|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-256 |
2.25e-130 |
|
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: 378.23 E-value: 2.25e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:COG1120 1 MLEAENLSVGYGGR-PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTADTTFAYKVKEVVALGRYPHQkGWLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDL 160
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRYPHL-GLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 161 LLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQLANVYETK 240
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVE 238
|
250
....*....|....*.
gi 1599980197 241 IRRNEHPTIPRPLVTF 256
Cdd:COG1120 239 ARVIEDPVTGRPLVLP 254
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-254 |
4.36e-109 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 323.99 E-value: 4.36e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:COG4559 1 MLEAENLSVRLGGRT-LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTADTTFAYKVKEVVALGRYPHQkgwlaSESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQ---- 156
Cdd:COG4559 80 LPQHSSLAFPFTVEEVVALGRAPHG-----SSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwep 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 157 ---EPDLLLLDEPTNHLDISHQMQLLDALKDWTRtRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQL 233
Cdd:COG4559 155 vdgGPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELL 233
|
250 260
....*....|....*....|.
gi 1599980197 234 ANVYETKIRRNEHPTIPRPLV 254
Cdd:COG4559 234 ERVYGADLRVLAHPEGGCPQV 254
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-254 |
9.33e-102 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 305.54 E-value: 9.33e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:PRK13548 2 MLEARNLSVRLGGRT-LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTADTTFAYKVKEVVALGRYPHqkgwlASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQ---- 156
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPH-----GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwep 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 157 --EPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQLA 234
Cdd:PRK13548 156 dgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLR 235
|
250 260
....*....|....*....|
gi 1599980197 235 NVYETKIRRNEHPTIPRPLV 254
Cdd:PRK13548 236 RVYGADVLVQPHPETGAPLV 255
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-219 |
9.46e-87 |
|
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: 263.91 E-value: 9.46e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 3 DAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLP 82
Cdd:cd03214 1 EVENLSVGYGGRT-VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 83 QtadttfaykvkevvalgryphqkgwlasesqedervireAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLL 162
Cdd:cd03214 80 Q---------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 163 LDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-246 |
3.86e-86 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 265.03 E-value: 3.86e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIadyhsKELAQKMAV 80
Cdd:COG1121 6 AIELENLTVSYGGR-PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQ--TADTTFAYKVKEVVALGRYPHqKGWLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEP 158
Cdd:COG1121 80 VPQraEVDWDFPITVRDVVLMGRYGR-RGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 159 DLLLLDEPTNHLDISHQMQLLDALKDWTRtRQLTVVAILHDLNMASLYCDRVLLLNeGRMVDLNSPRQVMTEHQLANVYE 238
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPEEVLTPENLSRAYG 236
|
....*...
gi 1599980197 239 TKIRRNEH 246
Cdd:COG1121 237 GPVALLAH 244
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-247 |
3.93e-79 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 246.92 E-value: 3.93e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:COG4604 1 MIEIKNVSKRYGGK-VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTADTTFAYKVKEVVALGRYPHQKGWLaseSQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDL 160
Cdd:COG4604 80 LRQENHINSRLTVRELVAFGRFPYSKGRL---TAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 161 LLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQLANVYETK 240
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTD 236
|
....*..
gi 1599980197 241 IRRNEHP 247
Cdd:COG4604 237 IEVEEID 243
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-253 |
2.07e-78 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 245.31 E-value: 2.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:PRK11231 2 TLRTENLTVGYGTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTADTTFAYKVKEVVALGRYPHQKGWlASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDL 160
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSPWLSLW-GRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 161 LLLDEPTNHLDISHQMQLLDALkdwtrtRQL-----TVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQLAN 235
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLM------RELntqgkTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRT 233
|
250
....*....|....*...
gi 1599980197 236 VYETKIRRNEHPTIPRPL 253
Cdd:PRK11231 234 VFDVEAEIHPEPVSGTPM 251
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-214 |
8.97e-77 |
|
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: 239.74 E-value: 8.97e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 4 AQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKelaqkMAVLPQ 83
Cdd:cd03235 2 VEDLTVSYGGH-PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 84 T--ADTTFAYKVKEVVALGRYPHqKGWLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLL 161
Cdd:cd03235 76 RrsIDRDFPISVRDVVLMGLYGH-KGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1599980197 162 LLDEPTNHLDISHQMQLLDALKDWTRtRQLTVVAILHDLNMASLYCDRVLLLN 214
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| CbiZ |
COG1865 |
Adenosylcobinamide amidohydrolase [Coenzyme transport and metabolism]; |
269-488 |
2.23e-76 |
|
Adenosylcobinamide amidohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 441470 Cd Length: 224 Bit Score: 239.00 E-value: 2.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 269 ISELEVFTSEQLIKVTSSIRWKTLSSAVLGAGFKWHQTFVNRHVSKDYYCDDVEREFQTFLSNVGVDGTDALGMMTAAIL 348
Cdd:COG1865 2 STGFEVRREDGVLVVRFPGPRRVLSTAVLNGGLREARAVFNHQVPEDYDRTDPEEYLAEVLARLGLPPGDTVGLLTAADM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 349 EDVAITEATYESFKVRVFVTAGISNAVDPAK--AHLRKRNEATVGTINTWVFIEGTLPDAAYVQALMTATEAKGRALAEK 426
Cdd:COG1865 82 ENAAIAEESFGGLSVTAVVTAGVSNAVRAGAdpASYYEPRPPPPGTINIIVLINAPLSDGALVNAVITATEAKTAALQEL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1599980197 427 EILDPVTGTLATGTSTDSVMIASSQTGTYFPYAGTITPLGQAIGKLVYDATIQAVTDNEKRR 488
Cdd:COG1865 162 GIGSRYSGGLATGTGTDAIAVAAPPDGEPLTYAGKHTKLGELIGRAVYEAVREALRRQNGLT 223
|
|
| CbiZ |
pfam01955 |
Adenosylcobinamide amidohydrolase; This prokaryotic protein family includes CbiZ which ... |
288-477 |
5.63e-72 |
|
Adenosylcobinamide amidohydrolase; This prokaryotic protein family includes CbiZ which converts adenosylcobinamide (AdoCbi) to adenosylcobyric acid (AdoCby), an intermediate of the de novo coenzyme B12 biosynthetic route.
Pssm-ID: 426529 Cd Length: 193 Bit Score: 226.67 E-value: 5.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 288 RWKTLSSAVLGAGFKWHQTFVNRHVSKDYYCDDVEREFQTFLSNVGVDGTDALGMMTAAILEDVAITEATYESFKVRVFV 367
Cdd:pfam01955 4 PRRVLSSAVLNGGLREARAVFNHQVPKGYDRDDPAEYLEEYLEELGLDPEDTVGLLTAADMENAAIAEESFEDLEVTAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 368 TAGISNAVDPAKAHLRkRNEATVGTINTWVFIEGTLPDAAYVQALMTATEAKGRALAEKEILDPVTGTLATGTSTDSVMI 447
Cdd:pfam01955 84 TAGVSNAVRAGDPASY-YLPPPPGTINIIVVINAPLTDGALVNALITATEAKTAALQDLGIRSRYSGGLATGTGTDAIAV 162
|
170 180 190
....*....|....*....|....*....|.
gi 1599980197 448 ASSQTG-TYFPYAGTITPLGQAIGKLVYDAT 477
Cdd:pfam01955 163 ASPPEGeRRIPYAGKHTKLGELIGRAVYEAV 193
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-267 |
7.96e-71 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 230.88 E-value: 7.96e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEkTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:PRK09536 3 MIDVSDLSVEFGD-TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTADTTFAYKVKEVVALGRYPHqKGWLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDL 160
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGRTPH-RSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 161 LLLDEPTNHLDISHQMQLLDALKDWTRTRQlTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQLANVYETK 240
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDAR 239
|
250 260
....*....|....*....|....*..
gi 1599980197 241 IRRNEHPTIPRPLVTFEPAAIRSKPSS 267
Cdd:PRK09536 240 TAVGTDPATGAPTVTPLPDPDRTEAAA 266
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
28-259 |
1.36e-69 |
|
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: 222.77 E-value: 1.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 28 GEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQTADTTFAYKVKEVVALGRYPHQKG 107
Cdd:TIGR03873 27 GSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVEQDSDTAVPLTVRDVVALGRIPHRSL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 108 WlASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTR 187
Cdd:TIGR03873 107 W-AGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAA 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1599980197 188 TrQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQLANVYETKIRRNEHPTIPRPLVTFEPA 259
Cdd:TIGR03873 186 T-GVTVVAALHDLNLAASYCDHVVVLDGGRVVAAGPPREVLTPALIRAVYGVDATVLTHPDTGRPIIAFSPL 256
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-233 |
1.79e-63 |
|
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: 205.64 E-value: 1.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVL 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADTT-FAYKVKEVVALGryPHQKGWlaSESQEDERViREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDL 160
Cdd:COG1122 81 FQNPDDQlFAPTVEEDVAFG--PENLGL--PREEIRERV-EEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1599980197 161 LLLDEPTNHLDISHQMQLLDALKDWTRtRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQL 233
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-232 |
7.93e-60 |
|
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: 196.95 E-value: 7.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEK---TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQK 77
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 78 MAVLPQTADTTF--AYKVKEVVALGRYPHQKGwlasesqEDERVIREAMEQ---TDTWKFRnKPLQtLSGGERQRALLAR 152
Cdd:COG1124 81 VQMVFQDPYASLhpRHTVDRILAEPLRIHGLP-------DREERIAELLEQvglPPSFLDR-YPHQ-LSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 153 ALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQ 232
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-254 |
3.00e-59 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 195.98 E-value: 3.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVL 81
Cdd:PRK10253 8 LRGEQLTLGYGKYT-VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADTTFAYKVKEVVALGRYPHQKgWLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLL 161
Cdd:PRK10253 87 AQNATTPGDITVQELVARGRYPHQP-LFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 162 LLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQLANVYETKI 241
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRC 245
|
250
....*....|...
