|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-253 |
3.64e-107 |
|
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: 317.37 E-value: 3.64e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGK---------TTllhlltgtlPAKEGRVYLAGKLLADYKPKE 71
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKstllralagLL---------KPSSGEVLLDGRDLASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 72 LAQIMAVLPQKTDQAFTFTVEETVAFGRYPFQtGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQA 151
Cdd:COG1120 73 LARRIAYVPQEPPAPFGLTVRELVALGRYPHL-GLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGT---AGPkqkPEYAVTE 228
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRivaQGP---PEEVLTP 228
|
250 260
....*....|....*....|....*
gi 1119636415 229 QSIKAVYDTDVTALVHQSSPKPMIV 253
Cdd:COG1120 229 ELLEEVYGVEARVIEDPVTGRPLVL 253
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-255 |
1.90e-86 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 264.33 E-value: 1.90e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQK 82
Cdd:PRK13548 5 ARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 83 TDQAFTFTVEETVAFGRYPFQTGlfrqqTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ------QP 156
Cdd:PRK13548 85 SSLSFPFTVEEVVAMGRAPHGLS-----RAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGT---AGPkqkPEYAVTEQSIKA 233
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRlvaDGT---PAEVLTPETLRR 236
|
250 260
....*....|....*....|..
gi 1119636415 234 VYDTDVTALVHQSSPKPMIVIQ 255
Cdd:PRK13548 237 VYGADVLVQPHPETGAPLVLPR 258
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-256 |
7.07e-85 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 260.43 E-value: 7.07e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLP 80
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTDQAFTFTVEETVAFGRYPFQTGlfrqqTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ------ 154
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPHGSS-----AAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 155 -QPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNG---TAGPkqkPEYAVTEQS 230
Cdd:COG4559 157 gGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGrlvAQGT---PEEVLTDEL 232
|
250 260
....*....|....*....|....*.
gi 1119636415 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 |
1.78e-76 |
|
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: 236.18 E-value: 1.78e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 ktdqaftftveetvafgrypfqtglfrqqtekdeaivqeAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:cd03214 81 ---------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1119636415 162 DEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-245 |
1.54e-67 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 215.34 E-value: 1.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKEGRVYLAGKLLADYKPKelaqiMAVLPQ 81
Cdd:COG1121 8 ELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKstllkailgllPPTSGTVRLFGKPPRRARRR-----IGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KT--DQAFTFTVEETVAFGRYPfQTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:COG1121 83 RAevDWDFPITVRDVVLMGRYG-RRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 160 FLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNG--TAGPkqkPEYAVTEQSIKAVYDT 237
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGlvAHGP---PEEVLTPENLSRAYGG 237
|
....*...
gi 1119636415 238 DVTALVHQ 245
Cdd:COG1121 238 PVALLAHG 245
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-254 |
2.40e-65 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 210.26 E-value: 2.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLP 80
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTDQAFTFTVEETVAFGRYPFQTgLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGRSPWLS-LWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 161 LDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKPEYAVTEQSIKAVYDTDvt 240
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVE-- 238
|
250
....*....|....*.
gi 1119636415 241 ALVHQS--SPKPMIVI 254
Cdd:PRK11231 239 AEIHPEpvSGTPMCVV 254
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-253 |
1.39e-63 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 205.32 E-value: 1.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLP 80
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTDQAFTFTVEETVAFGRYPFQTGlfrQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:COG4604 82 QENHINSRLTVRELVAFGRFPYSKG---RLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 161 LDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG---TAGPkqkPEYAVTEQSIKAVYDT 237
Cdd:COG4604 159 LDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGrvvAQGT---PEEIITPEVLSDIYDT 235
|
250
....*....|....*.
gi 1119636415 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 |
1.83e-60 |
|
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: 195.83 E-value: 1.83e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKlladyKPKELAQIMAVLPQ 81
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KTDQAFTF--TVEETVAFGRYPfQTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:cd03235 76 RRSIDRDFpiSVRDVVLMGLYG-HKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 160 FLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-236 |
1.15e-58 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 197.37 E-value: 1.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTD 84
Cdd:PRK09536 8 DLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 85 QAFTFTVEETVAFGRYPfQTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:PRK09536 88 LSFEFDVRQVVEMGRTP-HRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 165 TNFLDLAYQKDLLDLIKRLTrESGLAAVSVFHDLNTASLYCDELMFMKNG---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 |
5.66e-54 |
|
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: 180.78 E-value: 5.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLP 80
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTDQAFTFTVEETVAFGRYPFQtGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVALGRIPHR-SLWAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 161 LDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNG---TAGPkqkPEYAVTEQSIKAVYDT 237
Cdd:TIGR03873 161 LDEPTNHLDVRAQLETLALVRELAAT-GVTVVAALHDLNLAASYCDHVVVLDGGrvvAAGP---PREVLTPALIRAVYGV 236
|
250
....*....|....*....
gi 1119636415 238 DVTALVHQSSPKPMIVIQP 256
Cdd:TIGR03873 237 DATVLTHPDTGRPIIAFSP 255
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-253 |
5.15e-52 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 175.94 E-value: 5.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLP 80
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTDQAFTFTVEETVAFGRYPFQTgLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:PRK10253 88 QNATTPGDITVQELVARGRYPHQP-LFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 161 LDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKPEYAVTEQSIKAVYDTDVT 240
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCM 246
|
250
....*....|...
gi 1119636415 241 ALVHQSSPKPMIV 253
Cdd:PRK10253 247 IIDDPVAGTPLVV 259
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-251 |
2.07e-50 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 171.51 E-value: 2.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTDQAFTFTVEET 94
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 95 VAFGRYPFQTGLFRQQTEkDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQK 174
Cdd:PRK10575 106 VAIGRYPWHGALGRFGAA-DREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 175 DLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKPEYAVTEQSIKAVYDTDVTALVHQSSPKPM 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 |
2.39e-50 |
|
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: 169.57 E-value: 2.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSR--LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:cd03225 3 KNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KTD-QAFTFTVEETVAFGryPFQTGLFRqqtEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:cd03225 83 NPDdQFFGPTVEEEVAFG--LENLGLPE---EEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 161 LDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-215 |
6.38e-49 |
|
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: 166.35 E-value: 6.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSR-LINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKEGRVYLAGKLLADYKPKELAQIMAVLP 80
Cdd:COG1122 2 ELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKstllrllngllKPTSGEVLVDGKDITKKNLRELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTD-QAFTFTVEETVAFGryPFQTGLfrqqtEKDEA--IVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPR 157
Cdd:COG1122 82 QNPDdQLFAPTVEEDVAFG--PENLGL-----PREEIreRVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 158 ILFLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-214 |
1.52e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 152.53 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADyKPKELAQIMAVLPQK 82
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 83 TDQAFTFTVEETVAFgrypfQTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:COG1131 82 PALYPDLTVRENLRF-----FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 163 EPTNFLDLAYQKDLLDLIKRLtRESGlaaVSVF---HDLNTASLYCDELMFMKNG 214
Cdd:COG1131 157 EPTSGLDPEARRELWELLREL-AAEG---KTVLlstHYLEEAERLCDRVAIIDKG 207
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1-214 |
2.52e-42 |
|
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: 148.44 E-value: 2.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKlladykpkelaQIMAVLP 80
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR-----------DVTGVPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTDQAFTF---------TVEETVAFGrypfqtgLFRQQTEKDE--AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLA 149
Cdd:cd03259 70 ERRNIGMVFqdyalfphlTVAENIAFG-------LKLRGVPKAEirARVRELLELVGLEGLLNRYPHELSGGQQQRVALA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 150 QALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-214 |
3.30e-41 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 153.14 E-value: 3.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGY--GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK---EGRVYLAGKLLADYKPKELAQIMAV 78
Cdd:COG1123 8 RDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRIGM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 LPQKTDQAFT-FTVEETVAFGrypfqtgLFRQQTEKDEAI--VQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQ 155
Cdd:COG1123 88 VFQDPMTQLNpVTVGDQIAEA-------LENLGLSRAEARarVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1119636415 156 PRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDG 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
9-203 |
4.63e-41 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 144.68 E-value: 4.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 9 GYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGklladykpkelAQIMAVLPQKT--DQA 86
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSevPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 87 FTFTVEETVAFGRYPfQTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:NF040873 70 LPLTVRDLVAMGRWA-RRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 1119636415 167 FLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASL 203
Cdd:NF040873 149 GLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-234 |
7.22e-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: 149.67 E-value: 7.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGY-----GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI- 75
Cdd:COG1123 262 EVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELr 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 76 --MAVLPQKTDQAF--TFTVEETVAFG-RypfqtgLFRQQTEKD-EAIVQEAMEQTG-VADFAQKPIRELSGGEQQRVYL 148
Cdd:COG1123 342 rrVQMVFQDPYSSLnpRMTVGDIIAEPlR------LHGLLSRAErRERVAELLERVGlPPDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 149 AQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGT---AGPKQK---- 221
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRiveDGPTEEvfan 495
|
250
....*....|...
gi 1119636415 222 PEYAVTEQSIKAV 234
Cdd:COG1123 496 PQHPYTRALLAAV 508
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-214 |
1.37e-39 |
|
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: 142.63 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYG----DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMA 77
Cdd:COG1124 3 EVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 78 VLPQktdQAFT-----FTVEETVAfgrYPFQ-TGLFRQqtekdEAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQ 150
Cdd:COG1124 83 MVFQ---DPYAslhprHTVDRILA---EPLRiHGLPDR-----EERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119636415 151 ALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNG 215
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-215 |
1.52e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.11 E-value: 1.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KTdQAFTFTVEETVAFgryPFQtglFRQQtEKDEAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:COG4619 82 EP-ALWGGTVRDNLPF---PFQ---LRER-KFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 161 LDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-238 |
2.19e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 142.12 E-value: 2.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLI-NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI---MAVL 79
Cdd:COG3638 6 RNLSKRYPGGTPAlDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrrIGMI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 80 PQKtdqaftF------TVEETV---AFGRYPFQTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQ 150
Cdd:COG3638 86 FQQ------FnlvprlSVLTNVlagRLGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 151 ALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCD--------ELMFmkNGTAGpkqkp 222
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADriiglrdgRVVF--DGPPA----- 232
|
250
....*....|....*.
gi 1119636415 223 eyAVTEQSIKAVYDTD 238
Cdd:COG3638 233 --ELTDAVLREIYGGE 246
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-214 |
6.26e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 140.18 E-value: 6.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLS----GGYGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKEGRVYLAGKLLADYKPKELAQIM 76
Cdd:COG1136 5 LELRNLTksygTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKstllnilggldRPTSGEVLIDGQDISSLSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 77 A-----VLpqktdQAF----TFTVEETVAFGRYpfqtgLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVY 147
Cdd:COG1136 85 RrhigfVF-----QFFnllpELTALENVALPLL-----LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 148 LAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASlYCDELMFMKNG 214
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDG 220
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
14-253 |
8.58e-39 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 141.12 E-value: 8.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 14 RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK--------EGRVYLAGKLLADYKPKELAQIMAVLPQKTDQ 85
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 86 AFTFTVEETVAFGRYPF--QTGlfrQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ--------- 154
Cdd:PRK13547 95 AFAFSAREIVLLGRYPHarRAG---ALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 155 QPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKPEYAVTEQSIKAV 234
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARC 251
|
250
....*....|....*....
gi 1119636415 235 YDTDVTALVHQSSPKPMIV 253
Cdd:PRK13547 252 YGFAVRLVDAGDGVPPVIV 270
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-214 |
5.67e-38 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 138.08 E-value: 5.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSR-LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI---MAVL 79
Cdd:cd03256 4 ENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 80 PQKTDQAFTFTVEETV---AFGRYPFQTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:cd03256 84 FQQFNLIERLSVLENVlsgRLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
12-239 |
7.83e-38 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 137.66 E-value: 7.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 12 DSRLINnVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAkEGRVYLAGKLLADYKPKELAQIMAVLPQKTDQAFTFTV 91
Cdd:COG4138 9 AGRLGP-ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 92 EETVAFGRYPfqtglfRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ-------QPRILFLDEP 164
Cdd:COG4138 87 FQYLALHQPA------GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 165 TNFLDLAYQKDLLDLIKRLTrESGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKPEYAVTEQSIKAVYDTDV 239
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKF 234
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-236 |
1.13e-37 |
|
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: 137.43 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYG-DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI---M 76
Cdd:TIGR02315 2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLrrrI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 77 AVLPQKTDQAFTFTVEETV---AFGRYPFQTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALA 153
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVlhgRLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 154 QQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKPEyAVTEQSIKA 233
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPS-ELDDEVLRH 240
|
...
gi 1119636415 234 VYD 236
Cdd:TIGR02315 241 IYG 243
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-214 |
2.54e-37 |
|
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: 135.71 E-value: 2.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLS----GGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI-- 75
Cdd:cd03257 3 EVKNLSvsfpTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 76 -MAVLPQKTDQAF--TFTVEETVAFGrYPFQTGLFRQQtEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQAL 152
Cdd:cd03257 83 eIQMVFQDPMSSLnpRMTIGEQIAEP-LRIHGKLSKKE-ARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119636415 153 AQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-215 |
1.31e-36 |
|
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: 134.34 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI---MAVLP 80
Cdd:COG1127 9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrIGMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QktdQA--FT-FTVEETVAFgrypfqtGLfRQQTEKDEA----IVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALA 153
Cdd:COG1127 89 Q---GGalFDsLTVFENVAF-------PL-REHTDLSEAeireLVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119636415 154 QQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGK 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
1.70e-36 |
|
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: 133.38 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLS----GGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI-- 75
Cdd:cd03255 2 ELKNLSktygGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 76 --MAVLPQktdqAF----TFTVEETVAFgryPFQtgLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLA 149
Cdd:cd03255 82 rhIGFVFQ----SFnllpDLTALENVEL---PLL--LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 150 QALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASlYCDELMFMKNG 214
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDG 216
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-214 |
3.07e-36 |
|
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: 133.01 E-value: 3.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI---MAVLP 80
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QktDQA-FT-FTVEETVAFgrypfqtgLFRQQTEKDE----AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ 154
Cdd:cd03261 84 Q--SGAlFDsLTVFENVAF--------PLREHTRLSEeeirEIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 155 QPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
4-214 |
1.70e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.46 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtLPAKEGRVYLAGKLLADykpkelaqimaVLPQKT 83
Cdd:COG3842 9 ENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKttllrmiagfETPDSGRILLDGRDVTG-----------LPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 84 DQAFTF---------TVEETVAFgrypfqtGLFRQQTEKDE--AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQAL 152
Cdd:COG3842 78 NVGMVFqdyalfphlTVAENVAF-------GLRMRGVPKAEirARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119636415 153 AQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDG 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-214 |
2.64e-35 |
|
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: 128.67 E-value: 2.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADyKPKELAQIMAVLPQ 81
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KTDQAFTFTVEETVafgrypfqtglfrqqtekdeaivqeameqtgvadfaqkpirELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:cd03230 81 EPSLYENLTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1119636415 162 DEPTNFLDLAYQKDLLDLIKRLTRESglaaVSVF---HDLNTASLYCDELMFMKNG 214
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEG----KTILlssHILEEAERLCDRVAILNNG 171
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-214 |
7.57e-35 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 130.24 E-value: 7.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDS--RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADykPKELAQI---M 76
Cdd:TIGR04520 2 EVENVSFSYPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD--EENLWEIrkkV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 77 AVLPQKTDQAF-TFTVEETVAFGryPFQTGLfrqQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQ 155
Cdd:TIGR04520 80 GMVFQNPDNQFvGATVEDDVAFG--LENLGV---PREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1119636415 156 PRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTAsLYCDELMFMKNG 214
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKG 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-240 |
2.35e-34 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 128.66 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhl-ltgtlPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTDQAFT 88
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKstllslitgdlpPTYGNDVRLFGERRGGEDVWELRKRIGLVSPALQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 89 --FTVEETVAFGRYPfQTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:COG1119 93 rdETVLDVVLSGFFD-SIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 167 FLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGT---AGPKqkpEYAVTEQSIKAVYDTDVT 240
Cdd:COG1119 172 GLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRvvaAGPK---EEVLTSENLSEAFGLPVE 245
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-214 |
3.15e-34 |
|
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: 127.94 E-value: 3.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELA-------- 73
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgigrtf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 74 QIMAVLPqktdqafTFTVEETV-----AFGRYPFQTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYL 148
Cdd:cd03219 82 QIPRLFP-------ELTVLENVmvaaqARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119636415 149 AQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-215 |
3.18e-34 |
|
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: 128.05 E-value: 3.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQImAVLPQ 81
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-GVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KTDQAFTFTVEETVA-FGRypfqtgLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:COG4555 82 ERGLYDRLTVRENIRyFAE------LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 161 LDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNGT 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 ... |
4-214 |
3.51e-34 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 127.35 E-value: 3.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE-----LAQIMAV 78
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKrpvntVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 LPQktdqaftFTVEETVAFGrypfqtgLFRQQTEKDE--AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:cd03300 84 FPH-------LTVFENIAFG-------LRLKKLPKAEikERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKG 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-215 |
1.07e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 125.45 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 3 AEGLSGGYGDSRLI-NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKllaDYKPKELAQIMAVLPQ 81
Cdd:cd03226 2 IENISFSYKKGTEIlDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KTD-QAFTFTVEETVAFGRypfqtglfrQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:cd03226 79 DVDyQLFTDSVREELLLGL---------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 161 LDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-215 |
2.26e-33 |
|
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: 123.84 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYkpkelaqIMAVLP 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-------EDELPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTDQAFTF---------TVEETVAFGrypfqtglfrqqtekdeaivqeameqtgvadfaqkpireLSGGEQQRVYLAQA 151
Cdd:cd03229 74 LRRRIGMVFqdfalfphlTVLENIALG---------------------------------------LSGGQQQRVALARA 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119636415 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:cd03229 115 LAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-215 |
9.70e-33 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 121.20 E-value: 9.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 ktdqaftftveetvafgrypfqtglfrqqtekdeaivqeameqtgvadfaqkpireLSGGEQQRVYLAQALAQQPRILFL 161
Cdd:cd00267 81 --------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1119636415 162 DEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:cd00267 105 DEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-214 |
2.15e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 121.28 E-value: 2.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTDQAFT-FTVEET 94
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPDNQFVgATVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 95 VAFGrypfqtgLFRQQTEKDEAI--VQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAY 172
Cdd:PRK13635 103 VAFG-------LENIGVPREEMVerVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1119636415 173 QKDLLDLIKRLTRESGLAAVSVFHDLNTAsLYCDELMFMKNG 214
Cdd:PRK13635 176 RREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKG 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1-214 |
2.66e-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: 119.75 E-value: 2.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLiNNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPkELAQImAVLP 80
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP-EKRDI-SYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QktDQAF--TFTVEETVAFGrypfqtglFRQQTEKDEAIVQEAMEQTGVADFA----QKPiRELSGGEQQRVYLAQALAQ 154
Cdd:cd03299 78 Q--NYALfpHMTVYKNIAYG--------LKKRKVDKKEIERKVLEIAEMLGIDhllnRKP-ETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 155 QPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNG 206
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
16-215 |
2.80e-31 |
|
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: 120.53 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKttllhlltgTLPAKEGRVYLAGKLLADYKPKELA--------QIMAVLPQktdqaf 87
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKttlfnlitgFYRPTSGRILFDGRDITGLPPHRIArlgiartfQNPRLFPE------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 88 tFTVEETVAFGRY----------PFQTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPR 157
Cdd:COG0411 94 -LTVLENVLVAAHarlgrgllaaLLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 158 ILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:COG0411 173 LLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
