQkmdqaftftveET 94
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQ-----------DP 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 95 VAF-GRYPFQTGLFRQQTEKGeaiVQEAMEQTGVADF-AQKPIR----------ELSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:TIGR00957 1370 VLFsGSLRMNLDPFSQYSDEE---VWWALELAHLKTFvSALPDKldhecaeggeNLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1238244423 163 EPTNFLDLayQKDllDLIKRLTRES--GLAAVSVFHDLNT 200
Cdd:TIGR00957 1447 EATAAVDL--ETD--NLIQSTIRTQfeDCTVLTIAHRLNT 1482
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-205 |
9.74e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.04 E-value: 9.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKlladykpKELAQIMAVLPQKMdqaftfTVEETV 95
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-------AALIAISSGLNGQL------TGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 96 AFgrypfqTGLFRQQT-EKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQK 174
Cdd:PRK13545 107 EL------KGLMMGLTkEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180 190
....*....|....*....|....*....|.
gi 1238244423 175 DLLDLIKRLtRESGLAAVSVFHDLNTASLYC 205
Cdd:PRK13545 181 KCLDKMNEF-KEQGKTIFFISHSLSQVKSFC 210
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
12-170 |
1.58e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.02 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK--KGRVYLAGKLLADYKPKELAQimavlpQKMDQAFTF 89
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLELSPEDRAG------EGIFMAFQY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 90 TVEETVAFGRYPFQTGLFRQQTEKGeaivQEAMEQTGVADFAQKPIREL---------------SGGEQQRVYLAQALAQ 154
Cdd:PRK09580 87 PVEIPGVSNQFFLQTALNAVRSYRG----QEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVL 162
|
170
....*....|....*.
gi 1238244423 155 QPRILFLDEPTNFLDL 170
Cdd:PRK09580 163 EPELCILDESDSGLDI 178
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-214 |
1.76e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE-LAQIMAVLPQKMDQAFTFTVEET 94
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 95 VAFGRYPfqtglfrqqtEKGEAIVQEAMEQTGVADFAQKPIR--------ELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:PRK10982 94 MWLGRYP----------TKGMFVDQDKMYRDTKAIFDELDIDidprakvaTLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1238244423 167 FLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
138-220 |
2.88e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.32 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 138 LSGGEQQRVYLAQALAQQP-RILF-LDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASlYCDGLMFMkngt 215
Cdd:cd03238 88 LSGGELQRVKLASELFSEPpGTLFiLDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLS-SADWIIDF---- 161
|
....*
gi 1238244423 216 aGPKQ 220
Cdd:cd03238 162 -GPGS 165
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-178 |
3.51e-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: 49.56 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLladykpkelaqimAVLPQkmdQAF--T 88
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV-------------AYVPQ---QAWiqN 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 89 FTVEETVAFGRyPFQTGLFRQQTEKGEAIVQEAMEQTG-VADFAQKPIrELSGGEQQRVYLAQALAQQPRILFLDEPTNF 167
Cdd:TIGR00957 713 DSLRENILFGK-ALNEKYYQQVLEACALLPDLEILPSGdRTEIGEKGV-NLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170
....*....|.
gi 1238244423 168 LDLAYQKDLLD 178
Cdd:TIGR00957 791 VDAHVGKHIFE 801
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
16-214 |
4.04e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE--------LAQIMAVLPQkmdqaf 87
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsqeagigiIHQELNLIPQ------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 88 tFTVEETVAFGRyPFQTGLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNF 167
Cdd:PRK10762 94 -LTIAENIFLGR-EFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1238244423 168 LDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK10762 172 LTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-215 |
1.05e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.74 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQI-MAVL 79
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 80 PQkmdQAFTF---TVEETVAFGrypfqtglfRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:PRK15439 92 PQ---EPLLFpnlSVKENILFG---------LPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1238244423 157 RILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNGT 215
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGT 217
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-170 |
1.12e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.38 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKllaDYKPKELAQIMAVLP 80
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRGDRSRFMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 81 QKMDQAFTFTVEETVAF-----GRYPfqtglfRQQTEKGEAIVqeameqtGVADFAQKPIRELSGGEQQRVYLAQALAQQ 155
Cdd:PRK13543 89 HLPGLKADLSTLENLHFlcglhGRRA------KQMPGSALAIV-------GLAGYEDTLVRQLSAGQKKRLALARLWLSP 155
|
170
....*....|....*
gi 1238244423 156 PRILFLDEPTNFLDL 170
Cdd:PRK13543 156 APLWLLDEPYANLDL 170
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-163 |
1.43e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.40 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQkMDQAFTFTVEETV 95
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ-TPFLFSDTVANNI 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238244423 96 AFGRyPFQTglfRQQTEKGE--AIVQEAM------EQTGVADFAQKpireLSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PRK10789 410 ALGR-PDAT---QQEIEHVArlASVHDDIlrlpqgYDTEVGERGVM----LSGGQKQRISIARALLLNAEILILDD 477
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
132-170 |
1.63e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 1.63e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1238244423 132 QKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDL 170
Cdd:PRK10636 144 ERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL 182
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
128-170 |
2.06e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 2.06e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1238244423 128 ADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDL 170