gi 1599980197 242 RRNEHPTIPRPLV 254
Cdd:PRK10253 246 MIIDDPVAGTPLV 258
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
2-246 |
7.66e-59 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 194.29 E-value: 7.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGydektPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLsPSEGTITLQGKAIADYHSKELAQKMAVL 81
Cdd:COG4138 1 LQLNDVAVA-----GRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADTTFAYKVKEVVALGRYPHqkgwlaSESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQ----- 156
Cdd:COG4138 75 SQQQSPPFAMPVFQYLALHQPAG------ASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwpti 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 157 --EPDLLLLDEPTNHLDISHQMQLLDALKDWTRtRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQLA 234
Cdd:COG4138 149 npEGQLLLLDEPMNSLDVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLS 227
|
250
....*....|..
gi 1599980197 235 NVYETKIRRNEH 246
Cdd:COG4138 228 EVFGVKFRRLEV 239
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-217 |
7.33e-58 |
|
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: 190.37 E-value: 7.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 6 NVSVGY-DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQT 84
Cdd:cd03225 4 NLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 85 ADT-TFAYKVKEVVALGryPHQKGWlaSESQEDERViREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLL 163
Cdd:cd03225 84 PDDqFFGPTVEEEVAFG--LENLGL--PEEEIEERV-EEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 164 DEPTNHLDISHQMQLLDALKDWtRTRQLTVVAILHDLNMASLYCDRVLLLNEGR 217
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
6.04e-57 |
|
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: 197.05 E-value: 6.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEK----TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHS---KE 73
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 74 LAQKMAVLPQTADTTF--AYKVKEVVALGryPHQKGWLaSESQEDERViREAMEQTD-TWKFRNKPLQTLSGGERQRALL 150
Cdd:COG1123 340 LRRRVQMVFQDPYSSLnpRMTVGDIIAEP--LRLHGLL-SRAERRERV-AELLERVGlPPDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 151 ARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMT 229
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-237 |
7.21e-56 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 187.30 E-value: 7.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 17 IIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQTADTTFAYKVKEV 96
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 97 VALGRYPHQkGWLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQM 176
Cdd:PRK10575 106 VAIGRYPWH-GALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1599980197 177 QLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQLANVY 237
Cdd:PRK10575 185 DVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-246 |
1.90e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 184.88 E-value: 1.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADyHSKELAQKMAVL 81
Cdd:COG1131 1 IEVRGLTKRYGDKT-ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTAdttFAY---KVKEVVAL-GRYphqKGwlASESQEDERvIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQE 157
Cdd:COG1131 79 PQEP---ALYpdlTVRENLRFfARL---YG--LPRKEARER-IDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 158 PDLLLLDEPTNHLDISHQMQLLDALKDWtRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMtEHQLANVY 237
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK-ARLLEDVF 227
|
....*....
gi 1599980197 238 ETKIRRNEH 246
Cdd:COG1131 228 LELTGEEAR 236
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-222 |
7.23e-53 |
|
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: 178.08 E-value: 7.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEK---TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA-- 75
Cdd:cd03257 1 LLEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 -QKMAVLPQTADTTF--AYKVKEVVALGRYPHQKGWLASESQEDERVIREAMEQTDTWkFRNKPLQtLSGGERQRALLAR 152
Cdd:cd03257 81 rKEIQMVFQDPMSSLnpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEV-LNRYPHE-LSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 153 ALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLN 222
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-247 |
6.78e-52 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 176.94 E-value: 6.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPS--------EGTITLQGKAIADYHSK 72
Cdd:PRK13547 1 MLTADHLHVARRHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 73 ELAQKMAVLPQTADTTFAYKVKEVVALGRYPHQKGWLASeSQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLAR 152
Cdd:PRK13547 80 RLARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGAL-THRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 153 ALCQ---------EPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNS 223
Cdd:PRK13547 159 VLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
250 260
....*....|....*....|....
gi 1599980197 224 PRQVMTEHQLANVYETKIRRNEHP 247
Cdd:PRK13547 239 PADVLTPAHIARCYGFAVRLVDAG 262
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-238 |
1.65e-51 |
|
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: 175.05 E-value: 1.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYhSKELAQKMAV 80
Cdd:COG4555 1 MIEVENLSKKYGKV-PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE-PREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQtadttfaykvkevvALGRYPHQKGW-----LAS----ESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLA 151
Cdd:COG4555 79 LPD--------------ERGLYDRLTVReniryFAElyglFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 152 RALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWtRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEH 231
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEI 223
|
....*..
gi 1599980197 232 QLANVYE 238
Cdd:COG4555 224 GEENLED 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-218 |
8.22e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 169.23 E-value: 8.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVL 81
Cdd:COG4619 1 LELEGLSFRVGGK-PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADTtFAYKVKEVVALGryphqkgWLASESQEDERVIREAMEQTD-TWKFRNKPLQTLSGGERQRALLARALCQEPDL 160
Cdd:COG4619 80 PQEPAL-WGGTVRDNLPFP-------FQLRERKFDRERALELLERLGlPPDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 161 LLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRM 218
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-257 |
3.10e-49 |
|
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: 176.25 E-value: 3.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGY-DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPS---EGTITLQGKAIADYHSKELAQ 76
Cdd:COG1123 4 LLEVRDLSVRYpGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 77 KMAVLPQTADTTF-AYKVKEVVALGRYPHQkgwlASESQEDERVIrEAMEQTDTWKFRNKPLQTLSGGERQRALLARALC 155
Cdd:COG1123 84 RIGMVFQDPMTQLnPVTVGDQIAEALENLG----LSRAEARARVL-ELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 156 QEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQ-LA 234
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQaLA 238
|
250 260
....*....|....*....|....*.
gi 1599980197 235 NV---YETKIRRNEHPTIPRPLVTFE 257
Cdd:COG1123 239 AVprlGAARGRAAPAAAAAEPLLEVR 264
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-217 |
5.50e-49 |
|
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: 165.50 E-value: 5.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 4 AQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQ 83
Cdd:cd00267 2 IENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 84 tadttfaykvkevvalgryphqkgwlasesqedervireameqtdtwkfrnkplqtLSGGERQRALLARALCQEPDLLLL 163
Cdd:cd00267 81 --------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 164 DEPTNHLDISHQMQLLDALKDWTRtRQLTVVAILHDLNMASLYCDRVLLLNEGR 217
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-218 |
6.57e-48 |
|
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: 162.95 E-value: 6.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDeKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADyHSKELAQKMAVL 81
Cdd:cd03230 1 IEVRNLSKRYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADTtfaykvkevvalgrYPHQKGWlasesqedervirEAMEqtdtwkfrnkplqtLSGGERQRALLARALCQEPDLL 161
Cdd:cd03230 79 PEEPSL--------------YENLTVR-------------ENLK--------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 162 LLDEPTNHLDISHQMQLLDALKDWTRtRQLTVVAILHDLNMASLYCDRVLLLNEGRM 218
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-213 |
2.09e-47 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 162.40 E-value: 2.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 10 GYDeKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAiadyhskelaqKMAVLPQ--TADT 87
Cdd:NF040873 1 GYG-GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-----------RVAYVPQrsEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 88 TFAYKVKEVVALGRYPHQkGWLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPT 167
Cdd:NF040873 69 SLPLTVRDLVAMGRWARR-GLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1599980197 168 NHLDISHQMQLLDALKDWTRtRQLTVVAILHDLNMASLYcDRVLLL 213
Cdd:NF040873 148 TGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRA-DPCVLL 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-237 |
3.78e-47 |
|
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: 163.51 E-value: 3.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQ---KMAVL 81
Cdd:cd03256 4 ENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADTTFAYKVKEVV---ALGRYPHQKGWLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEP 158
Cdd:cd03256 84 FQQFNLIERLSVLENVlsgRLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 159 DLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVdLNSPRQVMTEHQLANVY 237
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV-FDGPPAELTDEVLDEIY 241
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-231 |
1.62e-46 |
|
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: 169.94 E-value: 1.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVL 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTAdTTFAYKVKEVVALGRyPHqkgwlASESQedervIREAMEQTDTWKF-RNKP--LQT--------LSGGERQRALL 150
Cdd:COG4988 417 PQNP-YLFAGTIRENLRLGR-PD-----ASDEE-----LEAALEAAGLDEFvAALPdgLDTplgeggrgLSGGQAQRLAL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 151 ARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMASLyCDRVLLLNEGRMVDLNSPRQVMTE 230
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
.