16-166 |
2.96e-30 |
|
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: 114.28 E-value: 2.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTDQAFTFTVEETV 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 96 AFGRYpfqtgLFRQQTEKDEAIVQEAMEQTGVADFAQKPIR----ELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:pfam00005 81 RLGLL-----LKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
12-214 |
3.18e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 117.87 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLaDYKPKELAQIMA----VLPQKTDQAF 87
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKtvgiVFQNPDDQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 88 TFTVEETVAFGryPFQTGLFRQQTEKDeaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNF 167
Cdd:PRK13639 93 APTVEEDVAFG--PLNLGLSKEEVEKR---VKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1119636415 168 LDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNG 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 ... |
1-213 |
1.15e-29 |
|
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: 114.88 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRL----INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKelaqiM 76
Cdd:cd03293 1 LEVRNVSKTYGGGGGavtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 77 AVLPQktdQAFTF---TVEETVAFGryPFQTGLFRQQTEkdeAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALA 153
Cdd:cd03293 76 GYVFQ---QDALLpwlTVLDNVALG--LELQGVPKAEAR---ERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 154 QQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKN 213
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-214 |
6.48e-29 |
|
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: 119.55 E-value: 6.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSR--LINNVSLTVEKGEFLGILGPNGSGKTTLlhlltgtlpAK---------EGRVYLAGKLLADYKPKEL 72
Cdd:COG2274 477 ENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTL---------LKlllglyeptSGRILIDGIDLRQIDPASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 73 AQIMAVLPQkTDQAFTFTVEETVAFGRypfqtglfrqqTEKDEAIVQEAMEQTGVADFAQK-------PIRE----LSGG 141
Cdd:COG2274 548 RRQIGVVLQ-DVFLFSGTIRENITLGD-----------PDATDEEIIEAARLAGLHDFIEAlpmgydtVVGEggsnLSGG 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1119636415 142 EQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSvfHDLNTASLyCDELMFMKNG 214
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIA--HRLSTIRL-ADRIIVLDKG 685
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
6.52e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.56 E-value: 6.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGD-SRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLaDYKPK---ELAQIM 76
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 77 AVLPQKTD-QAFTFTVEETVAFGryPFQTGLFRQQTEKDeaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQ 155
Cdd:PRK13636 85 GMVFQDPDnQLFSASVYQDVSFG--AVNLKLPEDEVRKR---VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119636415 156 PRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGTA 216
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
16-220 |
1.30e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 113.67 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTDQAFT-FTVEET 94
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPDNQFVgATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 95 VAFGrypfqtgLFRQQTEKDEAI--VQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAY 172
Cdd:PRK13650 103 VAFG-------LENKGIPHEEMKerVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1119636415 173 QKDLLDLIKRLTRESGLAAVSVFHDLNTASLyCDELMFMKNG----TAGPKQ 220
Cdd:PRK13650 176 RLELIKTIKGIRDDYQMTVISITHDLDEVAL-SDRVLVMKNGqvesTSTPRE 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-197 |
2.56e-28 |
|
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: 110.65 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtLPAKEGRVYLAGKLLADyKPKELAQIMAVLP 80
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKttllrilaglLPPSAGEVLWNGEPIRD-AREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTDQAFTFTVEETVAfgrypFQTGLFRQQTekDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:COG4133 82 HADGLKPELTVRENLR-----FWAALYGLRA--DREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1119636415 161 LDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHD 197
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQ 190
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-215 |
4.29e-28 |
|
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: 110.82 E-value: 4.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 14 RLINNVSLTVEKGEFLGILGPNGSGKTT---LLHLLTGTLPAKEGRVYLAGKLLadyKPKELAQIMAVLPQKTDQAFTFT 90
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNGQPR---KPDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 91 VEETVAFgrypfqTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRE-----LSGGEQQRVYLAQALAQQPRILFLDEPT 165
Cdd:cd03234 98 VRETLTY------TAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGnlvkgISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1119636415 166 NFLD--LAYQkdLLDLIKRLTRESGLAAVSVfHDlNTASLY--CDELMFMKNGT 215
Cdd:cd03234 172 SGLDsfTALN--LVSTLSQLARRNRIVILTI-HQ-PRSDLFrlFDRILLLSSGE 221
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
10-214 |
9.72e-28 |
|
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: 111.71 E-value: 9.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGklladY----KPKELAQIMAVLPQKT-- 83
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAG-----YdvvrEPRKVRRSIGIVPQYAsv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 84 DQAFTFTvEETVAFGRYpfqTGLFRQqtEKDEAIvQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:TIGR01188 78 DEDLTGR-ENLEMMGRL---YGLPKD--EAEERA-EELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1119636415 164 PTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHG 200
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
1.10e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.85 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSR--LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVL 79
Cdd:PRK13632 9 KVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 80 PQKTDQAFT-FTVEETVAFG----RYPFqtglfrqqtEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ 154
Cdd:PRK13632 89 FQNPDNQFIgATVEDDIAFGlenkKVPP---------KKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 155 QPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLyCDELMFMKNGTAGPKQKPEYAVTEQSI 231
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1-229 |
1.45e-27 |
|
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: 109.58 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTT------LLHLLTGTLPAkEGRVYLAGKLLA--DYKPKEL 72
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTllrllnRLNDLIPGAPD-EGEVLLDGKDIYdlDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 73 AQIMAVLPQKTDqAFTFTVEETVAFGrypfqtglFRQQTEKD----EAIVQEAMEQTG----VADFAQKpiRELSGGEQQ 144
Cdd:cd03260 80 RRRVGMVFQKPN-PFPGSIYDNVAYG--------LRLHGIKLkeelDERVEEALRKAAlwdeVKDRLHA--LGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 145 RVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSvfHDLNTASLYCDELMFMKNGtagpkQKPEY 224
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVT--HNMQQAARVADRTAFLLNG-----RLVEF 221
|
....*
gi 1119636415 225 AVTEQ 229
Cdd:cd03260 222 GPTEQ 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-214 |
1.48e-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: 109.16 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKpKELAQIMavlpQ 81
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDK-KNINELR----Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KTD---QAFTF----TVEETVAFGrypfQTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ 154
Cdd:cd03262 77 KVGmvfQQFNLfphlTVLENITLA----PIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 155 QPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-214 |
1.71e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 112.73 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE-----LAQIMAVL 79
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENrhvntVFQSYALF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 80 PQktdqaftFTVEETVAFGrypfqtgLFRQQTEKDE--AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPR 157
Cdd:PRK09452 99 PH-------MTVFENVAFG-------LRMQKTPAAEitPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 158 ILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-214 |
1.81e-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: 109.00 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGkLLADYKPKELAQIMAVLPQK 82
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG-HDVVREPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 83 --TDQAFTFTvEETVAFGR-YPFQTGLFRQQTEkdeaivqEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:cd03265 82 lsVDDELTGW-ENLYIHARlYGVPGAERRERID-------ELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 160 FLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHG 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-214 |
1.88e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.21 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGD-SRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKEL-AQIMAVLPQ 81
Cdd:PRK13647 8 EDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KTDQAFTFTVEETVAFGryPFQTGLFRQQTEKDeaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:PRK13647 88 PDDQVFSSTVWDDVAFG--PVNMGLDKDEVERR---VEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1119636415 162 DEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-214 |
1.96e-27 |
|
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: 114.86 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 3 AEGLSGGYGDSR-LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:COG4988 339 LEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KTdQAFTFTVEETVAFGRypfqtglfrqqTEKDEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLAQ 150
Cdd:COG4988 419 NP-YLFAGTIRENLRLGR-----------PDASDEELEAALEAAGLDEFVAAlpdgldtPLGEggrgLSGGQAQRLALAR 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119636415 151 ALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTResGLAAVSVFHDLNTASLyCDELMFMKNG 214
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDG 547
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
11-214 |
2.86e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 109.41 E-value: 2.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSRLINNVSLTVEKGEFLGILGPNGSGK----------TtllhlltgtlPAKEGRVYLAGKLLADYKPKelaqiMAVLP 80
Cdd:COG1116 22 GGVTALDDVSLTVAAGEFVALVGPSGCGKstllrliaglE----------KPTSGEVLVDGKPVTGPGPD-----RGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKtdqaFT----FTVEETVAFGrypfqtgLFRQQTEKDEA--IVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ 154
Cdd:COG1116 87 QE----PAllpwLTVLDNVALG-------LELRGVPKAERreRARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119636415 155 QPRILFLDEPtnF--LD----LAYQKDLLDLIkrltRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:COG1116 156 DPEVLLMDEP--FgaLDaltrERLQDELLRLW----QETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
12-248 |
3.03e-27 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 109.25 E-value: 3.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 12 DSRLINnVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAkEGRVYLAGKLLADYKPKELAQIMAVLPQKTDQAFTFTV 91
Cdd:PRK03695 9 STRLGP-LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 92 EETVAFGRYPfqtglfRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ-------QPRILFLDEP 164
Cdd:PRK03695 87 FQYLTLHQPD------KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 165 TNFLDLAYQKDLLDLIKRLTReSGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKPEYAVTEQSIKAVYDTDVTALVH 244
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLDV 239
|
....
gi 1119636415 245 QSSP 248
Cdd:PRK03695 240 EGHP 243
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-215 |
3.23e-27 |
|
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: 108.93 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSR-LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQK 82
Cdd:cd03295 4 ENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 83 TDQAFTFTVEETVAFgrYPfqtGLFRQQTEKDEAIVQEAMEQTGV--ADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:cd03295 84 IGLFPHMTVEENIAL--VP---KLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 161 LDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGE 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-186 |
9.70e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 107.06 E-value: 9.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLI-NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELA----QIMAV 78
Cdd:COG2884 5 ENVSKRYPGGREAlSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrrRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 ------LPQKTdqaftftVEETVAFgryPFQ-TGLFRQQTEKDeaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQA 151
Cdd:COG2884 85 fqdfrlLPDRT-------VYENVAL---PLRvTGKSRKEIRRR---VREVLDLVGLSDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190
....*....|....*....|....*....|....*
gi 1119636415 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRE 186
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINRR 186
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
10-216 |
1.33e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 106.76 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRLinNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKElaQIMAVLPQKTDqafTF 89
Cdd:COG3840 11 YGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLFQENN---LF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 90 ---TVEETVAFGRYPfqtGLfrQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:COG3840 84 phlTVAQNIGLGLRP---GL--KLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1119636415 167 FLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGTA 216
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRI 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-214 |
1.36e-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: 106.12 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGeFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYkPKELAQIMAVLPQ 81
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KTDQAFTFTVEETVAFgrypfQTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:cd03264 80 EFGVYPNFTVREFLDY-----IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1119636415 162 DEPTNFLDLAYQKDLLDLIKRLTrESGLAAVSVfHDLNTASLYCDELMFMKNG 214
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELG-EDRIVILST-HIVEDVESLCNQVAVLNKG 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-214 |
1.69e-26 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 104.77 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDS--RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:cd03228 4 KNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KTdQAFTFTVEETVafgrypfqtglfrqqtekdeaivqeameqtgvadfaqkpireLSGGEQQRVYLAQALAQQPRILFL 161
Cdd:cd03228 84 DP-FLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1119636415 162 DEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSvfHDLNTASLyCDELMFMKNG 214
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIA--HRLSTIRD-ADRIIVLDDG 170
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-214 |
2.01e-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: 107.34 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI-----------MAVLPQKTd 84
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkismvfqsFALLPHRT- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 85 qaftftVEETVAFGrYPFQtGLFRQQTEkdeAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:cd03294 119 ------VLENVAFG-LEVQ-GVPRAERE---ERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1119636415 165 TNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDG 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-215 |
2.03e-26 |
|
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: 111.78 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSR--LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVL 79
Cdd:COG4987 335 ELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 80 PQKTDqAFTFTVEETVAFGRyPfqtglfrqqtEKDEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYL 148
Cdd:COG4987 415 PQRPH-LFDTTLRENLRLAR-P----------DATDEELWAALERVGLGDWLAAlpdgldtWLGEggrrLSGGERRRLAL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 149 AQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSvfHDLNTASLyCDELMFMKNGT 215
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLIT--HRLAGLER-MDRILVLEDGR 546
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-245 |
3.54e-26 |
|
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: 105.88 E-value: 3.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE-----LAQIMAV 78
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErnvgfVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 LPQktdqaftFTVEETVAFGrypFQTGLFRQQTEKDE--AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:cd03296 86 FRH-------MTVFDNVAFG---LRVKPRSERPPEAEirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGtagpkqkpeyaVTEQ--SIKAV 234
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKG-----------RIEQvgTPDEV 224
|
250
....*....|.
gi 1119636415 235 YDTDVTALVHQ 245
Cdd:cd03296 225 YDHPASPFVYS 235
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1-214 |
4.00e-26 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 105.03 E-value: 4.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE--LA---QI 75
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDrdIAmvfQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 76 MAVLPQKtdqaftfTVEETVAFgrypfqtGLFRQQTEKDE--AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALA 153
Cdd:cd03301 81 YALYPHM-------TVYDNIAF-------GLKLRKVPKDEidERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119636415 154 QQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-214 |
5.19e-26 |
|
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: 105.36 E-value: 5.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 6 LSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI---MAVLPQK 82
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKArrrIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 83 TDQAFTFTVEETVAfgrYPFQtgLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:cd03258 91 FNLLSSRTVFENVA---LPLE--IAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1119636415 163 EPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03258 166 EATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKG 217
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
11-198 |
7.16e-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: 104.25 E-value: 7.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI---MAVLPQKTDQAF 87
Cdd:TIGR02673 13 GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLrrrIGVVFQDFRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 88 TFTVEETVAFgryPFQtgLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNF 167
Cdd:TIGR02673 93 DRTVYENVAL---PLE--VRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGN 167
|
170 180 190
....*....|....*....|....*....|.
gi 1119636415 168 LDLAYQKDLLDLIKRLTReSGLAAVSVFHDL 198
Cdd:TIGR02673 168 LDPDLSERILDLLKRLNK-RGTTVIVATHDL 197
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
16-223 |
7.36e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.99 E-value: 7.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTDQAFT-FTVEET 94
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQFVgSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 95 VAFGRYPFQTglfrqQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQK 174
Cdd:PRK13648 105 VAFGLENHAV-----PYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1119636415 175 DLLDLIKRLTRESGLAAVSVFHDLnTASLYCDELMFMKNGTAGPKQKPE 223
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDL-SEAMEADHVIVMNKGTVYKEGTPT 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-214 |
1.91e-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: 104.50 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQ---------- 74
Cdd:TIGR02769 16 GLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrdvqlvfq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 75 --IMAVLPQKTdqaftftVEETVafgRYPFQTGLFRQQTEKDEAIvQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQA 151
Cdd:TIGR02769 96 dsPSAVNPRMT-------VRQII---GEPLRHLTSLDESEQKARI-AELLDMVGLrSEDADKLPRQLSGGQLQRINIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1119636415 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-216 |
2.02e-25 |
|
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: 103.13 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTgtlpakegRVYL--AGKLLADYKPkelaqimav 78
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMIL--------GIILpdSGEVLFDGKP--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 lpqktdqaFTFTVEETvaFGRYPFQTGLFRQQTEKDEAI----------------VQEAMEQTGVADFAQKPIRELSGGE 142
Cdd:cd03269 64 --------LDIAARNR--IGYLPEERGLYPKMKVIDQLVylaqlkglkkeearrrIDEWLERLELSEYANKRVEELSKGN 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119636415 143 QQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNGTA 216
Cdd:cd03269 134 QQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-214 |
2.38e-25 |
|
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: 106.27 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKlladykpkelaQIMAVLP 80
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGR-----------DITRLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTDQAFTF---------TVEETVAFGrypfqtgLFRQQTEKDEAI--VQEAMEQTGVADFAQKPIRELSGGEQQRVYLA 149
Cdd:TIGR03265 74 QKRDYGIVFqsyalfpnlTVADNIAYG-------LKNRGMGRAEVAerVAELLDLVGLPGSERKYPGQLSGGQQQRVALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 150 QALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:TIGR03265 147 RALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHG 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-214 |
3.73e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 103.94 E-value: 3.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLT---GTLPAKEGRVYL-------AGKLLADYKpK 70
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSgliTGDKSAGSHIELlgrtvqrEGRLARDIR-K 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 71 ELAQIMAVLpQKTDQAFTFTVEETV---AFGRYPFQTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVY 147
Cdd:PRK09984 84 SRANTGYIF-QQFNLVNRLSVLENVligALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 148 LAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-215 |
3.74e-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: 3.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLI--NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLAdYKPKELAQIMAV 78
Cdd:cd03263 1 LQIRNLTKTYKKGTKPavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 LPQKtDQAFT-FTVEETVAF-GRYpfqTGLFRQQtekDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:cd03263 80 CPQF-DALFDeLTVREHLRFyARL---KGLPKSE---IKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119636415 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTRESglaavSVF---HDLNTASLYCDELMFMKNGT 215
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGR-----SIIlttHSMDEAEALCDRIAIMSDGK 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-215 |
4.21e-25 |
|
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: 102.80 E-value: 4.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTDQAFTF 89
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 90 TVEETVAFGRYPFQTGLFRQQTEKDEaiVQEAMEqtgVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKKRLDE--LSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1119636415 170 LAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:cd03267 186 VVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
16-216 |
5.53e-25 |
|
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: 102.54 E-value: 5.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELA--QIMAVLPQKTdqaftftVEE 93
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVvfQNYSLLPWLT-------VRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 94 TVAFGrypFQTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQ 173
Cdd:TIGR01184 74 NIALA---VDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1119636415 174 KDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGTA 216
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPA 193
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-199 |
7.97e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.71 E-value: 7.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQkTDQAFTFT 90
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQ-TPTLFGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 91 VEETVAFgryPFQtglFRQQTeKDEAIVQEAMEQTGVAD-FAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK10247 97 VYDNLIF---PWQ---IRNQQ-PDPAIFLDDLERFALPDtILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190
....*....|....*....|....*....|
gi 1119636415 170 LAYQKDLLDLIKRLTRESGLAAVSVFHDLN 199
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-216 |
8.07e-25 |
|
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: 100.37 E-value: 8.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSR--LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:cd03246 4 ENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KtDQAFTFTVEETVafgrypfqtglfrqqtekdeaivqeameqtgvadfaqkpireLSGGEQQRVYLAQALAQQPRILFL 161
Cdd:cd03246 84 D-DELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 162 DEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLyCDELMFMKNGTA 216
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-214 |
1.00e-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: 101.36 E-value: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI-MAVLP 80
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QkTDQAF-TFTVEETvafgrypFQTGLFRQQTEKDEAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRI 158
Cdd:cd03224 82 E-GRRIFpELTVEEN-------LLLGAYARRRAKRKARLERVYELFPRlKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 159 LFLDEPTnfLDLA--YQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03224 154 LLLDEPS--EGLApkIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERG 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-211 |
1.01e-24 |
|
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: 103.59 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLlhlltgtlpAK------------EGRVYLAGKLLADYKPKELAQI--- 75
Cdd:COG0444 16 GVVKAVDGVSFDVRRGETLGLVGESGSGKSTL---------ARailgllpppgitSGEILFDGEDLLKLSEKELRKIrgr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 76 -MAVLPQktDqAFT-----FTVEETVAfgrYPFQtgLFRQQTEKD-EAIVQEAMEQTGVADfaqkPIR-------ELSGG 141
Cdd:COG0444 87 eIQMIFQ--D-PMTslnpvMTVGDQIA---EPLR--IHGGLSKAEaRERAIELLERVGLPD----PERrldryphELSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 142 EQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFM 211
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVM 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-214 |
1.17e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 104.07 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGK-----------TtllhlltgtlpAKEGRVYLAGKLLADYKPkel 72
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKttllriiagleT-----------PDSGRIVLNGRDLFTNLP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 73 aqimavlPQKTDQAFTF---------TVEETVAFGrypfqtglFRQQTEKDEAIVQEAMEQ------TGVADfaQKPiRE 137
Cdd:COG1118 72 -------PRERRVGFVFqhyalfphmTVAENIAFG--------LRVRPPSKAEIRARVEELlelvqlEGLAD--RYP-SQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1119636415 138 LSGGEQQRVYLAQALAQQPRILFLDEPtnF--LDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:COG1118 134 LSGGQRQRVALARALAVEPEVLLLDEP--FgaLDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQG 210
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-214 |
1.24e-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: 102.22 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKllaDYKPKELAQI--------- 75