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
7-218 |
2.06e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 7 SGGY-GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLadykpkelaqiMAVLPQKMDQ 85
Cdd:PLN03073 515 SFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVR-----------MAVFSQHHVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 86 AFTFTVEETVAFGR-YPfqtGLFRQQtekgeaiVQEAMEQTGVA-DFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PLN03073 584 GLDLSSNPLLYMMRcFP---GVPEQK-------LRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDE 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 164 PTNFLDLayqkDLLD-LIKRLTR-ESGLAAVSvfHDLNTASLYCDGLMFMKNGTAGP 218
Cdd:PLN03073 654 PSNHLDL----DAVEaLIQGLVLfQGGVLMVS--HDEHLISGSVDELWVVSEGKVTP 704
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-215 |
2.25e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.50 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRL-INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKE-LAQIMAVlpqkmdqaF 87
Cdd:PRK10522 332 YQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyRKLFSAV--------F 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 88 T-FtveetvafgrYPFQTGLFRQQTEKGEAIVQEAMEQTGVAD---FAQKPIR--ELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:PRK10522 404 TdF----------HLFDQLLGPEGKPANPALVEKWLERLKMAHkleLEDGRISnlKLSKGQKKRLALLLALAEERDILLL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 162 DE------PTnFLDLAYQKdLLDLIkrltRESGLAAVSVFHDlNTASLYCDGLMFMKNGT 215
Cdd:PRK10522 474 DEwaadqdPH-FRREFYQV-LLPLL----QEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
129-169 |
2.53e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 2.53e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1238244423 129 DFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK15064 147 EQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-173 |
2.60e-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: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGY--GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLpAKKGRVYLAGKLLADYKPKELAQIMAV 78
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 79 LPQKMdqaFTFtveetvafgrypfqTGLFRQQTEKGEAIVQEAM----EQTGVAD-FAQKPIR----------ELSGGEQ 143
Cdd:TIGR01271 1297 IPQKV---FIF--------------SGTFRKNLDPYEQWSDEEIwkvaEEVGLKSvIEQFPDKldfvlvdggyVLSNGHK 1359
|
170 180 190
....*....|....*....|....*....|.
gi 1238244423 144 QRVYLAQALAQQPRILFLDEPTNFLD-LAYQ 173
Cdd:TIGR01271 1360 QLMCLARSILSKAKILLLDEPSAHLDpVTLQ 1390
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
134-198 |
6.18e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.53 E-value: 6.18e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238244423 134 PIRELSGGEQQRVYLAQALAQQPR---ILFLDEPTNFLDLAYQKDLLDLIKRLTrESGLAAVSVFHDL 198
Cdd:cd03271 166 PATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLV-DKGNTVVVIEHNL 232
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-170 |
9.57e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.86 E-value: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKtTLLHLLTGTLPAKK---GRVYLAGKLLADYKPKELAQIMA 77
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGK-STLSKVIAGHPAYKileGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 78 VLpqkmdqAFTFTVE----ETVAFGRYPFQTGL-FRQQTEKG-----EAIVQE----AMEQTgvadFAQKPIRE-LSGGE 142
Cdd:CHL00131 87 FL------AFQYPIEipgvSNADFLRLAYNSKRkFQGLPELDpleflEIINEKlklvGMDPS----FLSRNVNEgFSGGE 156
|
170 180
....*....|....*....|....*...
gi 1238244423 143 QQRVYLAQALAQQPRILFLDEPTNFLDL 170
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDI 184
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
135-188 |
1.47e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 1.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 135 IRELSGGEQQ------RVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESG 188
Cdd:PRK01156 799 IDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSS 858
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-198 |
2.05e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.85 E-value: 2.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238244423 138 LSGGEQQRVYLAQALAQQ---PRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDL 198
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNL 892
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
137-213 |
2.07e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 2.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238244423 137 ELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASlYCDGLMFMKN 213
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIR-YANTIFVLSN 654
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
25-180 |
3.95e-04 |
|
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: 40.82 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 25 KGEFLGILGPNGSGKTtllhlltgtlpakkgrvYLAGKLLADYKPKELAQIMAvlpqkmdqaftftveetvafgrypfqt 104
Cdd:smart00382 1 PGEVILIVGPPGSGKT-----------------TLARALARELGPPGGGVIYI--------------------------- 36
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238244423 105 glfrqqteKGEAIVQEAMEQTGVADFAQKPiRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLI 180
Cdd:smart00382 37 --------DGEDILEEVLDQLLLIIVGGKK-ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLE 103
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
124-182 |
4.42e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 39.14 E-value: 4.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238244423 124 QTGVADFAQKPIRELSGGEQQR-VY--LAQALAQQ----------PRILFLDEPTNFLDLAYQKDLLDLIKR 182
Cdd:pfam13558 19 EDGSEVETYRRSGGLSGGEKQLlAYlpLAAALAAQygsaegrppaPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
15-169 |
4.70e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYlAGKLLAdYKPKElAQIMAVlpqkmdqaftfTVEET 94
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-AERSIA-YVPQQ-AWIMNA-----------TVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 95 VAFgrypFqtglfrqqTEKGEAIVQEAMEQTGV-ADFAQKP------IRE----LSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PTZ00243 741 ILF----F--------DEEDAARLADAVRVSQLeADLAQLGggleteIGEkgvnLSGGQKARVSLARAVYANRDVYLLDD 808
|
....*.