gi 1599980197 231 H 231
Cdd:COG4988 562 N 562
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
2-249 |
6.58e-46 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 160.48 E-value: 6.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGydektPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLsPSEGTITLQGKAIADYHSKELAQKMAVL 81
Cdd:PRK03695 1 MQLNDVAVS-----TRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADTTFAYKVKEVVALGRYPHqkgwlaSESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQ----- 156
Cdd:PRK03695 75 SQQQTPPFAMPVFQYLTLHQPDK------TRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdi 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 157 --EPDLLLLDEPTNHLDISHQM---QLLDALkdwtrTRQ-LTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTE 230
Cdd:PRK03695 149 npAGQLLLLDEPMNSLDVAQQAaldRLLSEL-----CQQgIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTP 223
|
250 260
....*....|....*....|..
gi 1599980197 231 HQLANVYETKIRR---NEHPTI 249
Cdd:PRK03695 224 ENLAQVFGVNFRRldvEGHPML 245
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-217 |
8.03e-45 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 156.50 E-value: 8.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGY---DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA--- 75
Cdd:cd03255 1 IELKNLSKTYgggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 -QKMAVLPQtadttfAYK------VKEVVALGRYPHQKGWlasesQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRA 148
Cdd:cd03255 81 rRHIGFVFQ------SFNllpdltALENVELPLLLAGVPK-----KERRERAEELLERVGLGDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 149 LLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASlYCDRVLLLNEGR 217
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGK 217
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-231 |
8.61e-45 |
|
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: 165.32 E-value: 8.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGY-DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:COG4987 334 LELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTA---DTTfaykVKEVVALGRyPHqkgwlASESQedervIREAMEQT--DTWkFRNKP--LQT--------LSGGER 145
Cdd:COG4987 414 VPQRPhlfDTT----LRENLRLAR-PD-----ATDEE-----LWAALERVglGDW-LAALPdgLDTwlgeggrrLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 146 QRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMASLyCDRVLLLNEGRMVDLNSPR 225
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLER-MDRILVLEDGRIVEQGTHE 554
|
....*.
gi 1599980197 226 QVMTEH 231
Cdd:COG4987 555 ELLAQN 560
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-217 |
9.96e-45 |
|
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: 154.46 E-value: 9.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEK-TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTAdttfaykvkevvalgryphqkgWLASESqedervIREAMeqtdtwkfrnkplqtLSGGERQRALLARALCQEPDL 160
Cdd:cd03228 81 VPQDP----------------------FLFSGT------IRENI---------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 161 LLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMASLyCDRVLLLNEGR 217
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-228 |
1.87e-44 |
|
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: 166.16 E-value: 1.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDE-KTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQ 83
Cdd:COG2274 477 ENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 84 TaDTTFAYKVKEVVALGRyphqkgwlasESQEDERVIrEAMEQTDTWKF-RNKPL----------QTLSGGERQRALLAR 152
Cdd:COG2274 557 D-VFLFSGTIRENITLGD----------PDATDEEII-EAARLAGLHDFiEALPMgydtvvgeggSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1599980197 153 ALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMASLyCDRVLLLNEGRMVDLNSPRQVM 228
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-229 |
8.85e-44 |
|
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: 154.13 E-value: 8.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA------ 75
Cdd:cd03219 1 LEVRGLTKRFGGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 --QKMAVLPqtaDTTfaykVKEVVALGRYPHQKG------WLASESQEDERViREAMEQTDTWKFRNKPLQTLSGGERQR 147
Cdd:cd03219 80 tfQIPRLFP---ELT----VLENVMVAAQARTGSglllarARREEREARERA-EELLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 148 ALLARALCQEPDLLLLDEPT---NHLDISHQMQLLDALKDwtrtRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSP 224
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRE----RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
....*
gi 1599980197 225 RQVMT 229
Cdd:cd03219 228 DEVRN 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-242 |
1.14e-43 |
|
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: 154.47 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEG-TITLQGK-----AIAD------ 68
Cdd:COG1119 3 LLELRNVTVRRGGKT-ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggeDVWElrkrig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 69 YHSKELAQKMavlpqTADTTfaykVKEVVA------LGRYPHqkgwlasESQEDERVIREAMEQTDTWKFRNKPLQTLSG 142
Cdd:COG1119 82 LVSPALQLRF-----PRDET----VLDVVLsgffdsIGLYRE-------PTDEQRERARELLELLGLAHLADRPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 143 GERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLN 222
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG 225
|
250 260
....*....|....*....|
gi 1599980197 223 SPRQVMTEHQLANVYETKIR 242
Cdd:COG1119 226 PKEEVLTSENLSEAFGLPVE 245
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-220 |
3.31e-43 |
|
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: 152.24 E-value: 3.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEK---TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKelaqkM 78
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 79 AVLPQTaDTTFAYK-VKEVVALGryPHQKGWLASESQEderVIREAMEQTDTWKFRNK-PLQtLSGGERQRALLARALCQ 156
Cdd:cd03293 76 GYVFQQ-DALLPWLtVLDNVALG--LELQGVPKAEARE---RAEELLELVGLSGFENAyPHQ-LSGGMRQRVALARALAV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 157 EPDLLLLDEPTNHLDISHQMQLLDALKD-WTRTRQlTVVAILHDLNMASLYCDRVLLLNE--GRMVD 220
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDiWRETGK-TVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-220 |
1.03e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 150.96 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGY---DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA-- 75
Cdd:COG1136 4 LLELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 ---------QKMAVLPqtaDTTfaykVKEVVALgryPHQkgwLASES-QEDERVIREAMEQTDTWKFRNKPLQTLSGGER 145
Cdd:COG1136 84 rrrhigfvfQFFNLLP---ELT----ALENVAL---PLL---LAGVSrKERRERARELLERVGLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 146 QRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASlYCDRVLLLNEGRMVD 220
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVS 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-216 |
1.29e-42 |
|
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: 150.10 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 3 DAQNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIadyHSKELAQKMAVLP 82
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 83 QTADTTFAYK-VKEVVALGryphqkgwlASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLL 161
Cdd:cd03226 78 QDVDYQLFTDsVREELLLG---------LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 162 LLDEPTNHLDISHQMQLLDALKDWTRTRQlTVVAILHDLNMASLYCDRVLLLNEG 216
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-229 |
1.72e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 151.78 E-value: 1.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEK---TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIAdyhskELAQK 77
Cdd:COG1116 7 ALELRGVSKRFPTGgggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-----GPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 78 MAVLPQtADTTFAYK-VKEVVALGryPHQKGWLASESQEDervIREAMEQTDTWKFRNK-PLQtLSGGERQRALLARALC 155
Cdd:COG1116 82 RGVVFQ-EPALLPWLtVLDNVALG--LELRGVPKAERRER---ARELLELVGLAGFEDAyPHQ-LSGGMRQRVAIARALA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 156 QEPDLLLLDEPTNHLDI--SHQMQ--LLDAlkdWTRTRQlTVVAILHDLNMASLYCDRVLLLNE--GRM-----VDLNSP 224
Cdd:COG1116 155 NDPEVLLMDEPFGALDAltRERLQdeLLRL---WQETGK-TVLFVTHDVDEAVFLADRVVVLSArpGRIveeidVDLPRP 230
|
....*
gi 1599980197 225 RQVMT 229
Cdd:COG1116 231 RDREL 235
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-229 |
8.69e-42 |
|
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: 148.97 E-value: 8.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA---QK 77
Cdd:COG1127 5 MIEVRNLTKSFGDRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 78 MAVLPQTA----DTTfaykVKEVVALGRYPHQKgwlASESQEDERViREAMEQTDTWKFRNK-PLQtLSGGERQRALLAR 152
Cdd:COG1127 84 IGMLFQGGalfdSLT----VFENVAFPLREHTD---LSEAEIRELV-LEKLELVGLPGAADKmPSE-LSGGMRKRVALAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 153 ALCQEPDLLLLDEPTNHLD-IShqMQLLDAL-KDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMT 229
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDpIT--SAVIDELiRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-217 |
3.17e-41 |
|
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: 146.47 E-value: 3.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADyHSKELAQKMAV 80
Cdd:COG4133 2 MLEAENLSCRRGER-LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTADTTFAYKVKEVVALgrypHQKGWLASESQEDervIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDL 160
Cdd:COG4133 80 LGHADGLKPELTVRENLRF----WAALYGLRADREA---IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 161 LLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMAslyCDRVLLLNEGR 217
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA---AARVLDLGDFK 206
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-219 |
8.00e-41 |
|
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: 145.81 E-value: 8.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 6 NVSVGYDE-KTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQT 84
Cdd:cd03245 7 NVSFSYPNqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 85 AdTTFAYKVKEVVALGRYPHqkgwlasesqEDERVIReAMEQTDTWKF-RNKPL----------QTLSGGERQRALLARA 153
Cdd:cd03245 87 V-TLFYGTLRDNITLGAPLA----------DDERILR-AAELAGVTDFvNKHPNgldlqigergRGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1599980197 154 LCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMASLyCDRVLLLNEGRMV 219
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDL-VDRIIVMDSGRIV 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-228 |
1.01e-40 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 146.72 E-value: 1.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA----- 75
Cdd:COG0411 4 LLEVRGLTKRFGGLV-AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgia 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 ---QKMAVLPQ-TadttfaykVKEVVALGRYPHQKGWL----------ASESQEDERVIREAMEQTDTWKFRNKPLQTLS 141
Cdd:COG0411 83 rtfQNPRLFPElT--------VLENVLVAAHARLGRGLlaallrlpraRREEREARERAEELLERVGLADRADEPAGNLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 142 GGERQRALLARALCQEPDLLLLDEPT---NHLDISHQMQLLDALKDwtrTRQLTVVAILHDLNMASLYCDRVLLLNEGRM 218
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRD---ERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
250
....*....|
gi 1599980197 219 VDLNSPRQVM 228
Cdd:COG0411 232 IAEGTPAEVR 241
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-227 |
1.45e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 149.09 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEkTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADyhskelaqkmav 80
Cdd:COG3842 5 ALELENVSKRYGD-VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPqtadttfAYK-----------------VKEVVALGryPHQKGWlaSESQEDERViREAMEQTDTWKFRNKPLQTLSGG 143
Cdd:COG3842 72 LP-------PEKrnvgmvfqdyalfphltVAENVAFG--LRMRGV--PKAEIRARV-AELLELVGLEGLADRYPHQLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 144 ERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNS 223
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
....