Cdd:TIGR02323 8 GLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMR---SGAELELYQLseaerrrlm 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 76 ---MAVLPQKTDQAFTFTVEETVAFGRYPFQTGL-----FRQQTEKDEAIVQeaMEQTGVADfaqKPiRELSGGEQQRVY 147
Cdd:TIGR02323 85 rteWGFVHQNPRDGLRMRVSAGANIGERLMAIGArhygnIRATAQDWLEEVE--IDPTRIDD---LP-RAFSGGMQQRLQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 148 LAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQG 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
6-223 |
1.29e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.57 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 6 LSGGYGDSR--LINNVSLTVEKGEFLGILGPNGSGKTTLLHLltgtlpakegrvyLAGKLLADYKPKELAQIMAV-LPQK 82
Cdd:PRK13640 11 VSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKL-------------INGLLLPDDNPNSKITVDGItLTAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 83 T---------------DQAFT-FTVEETVAFGRYpfQTGLFRQQTEKdeaIVQEAMEQTGVADFAQKPIRELSGGEQQRV 146
Cdd:PRK13640 78 TvwdirekvgivfqnpDNQFVgATVGDDVAFGLE--NRAVPRPEMIK---IVRDVLADVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 147 YLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLyCDELMFMKNGTAGPKQKPE 223
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPV 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-214 |
1.91e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 102.09 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPK-ELAQIMAVLPQKTDQAFTFT-VEE 93
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIRNKAGMVFQNPDNQIVATiVEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 94 TVAFGryPFQTGLfrqQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQ 173
Cdd:PRK13633 106 DVAFG--PENLGI---PPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1119636415 174 KDLLDLIKRLTRESGLAAVSVFHDLNTAsLYCDELMFMKNG 214
Cdd:PRK13633 181 REVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSG 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-214 |
2.58e-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: 100.13 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 3 AEGLSGGYGDSRL----INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGkLLADYKPKELAQIMAV 78
Cdd:cd03266 4 ADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-FDVVKEPAEARRRLGF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 LPQKTDQAFTFTVEETVA-FGRYpfqTGLFRQQTEkdeAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPR 157
Cdd:cd03266 83 VSDSTGLYDRLTARENLEyFAGL---YGLKGDELT---ARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 158 ILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-220 |
2.88e-24 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 101.50 E-value: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLAdykpKELAQ-IMAVLPQ--KTDQAFTFTVE 92
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKnLVAYVPQseEVDWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 93 ETVAFGRYPfQTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAY 172
Cdd:PRK15056 99 DVVMMGRYG-HMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1119636415 173 QKDLLDLIKRLTRESGLAAVSVfHDLNTASLYCDELMFMKnGT---AGPKQ 220
Cdd:PRK15056 178 EARIISLLRELRDEGKTMLVST-HNLGSVTEFCDYTVMVK-GTvlaSGPTE 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
19-214 |
2.88e-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: 100.59 E-value: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 19 VSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAqimAVLPQKT---DQAF----TFTV 91
Cdd:COG4181 31 ISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARA---RLRARHVgfvFQSFqllpTLTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 92 EETVAfgrypfqTGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLA 171
Cdd:COG4181 108 LENVM-------LPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1119636415 172 YQKDLLDLIKRLTRESGLAAVSVFHDLNTASLyCDELMFMKNG 214
Cdd:COG4181 181 TGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAG 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-215 |
4.28e-24 |
|
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: 99.49 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 20 SLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKElaQIMAVLPQKTDQAFTFTVEETVAFGR 99
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 100 YPfqtGLfrQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDL 179
Cdd:cd03298 96 SP---GL--KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1119636415 180 IKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-209 |
4.78e-24 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 100.19 E-value: 4.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELaQIMAVLPqkt 83
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKL-YLDTTLP--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 84 dqaftFTVEEtvaFGRypfqtglFRQQTEKDEaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PRK09544 84 -----LTVNR---FLR-------LRPGTKKED--ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1119636415 164 PTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELM 209
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-214 |
4.99e-24 |
|
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: 104.38 E-value: 4.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 17 NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAkEGRVYLAGKLLADYKPKEL----AQIMAVL--------PQktd 84
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRALrplrRRMQVVFqdpfgslsPR--- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 85 qaftFTVEETVAFGRYPFQTGLFRQQTEkdeAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:COG4172 379 ----MTVGQIIAEGLRVHGPGLSAAERR---ARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1119636415 164 PTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:COG4172 452 PTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDG 502
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-215 |
5.34e-24 |
|
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: 98.83 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKeLAQIMAVLpq 81
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA-LRRIGALI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 ktdqaftftveETVAFgrYPFQTG-----LFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:cd03268 79 -----------EAPGF--YPNLTArenlrLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119636415 157 RILFLDEPTNFLDLAYQKDLLDLIKRLtRESGlaaVSVF---HDLNTASLYCDELMFMKNGT 215
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSL-RDQG---ITVLissHLLSEIQKVADRIGIINKGK 203
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-215 |
5.70e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.89 E-value: 5.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYG-----DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPK--ELA 73
Cdd:PRK13637 3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 74 QIMAVLPQKTD-QAFTFTVEETVAFGryPFQTGLFRQQTEKDeaiVQEAMEQTGVA--DFAQKPIRELSGGEQQRVYLAQ 150
Cdd:PRK13637 83 KKVGLVFQYPEyQLFEETIEKDIAFG--PINLGLSEEEIENR---VKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 151 ALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-197 |
7.70e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 101.69 E-value: 7.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKEGRVYLAGKLLADYKPKE--LAqiM----- 76
Cdd:COG3839 7 ENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKstllrmiagleDPTSGEILIGGRDVTDLPPKDrnIA--Mvfqsy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 77 AVLPQKtdqaftfTVEETVAFgrypfqtGLFRQQTEKDE--AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ 154
Cdd:COG3839 85 ALYPHM-------TVYENIAF-------PLKLRKVPKAEidRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1119636415 155 QPRILFLDEP-TNfLDLAYQKDLLDLIKRLTRESGLAAVSVFHD 197
Cdd:COG3839 151 EPKVFLLDEPlSN-LDAKLRVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1-198 |
1.09e-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: 103.59 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGY-GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVL 79
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 80 PQKTdQAFTFTVEETVAFGRypfqtglfrqqTEKDEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYL 148
Cdd:TIGR02868 415 AQDA-HLFDTTVRENLRLAR-----------PDATDEELWAALERVGLADWLRAlpdgldtVLGEggarLSGGERQRLAL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1119636415 149 AQALAQQPRILFLDEPTNFLDLAYQKDLLDLIkrLTRESGLAAVSVFHDL 198
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-204 |
2.58e-23 |
|
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: 102.36 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 3 AEGLSGGYGDSR-LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:TIGR02857 324 FSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 kTDQAFTFTVEETVAFGRypfqtglfrqqTEKDEAIVQEAMEQTGVADFAQ-------KPI----RELSGGEQQRVYLAQ 150
Cdd:TIGR02857 404 -HPFLFAGTIAENIRLAR-----------PDASDAEIREALERAGLDEFVAalpqgldTPIgeggAGLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1119636415 151 ALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTResGLAAVSVFHDLNTASLY 204
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA 523
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-214 |
3.32e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 98.23 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE--LAQIMAV 78
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERgvVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 LPQKTdqaftftVEETVAFGrypFQ-TGLFRQQTEkdeAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPR 157
Cdd:PRK11248 82 LPWRN-------VQDNVAFG---LQlAGVEKMQRL---EIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 158 ILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
11-214 |
4.32e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 98.34 E-value: 4.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTD-QAFTF 89
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDdQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 90 TVEETVAFGryPFQTGLfrqQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK13652 95 TVEQDIAFG--PINLGL---DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1119636415 170 LAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK13652 170 PQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKG 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-214 |
4.56e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 97.37 E-value: 4.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKEGRVYLAGKLLADyKPKELAQI-----M 76
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKstllrcinlleEPDSGTITVDGEDLTD-SKKDINKLrrkvgM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 77 aVLpqktdQAFT-F---TVEETVAFGryPFQTglfrQQTEKDEAIvQEAME---QTGVADFAQKPIRELSGGEQQRVYLA 149
Cdd:COG1126 82 -VF-----QQFNlFphlTVLENVTLA--PIKV----KKMSKAEAE-ERAMElleRVGLADKADAYPAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 150 QALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGG 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-214 |
4.94e-23 |
|
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: 96.50 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 18 NVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTdQAFTFTVEETVAF 97
Cdd:cd03245 22 NVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDV-TLFYGTLRDNITL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 98 GRyPFQTglfrqqtekDEAIVqEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:cd03245 101 GA-PLAD---------DERIL-RAAELAGVTDFVNKhpngldlQIGErgrgLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1119636415 167 FLDLAYQKDLLDLIKRLTRESGLaaVSVFHDLNTASLyCDELMFMKNG 214
Cdd:cd03245 170 AMDMNSEERLKERLRQLLGDKTL--IIITHRPSLLDL-VDRIIVMDSG 214
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
10-201 |
5.40e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 96.40 E-value: 5.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK---EGRVYLAGKLLADyKPKELAQImAVLPQkTDQA 86
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTA-LPAEQRRI-GILFQ-DDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 87 FT-FTVEETVAFGRYPFQTGLFRQQTekdeaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPT 165
Cdd:COG4136 88 FPhLSVGENLAFALPPTIGRAQRRAR------VEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1119636415 166 NFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTA 201
Cdd:COG4136 162 SKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA 197
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-214 |
6.38e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 101.39 E-value: 6.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSR-LINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKEGRVYLAGKLLADYKPKELAQIMAVLPQK 82
Cdd:COG1132 343 ENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKstlvnlllrfyDPTSGRILIDGVDIRDLTLESLRRQIGVVPQD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 83 TdQAFTFTVEETVAFGRypfqtglfrqqTEKDEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLAQA 151
Cdd:COG1132 423 T-FLFSGTIRENIRYGR-----------PDATDEEVEEAAKAAQAHEFIEAlpdgydtVVGErgvnLSGGQRQRIAIARA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1119636415 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTResGLAAVSVFHDLNTASLyCDELMFMKNG 214
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDG 550
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-229 |
7.53e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 98.75 E-value: 7.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQImAVLPQKTD 84
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARI-GVVPQFDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 85 QAFTFTVEET-VAFGRYpfqtglFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PRK13536 125 LDLEFTVRENlLVFGRY------FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119636415 164 PTNFLD-----LAYQKdLLDLIKRltresGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKPEYAVTEQ 229
Cdd:PRK13536 199 PTTGLDpharhLIWER-LRSLLAR-----GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-214 |
7.69e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 96.92 E-value: 7.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKllaDYKPKELAQIMAV-- 78
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR---DGQLRDLYALSEAer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 -LPQKTDQAFtftVEEtvafgrYPFQtGLFRQQT------EKDEA--------IVQEAMEQTGVADFAQKPI----RELS 139
Cdd:PRK11701 84 rRLLRTEWGF---VHQ------HPRD-GLRMQVSaggnigERLMAvgarhygdIRATAGDWLERVEIDAARIddlpTTFS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 140 GGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
1.36e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.98 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGD-SRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADY-KPKELAQIMAV 78
Cdd:PRK13644 2 IRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 LPQKTDQAFT-FTVEETVAFGryPFQTGLFRQQTEKdeaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPR 157
Cdd:PRK13644 82 VFQNPETQFVgRTVEEDLAFG--PENLCLPPIEIRK---RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 158 ILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLyCDELMFMKNGTAGPKQKPEYAVTEQSIK 232
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-211 |
1.64e-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: 94.99 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQImavlpQKT 83
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKF-----RRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 84 DQAFTF---------TVEETVAFGrypfQTGLFRQQTEKDEAIVqEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQ 154
Cdd:TIGR03608 77 KLGYLFqnfalieneTVEENLDLG----LKYKKLSKKEKREKKK-EALEKVGLNLKLKQKIYELSGGEQQRVALARAILK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 155 QPRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLyCDELMFM 211
Cdd:TIGR03608 152 PPPLILADEPTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDPEVAKQ-ADRVIEL 206
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-214 |
3.21e-22 |
|
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: 94.28 E-value: 3.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 18 NVSLTVEkGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKelaqiMAVLPQKTDQAFTF-------- 89
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKK-----INLPPQQRKIGLVFqqyalfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 90 -TVEETVAFGrypfqtgLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFL 168
Cdd:cd03297 90 lNVRENLAFG-------LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1119636415 169 DLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03297 163 DRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-189 |
4.59e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 94.15 E-value: 4.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI-MAVLP 80
Cdd:cd03218 2 RAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QktdQAFTF---TVEETVAfgrypfqtgLFRQQTEKDEAIVQEAMEQTgVADFAQKPIRE-----LSGGEQQRVYLAQAL 152
Cdd:cd03218 82 Q---EASIFrklTVEENIL---------AVLEIRGLSKKEREEKLEEL-LEEFHITHLRKskassLSGGERRRVEIARAL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 1119636415 153 AQQPRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGL 189
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGI 184
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-214 |
9.96e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 93.62 E-value: 9.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE---------LAQIMAVLP 80
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirqeagmVFQQFYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QktdqaftFTVEETVAFGryPFQT-GLFRQQTEKdeaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:PRK09493 91 H-------LTALENVMFG--PLRVrGASKEEAEK---QARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 160 FLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-190 |
1.37e-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: 93.12 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI-MAVLP 80
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QkTDQAF-TFTVEETVAFGRYPfqtglfRQQTEKDEAIVQEAMEQtgvadFaqkPI-RE--------LSGGEQQRVYLAQ 150
Cdd:COG0410 85 E-GRRIFpSLTVEENLLLGAYA------RRDRAEVRADLERVYEL-----F---PRlKErrrqragtLSGGEQQMLAIGR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1119636415 151 ALAQQPRILFLDEPTnfLDLA--YQKDLLDLIKRLtRESGLA 190
Cdd:COG0410 150 ALMSRPKLLLLDEPS--LGLAplIVEEIFEIIRRL-NREGVT 188
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
16-214 |
1.80e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 95.29 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE-----LAQIMAVLPQktdqaftFT 90
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQrpinmMFQSYALFPH-------MT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 91 VEETVAFGrypfqtgLFRQQTEKDE--AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFL 168
Cdd:PRK11607 108 VEQNIAFG-------LKQDKLPKAEiaSRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1119636415 169 DLA----YQKDLLDLIKRLtresGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK11607 181 DKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
12-241 |
3.00e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.23 E-value: 3.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTDQAFT-FT 90
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFVgAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 91 VEETVAFGrypfqtgLFRQQTEKDEAI--VQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFL 168
Cdd:PRK13642 99 VEDDVAFG-------MENQGIPREEMIkrVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 169 DLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASlYCDELMFMKNGTAGPKQKPE--YAVTEQSIKAVYDTDVTA 241
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIKEAAPSelFATSEDMVEIGLDVPFSS 245
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
16-214 |
3.28e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 93.61 E-value: 3.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRV---YLAGKLLADYKPKELAQIMAVLpQKTD-------- 84
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEKVLEKLVI-QKTRfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 85 ---------------QAFTFTVEETVAFGryPFQTGlfrqqTEKDEA--IVQEAMEQTGV-ADFAQKPIRELSGGEQQRV 146
Cdd:PRK13651 102 eirrrvgvvfqfaeyQLFEQTIEKDIIFG--PVSMG-----VSKEEAkkRAAKYIELVGLdESYLQRSPFELSGGQKRRV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 147 YLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-214 |
4.00e-21 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 95.52 E-value: 4.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLS----GGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK----EGRVYLAGKLLADYKPKELAQI 75
Cdd:COG4172 10 EDLSvafgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSERELRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 76 ------------MAVL-PQKT--DQaftftVEETVAFgrypfQTGLFRQQTEKdEAIvqEAMEQTGVADfAQKPIR---- 136
Cdd:COG4172 90 rgnriamifqepMTSLnPLHTigKQ-----IAEVLRL-----HRGLSGAAARA-RAL--ELLERVGIPD-PERRLDayph 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 137 ELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQG 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
14-215 |
6.40e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 92.39 E-value: 6.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 14 RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLL-ADYKPKELAqimaVLPQKTDQAFTF--- 89
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLK----PLRKKVGIVFQFpeh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 90 -----TVEETVAFGryPFQTGLFRqqtEKDEAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PRK13634 97 qlfeeTVEKDICFG--PMNFGVSE---EDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1119636415 164 PTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGT 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
6-214 |
6.96e-21 |
|
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: 93.25 E-value: 6.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 6 LSGGYGDSRLinNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYK-----PKELAQIMAVLP 80
Cdd:TIGR02142 5 FSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiflPPEKRRIGYVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTdqAFT-FTVEETVAFGrYPFQTGLFRQQteKDEAIVqeamEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:TIGR02142 83 EAR--LFPhLSVRGNLRYG-MKRARPSERRI--SFERVI----ELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 160 FLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDG 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-216 |
8.43e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.09 E-value: 8.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLAD-------YKPKE--L 72
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPedrrrigYLPEErgL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 73 AQIMAVLpqktDQAftftveetVAFGRYpfqTGLfrqqtEKDEAI--VQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQ 150
Cdd:COG4152 83 YPKMKVG----EQL--------VYLARL---KGL-----SKAEAKrrADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 151 ALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGlAAVsVF--HDLNTASLYCDELMFMKNGTA 216
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIREL-AAKG-TTV-IFssHQMELVEELCDRIVIINKGRK 207
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
1-229 |
1.01e-20 |
|
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: 90.82 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTL-----LHLLTGTLPAKEGRVYLAGKLLADYK--PKELA 73
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLlrslnRMNDLVPGVRIEGKVLFDGQDIYDKKidVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 74 QIMAVLPQKTDqAFTFTVEETVAFGrypfqtglFRQQTEKD----EAIVQEAMEQTG----VADFAQKPIRELSGGEQQR 145
Cdd:TIGR00972 82 RRVGMVFQKPN-PFPMSIYDNIAYG--------PRLHGIKDkkelDEIVEESLKKAAlwdeVKDRLHDSALGLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 146 VYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLtRESgLAAVSVFHDLNTASLYCDELMFMKNGTAgpkqkPEYA 225
Cdd:TIGR00972 153 LCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQEL-KKK-YTIVIVTHNMQQAARISDRTAFFYDGEL-----VEYG 225
|
....
gi 1119636415 226 VTEQ 229
Cdd:TIGR00972 226 PTEQ 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-214 |
1.27e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.45 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKlladykpkELAQIMAvlpQKT 83
Cdd:PRK10851 6 ANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT--------DVSRLHA---RDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 84 DQAFTF---------TVEETVAFGrypfQTGLFRQQTEKDEAIVQEAM---EQTGVADFAQKPIRELSGGEQQRVYLAQA 151
Cdd:PRK10851 75 KVGFVFqhyalfrhmTVFDNIAFG----LTVLPRRERPNAAAIKAKVTqllEMVQLAHLADRYPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1119636415 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-215 |
1.30e-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: 89.15 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 14 RLINNVSLTVEKGEFLGILGPNGSGKTT--LLHLLTGTLPAKEGRVYLAGKllaDYKPKELAQIMAVLPQKtDQAF-TFT 90
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTllNALAGRRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQD-DILHpTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 91 VEETVafgrypfqtglfrqqtekdeaivqeameqtgvaDFAQKpIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDL 170
Cdd:cd03213 99 VRETL---------------------------------MFAAK-LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1119636415 171 AYQKDLLDLIKRLtRESGLAAVSVFHDLnTASLY--CDELMFMKNGT 215
Cdd:cd03213 145 SSALQVMSLLRRL-ADTGRTIICSIHQP-SSEIFelFDKLLLLSQGR 189
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
17-211 |
1.43e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 92.10 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 17 NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKEL------AQIM-----AVL-PQKTd 84
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplrrrMQMVfqdpyASLnPRMT- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 85 qaftftVEETVAFgryPFQtgLFRQQTEKD-EAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:COG4608 114 ------VGDIIAE---PLR--IHGLASKAErRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1119636415 163 EPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFM 211
Cdd:COG4608 183 EPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVM 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-214 |
1.62e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.49 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLadYKPKELAQIMAV-LPQKTDQAFT-- 88
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVL--YFGKDIFQIDAIkLRKEVGMVFQqp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 89 -----FTVEETVAfgrYPFQTGLFRQQTEKDEaIVQEAMEQTG----VADFAQKPIRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:PRK14246 100 npfphLSIYDNIA---YPLKSHGIKEKREIKK-IVEECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 160 FLDEPTNFLDLAYQKDLLDLIKRLTREsgLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-199 |
1.71e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.54 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKEGRVYLAGKLLADYKPKElAQ---ImAV 78
Cdd:COG1129 6 EMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKstlmkilsgvyQPDSGEILLDGEPVRFRSPRD-AQaagI-AI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 LPQKTDQAFTFTVEETVAFGRYPFQTGLFRQQTEKDEAivQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRI 158
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRA--RELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1119636415 159 LFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLN 199
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLD 201
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
31-214 |
1.76e-20 |
|
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: 91.79 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 31 ILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE-----LAQIMAVLPQktdqaftFTVEETVAFGrypfqtg 105
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLrhinmVFQSYALFPH-------MTVEENVAFG------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 106 lFRQQTEKDEAI---VQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKR 182
Cdd:TIGR01187 67 -LKMRKVPRAEIkprVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKT 145
|
170 180 190
....*....|....*....|....*....|..