gi 1238244423 164 PTNFLD 169
Cdd:PTZ00243 809 PLSALD 814
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
138-165 |
5.78e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 5.78e-04
10 20
....*....|....*....|....*...
gi 1238244423 138 LSGGEQQRVYLAQALAQQPRILFLDEPT 165
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPT 432
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-165 |
1.15e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 1.15e-03
10 20 30
....*....|....*....|....*....|.
gi 1238244423 138 LSGGEQQRVYLAQALA--QQPRILF-LDEPT 165
Cdd:COG0178 827 LSGGEAQRVKLASELSkrSTGKTLYiLDEPT 857
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-214 |
2.09e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.88 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 19 VSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLADYKPKELAQIMAVLPQkmdQAFTFTveETVAFG 98
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQ---APVLFS--GTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 99 RYPFqtglfrqqTEKGEAIVQEAMEQTGVADFAQKPIREL-----------SGGEQQRVYLAQALAQQPRILFLDEPTNF 167
Cdd:PLN03130 1333 LDPF--------NEHNDADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1238244423 168 LDLAYQKdlldLIKRLTRES--GLAAVSVFHDLNTAsLYCDGLMFMKNG 214
Cdd:PLN03130 1405 VDVRTDA----LIQKTIREEfkSCTMLIIAHRLNTI-IDCDRILVLDAG 1448
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
138-200 |
3.83e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.78 E-value: 3.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238244423 138 LSGGEQQRVYLAQAL-AQQPRILF-LDEPTNFLdlaYQKD---LLDLIKRLtRESGLAAVSVFHDLNT 200
Cdd:cd03270 138 LSGGEAQRIRLATQIgSGLTGVLYvLDEPSIGL---HPRDndrLIETLKRL-RDLGNTVLVVEHDEDT 201
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-214 |
4.16e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.03 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLladykpkELAQIMAVLPQKMdqaftfTVEETV 95
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV-------SVIAISAGLSGQL------TGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 96 AFGRypFQTGLFRQQTEKgeaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKD 175
Cdd:PRK13546 107 EFKM--LCMGFKRKEIKA---MTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 1238244423 176 LLDLIKRLtRESGLAAVSVFHDLNTASLYCDGLMFMKNG 214
Cdd:PRK13546 182 CLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGG 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-169 |
5.27e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.57 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 16 INNVSLTVEKGEFLGILGPNGSGKTTllhlltgtlpakkgrvyLAGKLLADYKPKELAQI-----MAVLPQkMDQAFTFT 90
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTS-----------------LISAMLGELSHAETSSVvirgsVAYVPQ-VSWIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 91 VEETVAFGRyPFQTGLFrqqtekGEAIVQEAMeQTGVADFAQKPIRE-------LSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PLN03232 695 VRENILFGS-DFESERY------WRAIDVTAL-QHDLDLLPGRDLTEigergvnISGGQKQRVSMARAVYSNSDIYIFDD 766
|
....*.
gi 1238244423 164 PTNFLD 169
Cdd:PLN03232 767 PLSALD 772
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
10-196 |
8.07e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 37.62 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKKGRVYLAGKLLAdykpKELAqimavlpqKMDQAFTF 89
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLC--------TYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238244423 90 TVEETvafGRYPFQT----GLFRQQTEKGEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPT 165
Cdd:PRK13540 79 VGHRS---GINPYLTlrenCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|...
gi 1238244423 166 NFLDlayQKDLLDLIKRLT--RESGLAAVSVFH 196
Cdd:PRK13540 156 VALD---ELSLLTIITKIQehRAKGGAVLLTSH 185
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
135-171 |
9.33e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 38.55 E-value: 9.33e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1238244423 135 IRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLA 171
Cdd:TIGR00956 207 VRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSA 243
|
|
| |