gi 1599980197 224 PRQV 227
Cdd:COG3842 220 PEEI 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-168 |
2.13e-40 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 142.40 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 18 IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQtaDTTF--AYKVKE 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQ--DPQLfpRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 96 VVALGRYPhqKGWLASESQEDERVIREAMEQTDTWKFR-NKPLQTLSGGERQRALLARALCQEPDLLLLDEPTN 168
Cdd:pfam00005 79 NLRLGLLL--KGLSKREKDARAEEALEKLGLGDLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-219 |
2.94e-40 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 144.20 E-value: 2.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEkTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADY--HSKELA---Q 76
Cdd:cd03259 1 LELKGLSKTYGS-VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVppERRNIGmvfQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 77 KMAVLP-QTadttfaykVKEVVALGRYPHQKgwlaSESQEDERViREAMEQTDTWKFRNKPLQTLSGGERQRALLARALC 155
Cdd:cd03259 80 DYALFPhLT--------VAENIAFGLKLRGV----PKAEIRARV-RELLELVGLEGLLNRYPHELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 156 QEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-219 |
3.30e-40 |
|
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: 147.12 E-value: 3.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGY---DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSP---SEGTITLQGKAIADYHSKEL 74
Cdd:COG0444 1 LLEVRNLKVYFptrRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 75 AQ----KMAVLPQTADTTF--AYKVKEVVALGRYPHQKgwlASESQEDERVIrEAMEQ---TDTWKFRNK-PLQtLSGGE 144
Cdd:COG0444 81 RKirgrEIQMIFQDPMTSLnpVMTVGDQIAEPLRIHGG---LSKAEARERAI-ELLERvglPDPERRLDRyPHE-LSGGM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 145 RQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-217 |
4.94e-40 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 151.37 E-value: 4.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 4 AQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAiadyhskelaqKMAVLPQ 83
Cdd:COG0488 1 LENLSKSFGGR-PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 84 TADTTFAYKVKEVVALG---------RYPHQKGWLASESQEDERVIR--EAMEQTDTWKFR-----------------NK 135
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGdaelraleaELEELEAKLAEPDEDLERLAElqEEFEALGGWEAEaraeeilsglgfpeedlDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 136 PLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDIshqmqllDA---LKDWTRTRQLTVVAILHD---LNMAslyCDR 209
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-------ESiewLEEFLKNYPGTVLVVSHDryfLDRV---ATR 218
|
....*...
gi 1599980197 210 VLLLNEGR 217
Cdd:COG0488 219 ILELDRGK 226
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
23-227 |
1.16e-39 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 143.07 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 23 FQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAiadyhSKELAQKMAVLPQTADTTFAY--KVKEVVALG 100
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-----PGKGWRHIGYVPQRHEFAWDFpiSVAHTVMSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 101 RYPHQkGWLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLD 180
Cdd:TIGR03771 76 RTGHI-GWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1599980197 181 ALKDWTRTrQLTVVAILHDLNMASLYCDRVLLLNeGRMVDLNSPRQV 227
Cdd:TIGR03771 155 LFIELAGA-GTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQL 199
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-219 |
2.48e-39 |
|
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: 142.43 E-value: 2.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDeKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQK-MA 79
Cdd:COG0410 3 MLEVENLHAGYG-GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 80 VLPQT----ADTTfaykVKEVVALGRYPHQkgwlasesqeDERVIREAMEQTDTW-----KFRNKPLQTLSGGERQRALL 150
Cdd:COG0410 82 YVPEGrrifPSLT----VEENLLLGAYARR----------DRAEVRADLERVYELfprlkERRRQRAGTLSGGEQQMLAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1599980197 151 ARALCQEPDLLLLDEPTnhLDISHQM--QLLDALKDWtRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:COG0410 148 GRALMSRPKLLLLDEPS--LGLAPLIveEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIV 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-229 |
6.61e-39 |
|
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: 141.10 E-value: 6.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKEL---AQKMAVL 81
Cdd:cd03261 4 RGLTKSFGGRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTA----DTTfaykVKEVVALgryphqkgWLASESQEDERVIRE-AMEQTDTWKFRN----KPLQtLSGGERQRALLAR 152
Cdd:cd03261 83 FQSGalfdSLT----VFENVAF--------PLREHTRLSEEEIREiVLEKLEAVGLRGaedlYPAE-LSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 153 ALCQEPDLLLLDEPTNHLD-IShqMQLLDAL-KDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMT 229
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDpIA--SGVIDDLiRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-219 |
2.23e-38 |
|
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: 139.49 E-value: 2.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDeKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQK-MAV 80
Cdd:cd03224 1 LEVENLNAGYG-KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQT----ADTTfaykVKEVVALGRYPHQKgwlaSESQED-ERV------IREameqtdtwkFRNKPLQTLSGGERQRAL 149
Cdd:cd03224 80 VPEGrrifPELT----VEENLLLGAYARRR----AKRKARlERVyelfprLKE---------RRKQLAGTLSGGEQQMLA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 150 LARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDwTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:cd03224 143 IARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRE-LRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-219 |
2.29e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 147.23 E-value: 2.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQt 84
Cdd:COG1132 343 ENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQ- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 85 aDTT-FAYKVKEVVALGRyPHqkgwlASESQedervIREAMEQTDTWKF-RNKP--LQT--------LSGGERQRALLAR 152
Cdd:COG1132 422 -DTFlFSGTIRENIRYGR-PD-----ATDEE-----VEEAAKAAQAHEFiEALPdgYDTvvgergvnLSGGQRQRIAIAR 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 153 ALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMASLyCDRVLLLNEGRMV 219
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRN-ADRILVLDDGRIV 553
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-218 |
2.55e-38 |
|
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: 137.73 E-value: 2.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGY-DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTaDTTFAYKVKEVValgryphqkgwlasesqedervireameqtdtwkfrnkplqtLSGGERQRALLARALCQEPDL 160
Cdd:cd03246 81 LPQD-DELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 161 LLLDEPTNHLDISHQMQLLDALKDwTRTRQLTVVAILHDLNMASLyCDRVLLLNEGRM 218
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAA-LKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-217 |
3.82e-38 |
|
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: 137.32 E-value: 3.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADY--HSKELAQKMA 79
Cdd:cd03229 1 LELKNVSKRYGQKT-VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 80 VLPQTADTTFAYKVKEVVALGryphqkgwlasesqedervireameqtdtwkfrnkplqtLSGGERQRALLARALCQEPD 159
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 160 LLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGR 217
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-251 |
3.98e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 140.21 E-value: 3.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIaDYHSKELA---QK 77
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLevrKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 78 MAVLPQTADTT-FAYKVKEVVALGryPHQKGwLASEsqEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQ 156
Cdd:PRK13639 80 VGIVFQNPDDQlFAPTVEEDVAFG--PLNLG-LSKE--EVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 157 EPDLLLLDEPTNHLDISHQMQLLDALKDWTRtRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTehqlanv 236
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS------- 226
|
250
....*....|....*
gi 1599980197 237 yETKIRRNEHPTIPR 251
Cdd:PRK13639 227 -DIETIRKANLRLPR 240
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-220 |
4.30e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 138.65 E-value: 4.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA---QK 77
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 78 MAVLPQT----ADTTfaykVKEVVAL-----GRyphqkgwlasESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRA 148
Cdd:COG2884 81 IGVVFQDfrllPDRT----VYENVALplrvtGK----------SRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1599980197 149 LLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRtRQLTVVAILHDLNMASLYCDRVLLLNEGRMVD 220
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-220 |
8.35e-38 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 144.82 E-value: 8.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLqGKAIadyhskelaqKMAV 80
Cdd:COG0488 315 VLELEGLSKSYGDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQtadttfaykvkevvalgrypHQkgwlaSESQEDERV---IREAMEQTDTWKFRN-------------KPLQTLSGGE 144
Cdd:COG0488 383 FDQ--------------------HQ-----EELDPDKTVldeLRDGAPGGTEQEVRGylgrflfsgddafKPVGVLSGGE 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1599980197 145 RQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWtrtrQLTVVAILHDLNMASLYCDRVLLLNEGRMVD 220
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF----PGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-219 |
3.05e-37 |
|
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: 135.87 E-value: 3.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSkelaQKMAVL 81
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR----NRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADTTFAYKVKEV-VALGRYphqKGWLASESQEDervIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDL 160