gi 1119636415 183 LTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:TIGR01187 146 IQEQLGITFVFVTHDQEEAMTMSDRIAIMRKG 177
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-214 |
1.79e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 90.52 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELA----------- 73
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafrrdiqmvfq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 74 -QIMAVLPQKtdqaftfTVEETVafgRYPFQTGLFRQQTEKdEAIVQEAMEQTGVAD-FAQKPIRELSGGEQQRVYLAQA 151
Cdd:PRK10419 97 dSISAVNPRK-------TVREII---REPLRHLLSLDKAER-LARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1119636415 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNG 228
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
15-214 |
1.91e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 90.14 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAkeGRVYLAGKLLADYKPKELAQI----MAVLPQKTDQAF--- 87
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDGKPVAPCALrgrkIATIMQNPRSAFnpl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 88 ----TFTVEETVAFGRypfqtglfrqqtEKDEAIVQEAMEQTGVADFAQKPIR---ELSGGEQQRVYLAQALAQQPRILF 160
Cdd:PRK10418 96 htmhTHARETCLALGK------------PADDATLTAALEAVGLENAARVLKLypfEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1119636415 161 LDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHG 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-170 |
2.45e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.21 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlpakegRVyLAGKLLAD----YKPKELaqIMAV 78
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKst------------llKI-LAGELEPDsgevSIPKGL--RIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 LPQKTDQAFTFTVEETVAFGRypfqTGLFRQQTEKDEAI---------------VQEAMEQTG----------------- 126
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVLDGD----AELRALEAELEELEaklaepdedlerlaeLQEEFEALGgweaearaeeilsglgf 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1119636415 127 VADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDL 170
Cdd:COG0488 142 PEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
12-214 |
3.32e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.19 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLL-ADYKPKELAQIMA----VLPQKTDQA 86
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQIRKkvglVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 87 FTFTVEETVAFGRYPFQTglfrqQTEKDEAIVQEAMEQTGVAD--FAQKPIrELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:PRK13649 99 FEETVLKDVAFGPQNFGV-----SQEEAEALAREKLALVGISEslFEKNPF-ELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1119636415 165 TNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKG 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-235 |
5.57e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.80 E-value: 5.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI-MAVL 79
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 80 PQKTDQAFTFTVEETVaFGRYPFQTGLFRQQtEKDEAivQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:PRK10895 84 PQEASIFRRLSVYDNL-MAVLQIRDDLSAEQ-REDRA--NELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119636415 160 FLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKPEYAVTEQSIKAVY 235
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-248 |
7.98e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.48 E-value: 7.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQImAVLPQKT 83
Cdd:PRK13537 11 RNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV-GVVPQFD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 84 DQAFTFTVEETV-AFGRYpfqTGLFRQQTekdEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:PRK13537 90 NLDPDFTVRENLlVFGRY---FGLSAAAA---RALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 163 EPTNFLDLAYQKDLLDLIKRLTrESGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKPEYAVTEQ---SIKAVYDTDV 239
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEigcDVIEIYGPDP 242
|
....*....
gi 1119636415 240 TALVHQSSP 248
Cdd:PRK13537 243 VALRDELAP 251
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1-235 |
1.00e-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: 87.71 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI-MAVL 79
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 80 PQKTDQAFTFTVEETVAfGRYPFQTGLFR-QQTEKDEAIvqeaMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRI 158
Cdd:TIGR04406 82 PQEASIFRKLTVEENIM-AVLEIRKDLDRaEREERLEAL----LEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 159 LFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKPEYAVTEQSIKAVY 235
Cdd:TIGR04406 157 ILLDEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVY 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
2-218 |
1.09e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.38 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLS---GGYGDSRLI-NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKlladykpkelaqimA 77
Cdd:COG4525 5 TVRHVSvryPGGGQPQPAlQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV--------------P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 78 VLPQKTDQAFTF---------TVEETVAFGrypFQ-TGLFRQQTEkdeAIVQEAMEQTGVADFAQKPIRELSGGEQQRVY 147
Cdd:COG4525 71 VTGPGADRGVVFqkdallpwlNVLDNVAFG---LRlRGVPKAERR---ARAEELLALVGLADFARRRIWQLSGGMRQRVG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119636415 148 LAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMkngTAGP 218
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM---SPGP 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
16-181 |
1.87e-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: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELA---QIMAVLPQKTDQAFTFTVE 92
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 93 ETVAFgryPFQ-TGLFRQQTEKDeaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLA 171
Cdd:cd03292 97 ENVAF---ALEvTGVPPREIRKR---VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170
....*....|
gi 1119636415 172 YQKDLLDLIK 181
Cdd:cd03292 171 TTWEIMNLLK 180
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-214 |
2.29e-19 |
|
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: 85.06 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 6 LSGGYGDSR--LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKpKELAQIMAVLPQKT 83
Cdd:cd03247 6 VSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQRP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 84 dqaftftveetvafgrYPFQTGLfrqqtekdeaivqeaMEQTGvadfaqkpiRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:cd03247 85 ----------------YLFDTTL---------------RNNLG---------RRFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1119636415 164 PTNFLDLAYQKDLLDLIKRLTRESGLAAVSvfHDLnTASLYCDELMFMKNG 214
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLKDKTLIWIT--HHL-TGIEHMDKILFLENG 172
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-171 |
2.48e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.12 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTllhlltgtlpakegrvyLAgKLLADykpkELAQimavlpqk 82
Cdd:COG0488 318 LEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKST-----------------LL-KLLAG----ELEP-------- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 83 tdQAFTFTVEETVAFGrYpfqtglFRQQTE--KDEAIVQEAMEQTG-----------VADF------AQKPIRELSGGEQ 143
Cdd:COG0488 368 --DSGTVKLGETVKIG-Y------FDQHQEelDPDKTVLDELRDGApggteqevrgyLGRFlfsgddAFKPVGVLSGGEK 438
|
170 180
....*....|....*....|....*...
gi 1119636415 144 QRVYLAQALAQQPRILFLDEPTNFLDLA 171
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDIE 466
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-220 |
3.02e-19 |
|
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: 90.19 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 3 AEGLSGGYGDSR--LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLP 80
Cdd:COG4618 333 VENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTdQAFTFTVEETVAfgrypfqtglfRQQTEKDEAIVqEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLA 149
Cdd:COG4618 413 QDV-ELFDGTIAENIA-----------RFGDADPEKVV-AAAKLAGVHEMILRlpdgydtRIGEggarLSGGQRQRIGLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119636415 150 QALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLyCDELMFMKNGTA---GPKQ 220
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA-VDKLLVLRDGRVqafGPRD 551
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-217 |
3.38e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 86.66 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKegrvylAGKLLADYKP----KELAQIM--- 76
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPS------AGELLAGTAPlaeaREDTRLMfqd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 77 -AVLPQKTdqaftftVEETVAFGRypfqTGLFRQQTEkdeaivqEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQ 155
Cdd:PRK11247 90 aRLLPWKK-------VIDNVGLGL----KGQWRDAAL-------QALAAVGLADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119636415 156 PRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGTAG 217
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIG 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
4.11e-19 |
|
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: 84.02 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKElaqimavlpq 81
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 ktdqaftftveetvafgrypfqtglfrqqtekdeaivqeaMEQTGVADFAQkpireLSGGEQQRVYLAQALAQQPRILFL 161
Cdd:cd03216 72 ----------------------------------------ARRAGIAMVYQ-----LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1119636415 162 DEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-214 |
4.76e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.38 E-value: 4.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAkEGRVYLAGKLLADYKPKELAQI---MAVLPQKTDQAF 87
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPLHNLNRRQLLPVrhrIQVVFQDPNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 88 T--FTVEETVAFGRYPFQTGLFRQQTEkdeAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:PRK15134 376 NprLNVLQIIEEGLRVHQPTLSAAQRE---QQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1119636415 165 TNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-214 |
6.72e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 87.44 E-value: 6.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 17 NNVSLTVEKGEFLGILGPNGSGKttllhlltgtlpakEGRVYLAGKLLADYKPKELAQI-----M-----AVLPQKTdqa 86
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKstlircinllerptSGSVLVDGVDLTALSERELRAArrkigMifqhfNLLSSRT--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 87 ftftVEETVAFgryPFQ-TGLFRQQTEKdeaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPT 165
Cdd:COG1135 99 ----VAENVAL---PLEiAGVPKAEIRK---RVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1119636415 166 NFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:COG1135 169 SALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENG 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-214 |
9.00e-19 |
|
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: 84.97 E-value: 9.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 9 GYGDSR-LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTdQAF 87
Cdd:cd03253 9 AYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDT-VLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 88 TFTVEETVAFGRyPFQTglfrqqtekDEAIVqEAMEQTGVADFAQK-P------IRE----LSGGEQQRVYLAQALAQQP 156
Cdd:cd03253 88 NDTIGYNIRYGR-PDAT---------DEEVI-EAAKAAQIHDKIMRfPdgydtiVGErglkLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTResGLAAVSVFHDLNTASlYCDELMFMKNG 214
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIV-NADKIIVLKDG 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-215 |
1.31e-18 |
|
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: 82.11 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTllhlltgtlpakegrvylagklladykpkeLAQIMAvlpq 81
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKST------------------------------LLKLIA---- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 ktdqaftftveetvafgrypfqtglfrQQTEKDEAIVqEAMEQTGVADFAQkpireLSGGEQQRVYLAQALAQQPRILFL 161
Cdd:cd03221 48 ---------------------------GELEPDEGIV-TWGSTVKIGYFEQ-----LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 162 DEPTNFLDLAYQKDLLDLIKRLtrESGLAAVSvfHD---LNTAslyCDELMFMKNGT 215
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEY--PGTVILVS--HDryfLDQV---ATKIIELEDGK 144
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-222 |
1.46e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.44 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 14 RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVylagkLLADYK-PKELAQIMAVLPQKTD-------- 84
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-----IVGDYAiPANLKKIKEVKRLRKEiglvfqfp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 85 --QAFTFTVEETVAFGryPFQTGLFRQQTEKDeaiVQEAMEQTGVA-DFAQKPIRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:PRK13645 100 eyQLFQETIEKDIAFG--PVNLGENKQEAYKK---VPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119636415 162 DEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKP 222
Cdd:PRK13645 175 DEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
10-214 |
6.03e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 82.75 E-value: 6.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLaDYKPKELAQIMAVLPQKTDQAFT- 88
Cdd:COG4161 12 YGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF-DFSQKPSEKAIRLLRQKVGMVFQq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 89 ------FTVEETVAfgRYPFQT-GLFRQQTeKDEAivQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:COG4161 91 ynlwphLTVMENLI--EAPCKVlGLSKEQA-REKA--MKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1119636415 162 DEPTNFLDLAYQKDLLDLIKRLTrESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:COG4161 166 DEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKG 217
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-215 |
6.31e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.77 E-value: 6.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE-----LAQIMAVLPQktd 84
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQrdicmVFQSYALFPH--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 85 qaftFTVEETVAFGrypfqtgLFRQQTEKDE--AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:PRK11432 93 ----MSLGENVGYG-------LKMLGVPKEErkQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1119636415 163 EPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-164 |
8.52e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.38 E-value: 8.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI-MAVLP 80
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QktdQAFTF---TVEETVAfgrypfqtgLFRQQTEKD----EAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALA 153
Cdd:COG1137 85 Q---EASIFrklTVEDNIL---------AVLELRKLSkkerEERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170
....*....|.
gi 1119636415 154 QQPRILFLDEP 164
Cdd:COG1137 153 TNPKFILLDEP 163
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-214 |
8.56e-18 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 82.28 E-value: 8.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTdqaFTF--TVEE 93
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDV---FLFndTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 94 TVAFGRypfqtglfrqqTEKDEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:cd03251 95 NIAYGR-----------PGATREEVEEAARAANAHEFIMElpegydtVIGErgvkLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1119636415 163 EPTNFLDLAYQKDLLDLIKRLTResGLAAVSVFHDLNTASlYCDELMFMKNG 214
Cdd:cd03251 164 EATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIE-NADRIVVLEDG 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
12-170 |
9.73e-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: 81.75 E-value: 9.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTdQAFTFTV 91
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEP-VLFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 92 EETVAFgrypfqtGLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRE-------LSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:cd03248 105 QDNIAY-------GLQSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEA 177
|
....*.
gi 1119636415 165 TNFLDL 170
Cdd:cd03248 178 TSALDA 183
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
10-214 |
1.11e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 81.98 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGK---LLADYKPKELAQimavLPQKTDQA 86
Cdd:PRK11124 12 YGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdFSKTPSDKAIRE----LRRNVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 87 FT-------FTVEETVAfgRYPFQT-GLfrqqtEKDEAIvQEAME---QTGVADFAQKPIRELSGGEQQRVYLAQALAQQ 155
Cdd:PRK11124 88 FQqynlwphLTVQQNLI--EAPCRVlGL-----SKDQAL-ARAEKlleRLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1119636415 156 PRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENG 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-231 |
1.21e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE-LAQIMA-VLPQKTDQAF-- 87
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDaVKKGMAyITESRRDNGFfp 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 88 TFTVEETVAF------GRYPFQTGLFRQQTEKDEAIVQEAMEQTGVADFAQKpIRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:PRK09700 355 NFSIAQNMAIsrslkdGGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQN-ITELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 162 DEPTNFLDLAYQKDLLDLIKRLTrESGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKPEYAVTEQSI 231
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEI 502
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-259 |
1.29e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.21 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLhlltgtlpaK---------EGRVYLAGklladYKP----KELA-QIMAVLPQ 81
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTI---------KmltgilvptSGEVRVLG-----YVPfkrrKEFArRIGVVFGQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KTDQAFTFTVEETvafgrypFQtgLFRQQTEKDEAIVQEAM----EQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPR 157
Cdd:COG4586 104 RSQLWWDLPAIDS-------FR--LLKAIYRIPDAEYKKRLdelvELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 158 ILFLDEPTNFLDLAYQKDLLDLIKRLTRESGlaaVSVF---HDLN-TASLyCDELMFMKNGtagpkqkpeyavteqsiKA 233
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNRERG---TTILltsHDMDdIEAL-CDRVIVIDHG-----------------RI 233
|
250 260
....*....|....*....|....*.
gi 1119636415 234 VYDTDVTALVHQSSPKPMIVIQPEKD 259
Cdd:COG4586 234 IYDGSLEELKERFGPYKTIVLELAEP 259
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-214 |
1.33e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 82.57 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGK-LLADYKPKELAQIMA----VLPQKTDQAFTFT 90
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhITPETGNKNLKKLRKkvslVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 91 VEETVAFGryPFQTGlFRQQTEKDEAIvqEAMEQTGVA-DFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK13641 103 VLKDVEFG--PKNFG-FSEDEAKEKAL--KWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1119636415 170 LAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-214 |
1.78e-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: 84.49 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLP--AKEGRVYLAGKLL--ADYKPKELAQIm 76
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLkaSNIRDTERAGI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 77 AVLPQKTDQAFTFTVEETVAFGRYPFQTGlfrQQTEKDEAIV--QEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALA 153
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPG---GRMAYNAMYLraKNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119636415 154 QQPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
17-209 |
1.88e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 84.47 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 17 NNVSLTVE-----KGEFLGILGPNGSGKTTLlhlltgtlpAKegrvYLAGKLLADYKPKELAQIMAVLPQKTDQAFTFTV 91
Cdd:PRK13409 351 GDFSLEVEggeiyEGEVIGIVGPNGIGKTTF---------AK----LLAGVLKPDEGEVDPELKISYKPQYIKPDYDGTV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 92 EEtvafgrypfqtgLFRQQTEK--DEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK13409 418 ED------------LLRSITDDlgSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1119636415 170 LAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELM 209
Cdd:PRK13409 486 VEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
15-202 |
1.91e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.02 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLL--------ADYKPKELA---QIMAVLPQkt 83
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssaakAELRNQKLGfiyQFHHLLPD-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 84 dqaftFTVEETVAFgryPFQTGLFRQQTEKDEAivQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PRK11629 102 -----FTALENVAM---PLLIGKKKPAEINSRA--LEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1119636415 164 PTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTAS 202
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAK 210
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-214 |
2.41e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.21 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLP--AKEGRVYLAGKLLADYKPKE--------LAQIMAVL 79
Cdd:PRK13549 15 FGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDteragiaiIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 80 PQktdqaftFTVEETVAFGRYPFQTGLFrqqteKDEAIVQEA---MEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:PRK13549 95 KE-------LSVLENIFLGNEITPGGIM-----DYDAMYLRAqklLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 157 RILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-214 |
2.62e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.09 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 13 SRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLL-ADYKPKELA----QIMAVLPQKTDQAF 87
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsSTSKQKEIKpvrkKVGVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 88 TFTVEETVAFGryPFQTGLFRQQTEKdeaIVQEAMEQTGVA-DFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:PRK13643 99 EETVLKDVAFG--PQNFGIPKEKAEK---IAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1119636415 167 FLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK13643 174 GLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
20-201 |
2.88e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.78 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 20 SLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKllaDYKPKELAQ-IMAVLPQKTDQAFTFTVEETVAFG 98
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ---DHTTTPPSRrPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 99 RYPfqtGL--FRQQTEKDEAIVQeameQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDL 176
Cdd:PRK10771 96 LNP---GLklNAAQREKLHAIAR----QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180
....*....|....*....|....*
gi 1119636415 177 LDLIKRLTRESGLAAVSVFHDLNTA 201
Cdd:PRK10771 169 LTLVSQVCQERQLTLLMVSHSLEDA 193
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
9-215 |
3.00e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.59 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 9 GYGDSRL--INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTDQA 86
Cdd:PRK10584 17 GQGEHELsiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 87 F----TFTVEETVAFgrypfqTGLFRQQTEKD-EAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:PRK10584 97 FmlipTLNALENVEL------PALLRGESSRQsRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1119636415 162 DEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASlYCDELMFMKNGT 215
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAA-RCDRRLRLVNGQ 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-190 |
3.15e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.53 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGygdsRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE-LAQIMAVL 79
Cdd:COG1129 257 LEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 80 PQ--KTDQAF-TFTVEETVAFGRYPFQT--GLFRQQTEKdeAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALA 153
Cdd:COG1129 333 PEdrKGEGLVlDLSIRENITLASLDRLSrgGLLDRRRER--ALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLA 410
|
170 180 190
....*....|....*....|....*....|....*..
gi 1119636415 154 QQPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsGLA 190
Cdd:COG1129 411 TDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKA 446
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-214 |
3.93e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 3.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 18 NVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE-LAQIMAVLPQKT-------DQAFTF 89
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRqssglylDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 90 TVEeTVAFGRYPFQtglfrQQTEKDEAIVQEAMEQTGVA-DFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFL 168
Cdd:PRK15439 361 NVC-ALTHNRRGFW-----IKPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1119636415 169 DLAYQKDLLDLIKRLTrESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK15439 435 DVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
20-209 |
4.34e-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: 83.68 E-value: 4.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 20 SLTVE-----KGEFLGILGPNGSGKTTLlhlltgtlpAKegrvYLAGKLLADYKPKELAQIMAVLPQKTDQAFTFTVEE- 93
Cdd:COG1245 355 SLEVEggeirEGEVLGIVGPNGIGKTTF---------AK----ILAGVLKPDEGEVDEDLKISYKPQYISPDYDGTVEEf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 94 -----TVAFGRYPFQTglfrqqtekdeaivqEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFL 168
Cdd:COG1245 422 lrsanTDDFGSSYYKT---------------EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1119636415 169 DLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELM 209
Cdd:COG1245 487 DVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-237 |
5.35e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.47 E-value: 5.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK-----EGRVYLAGKLLADYK---PKEL 72
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRvnlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 73 AQIMAVLPQKtdQAFTFTVEETVAFGrypFQTGLFRQQTEKDEaIVQEAMEQTGVADFAQKPIR----ELSGGEQQRVYL 148
Cdd:PRK14258 88 RQVSMVHPKP--NLFPMSVYDNVAYG---VKIVGWRPKLEIDD-IVESALKDADLWDEIKHKIHksalDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 149 AQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKPEYAVTE 228
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEFGLTK 241
|
....*....
gi 1119636415 229 QSIKAVYDT 237
Cdd:PRK14258 242 KIFNSPHDS 250
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1-208 |
5.40e-17 |
|
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: 79.07 E-value: 5.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPkELAQIMAVLP 80
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTDQAFTFTVEETVAFGRypfqtglfrqqTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:cd03231 80 HAPGIKTTLSVLENLRFWH-----------ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1119636415 161 LDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDEL 208
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-248 |
7.53e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.83 E-value: 7.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 14 RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK-----EGRVYLAGKLLADYKPKELAQI----MAVLPQKTD 84
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 85 QAFT--FTVE----ETVAFGRypfqtGLfRQQTEKDEAIvqEAMEQTGVADFAQK----PiRELSGGEQQRVYLAQALAQ 154
Cdd:PRK15134 103 VSLNplHTLEkqlyEVLSLHR-----GM-RREAARGEIL--NCLDRVGIRQAAKRltdyP-HQLSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 155 QPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQK-------PEYAVT 227
Cdd:PRK15134 174 RPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRaatlfsaPTHPYT 253
|
250 260
....*....|....*....|.
gi 1119636415 228 EQSIKAVYDTDVTALVHQSSP 248
Cdd:PRK15134 254 QKLLNSEPSGDPVPLPEPASP 274
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-214 |
1.10e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.15 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 6 LSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYkpkELAQIM----AVLPQ 81
Cdd:PRK11614 11 VSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QTAKIMreavAIVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KTDQAFTFTVEETVAFGRYPFQTGLFRQQTEKDEAIVQEAMEQTgvadfAQKPiRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:PRK11614 88 GRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERR-----IQRA-GTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1119636415 162 DEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-180 |
1.44e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.79 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRL--INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQ 81
Cdd:PRK11160 342 NNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KTDqAFTFTVEETVAFGrypfqtglfrQQTEKDEAIVqEAMEQTGVADFAQ--KPI--------RELSGGEQQRVYLAQA 151
Cdd:PRK11160 422 RVH-LFSATLRDNLLLA----------APNASDEALI-EVLQQVGLEKLLEddKGLnawlgeggRQLSGGEQRRLGIARA 489
|
170 180
....*....|....*....|....*....
gi 1119636415 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLI 180
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELL 518
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-223 |
2.14e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.49 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVlp 80
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 qKTDQAF----TFTVEET--VAFGRYpFQTGLFR--------QQTEKdEAIVQEA--MEQTGVADFAQKPIRELSGGEQQ 144
Cdd:PRK11300 84 -RTFQHVrlfrEMTVIENllVAQHQQ-LKTGLFSgllktpafRRAES-EALDRAAtwLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1119636415 145 RVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKPE 223
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-214 |
3.01e-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: 76.32 E-value: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGygdsRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI-MAVL 79
Cdd:cd03215 5 LEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 80 PqktdqaftftvEEtvafgryPFQTGLFRQQTEKDEAIVQeameqtgvadfaqkpiRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:cd03215 81 P-----------ED-------RKREGLVLDLSVAENIALS----------------SLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 160 FLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-214 |
3.12e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.92 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 18 NVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTdQAFTFTVEETVAF 97
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEP-VLFSGSVRENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 98 GRypfqtglfrQQTEKDEaiVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:TIGR00958 578 GL---------TDTPDEE--IMAAAKAANAHDFIMEfpngydtEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1119636415 167 FLDLAYQKDLLDLIKRltreSGLAAVSVFHDLNTASlYCDELMFMKNG 214
Cdd:TIGR00958 647 ALDAECEQLLQESRSR----ASRTVLLIAHRLSTVE-RADQILVLKKG 689
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-214 |
3.68e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 80.25 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK-EGRVYLAGKLLADYKP-KELAQIMAVLPQKTDQ---AFTFT 90
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPaQAIRAGIAMVPEDRKRhgiVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 91 VEETVAFGRYPFQTGLFRQQTEKDEAIVQEAMEQTGVADFAQK-PIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:TIGR02633 356 VGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFlPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1119636415 170 LAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
16-215 |
3.84e-16 |
|
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: 77.09 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLA---GKL-LADYKPKEL-----------AQIMAVLP 80
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdgGWVdLAQASPREIlalrrrtigyvSQFLRVIP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTdqaftftVEETVAfgrypfqTGLFRQQTEKDEAI--VQEAMEQTGV---------ADFaqkpirelSGGEQQRVYLA 149
Cdd:COG4778 107 RVS-------ALDVVA-------EPLLERGVDREEARarARELLARLNLperlwdlppATF--------SGGEQQRVNIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119636415 150 QALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:COG4778 165 RGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
5-219 |
3.88e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 78.85 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQ----IMAVL- 79
Cdd:PRK11308 20 GLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLlrqkIQIVFq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 80 -------PQKTDQAftfTVEETVAFgrypfQTGLFRQQ-TEKdeaiVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQ 150
Cdd:PRK11308 100 npygslnPRKKVGQ---ILEEPLLI-----NTSLSAAErREK----ALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIAR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119636415 151 ALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGTA---GPK 219
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCvekGTK 239
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
6-214 |
4.01e-16 |
|
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: 79.37 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 6 LSGGYGDSRLinNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYkpkelAQIMAVLPQKTDQ 85
Cdd:COG4148 7 FRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDS-----ARGIFLPPHRRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 86 AFTF---------TVEETVAFGRypFQTGLFRQQTEKDEAIvqeamEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:COG4148 80 GYVFqearlfphlSVRGNLLYGR--KRAPRAERRISFDEVV-----ELLGIGHLLDRRPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQG 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-214 |
4.41e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.07 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 17 NNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKEGRVYLAGKLLADYKPKE--------------LAQimavlpqk 82
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKstlmkilyglyQPDSGEILIDGKPVRIRSPRDaialgigmvhqhfmLVP-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 83 tdqafTFTVEETVAFGRYPfqTGLFRQQTEKDEAIVQEAMEQTGVA-DfAQKPIRELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:COG3845 94 -----NLTVAENIVLGLEP--TKGGRLDRKAARARIRELSERYGLDvD-PDAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1119636415 162 DEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:COG3845 166 DEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-214 |
5.88e-16 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 78.21 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRL-INNVSLTVEKGEFLGILGPNGSGKTTLLhlltgtlpaK---------EGRVYLAGKLLADYKPKEL- 72
Cdd:COG1125 5 ENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTL---------RminrlieptSGRILIDGEDIRDLDPVELr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 73 -------AQImAVLPqktdqafTFTVEETVAfgrypfqT--GLFRQQTEKDEAIVQEAMEQTG--VADFAQKPIRELSGG 141
Cdd:COG1125 76 rrigyviQQI-GLFP-------HMTVAENIA-------TvpRLLGWDKERIRARVDELLELVGldPEEYRDRYPHELSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 142 EQQRVYLAQALAQQPRILFLDEPtnF--LDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:COG1125 141 QQQRVGVARALAADPPILLMDEP--FgaLDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREG 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-200 |
6.07e-16 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 76.76 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSRLI-NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKEL-AQIMAVLPQKTdqAFT 88
Cdd:cd03252 12 PDGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLrRQVGVVLQENV--LFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 89 FTVEETVAFGRypfqTGLFRQQtekdeaiVQEAMEQTGVADFAQKpIRE------------LSGGEQQRVYLAQALAQQP 156
Cdd:cd03252 90 RSIRDNIALAD----PGMSMER-------VIEAAKLAGAHDFISE-LPEgydtivgeqgagLSGGQRQRIAIARALIHNP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1119636415 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTreSGLAAVSVFHDLNT 200
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLST 199
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-228 |
7.00e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.35 E-value: 7.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLaDYKPK---ELAQIMAVLPQKTDQA 86
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 87 FTFT-VEETVAFGrypfqtglFRQQTEKDEAI---VQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:PRK13638 90 IFYTdIDSDIAFS--------LRNLGVPEAEItrrVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 163 EPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVfHDLNTASLYCDELMFMKNGTAGPKQKPE--YAVTE 228
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQGNHVIISS-HDIDLIYEISDAVYVLRQGQILTHGAPGevFACTE 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-216 |
7.43e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 78.21 E-value: 7.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQImavlpqKTDQAFTF------ 89
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAV------RSDIQMIFqdplas 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 90 -----TVEETVAFGRYPFQTGLFRQQTeKDEaiVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PRK15079 111 lnprmTIGEIIAEPLRTYHPKLSRQEV-KDR--VKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1119636415 164 PTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGTA 216
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 240
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-165 |
7.85e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 76.69 E-value: 7.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELA--------QI 75
Cdd:COG4674 14 EDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIArlgigrkfQK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 76 MAVLPQktdqaftFTVEE----TVAFGRYPFQTgLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQA 151
Cdd:COG4674 94 PTVFEE-------LTVFEnlelALKGDRGVFAS-LFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGML 165
|
170
....*....|....
gi 1119636415 152 LAQQPRILFLDEPT 165
Cdd:COG4674 166 LAQDPKLLLLDEPV 179
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-201 |
8.10e-16 |
|
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: 75.47 E-value: 8.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPkELAQIMAVLPQK 82
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 83 TDQAFTFTVEETVAFGRYPFQTglfrqqtekDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:TIGR01189 82 PGLKPELSALENLHFWAAIHGG---------AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1119636415 163 EPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTA 201
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-169 |
1.61e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 76.23 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGK---------------TtllhlltgtlpAK-EGRVYLAGK-- 62
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKstllrclnrmndlipG-----------ARvEGEILLDGEdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 63 LLADYKPKEL-AQIMAVLPQKTdqAFTFTVEETVAFG-RYpfqTGLfRQQTEKDEaIVQEAMEQTG----VADFAQKPIR 136
Cdd:COG1117 81 YDPDVDVVELrRRVGMVFQKPN--PFPKSIYDNVAYGlRL---HGI-KSKSELDE-IVEESLRKAAlwdeVKDRLKKSAL 153
|
170 180 190
....*....|....*....|....*....|...
gi 1119636415 137 ELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-215 |
1.96e-15 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 75.34 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTdqaFTF--TVEE 93
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDT---FLFsgTIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 94 TVAFGRypfqtglfrqqTEKDEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:cd03254 96 NIRLGR-----------PNATDEEVIEAAKEAGAHDFIMKlpngydtVLGEnggnLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 163 EPTNFLD----LAYQKDLLDLIKRLTresglaAVSVFHDLNTAsLYCDELMFMKNGT 215
Cdd:cd03254 165 EATSNIDteteKLIQEALEKLMKGRT------SIIIAHRLSTI-KNADKILVLDDGK 214
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
12-196 |
2.15e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.31 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 12 DSRLINNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKEGRVYLagklladykPkELAQIMaVLPQKT-------D 84
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKstllraiaglwPYGSGRIAR---------P-AGARVL-FLPQRPylplgtlR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 85 QAFTftveetvafgrYPFQTGLFrqqtekDEAIVQEAMEQTGVADFAQKP------IRELSGGEQQRVYLAQALAQQPRI 158
Cdd:COG4178 444 EALL-----------YPATAEAF------SDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDW 506
|
170 180 190
....*....|....*....|....*....|....*...
gi 1119636415 159 LFLDEPTNFLDLAYQKDLLDLIKRLTRESGLaaVSVFH 196
Cdd:COG4178 507 LFLDEATSALDEENEAALYQLLREELPGTTV--ISVGH 542
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
11-214 |
2.26e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.38 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTDQAFTF- 89
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALm 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 90 ---TVEETVAFGrypFQTGLFRQQTEKDEAIvqEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:PRK10070 119 phmTVLDNTAFG---MELAGINAEERREKAL--DALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1119636415 167 FLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-231 |
2.52e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 75.33 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHL-----LTGTLPAKEGRVYLAGKLLADYKPKELAQI 75
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrliELYPEARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 76 MAVLPQKTDQAFTFTVEETVAFGryPFQTGLFRQQTEKDEAiVQEAMEQTG----VADFAQKPIRELSGGEQQRVYLAQA 151
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALG--LKLNRLVKSKKELQER-VRWALEKAQlwdeVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 152 LAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsgLAAVSVFHDLNTASLYCDELMFMKNGT---AGPKQ----KPEY 224
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQiveWGPTRevftNPRH 238
|
....*..
gi 1119636415 225 AVTEQSI 231
Cdd:PRK14247 239 ELTEKYV 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-228 |
2.58e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.92 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 14 RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVY-LAGKLLADY-KPKEL-----AQIMAVLPQKtdqa 86
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEWVDMtKPGPDgrgraKRYIGILHQE---- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 87 ftftveetvaFGRYPFQTGLfRQQTEK------DEAIVQEAMEQTGVADFAQKPIR--------ELSGGEQQRVYLAQAL 152
Cdd:TIGR03269 374 ----------YDLYPHRTVL-DNLTEAiglelpDELARMKAVITLKMVGFDEEKAEeildkypdELSEGERHRVALAQVL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119636415 153 AQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKPEYAVTE 228
Cdd:TIGR03269 443 IKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
12-214 |
3.47e-15 |
|
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: 74.88 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTdQAFTFTV 91
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEP-VLFDGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 92 EETVAFGRYPfqtglfRQQTEkdeaiVQEAMEQTGVADFAQK-PIR----------ELSGGEQQRVYLAQALAQQPRILF 160
Cdd:cd03249 94 AENIRYGKPD------ATDEE-----VEEAAKKANIHDFIMSlPDGydtlvgergsQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1119636415 161 LDEPTNFLDLAYQKDLLDLIKRLTResGLAAVSVFHDLNTASlYCDELMFMKNG 214
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIR-NADLIAVLQNG 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-214 |
3.53e-15 |
|
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: 74.49 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 8 GGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLAdykPKELAqiMAVLPQktdqaf 87
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS---LLGLG--GGFNPE------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 88 tFTVEETVAF-GRypfqtgLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:cd03220 99 -LTGRENIYLnGR------LLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1119636415 167 FLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:cd03220 172 VGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKG 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
17-214 |
3.61e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 76.38 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 17 NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELA----QIMAVLpqktdQAFTF--- 89
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRkarrQIGMIF-----QHFNLlss 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 90 -TVEETVAFgryPfqtgLFRQQTEKDE--AIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:PRK11153 97 rTVFDNVAL---P----LELAGTPKAEikARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1119636415 167 FLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK11153 170 ALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
13-214 |
8.11e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.62 E-value: 8.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 13 SRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPA---KEGRVYLAGKLLadyKPKELAQIMAVLPQktDQAF-- 87
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI---DAKEMRAISAYVQQ--DDLFip 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 88 TFTVEETVAFgrypfqTGLFR--QQTEKDE--AIVQEAMEQTGVADFAQKPI------RELSGGEQQRVYLAQALAQQPR 157
Cdd:TIGR00955 113 TLTVREHLMF------QAHLRmpRRVTKKEkrERVDEVLQALGLRKCANTRIgvpgrvKGLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119636415 158 ILFLDEPTNFLD--LAYQkdLLDLIKRLTrESGLAAVSVFHDlNTASLYC--DELMFMKNG 214
Cdd:TIGR00955 187 LLFCDEPTSGLDsfMAYS--VVQVLKGLA-QKGKTIICTIHQ-PSSELFElfDKIILMAEG 243
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-215 |
9.10e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.43 E-value: 9.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAG-KLLADYKPKELAQIMA----VLPQKTDQAFTFT 90
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKYIRPVRKrigmVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 91 VEETVAFGRYPFQTGLfrqQTEKDEAIvQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDL 170
Cdd:PRK13646 103 VEREIIFGPKNFKMNL---DEVKNYAH-RLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1119636415 171 AYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGS 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
10-223 |
1.06e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.85 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGK---LLADYK------PKELAQIMAVLP 80
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinLVRDKDgqlkvaDKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTDQAFTF----TVEETVAfgRYPFQTGLFRQQTEKDEAIvqEAMEQTGVADFAQ-KPIRELSGGEQQRVYLAQALAQQ 155
Cdd:PRK10619 95 TMVFQHFNLwshmTVLENVM--EAPIQVLGLSKQEARERAV--KYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 156 PRILFLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKPE 223
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPE 237
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-214 |
1.08e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 73.66 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEgRVYLAGKLLAD----YKPK----EL 72
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNP-EVTITGSIVYNghniYSPRtdtvDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 73 AQIMAVLPQKTDqAFTFTVEETVAFGrypfqtglFRQQTEKDEAIVQEAMEQT--------GVADFAQKPIRELSGGEQQ 144
Cdd:PRK14239 85 RKEIGMVFQQPN-PFPMSIYENVVYG--------LRLKGIKDKQVLDEAVEKSlkgasiwdEVKDRLHDSALGLSGGQQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 145 RVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSvfHDLNTASLYCDELMFMKNG 214
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT--RSMQQASRISDRTGFFLDG 223
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-229 |
1.09e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 73.72 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHL----LTGTLPAK-EGRVYLAGKLL--ADYKPKELAQIMAVLPQK 82
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrlLELNEEARvEGEVRLFGRNIysPDVDPIEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 83 TDQAFTFTVEETVAFG-RYpfqTGLFRQQTEKDEaIVQEAMEQTGVADFAQKPIRE----LSGGEQQRVYLAQALAQQPR 157
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGvKL---NGLVKSKKELDE-RVEWALKKAALWDEVKDRLNDypsnLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1119636415 158 ILFLDEPTNFLDLAYQKDLLDLIKRLTREsgLAAVSVFHDLNTASLYCDELMFMKNGT---AGPKQK----PEYAVTEQ 229
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKlieVGPTRKvfenPEHELTEK 246
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-214 |
1.12e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 73.63 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLaGKLLADyKPKELAQIMAVLPQKT 83
Cdd:PRK11264 7 KNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITID-TARSLSQQKGLIRQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 84 DQA-FTFTveetvAFGRYPFQTGL--------FRQQTEKDEAIV--QEAMEQTGVADFAQKPIRELSGGEQQRVYLAQAL 152
Cdd:PRK11264 85 QHVgFVFQ-----NFNLFPHRTVLeniiegpvIVKGEPKEEATAraRELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119636415 153 AQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESgLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
11-202 |
1.55e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.14 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPkELAQIMAVLPQ----KTDqa 86
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLGHqpgiKTE-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 87 ftFTVEETVAFgrypfqtgLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:PRK13538 89 --LTALENLRF--------YQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1119636415 167 FLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTAS 202
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVAS 194
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-198 |
1.58e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.39 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDS----RLINNVSLTVEKGEFLGILGPNGSGKTTLLHlltgtlpAKEGRVYLAGKLLAD---------- 66
Cdd:PRK11022 4 LNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSL-------AIMGLIDYPGRVMAEklefngqdlq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 67 -YKPKELAQI----MAVLPQK--TDQAFTFTVEETVAFGRYPFQTGlfRQQTEKDEAIvqEAMEQTGVADFAQK----Pi 135
Cdd:PRK11022 77 rISEKERRNLvgaeVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGG--NKKTRRQRAI--DLLNQVGIPDPASRldvyP- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1119636415 136 RELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDL 198
Cdd:PRK11022 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDL 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-210 |
2.07e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.89 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTL-----LHLLTGTLPAKEGRVYLAGKLL--ADYKPKELA 73
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTIlrcfnRLNDLIPGFRVEGKVTFHGKNLyaPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 74 QIMAVLPQKTDqAFTFTVEETVAFGryPFQTGLfrqQTEKDEaIVQEAMEQTGVADFAQKPIRE----LSGGEQQRVYLA 149
Cdd:PRK14243 91 RRIGMVFQKPN-PFPKSIYDNIAYG--ARINGY---KGDMDE-LVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119636415 150 QALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLaaVSVFHDLNTASLYCDELMF 210
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSDMTAF 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-202 |
2.12e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.83 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIM----AV 78
Cdd:PRK13539 5 GEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLghrnAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 LPqktdqafTFTVEETVAFGRypfqtGLFRQqtekDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRI 158
Cdd:PRK13539 85 KP-------ALTVAENLEFWA-----AFLGG----EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1119636415 159 LFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTAS 202
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHIPLGLPG 192
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-170 |
2.35e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 74.93 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVylagklladyKPKELAQImAVLPQk 82
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------KWSENANI-GYYAQ- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 83 tDQAFTFTVEETVafgrypFQ-TGLFRQQTEKDEAIvqeameqTGV-------ADFAQKPIRELSGGEQQRVYLAQALAQ 154
Cdd:PRK15064 390 -DHAYDFENDLTL------FDwMSQWRQEGDDEQAV-------RGTlgrllfsQDDIKKSVKVLSGGEKGRMLFGKLMMQ 455
|
170
....*....|....*.