Cdd:cd03269 76 PEERGLYPKMKVIDQlVYLAQL---KGLKKEEARRR---IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 161 LLLDEPTNHLDISHQMQLLDALKDWTRtRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-217 |
4.49e-37 |
|
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: 133.34 E-value: 4.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAiadyhskelaqKMAVL 81
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQtadttfaykvkevvalgryphqkgwlasesqedervireameqtdtwkfrnkplqtLSGGERQRALLARALCQEPDLL 161
Cdd:cd03221 69 EQ--------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1599980197 162 LLDEPTNHLDISHQMQLLDALKDWTRtrqlTVVAILHDLNMASLYCDRVLLLNEGR 217
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-229 |
5.89e-37 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 136.28 E-value: 5.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQT 84
Cdd:cd03295 4 ENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 85 ADTTFAYKVKEVVALgrYPHQKGWlaSESQEDERViREAME--QTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLL 162
Cdd:cd03295 84 IGLFPHMTVEENIAL--VPKLLKW--PKEKIRERA-DELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 163 LDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMT 229
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-213 |
1.10e-36 |
|
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: 142.04 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVL 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTAdTTFAYKVKEVVALGRyphqkgwlaSESQEDErvIREAMEQTDTWKF---RNKPLQT--------LSGGERQRALL 150
Cdd:TIGR02857 402 PQHP-FLFAGTIAENIRLAR---------PDASDAE--IREALERAGLDEFvaaLPQGLDTpigeggagLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1599980197 151 ARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMASLyCDRVLLL 213
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-227 |
1.46e-36 |
|
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: 134.62 E-value: 1.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLL-----SPSEGTITLQGKAIA--DYHSKEL 74
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYdlDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 75 AQKMAVLPQTAdTTFAYKVKEVVALGRYPHQKgwlASESQEDERViREAMEQTDTW---KFRNKPLQtLSGGERQRALLA 151
Cdd:cd03260 80 RRRVGMVFQKP-NPFPGSIYDNVAYGLRLHGI---KLKEELDERV-EEALRKAALWdevKDRLHALG-LSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 152 RALCQEPDLLLLDEPTNHLDISHQM---QLLDALKdwtrtRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQV 227
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAkieELIAELK-----KEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-227 |
2.05e-36 |
|
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: 134.63 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDE---KTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKEL--- 74
Cdd:cd03258 1 MIELKNVSKVFGDtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 75 AQKMAVLPQTADTTFAYKVKEVVAlgrYPHQkgwLASESQED-ERVIREAMEQTD-TWKFRNKPLQtLSGGERQRALLAR 152
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVA---LPLE---IAGVPKAEiEERVLELLELVGlEDKADAYPAQ-LSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 153 ALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQV 227
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-230 |
7.38e-36 |
|
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: 133.92 E-value: 7.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 15 TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA-----------QKMAVLPQ 83
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRelrrkkismvfQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 84 -TADTTFAYKVkEVVALGRyphqkgwlasesQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLL 162
Cdd:cd03294 117 rTVLENVAFGL-EVQGVPR------------AEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 163 LDEPTNHLD--ISHQMQllDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTE 230
Cdd:cd03294 184 MDEAFSALDplIRREMQ--DELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-219 |
8.76e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 134.47 E-value: 8.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE------- 73
Cdd:COG4152 1 MLELKGLTKRFGDKT-AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 74 --LAQKMAVLPQtadttfaykvkeVVALGRYphqKGWLAsesqederviREAMEQTDTW--KF-----RNKPLQTLSGGE 144
Cdd:COG4152 80 rgLYPKMKVGEQ------------LVYLARL---KGLSK----------AEAKRRADEWleRLglgdrANKKVEELSKGN 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 145 RQRALLARALCQEPDLLLLDEPTNHLD-IShqmqlLDALKDWTRTRQLTVVAIL---HDLNMASLYCDRVLLLNEGRMV 219
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLDpVN-----VELLKDVIRELAAKGTTVIfssHQMELVEELCDRIVIINKGRKV 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-217 |
1.73e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 131.80 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTpiiQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKElaQKMAV 80
Cdd:COG3840 1 MLRLDDLTYRYGDFP---LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQtaDTT-FAY-KVKEVVALGRYPHQKgwLaseSQEDERVIREAMEQTDTWKFRN-KPlQTLSGGERQRALLARALCQE 157
Cdd:COG3840 76 LFQ--ENNlFPHlTVAQNIGLGLRPGLK--L---TAEQRAQVEQALERVGLAGLLDrLP-GQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 158 PDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGR 217
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
2.09e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.81 E-value: 2.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYD-EKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMA 79
Cdd:PRK13632 7 MIKVENVSFSYPnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 80 VLPQTADTTF-AYKVKEVVALG----RYPHQKGWlasesqedeRVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARAL 154
Cdd:PRK13632 87 IIFQNPDNQFiGATVEDDIAFGlenkKVPPKKMK---------DIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 155 CQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLyCDRVLLLNEGRMVDLNSPRQVMTEHQ 232
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
21-224 |
4.67e-35 |
|
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: 130.57 E-value: 4.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 21 LSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADyHSKELAQKMAVLPQTADTTFAYKVKEVVALg 100
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGWENLYI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 101 rypHQKGWLASESQEDERvIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLD 180
Cdd:cd03265 97 ---HARLYGVPGAERRER-IDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1599980197 181 ALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSP 224
Cdd:cd03265 173 YIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-227 |
6.16e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.68 E-value: 6.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDE-KTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:PRK13635 6 IRVEHISFRYPDaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTADTTF-AYKVKEVVALGRYPHQkgwlASESQEDERViREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPD 159
Cdd:PRK13635 86 VFQNPDNQFvGATVQDDVAFGLENIG----VPREEMVERV-DQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 160 LLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMAsLYCDRVLLLNEGRMVDLNSPRQV 227
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-227 |
2.03e-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: 128.89 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADY-----HSKELAQ 76
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLpphkrPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 77 KMAVLPQ---TADTTFAYKVKEVvalgryphqkgwlaSESQEDERViREAMEQTDTWKFRNKPLQTLSGGERQRALLARA 153
Cdd:cd03300 80 NYALFPHltvFENIAFGLRLKKL--------------PKAEIKERV-AEALDLVQLEGYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 154 LCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQV 227
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-227 |
2.93e-34 |
|
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: 128.61 E-value: 2.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 21 LSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKElaQKMAVLPQTAdTTFAYK-VKEVVAL 99
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNY-ALFPHMtVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 100 GrYPHQKgwlaSESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLL 179
Cdd:cd03299 95 G-LKKRK----VDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1599980197 180 DALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQV 227
Cdd:cd03299 170 EELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
15-226 |
3.21e-34 |
|
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: 128.01 E-value: 3.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 15 TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIAdYHSKELAQKMAVLPQTaDTTFAY-KV 93
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGYCPQF-DALFDElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 94 KEVVAL-GRyphqkgwLASESQEDERVIREAM-EQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLD 171
Cdd:cd03263 93 REHLRFyAR-------LKGLPKSEIKEEVELLlRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 172 ISHQMQLLDALKDWTRTRqlTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQ 226
Cdd:cd03263 166 PASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-246 |
3.33e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 129.97 E-value: 3.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIaDYHSK---ELAQK 77
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 78 MAVLPQTADTT-FAYKVKEVVALGRYPhqkgwLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQ 156
Cdd:PRK13636 84 VGMVFQDPDNQlFSASVYQDVSFGAVN-----LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 157 EPDLLLLDEPTNHLD---ISHQMQLldaLKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQL 233
Cdd:PRK13636 159 EPKVLVLDEPTAGLDpmgVSEIMKL---LVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
250
....*....|...