gi 1119636415 155 QPRILFLDEPTNFLDL 170
Cdd:PRK15064 456 KPNVLVMDEPTNHMDM 471
|
|
| CbiZ |
COG1865 |
Adenosylcobinamide amidohydrolase [Coenzyme transport and metabolism]; |
276-440 |
2.68e-14 |
|
Adenosylcobinamide amidohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 441470 Cd Length: 224 Bit Score: 71.83 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 276 RDDILLQTEIPLRTLSSTPIGAGFSWSRTLIHKRLP---DQPDPIEGLTACLSESGFQLQETCAMASSERLDHFVYRTYE 352
Cdd:COG1865 11 DGVLVVRFPGPRRVLSTAVLNGGLREARAVFNHQVPedyDRTDPEEYLAEVLARLGLPPGDTVGLLTAADMENAAIAEES 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 353 DGELSVFICVQTGFS------------------------IWILINGYAADQFFIKALM-AAEAeRTKVLGD--------- 398
Cdd:COG1865 91 FGGLSVTAVVTAGVSnavragadpasyyeprppppgtinIIVLINAPLSDGALVNAVItATEA-KTAALQElgigsrysg 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1119636415 399 GRGTG---D-ILIAATqtqQSENIEQ------RLNQLIKKGTAECVKEAAEL 440
Cdd:COG1865 170 GLATGtgtDaIAVAAP---PDGEPLTyagkhtKLGELIGRAVYEAVREALRR 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-194 |
4.25e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.88 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSG-GygdsrlINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE-LAQIMAV 78
Cdd:PRK10762 258 LKVDNLSGpG------VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 LPQ--KTDQ-AFTFTVEETVAFgrypfqTGLfrQQTEKDEAIVQEAMEQTGVADFAQ----------KPIRELSGGEQQR 145
Cdd:PRK10762 332 ISEdrKRDGlVLGMSVKENMSL------TAL--RYFSRAGGSLKHADEQQAVSDFIRlfniktpsmeQAIGLLSGGNQQK 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1119636415 146 VYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSV 194
Cdd:PRK10762 404 VAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILV 451
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-220 |
4.69e-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: 71.67 E-value: 4.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 20 SLTVEKGEF-----LGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLAdYKPKelaQIMAVLPQKTDQaftFTVEET 94
Cdd:cd03237 14 TLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQ---YIKADYEGTVRD---LLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 95 VAFGRYP-FQTglfrqqtekdeaivqEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQ 173
Cdd:cd03237 87 KDFYTHPyFKT---------------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1119636415 174 KDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFM-----KNGTAGPKQ 220
Cdd:cd03237 152 LMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFegepsVNGVANPPQ 203
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-289 |
6.82e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.74 E-value: 6.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLL----------ADYKPKELAQI----MAVLPQ 81
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrsrqvielSEQSAAQMRHVrgadMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 K--TDQAFTFTVEETVAfgrypfQTGLFRQQTEKDEAIVQ--EAMEQTGVAD----FAQKPiRELSGGEQQRVYLAQALA 153
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIA------ESIRLHQGASREEAMVEakRMLDQVRIPEaqtiLSRYP-HQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 154 QQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGTA---GPKQK----PEYAV 226
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAvetGSVEQifhaPQHPY 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1119636415 227 TEQSIKAVydTDVTALVHQSSPK--PMIVI-QPEKDSVKQQS---IPFEALLQAgRDdilLQTEIPLRT 289
Cdd:PRK10261 265 TRALLAAV--PQLGAMKGLDYPRrfPLISLeHPAKQEPPIEQdtvVDGEPILQV-RN---LVTRFPLRS 327
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-214 |
7.13e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 71.27 E-value: 7.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 14 RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKL---LADYKpkeLAQIMAVLPQ--KTDQAFT 88
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYK---RAKYIGRVFQdpMMGTAPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 89 FTVEE--TVAFGRyPFQTGLFRQQTEKDEAIVQEAMEQT--GVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:COG1101 97 MTIEEnlALAYRR-GKRRGLRRGLTKKRRELFRELLATLglGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1119636415 165 TNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:COG1101 176 TAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-185 |
1.31e-13 |
|
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: 72.93 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLI-NNVSLTVEKGEFLGILGPNGSGKTTLlhlltgtlpAK---------EGRVYLAGKLLADYKPKELA 73
Cdd:COG5265 361 ENVSFGYDPERPIlKGVSFEVPAGKTVAIVGPSGAGKSTL---------ARllfrfydvtSGRILIDGQDIRDVTQASLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 74 QIMAVLPQKTdQAFTFTVEETVAFGRypfqtglfrqqTEKDEAIVQEAMEQTGVADFaqkpIRE---------------L 138
Cdd:COG5265 432 AAIGIVPQDT-VLFNDTIAYNIAYGR-----------PDASEEEVEAAARAAQIHDF----IESlpdgydtrvgerglkL 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1119636415 139 SGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTR 185
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR 542
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
11-196 |
1.32e-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: 69.09 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK--EGRVYLAGKLLADYKPKELAQiMAVlpqktdqaft 88
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPEERAR-LGI---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 89 ftveeTVAFgrypfqtglfrqqtekdeaivQEAMEQTGV--ADFaqkpIREL----SGGEQQRVYLAQALAQQPRILFLD 162
Cdd:cd03217 80 -----FLAF---------------------QYPPEIPGVknADF----LRYVnegfSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190
....*....|....*....|....*....|....
gi 1119636415 163 EPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFH 196
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKL-REEGKSVLIITH 162
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
10-214 |
2.50e-13 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 69.83 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLL------------ADykPKELAQIMA 77
Cdd:COG4598 18 FGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgelvpAD--RRQLQRIRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 78 VLpqktdqAFTF---------TVEETVAFGryPFQTglfrQQTEKDEAIVQ-EAM-EQTGVADFAQKPIRELSGGEQQRV 146
Cdd:COG4598 96 RL------GMVFqsfnlwshmTVLENVIEA--PVHV----LGRPKAEAIERaEALlAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 147 YLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQG 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-194 |
5.42e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.73 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 14 RLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLP-AKEGRVYLAGKLLADYKPKE-LAQIMAVLPQ--KTD----- 84
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQaIAQGIAMVPEdrKRDgivpv 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 85 ----QAFTFTVEETVAFGRypfqtglfRQQTEKDEAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:PRK13549 356 mgvgKNITLAALDRFTGGS--------RIDDAAELKTILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190
....*....|....*....|....*....|....*
gi 1119636415 160 FLDEPTNFLDLAYQKDLLDLIKRLTREsGLAAVSV 194
Cdd:PRK13549 428 ILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVI 461
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-169 |
5.57e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 70.73 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTllhlltgtlpakegrvylagklladykpkeLAQIMAvlP 80
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKST------------------------------LFRMIT--G 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTDQAFTFTVEETVAFGrYPFQTglfRQQTEKDEAIVQEAME-----QTG---------VADFA------QKPIRELSG 140
Cdd:TIGR03719 371 QEQPDSGTIEIGETVKLA-YVDQS---RDALDPNKTVWEEISGgldiiKLGkreipsrayVGRFNfkgsdqQKKVGQLSG 446
|
170 180
....*....|....*....|....*....
gi 1119636415 141 GEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-215 |
5.66e-13 |
|
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: 67.90 E-value: 5.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTdQAFTFTVEETV 95
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDP-VLFSGTIRSNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 96 A-FGRYPfqtglfrqqtekDEAIvQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:cd03244 99 DpFGEYS------------DEEL-WQALERVGLKEFVESlpggldtVVEEggenLSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1119636415 164 PTNFLDlaYQKDllDLIKRLTRESgLAAVSVF---HDLNTAsLYCDELMFMKNGT 215
Cdd:cd03244 166 ATASVD--PETD--ALIQKTIREA-FKDCTVLtiaHRLDTI-IDSDRILVLDKGR 214
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1-214 |
9.03e-13 |
|
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: 67.05 E-value: 9.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGD--SRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAV 78
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 LPQKTdQAFTFTVEETV-AFGRYpfqtglfrqqtekDEAIVQEAMEQTGVADfaqkpirELSGGEQQRVYLAQALAQQPR 157
Cdd:cd03369 87 IPQDP-TLFSGTIRSNLdPFDEY-------------SDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1119636415 158 ILFLDEPTNFLDlaYQKDLldLIKRLTRE--SGLAAVSVFHDLNTAsLYCDELMFMKNG 214
Cdd:cd03369 146 VLVLDEATASID--YATDA--LIQKTIREefTNSTILTIAHRLRTI-IDYDKILVMDAG 199
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-197 |
1.22e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.90 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE-----LAQIMAVLPQktd 84
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAErgvgmVFQSYALYPH--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 85 qaftFTVEETVAFgrypfqtGLFRQQTEKDEaiVQEAMEQtgVADFAQ-------KPiRELSGGEQQRVYLAQALAQQPR 157
Cdd:PRK11000 90 ----LSVAENMSF-------GLKLAGAKKEE--INQRVNQ--VAEVLQlahlldrKP-KALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1119636415 158 ILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHD 197
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHD 193
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
11-214 |
1.24e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.60 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLpAKEGRV----YLAGKLLADYKPKELAQIMAvlpqktdqa 86
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIggsaTFNGREILNLPEKELNKLRA--------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 87 ftftveETVAFgryPFQ---TGL------FRQQTE---------KDEAiVQEAMEQTGVADF--AQKPIR----ELSGGE 142
Cdd:PRK09473 97 ------EQISM---IFQdpmTSLnpymrvGEQLMEvlmlhkgmsKAEA-FEESVRMLDAVKMpeARKRMKmyphEFSGGM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119636415 143 QQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-296 |
1.28e-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: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 14 RLINNVSLTVEKGEFLGILGPNGSGKTTLlhlltgtlpAK-------------EGRVYLAGKLLADYKPKELAQIM---- 76
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLI---------AKaicgitkdnwhvtADRFRWNGIDLLKLSPRERRKIIgrei 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 77 AVL---------PQKT--DQaftftVEETVAFGRYpfqTGLF--RQQTEKDEAIvqEAMEQTGVADfaQKPIR-----EL 138
Cdd:COG4170 92 AMIfqepsscldPSAKigDQ-----LIEAIPSWTF---KGKWwqRFKWRKKRAI--ELLHRVGIKD--HKDIMnsyphEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 139 SGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGtagp 218
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCG---- 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 219 kQKPEYAVTEQSIKAVYDTDVTALVHqSSPKpmiviqpekdsvKQQSIPFEALLQAgrddilLQTEIPlrTLSSTPIG 296
Cdd:COG4170 236 -QTVESGPTEQILKSPHHPYTKALLR-SMPD------------FRQPLPHKSRLNT------LPGSIP--PLQHLPIG 291
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-196 |
1.84e-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: 69.06 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLL--TGTLPAKEGRV-----------YL-------- 59
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgYVerpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 60 -----AGKL---------LADYKPKELAQIMAVLPQKTdqaFTFTVEETVAFGrypFQTGLFRQQTEKDEAIVQ--EAME 123
Cdd:TIGR03269 81 pcpvcGGTLepeevdfwnLSDKLRRRIRKRIAIMLQRT---FALYGDDTVLDN---VLEALEEIGYEGKEAVGRavDLIE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1119636415 124 QTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFH 196
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-209 |
2.15e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.90 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 2 KAEGLS--GGYGDSRLiNNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI-MAV 78
Cdd:COG3845 259 EVENLSvrDDRGVPAL-KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 LP---QKTDQAFTFTVEETVAFGRY---PFQTGLF-RQQTEKDEAivQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQ 150
Cdd:COG3845 338 IPedrLGRGLVPDMSVAENLILGRYrrpPFSRGGFlDRKAIRAFA--EELIEEFDVrTPGPDTPARSLSGGNQQKVILAR 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119636415 151 ALAQQPRILFLDEPTNFLDLA-----YQKdLLDLikrltRESGLAAVSVFHDLntaslycDELM 209
Cdd:COG3845 416 ELSRDPKLLIAAQPTRGLDVGaiefiHQR-LLEL-----RDAGAAVLLISEDL-------DEIL 466
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-198 |
3.05e-12 |
|
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: 66.24 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 22 TVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRV-----------YLAGKLLADYKPKELAQIM--AVLPQKTDQ--- 85
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNYFTKLLEGDVkvIVKPQYVDLipk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 86 AFTFTVEEtvafgrypfqtgLFRQQTEKDEaiVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPT 165
Cdd:cd03236 102 AVKGKVGE------------LLKKKDERGK--LDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|...
gi 1119636415 166 NFLDLAYQKDLLDLIKRLTREsGLAAVSVFHDL 198
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAED-DNYVLVVEHDL 199
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
11-214 |
3.19e-12 |
|
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: 68.20 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSR-LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKpkeLAQIMAVLPQKTDQAFTF 89
Cdd:TIGR02203 342 GRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLRRQVALVSQDVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 90 --TVEETVAFGRypfqtglfrqQTEKDEAIVQEAMEQTGVADFA-------QKPIRE----LSGGEQQRVYLAQALAQQP 156
Cdd:TIGR02203 419 ndTIANNIAYGR----------TEQADRAEIERALAAAYAQDFVdklplglDTPIGEngvlLSGGQRQRLAIARALLKDA 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTResGLAAVSVFHDLNTASlYCDELMFMKNG 214
Cdd:TIGR02203 489 PILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIE-KADRIVVMDDG 543
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-214 |
3.25e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.18 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRV-----YLAGKLLADYKP-----------KELAQIMAVL 79
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiYIGDKKNNHELItnpyskkiknfKELRRRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 80 PQKTD-QAFTFTVEETVAFGryPFQTGLFRQQTEKDEAIVQEAMeqtGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPR 157
Cdd:PRK13631 122 FQFPEyQLFKDTIEKDIMFG--PVALGVKKSEAKKLAKFYLNKM---GLdDSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 158 ILFLDEPTNFLDLAYQKDLLDLIKRlTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
137-246 |
4.90e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 66.75 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 137 ELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG-- 214
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGqt 237
|
90 100 110
....*....|....*....|....*....|....*..
gi 1119636415 215 --TAGPKQ---KPEYAVTEQSIKAVYDTDvTALVHQS 246
Cdd:PRK15093 238 veTAPSKElvtTPHHPYTQALIRAIPDFG-SAMPHKS 273
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-198 |
8.13e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.17 E-value: 8.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI---MAVLPQ 81
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVrkrMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 kTDQAFT-FTVEETVAfgrYPfqtglFRQQTEKDEAIVQEA----MEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:PRK11831 92 -SGALFTdMNVFDNVA---YP-----LREHTQLPAPLLHSTvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1119636415 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDL 198
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDV 204
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-231 |
1.21e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGygdsRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE-LAQIMAVL 79
Cdd:PRK11288 258 LRLDGLKGP----GLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaIRAGIMLC 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 80 PQ--KTDQAF-TFTVEETVAFG--RYPFQTGLF-RQQTEKDEA---IVQEAMEQTGvadfAQKPIRELSGGEQQRVYLAQ 150
Cdd:PRK11288 334 PEdrKAEGIIpVHSVADNINISarRHHLRAGCLiNNRWEAENAdrfIRSLNIKTPS----REQLIMNLSGGNQQKAILGR 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 151 ALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTrESGLAAVSVFHDLNTASLYCDELMFMKNG-TAGPKQKPEyaVTEQ 229
Cdd:PRK11288 410 WLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGrIAGELAREQ--ATER 486
|
..
gi 1119636415 230 SI 231
Cdd:PRK11288 487 QA 488
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
9-197 |
1.55e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 66.29 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 9 GYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQImavlpqkTDQAFT 88
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL-------RREHFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 89 FTveetvaFGRYPFQTGLFRQQ------------TEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:PRK10535 90 FI------FQRYHLLSHLTAAQnvevpavyagleRKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1119636415 157 RILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHD 197
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHD 203
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-198 |
1.98e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.99 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 22 TVEKGEFLGILGPNGSGKTTLLHL----------LTGTLPAKEgRV--YLAGKLLADYKpKELA--QIMAVL-PQKTDQ- 85
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKIlsgelipnlgDYEEEPSWD-EVlkRFRGTELQNYF-KKLYngEIKVVHkPQYVDLi 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 86 --AFTFTVEEtvafgrypfqtgLFRQQTEKDeaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PRK13409 173 pkVFKGKVRE------------LLKKVDERG--KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....*.
gi 1119636415 164 PTNFLDLaYQK-DLLDLIKRLTRESglAAVSVFHDL 198
Cdd:PRK13409 239 PTSYLDI-RQRlNVARLIRELAEGK--YVLVVEHDL 271
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-215 |
2.21e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI-MAVL 79
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 80 PQKTDQAFTFTVEETVAFGRYPFQT--GLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPR 157
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKKvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 158 ILFLDEPTNFLDLAyQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:PRK09700 166 VIIMDEPTSSLTNK-EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGS 222
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
9-202 |
2.44e-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: 65.92 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 9 GYGdSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTdQAFT 88
Cdd:TIGR01193 484 GYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEP-YIFS 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 89 FTVEETVAFGRYPfqtGLFRQQTEKDEAIVQ-----EAMEQTGVADFAQKPiRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:TIGR01193 562 GSILENLLLGAKE---NVSQDEIWAACEIAEikddiENMPLGYQTELSEEG-SSISGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190
....*....|....*....|....*....|....*....
gi 1119636415 164 PTNFLDLAYQKDLLDLIKRLTRESglaAVSVFHDLNTAS 202
Cdd:TIGR01193 638 STSNLDTITEKKIVNNLLNLQDKT---IIFVAHRLSVAK 673
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-196 |
3.55e-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: 61.40 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYlagklladyKPkELAQIMaVLPQKTdqaftftveet 94
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG---------MP-EGEDLL-FLPQRP----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 95 vafgrYpFQTGLFRQQtekdeaIVqeameqtgvadfaqKP-IRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQ 173
Cdd:cd03223 74 -----Y-LPLGTLREQ------LI--------------YPwDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180
....*....|....*....|...
gi 1119636415 174 KDLLDLIKrltrESGLAAVSVFH 196
Cdd:cd03223 128 DRLYQLLK----ELGITVISVGH 146
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-214 |
4.16e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.55 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 5 GLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE-LAQIMAVLPQKT 83
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 84 DQAFTFTVEETVAFGRYPFQTGLFRQQTEKDEAivQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PRK11288 89 HLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEA--REQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1119636415 164 PTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-211 |
5.16e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.76 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLAdykPKELAQ-----IMA 77
Cdd:NF033858 269 ARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDIATrrrvgYMS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 78 vlpqktdQAFTFTVEETV-------AfgRypfqtgLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQ 150
Cdd:NF033858 346 -------QAFSLYGELTVrqnlelhA--R------LFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAV 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119636415 151 ALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGlaaVSVF---HDLNTAsLYCDELMFM 211
Cdd:NF033858 411 AVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDG---VTIFistHFMNEA-ERCDRISLM 470
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-198 |
5.31e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.42 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 22 TVEKGEFLGILGPNGSGKTTLLHL----------LTGTLPAKEgRV--YLAGKLLADYKpKELA--QIMAVL-PQKTDQ- 85
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKIlsgelkpnlgDYDEEPSWD-EVlkRFRGTELQDYF-KKLAngEIKVAHkPQYVDLi 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 86 --AFTFTVEEtvafgrypfqtgLFRQQTEKDeaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:COG1245 173 pkVFKGTVRE------------LLEKVDERG--KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....*.
gi 1119636415 164 PTNFLDLaYQK-DLLDLIKRLTREsGLAAVSVFHDL 198
Cdd:COG1245 239 PSSYLDI-YQRlNVARLIRELAEE-GKYVLVVEHDL 272
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-169 |
9.92e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 9.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 6 LSGGY---GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLladykpkelaqIMAVLPQK 82
Cdd:PRK11147 6 IHGAWlsfSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDL-----------IVARLQQD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 83 TDQAFTFTVEETVAFG---------RY----------PFQTGLFRQQTEKD----------EAIVQEAMEQTGVAdfAQK 133
Cdd:PRK11147 75 PPRNVEGTVYDFVAEGieeqaeylkRYhdishlvetdPSEKNLNELAKLQEqldhhnlwqlENRINEVLAQLGLD--PDA 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 1119636415 134 PIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK11147 153 ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-215 |
1.53e-10 |
|
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: 60.81 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI----MAVLPQKTdQAFTFTV 91
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKP-WLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 92 EETVAFGRyPFQTGLFRQQTekDEAIVQEAMEQTGVADfaQKPIRE----LSGGEQQRVYLAQALAQQPRILFLDEPTNF 167
Cdd:cd03290 96 EENITFGS-PFNKQRYKAVT--DACSLQPDIDLLPFGD--QTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1119636415 168 LDLAYQKDLLDL-IKRLTRESGLAAVSVFHDLNTASlYCDELMFMKNGT 215
Cdd:cd03290 171 LDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLP-HADWIIAMKDGS 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-215 |
1.60e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 61.25 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 17 NNVSLTVEKGEFLGILGPNGSGKttllhlltgtlPAKEGRVYLAGK---LLadykpkELAqiMAVLPQktdqaftFTVEE 93
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKstllkliagilEPTSGRVEVNGRvsaLL------ELG--AGFHPE-------LTGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 94 TVAF-GRYpfqTGLFRQQTekdEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAY 172
Cdd:COG1134 108 NIYLnGRL---LGLSRKEI---DEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAF 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1119636415 173 QKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:COG1134 182 QKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-214 |
1.73e-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: 63.49 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLaDYKPKELAQIMAVLPQKTDQAFTFTVEETV 95
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 96 AFgrypfqTGLFRQQTEKDEAIVQEAM-EQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQK 174
Cdd:TIGR01257 1025 LF------YAQLKGRSWEEAQLEMEAMlEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1119636415 175 DLLDLIkrLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:TIGR01257 1099 SIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-234 |
2.05e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.27 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVY-----LAGKLLADYKPK-ELAQ 74
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIFNYRDVlEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 75 IMAVLPQKTDqAFTFTVEETVAFGRYPFQTgLFRQQTEkdeAIVQEAMEQTGVAD-----FAQKPIReLSGGEQQRVYLA 149
Cdd:PRK14271 102 RVGMLFQRPN-PFPMSIMDNVLAGVRAHKL-VPRKEFR---GVAQARLTEVGLWDavkdrLSDSPFR-LSGGQQQLLCLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 150 QALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTREsgLAAVSVFHDLNTASLYCDELMFMKNG---TAGPKQK----P 222
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGrlvEEGPTEQlfssP 253
|
250
....*....|..
gi 1119636415 223 EYAVTEQSIKAV 234
Cdd:PRK14271 254 KHAETARYVAGL 265
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-218 |
2.95e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.11 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGK-------------LLADY 67
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGiklgyfaqhqlefLRADE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 68 KPkeLAQIMAVLPQKTDQAFTFTVeetvafGRYPFQtglfrqqtekdeaivqeameqtgvADFAQKPIRELSGGEQQRVY 147
Cdd:PRK10636 393 SP--LQHLARLAPQELEQKLRDYL------GGFGFQ------------------------GDKVTEETRRFSGGEKARLV 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119636415 148 LAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIkrLTRESGLAAVSvfHDLNTASLYCDELMFMKNGTAGP 218
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL--IDFEGALVVVS--HDRHLLRSTTDDLYLVHDGKVEP 507
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-169 |
3.92e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLhlltgtlpakegrvylagKLLADykpkelaqimavlpQK 82
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLF------------------KMITG--------------QE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 83 TDQAFTFTVEETVAFGrYPFQtglFRQQTEKDEAIVQEAME-----QTG---------VADFA------QKPIRELSGGE 142
Cdd:PRK11819 375 QPDSGTIKIGETVKLA-YVDQ---SRDALDPNKTVWEEISGgldiiKVGnreipsrayVGRFNfkggdqQKKVGVLSGGE 450
|
170 180
....*....|....*....|....*..
gi 1119636415 143 QQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-169 |
4.37e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 3 AEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYkpkeLAQIMAVL-PQ 81
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAY----FDQHRAELdPE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KtdqaftfTVEETVAFGRypfqtglfrqqtekdeaivQEAMeQTGVA--------DF------AQKPIRELSGGEQQRVY 147
Cdd:PRK11147 398 K-------TVMDNLAEGK-------------------QEVM-VNGRPrhvlgylqDFlfhpkrAMTPVKALSGGERNRLL 450
|
170 180
....*....|....*....|..
gi 1119636415 148 LAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLD 472
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-198 |
5.64e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.12 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGY-GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE---LAQIM 76
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 77 AVLPQKTDQAFTFTVEETVAFgryPFQTGlfRQQTEKDEAIVQEAMEQTGVADFAQK-PIrELSGGEQQRVYLAQALAQQ 155
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAI---PLIIA--GASGDDIRRRVSAALDKVGLLDKAKNfPI-QLSGGEQQRVGIARAVVNK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1119636415 156 PRILFLDEPTNFLDLAYQKDLLDLIKRLTReSGLAAVSVFHDL 198
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDI 197
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-216 |
6.20e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 60.63 E-value: 6.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKElaqimavlpqkTDQAFTF- 89
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-----------RDIAMVFq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 90 --------TVEETVAFGrypfqtgLFRQQTEKDE--AIVQEAMEQTGVADFAQ-KPiRELSGGEQQRVYLAQALAQQPRI 158
Cdd:PRK11650 84 nyalyphmSVRENMAYG-------LKIRGMPKAEieERVAEAARILELEPLLDrKP-RELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 159 LFLDEPTNFLD--LAYQKDLldLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNGTA 216
Cdd:PRK11650 156 FLFDEPLSNLDakLRVQMRL--EIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-198 |
7.00e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTDQAFTFTV 91
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNNTDMLSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 92 EETvaFGRYPFQTglfRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLA 171
Cdd:PRK10938 95 EDD--TGRTTAEI---IQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190
....*....|....*....|....*....|
gi 1119636415 172 YQKDLLDLIKRLTREsGLAAVSV---FHDL 198
Cdd:PRK10938 170 SRQQLAELLASLHQS-GITLVLVlnrFDEI 198
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-291 |
8.42e-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: 61.18 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 13 SRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADyKPKELAQIMAVLPQktdqaftFTVE 92
Cdd:TIGR01257 1952 SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQ-------FDAI 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 93 ETVAFGR-----YPFQTGLFRQQTEKdeaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNF 167
Cdd:TIGR01257 2024 DDLLTGRehlylYARLRGVPAEEIEK---VANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 168 LDLAYQKDLLDLIKRLTREsGLAAVSVFHDLNTASLYCDELMFMKNGTAgpkqkpEYAVTEQSIKAVYDTDVTALVHQSS 247
Cdd:TIGR01257 2101 MDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAF------QCLGTIQHLKSKFGDGYIVTMKIKS 2173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1119636415 248 PKPMIViqPEKDSVKQ--QSiPFEALLQAGRDDILLQTEIPLRTLS 291
Cdd:TIGR01257 2174 PKDDLL--PDLNPVEQffQG-NFPGSVQRERHYNMLQFQVSSSSLA 2216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-184 |
1.08e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.42 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKTdQAFTFTVEETV 95
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNV-HLFNDTIANNI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 96 AFGRYPFQTglfRQQTEKdEAIVQEAMeqtgvaDFAQK-------PIRE----LSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:PRK11176 438 AYARTEQYS---REQIEE-AARMAYAM------DFINKmdngldtVIGEngvlLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180
....*....|....*....|....
gi 1119636415 165 TNFLD----LAYQKDLLDLIKRLT 184
Cdd:PRK11176 508 TSALDteseRAIQAALDELQKNRT 531
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-248 |
1.48e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQKtdqafTFTVEET 94
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQS-----PVLFSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 95 VAFGRYPFqtglfrqqTEKDEAIVQEAMEQTGVAD-FAQKPI----------RELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PLN03232 1326 VRFNIDPF--------SEHNDADLWEALERAHIKDvIDRNPFgldaevseggENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 164 PTNFLDLAYQKdlldLIKRLTRES--GLAAVSVFHDLNTAsLYCDELMFMKNGTAGPKQKPEYAVTEQSikavydTDVTA 241
Cdd:PLN03232 1398 ATASVDVRTDS----LIQRTIREEfkSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSRDT------SAFFR 1466
|
....*..
gi 1119636415 242 LVHQSSP 248
Cdd:PLN03232 1467 MVHSTGP 1473
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
11-164 |
1.49e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.15 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLlhlltgtlpAK-----------EGRVYLAGKLLADYKPKELAQ--IMa 77
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTL---------AKvlmghpkyevtSGSILLDGEDILELSPDERARagIF- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 78 vlpqktdqaftftveetVAFgRYP-----------FQTGLFRQQTEKDEAI-----VQEAMEQTGV-ADFAQKPIRE-LS 139
Cdd:COG0396 81 -----------------LAF-QYPveipgvsvsnfLRTALNARRGEELSAReflklLKEKMKELGLdEDFLDRYVNEgFS 142
|
170 180
....*....|....*....|....*
gi 1119636415 140 GGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:COG0396 143 GGEKKRNEILQMLLLEPKLAILDET 167
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-169 |
1.59e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.86 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAkEGRVYLAGKLLADYKPKELAQIMAVLPQKTdQAFTFTV 91
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESWRKHLSWVGQNP-QLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 92 EETVAFGRypfqtglfrqqTEKDEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLAQALAQQPRILF 160
Cdd:PRK11174 440 RDNVLLGN-----------PDASDEQLQQALENAWVSEFLPLlpqgldtPIGDqaagLSVGQAQRLALARALLQPCQLLL 508
|
....*....
gi 1119636415 161 LDEPTNFLD 169
Cdd:PRK11174 509 LDEPTASLD 517
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-164 |
2.28e-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: 57.09 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 7 SGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKlladykpkelaqiMAVLPQktdQA 86
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-------------IAYVSQ---EP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 87 FTF--TVEETVAFGrYPFqtglfrqqtekDEAIVQEAMEQTG-VADFAQKP------IRE----LSGGEQQRVYLAQALA 153
Cdd:cd03250 76 WIQngTIRENILFG-KPF-----------DEERYEKVIKACAlEPDLEILPdgdlteIGEkginLSGGQKQRISLARAVY 143
|
170
....*....|.
gi 1119636415 154 QQPRILFLDEP 164
Cdd:cd03250 144 SDADIYLLDDP 154
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1-186 |
2.46e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.59 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKElAQIMAVLP 80
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRRALR-RTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTDQAFTFTVEETVafgrypFQTGLFRQQTEKD-EAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:NF000106 93 VR*GRRESFSGRENL------YMIGR*LDLSRKDaRARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180
....*....|....*....|....*..
gi 1119636415 160 FLDEPTNFLDLAYQKDLLDLIKRLTRE 186
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRD 193
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-169 |
3.09e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.12 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHlltgtlpAKEGRVY---LAGKLLA-DYKP-KELAQIMAVLPQKTDQAFTF 89
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLN-------ALAGRIQgnnFTGTILAnNRKPtKQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 90 TVEETVAFG---RYPfqTGLFRQ-QTEKDEAIVQE-AMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:PLN03211 156 TVRETLVFCsllRLP--KSLTKQeKILVAESVISElGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
....*
gi 1119636415 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 |
3.39e-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: 56.10 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTlpaKEGRVyLAGKLLADYKPKelaqimavlpqktdqaftft 90
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGR---KTAGV-ITGEILINGRPL-------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 91 veeTVAFGRYpfqTGLFRQQ-TEKDEAIVQEAMEqtgvadFAQKpIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:cd03232 74 ---DKNFQRS---TGYVEQQdVHSPNLTVREALR------FSAL-LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1119636415 170 LAYQKDLLDLIKRLTrESGLAAVSVFHDLNTASL-YCDELMFMKNG 214
Cdd:cd03232 141 SQAAYNIVRFLKKLA-DSGQAILCTIHQPSASIFeKFDRLLLLKRG 185
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-169 |
3.99e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.58 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLI-NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLpQK 82
Cdd:PRK10790 344 DNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV-QQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 83 TDQAFTFTVEETVAFGRypfqtglfrqqtEKDEAIVQEAMEQTGVADFAQK-------PIRE----LSGGEQQRVYLAQA 151
Cdd:PRK10790 423 DPVVLADTFLANVTLGR------------DISEEQVWQALETVQLAELARSlpdglytPLGEqgnnLSVGQKQLLALARV 490
|
170
....*....|....*...
gi 1119636415 152 LAQQPRILFLDEPTNFLD 169
Cdd:PRK10790 491 LVQTPQILILDEATANID 508
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1-220 |
8.63e-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: 54.89 E-value: 8.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLinNVSL-TVEKGEFLGILGPNGSGKTTLLHLltgtlpakegrvyLAGKLLADYKPKELAQI-MAV 78
Cdd:cd03222 1 QLYPDCVKRYGVFFL--LVELgVVKEGEVIGIVGPNGTGKTTAVKI-------------LAGQLIPNGDNDEWDGItPVY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 LPQKTDqaftftveetvafgrypfqtglfrqqtekdeaivqeameqtgvadfaqkpireLSGGEQQRVYLAQALAQQPRI 158
Cdd:cd03222 66 KPQYID-----------------------------------------------------LSGGELQRVAIAAALLRNATF 92
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 159 LFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFM-----KNGTAGPKQ 220
Cdd:cd03222 93 YLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFegepgVYGIASQPK 159
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-198 |
8.73e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.56 E-value: 8.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGK---LLADYKPKELAQIMAVLPQktDQAFTFTVE 92
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQ--DPYASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 93 ETVAFG-RYPFQT-GLFrqQTEKDEAIVQEAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK10261 418 QTVGDSiMEPLRVhGLL--PGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180
....*....|....*....|....*....
gi 1119636415 170 LAYQKDLLDLIKRLTRESGLAAVSVFHDL 198
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDM 524
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-214 |
9.52e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 9.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQimavlpqktdQAFTFTVEETV 95
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAIN----------HGFALVTEERR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 96 AFGRYPF-----------------QTGLFR-QQTEKDEAIVQEAMEqtgVADFAQK-PIRELSGGEQQRVYLAQALAQQP 156
Cdd:PRK10982 334 STGIYAYldigfnslisnirnyknKVGLLDnSRMKSDTQWVIDSMR---VKTPGHRtQIGSLSGGNQQKVIIGRWLLTQP 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1119636415 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTRES-GLAAVSvfHDLNTASLYCDELMFMKNG 214
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKFEIYQLIAELAKKDkGIIIIS--SEMPELLGITDRILVMSNG 467
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-169 |
1.04e-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: 57.25 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 5 GLSGGYGDSRLI-NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE------------ 71
Cdd:TIGR03719 9 RVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEpqldptktvren 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 72 ----LAQIMAVLpQKTDQAFTFTVEETVAFgrypfqTGLFRQQTEkdeaiVQEAMEQTGVADFAQK-------------- 133
Cdd:TIGR03719 89 veegVAEIKDAL-DRFNEISAKYAEPDADF------DKLAAEQAE-----LQEIIDAADAWDLDSQleiamdalrcppwd 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1119636415 134 -PIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:TIGR03719 157 aDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-241 |
1.31e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.57 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLA----DYKPKELAQIM-----AVLP-QKTDQ 85
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySYRSQRIRMIFqdpstSLNPrQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 86 AFTFtveetvafgryPFQTGLFRQQTEKDEAIVQeAMEQTGV-ADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:PRK15112 109 ILDF-----------PLRLNTDLEPEQREKQIIE-TLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 165 TNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG-------TAGPKQKPEYAVTEQSIKAVYDT 237
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGevvergsTADVLASPLHELTKRLIAGHFGE 256
|
....
gi 1119636415 238 DVTA 241
Cdd:PRK15112 257 ALTA 260
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-214 |
1.44e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.23 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLlaDYKPkelaQIMAVLPQktdqaftfTVEET 94
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRI--SFSP----QTSWIMPG--------TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 95 VAFG----RYPFQTGLFRQQTEKDEAIVQE----AMEQTGVAdfaqkpireLSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:TIGR01271 507 IIFGlsydEYRYTSVIKACQLEEDIALFPEkdktVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1119636415 167 FLDLAYQKDLLD--LIKRLTRESGLAAVSVFHDLNTAslycDELMFMKNG 214
Cdd:TIGR01271 578 HLDVVTEKEIFEscLCKLMSNKTRILVTSKLEHLKKA----DKILLLHEG 623
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-174 |
3.44e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.19 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 55 GRVYLAGKLLADYKPKELAQIMAVLPQKTdQAFTFTVEETVAFGRypfqtglfRQQTEKDE------AIVQEAMEQ---- 124
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEP-MLFNMSIYENIKFGK--------EDATREDVkrackfAAIDEFIESlpnk 1347
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1119636415 125 --TGVADFAqkpiRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQK 174
Cdd:PTZ00265 1348 ydTNVGPYG----KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1395
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-196 |
3.49e-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: 55.91 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVylagklladYKPKElaQIMAVLPQKTdqAFTF-TVEE 93
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL---------TKPAK--GKLFYVPQRP--YMTLgTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 94 TVAfgrYP------FQTGLFRQQTEKD------EAIVQEAMEQTGVADFAQkpirELSGGEQQRVYLAQALAQQPRILFL 161
Cdd:TIGR00954 534 QII---YPdssedmKRRGLSDKDLEQIldnvqlTHILEREGGWSAVQDWMD----VLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*
gi 1119636415 162 DEPTNfldlAYQKDLLDLIKRLTRESGLAAVSVFH 196
Cdd:TIGR00954 607 DECTS----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
138-214 |
4.20e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.88 E-value: 4.20e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 138 LSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQG 205
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-199 |
5.62e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 17 NNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK--EGRVYLAGKLLA--DYKPKELAQI------MAVLPQktdqa 86
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRfkDIRDSEALGIviihqeLALIPY----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 87 ftFTVEETVAFGRYPFQTGLF-RQQTEKDEAivqEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPT 165
Cdd:NF040905 93 --LSIAENIFLGNERAKRGVIdWNETNRRAR---ELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190
....*....|....*....|....*....|....
gi 1119636415 166 NFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLN 199
Cdd:NF040905 168 AALNEEDSAALLDLLLEL-KAQGITSIIISHKLN 200
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-171 |
6.39e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.97 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQktdQAFTF- 89
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQ---DAGLFn 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 90 -TVEETVAFGRypfqtglfrqqTEKDEAIVQEAMEQTGVADF-AQKPI----------RELSGGEQQRVYLAQALAQQPR 157
Cdd:PRK13657 423 rSIEDNIRVGR-----------PDATDEEMRAAAERAQAHDFiERKPDgydtvvgergRQLSGGERQRLAIARALLKDPP 491
|
170
....*....|....
gi 1119636415 158 ILFLDEPTNFLDLA 171
Cdd:PRK13657 492 ILILDEATSALDVE 505
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-165 |
7.55e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.75 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 4 EGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKElaqimAVLPQKt 83
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRR-----AVCPRI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 84 dqAF-----------TFTVEETVAF-GRypfqtgLFRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQA 151
Cdd:NF033858 79 --AYmpqglgknlypTLSVFENLDFfGR------LFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCA 150
|
170
....*....|....