gi 1599980197 234 ANVYETKIRRNEH 246
Cdd:PRK13636 236 LRKVNLRLPRIGH 248
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-219 |
4.04e-34 |
|
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: 127.69 E-value: 4.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDeKTPIIQQLSFQVHKGeIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADyHSKELAQKMAVL 81
Cdd:cd03264 1 LQLENLTKRYG-KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADTTFAYKVKEVVAlgrypHQkGWLA--SESQEDERVIReAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPD 159
Cdd:cd03264 78 PQEFGVYPNFTVREFLD-----YI-AWLKgiPSKEVKARVDE-VLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 160 LLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-219 |
6.34e-34 |
|
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: 127.83 E-value: 6.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 16 PIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQTADTTFAYKVKE 95
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 96 VVALGRYPHQkgwlASESQEDERViREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQ 175
Cdd:cd03267 115 SFYLLAAIYD----LPPARFKKRL-DELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1599980197 176 MQLLDALKDWTRTRQLTVVAILHDL-NMASLyCDRVLLLNEGRMV 219
Cdd:cd03267 190 ENIRNFLKEYNRERGTTVLLTSHYMkDIEAL-ARRVLVIDKGRLL 233
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-220 |
7.04e-34 |
|
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: 127.10 E-value: 7.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTPIIQ---QLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGkaIADYHSK-ELAQ 76
Cdd:cd03266 1 MITADALTKRFRDVKKTVQavdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPaEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 77 KMAVLPqtaDTTFAYK---VKEVVA-LGRYPHQKGwlasesQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLAR 152
Cdd:cd03266 79 RLGFVS---DSTGLYDrltARENLEyFAGLYGLKG------DELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 153 ALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWtRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVD 220
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-238 |
3.33e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 128.80 E-value: 3.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADyHSKELAQKMAVL 81
Cdd:PRK13536 42 IDLAGVSKSYGDK-AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADTTFAYKVKE-VVALGRYphqkgwLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDL 160
Cdd:PRK13536 120 PQFDNLDLEFTVREnLLVFGRY------FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 161 LLLDEPTNHLDiSHQMQLLdalkdWTRTRQL-----TVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQLAN 235
Cdd:PRK13536 194 LILDEPTTGLD-PHARHLI-----WERLRSLlargkTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQ 267
|
...
gi 1599980197 236 VYE 238
Cdd:PRK13536 268 VIE 270
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-200 |
1.18e-32 |
|
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: 130.56 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVL 81
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADtTFAYKVKEVVALGR--YPHQKGWLASESQEDERVIREAMEQTDTWKFRNKplQTLSGGERQRALLARALCQEPD 159
Cdd:TIGR02868 415 AQDAH-LFDTTVRENLRLARpdATDEELWAALERVGLADWLRALPDGLDTVLGEGG--ARLSGGERQRLALARALLADAP 491
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1599980197 160 LLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDL 200
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-230 |
1.47e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 125.20 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGY-----DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADY-HSKEL 74
Cdd:PRK13633 4 MIKCKNVSYKYesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 75 AQKMAVLPQTADTTF-AYKVKEVVALGryPHQKGWLASESQEdeRViREAMEQTDTWKFRNKPLQTLSGGERQRALLARA 153
Cdd:PRK13633 84 RNKAGMVFQNPDNQIvATIVEEDVAFG--PENLGIPPEEIRE--RV-DESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 154 LCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMAsLYCDRVLLLNEGRMVDLNSPRQVMTE 230
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-228 |
1.66e-32 |
|
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: 130.25 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGY-DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:COG4618 331 LSVENLTVVPpGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQtaDTT-FAYKVKEVVAlgRYPhqkgwlaseSQEDERVIREA-------MEQT-----DTwkfrnkPL----QTLSGG 143
Cdd:COG4618 411 LPQ--DVElFDGTIAENIA--RFG---------DADPEKVVAAAklagvheMILRlpdgyDT------RIgeggARLSGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 144 ERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWtRTRQLTVVAILHDLNMASLyCDRVLLLNEGRMVDLNS 223
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGP 549
|
....*
gi 1599980197 224 PRQVM 228
Cdd:COG4618 550 RDEVL 554
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-233 |
1.89e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 125.30 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGY-DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSP---SEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:PRK13640 9 KHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREKVGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTADTTF-AYKVKEVVALGRYPHQkgwlaSESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPD 159
Cdd:PRK13640 89 VFQNPDNQFvGATVGDDVAFGLENRA-----VPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 160 LLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLyCDRVLLLNEGRMVDLNSPRQVMTEHQL 233
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-229 |
1.96e-32 |
|
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: 129.80 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTPIIQQ----------LSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLsPSEGTITLQGKAIADYHS 71
Cdd:COG4172 276 LEARDLKVWFPIKRGLFRRtvghvkavdgVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 72 KELA---QKMAVLPQtaDTtFA-----YKVKEVVALGRYPHQKGWlaSESQEDERVIrEAMEQTD-TWKFRNKPLQTLSG 142
Cdd:COG4172 355 RALRplrRRMQVVFQ--DP-FGslsprMTVGQIIAEGLRVHGPGL--SAAERRARVA-EALEEVGlDPAARHRYPHEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 143 GERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLN 222
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQG 508
|
....*..
gi 1599980197 223 SPRQVMT 229
Cdd:COG4172 509 PTEQVFD 515
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-228 |
4.26e-32 |
|
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: 122.72 E-value: 4.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 6 NVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQta 85
Cdd:cd03254 7 NVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQ-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 86 DTT-FAYKVKEVVALGRyphqkgwlasESQEDERVIREAMEQ--TDTWKFRNKPLQT--------LSGGERQRALLARAL 154
Cdd:cd03254 85 DTFlFSGTIMENIRLGR----------PNATDEEVIEAAKEAgaHDFIMKLPNGYDTvlgenggnLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 155 CQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMAsLYCDRVLLLNEGRMVDLNSPRQVM 228
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDELL 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-219 |
1.82e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 121.89 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYD---EKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAI----ADyhSKE 73
Cdd:COG4525 3 MLTVRHVSVRYPgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgAD--RGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 74 LAQKMAVLP-QTadttfaykVKEVVALG-RyphqkgwLASES-QEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALL 150
Cdd:COG4525 81 VFQKDALLPwLN--------VLDNVAFGlR-------LRGVPkAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 151 ARALCQEPDLLLLDEPTNHLD--ISHQMQ-LLdaLKDWTRTRQlTVVAILHDLNMASLYCDRVLLL--NEGRMV 219
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDalTREQMQeLL--LDVWQRTGK-GVFLITHSVEEALFLATRLVVMspGPGRIV 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-229 |
3.01e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 122.61 E-value: 3.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADyHSKELAQKMAVL 81
Cdd:PRK13537 8 IDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADTTFAYKVKE-VVALGRYphqkgwLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDL 160
Cdd:PRK13537 86 PQFDNLDPDFTVREnLLVFGRY------FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1599980197 161 LLLDEPTNHLD--ISHQMqlldalkdWTRTRQL-----TVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMT 229
Cdd:PRK13537 160 LVLDEPTTGLDpqARHLM--------WERLRSLlargkTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-219 |
3.83e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 121.38 E-value: 3.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQT 84
Cdd:PRK13647 8 EDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 85 AD-TTFAYKVKEVVALGryPHQKGWLASESqeDERViREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLL 163
Cdd:PRK13647 88 PDdQVFSSTVWDDVAFG--PVNMGLDKDEV--ERRV-EEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 164 DEPTNHLDISHQ---MQLLDALKDwtrtRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:PRK13647 163 DEPMAYLDPRGQetlMEILDRLHN----QGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-227 |
3.92e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 121.38 E-value: 3.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKT--PIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKM 78
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 79 AVLPQTADTTF-AYKVKEVVALGRypHQKGWLASESQEdeRViREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQE 157
Cdd:PRK13650 84 GMVFQNPDNQFvGATVEDDVAFGL--ENKGIPHEEMKE--RV-NEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 158 PDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLyCDRVLLLNEGRMVDLNSPRQV 227
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVAL-SDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-220 |
4.09e-31 |
|
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: 119.24 E-value: 4.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKelAQKMAVLpqt 84
Cdd:cd03268 4 NDLTKTYGKKR-VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--LRRIGAL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 85 adttfaykvkeVVALGRYPHQKG-----WLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPD 159
Cdd:cd03268 78 -----------IEAPGFYPNLTArenlrLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1599980197 160 LLLLDEPTNHLDISHQMQLLDALKDWtRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVD 220
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-219 |
1.85e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 120.58 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 18 IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITlqgkaIADY----HSKELAQKMAV-----------LP 82
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR-----VLGYvpfkRRKEFARRIGVvfgqrsqlwwdLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 83 qTADTtFA-----YKVkevvalgryphqkgwlaSESQEDERV--IREAMEQTDtwkFRNKPLQTLSGGERQRALLARALC 155
Cdd:COG4586 113 -AIDS-FRllkaiYRI-----------------PDAEYKKRLdeLVELLDLGE---LLDTPVRQLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 156 QEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVvaIL--HDLN-MASLyCDRVLLLNEGRMV 219
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTI--LLtsHDMDdIEAL-CDRVIVIDHGRII 234
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-227 |
2.10e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 121.02 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDeKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGK-AIADYHSKE-----LA 75
Cdd:COG1118 3 IEVRNISKRFG-SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdLFTNLPPRErrvgfVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 QKMA----------------VLPQTADTTFAyKVKEVVAL-------GRYPHQkgwlasesqedervireameqtdtwkf 132
Cdd:COG1118 82 QHYAlfphmtvaeniafglrVRPPSKAEIRA-RVEELLELvqleglaDRYPSQ--------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 133 rnkplqtLSGGERQRALLARALCQEPDLLLLDEPTNHLDIshqmQLLDALKDWTRT--RQLTVVAIL--HDLNMASLYCD 208
Cdd:COG1118 134 -------LSGGQRQRVALARALAVEPEVLLLDEPFGALDA----KVRKELRRWLRRlhDELGGTTVFvtHDQEEALELAD 202
|
250
....*....|....*....
gi 1599980197 209 RVLLLNEGRMVDLNSPRQV 227
Cdd:COG1118 203 RVVVMNQGRIEQVGTPDEV 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
7-213 |
2.31e-30 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 119.22 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 7 VSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIadyhSKELAQKM-AVLPQT- 84
Cdd:PRK15056 12 VTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT----RQALQKNLvAYVPQSe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 85 -ADTTFAYKVKEVVALGRYPHQkGWLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLL 163
Cdd:PRK15056 88 eVDWSFPVLVEDVVMMGRYGHM-GWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1599980197 164 DEPTNHLDISHQMQLLDALKDwTRTRQLTVVAILHDLNMASLYCDRVLLL 213
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRE-LRDEGKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
16-227 |
3.35e-30 |
|
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: 117.83 E-value: 3.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 16 PIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE-----LAQKMAVLPQTAdttfa 90
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErnvgfVFQHYALFRHMT----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 91 ykVKEVVALGRYPHQKGWLASESQEDERViREAME--QTDtWKFRNKPLQtLSGGERQRALLARALCQEPDLLLLDEPTN 168
Cdd:cd03296 91 --VFDNVAFGLRVKPRSERPPEAEIRAKV-HELLKlvQLD-WLADRYPAQ-LSGGQRQRVALARALAVEPKVLLLDEPFG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1599980197 169 HLDishqMQLLDALKDWTRTRQ----LTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQV 227
Cdd:cd03296 166 ALD----AKVRKELRRWLRRLHdelhVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-219 |
4.04e-30 |
|
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: 115.49 E-value: 4.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEK-TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYhSKELAQKMAV 80
Cdd:cd03247 1 LSINNVSFSYPEQeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTA---DTTfaykvkevvalgryphqkgwlasesqedervireameqtdtwkFRNKPLQTLSGGERQRALLARALCQE 157
Cdd:cd03247 80 LNQRPylfDTT-------------------------------------------LRNNLGRRFSGGERQRLALARILLQD 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1599980197 158 PDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMASlYCDRVLLLNEGRMV 219
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIE-HMDKILFLENGKII 175
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-227 |
1.59e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 118.64 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDeKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKElaQKMAV 80
Cdd:COG3839 3 SLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTadttfaYkvkevvALgrYPH-------------QKgwlASESQEDERViREAMEQTDTWKFRN-KPLQtLSGGERQ 146
Cdd:COG3839 80 VFQS------Y------AL--YPHmtvyeniafplklRK---VPKAEIDRRV-REAAELLGLEDLLDrKPKQ-LSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 147 RALLARALCQEPDLLLLDEP-TNhldishqmqlLDA-LKDWTRT------RQL--TVVAILHD----LNMAslycDRVLL 212
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPlSN----------LDAkLRVEMRAeikrlhRRLgtTTIYVTHDqveaMTLA----DRIAV 206
|
250
....*....|....*
gi 1599980197 213 LNEGRMVDLNSPRQV 227
Cdd:COG3839 207 MNDGRIQQVGTPEEL 221
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-231 |
1.62e-29 |
|
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: 115.79 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 6 NVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQta 85
Cdd:cd03253 5 NVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 86 DTT-FAYKVKEVVALGRyphqkgWLASEsQEDERVIREAMEQTDTWKFRNKpLQT--------LSGGERQRALLARALCQ 156
Cdd:cd03253 83 DTVlFNDTIGYNIRYGR------PDATD-EEVIEAAKAAQIHDKIMRFPDG-YDTivgerglkLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 157 EPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMASlYCDRVLLLNEGRMVDLNSPRQVMTEH 231
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIV-NADKIIVLKDGRIVERGTHEELLAKG 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-215 |
4.43e-29 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 114.83 E-value: 4.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYhskeLAQKMAV 80
Cdd:PRK09544 4 LVSLENVSVSFGQRR-VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGY----VPQKLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 lpqtaDTTFAYKVKEVVALgrYPHQKgwlasesQEDervIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDL 160
Cdd:PRK09544 79 -----DTTLPLTVNRFLRL--RPGTK-------KED---ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 161 LLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNE 215
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-230 |
6.51e-29 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 119.76 E-value: 6.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGY-DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:TIGR01842 317 LSVENVTIVPpGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTADTtFAYKVKEVVAlgRYphqkgwlaSESQEDERVIrEAMEQTDTWKFRNKPLQ-----------TLSGGERQRAL 149
Cdd:TIGR01842 397 LPQDVEL-FPGTVAENIA--RF--------GENADPEKII-EAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIA 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 150 LARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDwTRTRQLTVVAILHDLNMASLyCDRVLLLNEGRMVDLNSPRQVMT 229
Cdd:TIGR01842 465 LARALYGDPKLVVLDEPNSNLDEEGEQALANAIKA-LKARGITVVVITHRPSLLGC-VDKILVLQDGRIARFGERDEVLA 542
|
.
gi 1599980197 230 E 230
Cdd:TIGR01842 543 K 543
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-218 |
8.39e-29 |
|
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: 113.33 E-value: 8.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEK--TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLP 82
Cdd:cd03248 15 QNVTFAYPTRpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 83 QTAdTTFAYKVKEVVALGryphqkgwLASESQEDervIREAMEQTDTWKFRNKPLQ-----------TLSGGERQRALLA 151
Cdd:cd03248 95 QEP-VLFARSLQDNIAYG--------LQSCSFEC---VKEAAQKAHAHSFISELASgydtevgekgsQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 152 RALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMASlYCDRVLLLNEGRM 218
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-220 |
8.55e-29 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 113.22 E-value: 8.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGY---DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA-- 75
Cdd:TIGR02211 1 LLKCENLGKRYqegKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAkl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 --QKMAVLPQTADTTFAYKVKEVVALgryP----HQKgwlASESQEDERVIREAMEQTDtwKFRNKPLQtLSGGERQRAL 149
Cdd:TIGR02211 81 rnKKLGFIYQFHHLLPDFTALENVAM---PlligKKS---VKEAKERAYEMLEKVGLEH--RINHRPSE-LSGGERQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1599980197 150 LARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYcDRVLLLNEGRMVD 220
Cdd:TIGR02211 152 IARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-220 |
8.75e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 114.41 E-value: 8.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE--LAQKM 78
Cdd:PRK11248 1 MLQISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERgvVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 79 AVLPQTadttfayKVKEVVALGRYphqkgwLASESQEDERVI-REAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQE 157
Cdd:PRK11248 80 GLLPWR-------NVQDNVAFGLQ------LAGVEKMQRLEIaHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAAN 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 158 PDLLLLDEPTNHLD--ISHQMQLLdALKDWTRTRQlTVVAILHDLNMASLYCDRVLLL--NEGRMVD 220
Cdd:PRK11248 147 PQLLLLDEPFGALDafTREQMQTL-LLKLWQETGK-QVLLITHDIEEAVFMATELVLLspGPGRVVE 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-219 |
1.47e-28 |
|
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: 112.39 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 20 QLSFQVhKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHskelaQKMAVLPQtaDTTFAYKVKEVvAL 99
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSR-----KKINLPPQ--QRKIGLVFQQY-AL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 100 grYPHQK-------GWLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDI 172
Cdd:cd03297 87 --FPHLNvrenlafGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1599980197 173 SHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-219 |
1.50e-28 |
|
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: 112.20 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 21 LSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGkaiADYHSKELAQKMAVLPQTADTTFAY-KVKEVVAL 99
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING---VDVTAAPPADRPVSMLFQENNLFAHlTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 100 GRYPHQKgwlasESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLL 179
Cdd:cd03298 94 GLSPGLK-----LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1599980197 180 DALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-230 |
1.59e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 116.20 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADY-----HSKELAQKMA 79
Cdd:PRK09452 18 RGISKSFDGKE-VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaenrHVNTVFQSYA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 80 VLPQTAdttfaykVKEVVALG-RYphQKgwlASESQEDERViREA--MEQTDTWKFRnKPLQtLSGGERQRALLARALCQ 156
Cdd:PRK09452 97 LFPHMT-------VFENVAFGlRM--QK---TPAAEITPRV-MEAlrMVQLEEFAQR-KPHQ-LSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1599980197 157 EPDLLLLDEPTNHLD--ISHQMQLldALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTE 230
Cdd:PRK09452 162 KPKVLLLDESLSALDykLRKQMQN--ELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-233 |
2.90e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 113.16 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHS-KELAQKMA 79