gi 1119636415 152 LAQQPRILFLDEPT 165
Cdd:NF033858 151 LIHDPDLLILDEPT 164
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-200 |
8.05e-08 |
|
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: 54.95 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQktdqaftftveET 94
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQ-----------DP 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 95 VAF-GRYPFQTGLFRQQTEKDeaiVQEAMEQTGVADF-AQKPIR----------ELSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:TIGR00957 1370 VLFsGSLRMNLDPFSQYSDEE---VWWALELAHLKTFvSALPDKldhecaeggeNLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1119636415 163 EPTNFLDLayQKDllDLIKRLTRES--GLAAVSVFHDLNT 200
Cdd:TIGR00957 1447 EATAAVDL--ETD--NLIQSTIRTQfeDCTVLTIAHRLNT 1482
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-178 |
8.55e-08 |
|
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: 53.32 E-value: 8.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLlaDYKPkelaQIMAVLPQktdqaftfTVEET 94
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRI--SFSS----QFSWIMPG--------TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 95 VAFG----RYPFQTGLFRQQTEKDeaivqeameqtgVADFAQK---PIRE----LSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:cd03291 118 IIFGvsydEYRYKSVVKACQLEED------------ITKFPEKdntVLGEggitLSGGQRARISLARAVYKDADLYLLDS 185
|
170
....*....|....*
gi 1119636415 164 PTNFLDLAYQKDLLD 178
Cdd:cd03291 186 PFGYLDVFTEKEIFE 200
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-266 |
9.51e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE-LAQIMAVLPQKTDQAFTFTVEET 94
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 95 VAFGRYPFQtGLFrqqtekdeaIVQEAMEQTGVADFAQKPIR--------ELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:PRK10982 94 MWLGRYPTK-GMF---------VDQDKMYRDTKAIFDELDIDidprakvaTLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 167 FLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNGTAGPKQKPEYAVTEQSIKAVYDTDVTALV--H 244
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQRFpdK 242
|
250 260
....*....|....*....|..
gi 1119636415 245 QSSPKPMIVIQPEKDSVKQQSI 266
Cdd:PRK10982 243 ENKPGEVILEVRNLTSLRQPSI 264
|
|
| 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 1119636415 134 PIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK11819 160 KVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-196 |
1.27e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.27 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLlhlltgtlpakegrvylaGKLLADYKPKELAQIMAVLP 80
Cdd:COG2401 31 LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTL------------------LRLLAGALKGTPVAGCVDVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKtdqafTFTVEETV--AFGRypfqtglfrqQTEKDEAIvqEAMEQTGVAD--FAQKPIRELSGGEQQRVYLAQALAQQP 156
Cdd:COG2401 93 DN-----QFGREASLidAIGR----------KGDFKDAV--ELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1119636415 157 RILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFH 196
Cdd:COG2401 156 KLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-192 |
2.92e-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: 50.72 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK---EGRVYLAGKLLADYKPKELAQIMAVLPQKTDQAfTFTV 91
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFP-TLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 92 EETVafgrypfqtglfrqqtekdeaivqeameqtgvaDFAQKP-----IRELSGGEQQRVYLAQALAQQPRILFLDEPTN 166
Cdd:cd03233 101 RETL---------------------------------DFALRCkgnefVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180
....*....|....*....|....*.
gi 1119636415 167 FLDLAYQKDLLDLIKRLTRESGLAAV 192
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTTTF 173
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
138-220 |
4.82e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.63 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 138 LSGGEQQRVYLAQALAQQP-RILF-LDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASlYCDELMFMkngt 215
Cdd:cd03238 88 LSGGELQRVKLASELFSEPpGTLFiLDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLS-SADWIIDF---- 161
|
....*
gi 1119636415 216 aGPKQ 220
Cdd:cd03238 162 -GPGS 165
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-214 |
6.13e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.81 E-value: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKlladykpkelAQIMAVLPQKTDQaftFTVEETV 95
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS----------AALIAISSGLNGQ---LTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 96 AFgrypfqTGLFRQQT-EKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQK 174
Cdd:PRK13545 107 EL------KGLMMGLTkEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1119636415 175 DLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK13545 181 KCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYG 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-169 |
6.53e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKE-------GRVYLAGKLLADYKPKelaqIMAVLPQ- 81
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYsndltlfGRRRGSGETIWDIKKH----IGYVSSSl 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 82 KTDQAFTFTVEETVAFGrYPFQTGLFRQQTEKDEAIVQEAMEQTGVAD-FAQKPIRELSGGEQQRVYLAQALAQQPRILF 160
Cdd:PRK10938 346 HLDYRVSTSVRNVILSG-FFDSIGIYQAVSDRQQKLAQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPTLLI 424
|
....*....
gi 1119636415 161 LDEPTNFLD 169
Cdd:PRK10938 425 LDEPLQGLD 433
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-178 |
1.04e-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: 51.48 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLladykpkelaqimAVLPQktdQAF--T 88
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV-------------AYVPQ---QAWiqN 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 89 FTVEETVAFGRyPFQTGLFRQQTEKDEAIVQEAMEQTG-VADFAQKPIrELSGGEQQRVYLAQALAQQPRILFLDEPTNF 167
Cdd:TIGR00957 713 DSLRENILFGK-ALNEKYYQQVLEACALLPDLEILPSGdRTEIGEKGV-NLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170
....*....|.
gi 1119636415 168 LDLAYQKDLLD 178
Cdd:TIGR00957 791 VDAHVGKHIFE 801
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
12-170 |
1.08e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.79 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 12 DSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAK--EGRVYLAGKLLADYKPKELAQIMAVLpqktdqAFTF 89
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLELSPEDRAGEGIFM------AFQY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 90 TVEETVAFGRYPFQTGL-----FRQQTEKD----EAIVQEAMEQTGV-ADFAQKPIRE-LSGGEQQRVYLAQALAQQPRI 158
Cdd:PRK09580 87 PVEIPGVSNQFFLQTALnavrsYRGQEPLDrfdfQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAVLEPEL 166
|
170
....*....|..
gi 1119636415 159 LFLDEPTNFLDL 170
Cdd:PRK09580 167 CILDESDSGLDI 178
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
16-214 |
1.69e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.00 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE--------LAQIMAVLPQktdqaf 87
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsqeagigiIHQELNLIPQ------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 88 tFTVEETVAFGRyPFQTGLFRQQTEKdeaIVQEA---MEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEP 164
Cdd:PRK10762 94 -LTIAENIFLGR-EFVNRFGRIDWKK---MYAEAdklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1119636415 165 TNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK10762 169 TDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-163 |
2.03e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.10 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQkTDQAFTFTVEETV 95
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ-TPFLFSDTVANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 96 AFGRyPFQTglfrqqtekdeaivQEAMEQtgVADFA-------------QKPIRE----LSGGEQQRVYLAQALAQQPRI 158
Cdd:PRK10789 410 ALGR-PDAT--------------QQEIEH--VARLAsvhddilrlpqgyDTEVGErgvmLSGGQKQRISIARALLLNAEI 472
|
....*
gi 1119636415 159 LFLDE 163
Cdd:PRK10789 473 LILDD 477
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
7-218 |
2.03e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 7 SGGY-GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLadykpkelaqiMAVLPQKTDQ 85
Cdd:PLN03073 515 SFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVR-----------MAVFSQHHVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 86 AFTFTVEETVAFGR-YPfqtGLFRQQtekdeaiVQEAMEQTGVA-DFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PLN03073 584 GLDLSSNPLLYMMRcFP---GVPEQK-------LRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDE 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 164 PTNFLDLayqkDLLD-LIKRLTR-ESGLAAVSvfHDLNTASLYCDELMFMKNGTAGP 218
Cdd:PLN03073 654 PSNHLDL----DAVEaLIQGLVLfQGGVLMVS--HDEHLISGSVDELWVVSEGKVTP 704
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-215 |
2.49e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.66 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQI-MAVL 79
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 80 PQKTDQAFTFTVEETVAFGrypfqtglfRQQTEKDEAIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRIL 159
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFG---------LPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1119636415 160 FLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNGT 215
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGT 217
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-215 |
3.42e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.20 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRL-INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKE-LAQIMAVLpqkTDqaF 87
Cdd:PRK10522 332 YQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyRKLFSAVF---TD--F 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 88 tftveetvafgrYPFQTGLFRQQTEKDEAIVQEAMEQTGVAD---FAQKPIR--ELSGGEQQRVYLAQALAQQPRILFLD 162
Cdd:PRK10522 407 ------------HLFDQLLGPEGKPANPALVEKWLERLKMAHkleLEDGRISnlKLSKGQKKRLALLLALAEERDILLLD 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1119636415 163 E------PTnFLDLAYQKdLLDLIkrltRESGLAAVSVFHDlNTASLYCDELMFMKNGT 215
Cdd:PRK10522 475 EwaadqdPH-FRREFYQV-LLPLL----QEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-173 |
4.37e-06 |
|
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: 49.14 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGY--GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLpAKEGRVYLAGKLLADYKPKELAQIMAV 78
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 LPQKTdqaFTFTveetvafgrypfqtGLFRQQTE-----KDEAIVQEAMEQTGVADFAQKPIR----------ELSGGEQ 143
Cdd:TIGR01271 1297 IPQKV---FIFS--------------GTFRKNLDpyeqwSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyVLSNGHK 1359
|
170 180 190
....*....|....*....|....*....|.
gi 1119636415 144 QRVYLAQALAQQPRILFLDEPTNFLD-LAYQ 173
Cdd:TIGR01271 1360 QLMCLARSILSKAKILLLDEPSAHLDpVTLQ 1390
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-170 |
5.21e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.71 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKtTLLHLLTGTLPA---KEGRVYLAGKLLADYKPKELAQIMA 77
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGK-STLSKVIAGHPAykiLEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 78 VLpqktdqAFTFTVE----ETVAFGRYPFQTGL-FRQQTEKD-----EAIVQE----AMEQTgvadFAQKPIRE-LSGGE 142
Cdd:CHL00131 87 FL------AFQYPIEipgvSNADFLRLAYNSKRkFQGLPELDpleflEIINEKlklvGMDPS----FLSRNVNEgFSGGE 156
|
170 180
....*....|....*....|....*...
gi 1119636415 143 QQRVYLAQALAQQPRILFLDEPTNFLDL 170
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDI 184
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-170 |
1.33e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.00 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKllaDYKPKELAQIMAVLP 80
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRGDRSRFMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 81 QKTDQAFTFTVEETVAF-----GRYPFQTGlfrqqtekdeaivQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQ 155
Cdd:PRK13543 89 HLPGLKADLSTLENLHFlcglhGRRAKQMP-------------GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSP 155
|
170
....*....|....*
gi 1119636415 156 PRILFLDEPTNFLDL 170
Cdd:PRK13543 156 APLWLLDEPYANLDL 170
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
132-170 |
1.74e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 1.74e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1119636415 132 QKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDL 170
Cdd:PRK10636 144 ERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL 182
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
128-170 |
2.17e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 2.17e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1119636415 128 ADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDL 170
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
129-169 |
2.47e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 2.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1119636415 129 DFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLD 169
Cdd:PRK15064 147 EQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
15-169 |
3.62e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.31 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 15 LINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYlAGKLLAdYKPKElAQIMAVlpqktdqaftfTVEET 94
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-AERSIA-YVPQQ-AWIMNA-----------TVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 95 VAFgrypFqtglfrqqTEKDEAIVQEAMEQTGV-ADFAQKP------IRE----LSGGEQQRVYLAQALAQQPRILFLDE 163
Cdd:PTZ00243 741 ILF----F--------DEEDAARLADAVRVSQLeADLAQLGggleteIGEkgvnLSGGQKARVSLARAVYANRDVYLLDD 808
|
....*.
gi 1119636415 164 PTNFLD 169
Cdd:PTZ00243 809 PLSALD 814
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
134-198 |
6.07e-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: 6.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 134 PIRELSGGEQQRVYLAQALAQQPR---ILFLDEPTNFLDLAYQKDLLDLIKRLTrESGLAAVSVFHDL 198
Cdd:cd03271 166 PATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLV-DKGNTVVVIEHNL 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
137-213 |
1.66e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 1.66e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119636415 137 ELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLIKRLTRESGLAAVSVFHDLNTASlYCDELMFMKN 213
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIR-YANTIFVLSN 654
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
135-188 |
1.75e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 1.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 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 |
2.02e-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: 2.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119636415 138 LSGGEQQRVYLAQALAQQ---PRILFLDEPTNFLDLAYQKDLLDLIKRLtRESGLAAVSVFHDL 198
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNL 892
|
|
| 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 1119636415 124 QTGVADFAQKPIRELSGGEQQR-VY--LAQALAQQ----------PRILFLDEPTNFLDLAYQKDLLDLIKR 182
Cdd:pfam13558 19 EDGSEVETYRRSGGLSGGEKQLlAYlpLAAALAAQygsaegrppaPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
136-180 |
4.87e-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: 40.43 E-value: 4.87e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1119636415 136 RELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKDLLDLI 180
Cdd:smart00382 59 ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLE 103
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
138-165 |
5.63e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 5.63e-04
10 20
....*....|....*....|....*...
gi 1119636415 138 LSGGEQQRVYLAQALAQQPRILFLDEPT 165
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPT 432
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-171 |
5.97e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.40 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 14 RLINNVSLTVEKGEFLGILGPNGSGK----TTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQImaVLPQKTDQAF-T 88
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCstllKTIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDV--VYNAETDVHFpH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 89 FTVEETVAFG---RYPfQT---GLFRQQTEKDEAIVQEAM------EQTGVA-DFaqkpIRELSGGEQQRVYLAQALAQQ 155
Cdd:TIGR00956 153 LTVGETLDFAarcKTP-QNrpdGVSREEYAKHIADVYMATyglshtRNTKVGnDF----VRGVSGGERKRVSIAEASLGG 227
|
170
....*....|....*.
gi 1119636415 156 PRILFLDEPTNFLDLA 171
Cdd:TIGR00956 228 AKIQCWDNATRGLDSA 243
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-214 |
8.19e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 19 VSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLLADYKPKELAQIMAVLPQkTDQAFTFTVEetvaFG 98
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQ-APVLFSGTVR----FN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 99 RYPFqtglfrqqTEKDEAIVQEAMEQTGVADFAQKPIREL-----------SGGEQQRVYLAQALAQQPRILFLDEPTNF 167
Cdd:PLN03130 1333 LDPF--------NEHNDADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1119636415 168 LDLAYQKdlldLIKRLTRES--GLAAVSVFHDLNTAsLYCDELMFMKNG 214
Cdd:PLN03130 1405 VDVRTDA----LIQKTIREEfkSCTMLIIAHRLNTI-IDCDRILVLDAG 1448
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-252 |
9.25e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 40.99 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGY--GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLpAKEGRVYLAGKLLADYKPKELAQIMAV 78
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 79 LPQKTdqaFTFtveetvafgrypfqTGLFRQQTE-----KDEAIVQEAMEQTGVADFAQKPIR----------ELSGGEQ 143
Cdd:cd03289 82 IPQKV---FIF--------------SGTFRKNLDpygkwSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcVLSHGHK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 144 QRVYLAQALAQQPRILFLDEPTNFLD-LAYQkdlldLIKRLTRESgLAAVSVF---HDLNtASLYCDELMFMKNGTAGPK 219
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLDpITYQ-----VIRKTLKQA-FADCTVIlseHRIE-AMLECQRFLVIEENKVRQY 217
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1119636415 220 QKPEYAVTEQSI--KAVYDTDVTALV-------HQSSPKPMI 252
Cdd:cd03289 218 DSIQKLLNEKSHfkQAISPSDRLKLFprrnsskSKRKPRPQI 259
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-214 |
1.00e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.57 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAGKLladykpkelaQIMAVLPQKTDQaftFTVEETV 95
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV----------SVIAISAGLSGQ---LTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 96 AFGRypFQTGLFRQQTEKdeaIVQEAMEQTGVADFAQKPIRELSGGEQQRVYLAQALAQQPRILFLDEPTNFLDLAYQKD 175
Cdd:PRK13546 107 EFKM--LCMGFKRKEIKA---MTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 1119636415 176 LLDLIKRLtRESGLAAVSVFHDLNTASLYCDELMFMKNG 214
Cdd:PRK13546 182 CLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGG 219
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-165 |
1.12e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 1.12e-03
10 20 30
....*....|....*....|....*....|.
gi 1119636415 138 LSGGEQQRVYLAQALA--QQPRILF-LDEPT 165
Cdd:COG0178 827 LSGGEAQRVKLASELSkrSTGKTLYiLDEPT 857
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-234 |
1.53e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.98 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 1 MKAEGLSGGYGDSRL--INNVSLTVEKGEFLGILGPNGSGKTTLLHLLTgtlpakeGRV---YLAGKLLADYKPKE---L 72
Cdd:PLN03140 879 MPAEMKEQGVTEDRLqlLREVTGAFRPGVLTALMGVSGAGKTTLMDVLA-------GRKtggYIEGDIRISGFPKKqetF 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 73 AQIMAVLPQKTDQAFTFTVEETV---AFGRYPFQTGLFRQQTEKDEaiVQEAMEQTGVAD--FAQKPIRELSGGEQQRVY 147
Cdd:PLN03140 952 ARISGYCEQNDIHSPQVTVRESLiysAFLRLPKEVSKEEKMMFVDE--VMELVELDNLKDaiVGLPGVTGLSTEQRKRLT 1029
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 148 LAQALAQQPRILFLDEPTNFLDlAYQKDLLDLIKRLTRESGLAAVSVFH----DLNTASlycDELMFMKNGT----AGPK 219
Cdd:PLN03140 1030 IAVELVANPSIIFMDEPTSGLD-ARAAAIVMRTVRNTVDTGRTVVCTIHqpsiDIFEAF---DELLLMKRGGqviySGPL 1105
|
250
....*....|....*..
gi 1119636415 220 QKPEYAVTE--QSIKAV 234
Cdd:PLN03140 1106 GRNSHKIIEyfEAIPGV 1122
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
138-200 |
3.40e-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: 3.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 138 LSGGEQQRVYLAQAL-AQQPRILF-LDEPTNFLdlaYQKD---LLDLIKRLtRESGLAAVSVFHDLNT 200
Cdd:cd03270 138 LSGGEAQRIRLATQIgSGLTGVLYvLDEPSIGL---HPRDndrLIETLKRL-RDLGNTVLVVEHDEDT 201
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
10-196 |
4.36e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 38.39 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 10 YGDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTLPAKEGRVYLAG----KLLADYKpkelaQIMAVLPQKTDQ 85
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikKDLCTYQ-----KQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 86 AFTFTVEETVAFGRYPFQTGLfrqqtEKDEAIVQEAMEQtgVADFaqkPIRELSGGEQQRVYLAQALAQQPRILFLDEPT 165
Cdd:PRK13540 86 NPYLTLRENCLYDIHFSPGAV-----GITELCRLFSLEH--LIDY---PCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|...
gi 1119636415 166 NFLDlayQKDLLDLIKRLT--RESGLAAVSVFH 196
Cdd:PRK13540 156 VALD---ELSLLTIITKIQehRAKGGAVLLTSH 185
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-214 |
8.28e-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: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 11 GDSRLINNVSLTVEKGEFLGILGPNGSGKTTLLHLLTGTlpaKEGRVYLAGKLLADYKPKE--LAQIMAVLPQKTDQAFT 88
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAER---VTTGVITGGDRLVNGRPLDssFQRSIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 89 FTVEETVAFGRYpfqtglFRQ-----QTEKDEaIVQEAMEQTGVADFAQKPIRELSGG---EQ-QRVYLAQALAQQPR-I 158
Cdd:TIGR00956 851 STVRESLRFSAY------LRQpksvsKSEKME-YVEEVIKLLEMESYADAVVGVPGEGlnvEQrKRLTIGVELVAKPKlL 923
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119636415 159 LFLDEPTNFLDLAYQKDLLDLIKRLTrESGLAAVSVFHDlNTASLYC--DELMFMKNG 214
Cdd:TIGR00956 924 LFLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIHQ-PSAILFEefDRLLLLQKG 979
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-169 |
8.67e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 38.80 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 16 INNVSLTVEKGEFLGILGPNGSGKTTllhlltgtlpakegrvyLAGKLLADYKPKELAQI-----MAVLPQkTDQAFTFT 90
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTS-----------------LISAMLGELSHAETSSVvirgsVAYVPQ-VSWIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636415 91 VEETVAFGRyPFQTGlfRQQTEKDEAIVQEAMEQTGVADFAQKPIR--ELSGGEQQRVYLAQALAQQPRILFLDEPTNFL 168
Cdd:PLN03232 695 VRENILFGS-DFESE--RYWRAIDVTALQHDLDLLPGRDLTEIGERgvNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
.
gi 1119636415 169 D 169
Cdd:PLN03232 772 D 772
|
|
|