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 80 VLPQTADTTFAYK-VKEVVALGryPHQkgwLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEP 158
Cdd:PRK13644 81 IVFQNPETQFVGRtVEEDLAFG--PEN---LCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1599980197 159 DLLLLDEPTNHLDISHQMQLLDALKDWTRTRQlTVVAILHdlNMASLY-CDRVLLLNEGRMVDLNSPRQVMTEHQL 233
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITH--NLEELHdADRIIVMDRGKIVLEGEPENVLSDVSL 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-229 |
5.18e-28 |
|
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: 111.48 E-value: 5.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYdEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQK-MAV 80
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTADTTFAYKVKEVVAlgryphqkgwLASESQEDERVIREA-----MEQTDTWKFRNKPLQTLSGGERQRALLARALC 155
Cdd:cd03218 80 LPQEASIFRKLTVEENIL----------AVLEIRGLSKKEREEkleelLEEFHITHLRKSKASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 156 QEPDLLLLDEPTNHLD---ISHQMQLLDALKDwtrtRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMT 229
Cdd:cd03218 150 TNPKFLLLDEPFAGVDpiaVQDIQKIIKILKD----RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-228 |
1.08e-27 |
|
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: 110.40 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEK-TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:cd03251 1 VEFKNVTFRYPGDgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQtaDT-TFAYKVKEVVALGRyphqkgwlASESQEDervIREAMEQTDTWKF-RNKPLQ----------TLSGGERQRA 148
Cdd:cd03251 81 VSQ--DVfLFNDTVAENIAYGR--------PGATREE---VEEAARAANAHEFiMELPEGydtvigergvKLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 149 LLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMASlYCDRVLLLNEGRMVDLNSPRQVM 228
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIE-NADRIVVLEDGKIVERGTHEELL 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-229 |
1.36e-27 |
|
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: 115.55 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGY---DEKTPIIQQLSFQVHKGEIFGILGPNGSGKT-TLLkAVSGLLSPS----EGTITLQGKAIADYHSK 72
Cdd:COG4172 6 LLSVEDLSVAFgqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTAL-SILRLLPDPaahpSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 73 ELAQ----KMAVL---PQTADT---TFAYKVKEVVALgrypHQKgwlASESQEDERVIrEAMEQT--DTWKFRNK--PLQ 138
Cdd:COG4172 85 ELRRirgnRIAMIfqePMTSLNplhTIGKQIAEVLRL----HRG---LSGAAARARAL-ELLERVgiPDPERRLDayPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 139 tLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRM 218
Cdd:COG4172 157 -LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
250
....*....|.
gi 1599980197 219 VDLNSPRQVMT 229
Cdd:COG4172 236 VEQGPTAELFA 246
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
5-227 |
1.53e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.00 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTPI-IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQ 83
Cdd:PRK13648 11 KNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 84 TADTTF-AYKVKEVVALGRYPHqkgwlASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLL 162
Cdd:PRK13648 91 NPDNQFvGSIVKYDVAFGLENH-----AVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 163 LDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMAsLYCDRVLLLNEGRMVDLNSPRQV 227
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-217 |
2.23e-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: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIAD--YHSKELAQKMA 79
Cdd:cd03262 1 IEIKNLHKSFGDFH-VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 80 VLPQTADtTFAYK-VKEVVALGryPhQKGWLASESQEDERViREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEP 158
Cdd:cd03262 80 MVFQQFN-LFPHLtVLENITLA--P-IKVKGMSKAEAEERA-LELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 159 DLLLLDEPTNHLDISHQMQLLDALKDWTRTrQLTVVAILHDLNMASLYCDRVLLLNEGR 217
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-221 |
3.44e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 111.36 E-value: 3.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 22 SFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA---QKMAVLPQtaDTtFA-----YKV 93
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRplrRRMQMVFQ--DP-YAslnprMTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 94 KEVVALGRYPHQkgwLASESQEDERViREAMEQ----TDtwkFRNK-PLQtLSGGERQRALLARALCQEPDLLLLDEPTN 168
Cdd:COG4608 115 GDIIAEPLRIHG---LASKAERRERV-AELLELvglrPE---HADRyPHE-FSGGQRQRIGIARALALNPKLIVCDEPVS 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1599980197 169 HLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDL 221
Cdd:COG4608 187 ALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEI 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-218 |
3.69e-27 |
|
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: 107.52 E-value: 3.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTpiiqqLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE-LAQKMA 79
Cdd:cd03215 4 VLEVRGLSVKGAVRD-----VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 80 VLPqtADttfaykvkevvalgryPHQKGWLASESQEDERVIReameqtdtwkfrnkplQTLSGGERQRALLARALCQEPD 159
Cdd:cd03215 79 YVP--ED----------------RKREGLVLDLSVAENIALS----------------SLLSGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 160 LLLLDEPTNHLDIS-----HqmQLLDALKDwtrtRQLTVVAILHDLNMASLYCDRVLLLNEGRM 218
Cdd:cd03215 125 VLILDEPTRGVDVGakaeiY--RLIRELAD----AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-220 |
6.96e-27 |
|
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: 108.29 E-value: 6.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGY---DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA-- 75
Cdd:COG4181 8 IIELRGLTKTVgtgAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARArl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 --QKMAVLPQ--------TAdttfaykvKEVVALgryPHQkgwLASEsqederviREAMEQTDTW--------KFRNKPL 137
Cdd:COG4181 88 raRHVGFVFQsfqllptlTA--------LENVML---PLE---LAGR--------RDARARARALlervglghRLDHYPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 138 QtLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLyCDRVLLLNEGR 217
Cdd:COG4181 146 Q-LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGR 223
|
...
gi 1599980197 218 MVD 220
Cdd:COG4181 224 LVE 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-231 |
8.55e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 113.77 E-value: 8.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGY-DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLkavsGLLS----PSEGTITLQGKAIADYHSKELAQ 76
Cdd:PRK11160 339 LTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL----QLLTrawdPQQGEILLNGQPIADYSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 77 KMAVLPQTADTtFAYKVKEVVALgryphqkgwlASESQEDERVIrEAMEQTDTWKF--RNKPLQT--------LSGGERQ 146
Cdd:PRK11160 415 AISVVSQRVHL-FSATLRDNLLL----------AAPNASDEALI-EVLQQVGLEKLleDDKGLNAwlgeggrqLSGGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 147 RALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLN-MASLycDRVLLLNEGRMVDLNSPR 225
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTgLEQF--DRICVMDNGQIIEQGTHQ 558
|
....*.
gi 1599980197 226 QVMTEH 231
Cdd:PRK11160 559 ELLAQQ 564
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-237 |
9.30e-27 |
|
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: 108.13 E-value: 9.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQK-MAV 80
Cdd:TIGR04406 2 LVAENLIKSYKKRK-VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLgIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTADT----TFAYKVKEVVALgryphqKGWLASESQEDERVirEAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQ 156
Cdd:TIGR04406 81 LPQEASIfrklTVEENIMAVLEI------RKDLDRAEREERLE--ALLEEFQISHLRDNKAMSLSGGERRRVEIARALAT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 157 EPDLLLLDEPTNHLD---ISHQMQLLDALKDwtrtRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQL 233
Cdd:TIGR04406 153 NPKFILLDEPFAGVDpiaVGDIKKIIKHLKE----RGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKV 228
|
....
gi 1599980197 234 ANVY 237
Cdd:TIGR04406 229 RRVY 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-279 |
9.95e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.37 E-value: 9.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTPI----IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSK--ELAQKM 78
Cdd:PRK13637 6 ENLTHIYMEGTPFekkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 79 AVLPQTAD-TTFAYKVKEVVALGryPHQKGwlASESQEDERViREAMEQT--DTWKFRNKPLQTLSGGERQRALLARALC 155
Cdd:PRK13637 86 GLVFQYPEyQLFEETIEKDIAFG--PINLG--LSEEEIENRV-KRAMNIVglDYEDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 156 QEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEhqlan 235
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE----- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1599980197 236 vyetkIRRNEHPTIPRPLVTFEPAAIRSKpSSPISElEVFTSEQ 279
Cdd:PRK13637 236 -----VETLESIGLAVPQVTYLVRKLRKK-GFNIPD-DIFTIEE 272
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-201 |
1.14e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 107.18 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSP---SEGTITLQGKAIADYhsKELAQK 77
Cdd:COG4136 1 MLSLENLTITLGGR-PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAL--PAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 78 MAVLPQTaDTTFAY-KVKEVVALGRYPHQKGwlaseSQEDERVIrEAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQ 156
Cdd:COG4136 78 IGILFQD-DLLFPHlSVGENLAFALPPTIGR-----AQRRARVE-QALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1599980197 157 EPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLN 201
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-234 |
1.35e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 112.88 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGY-----------DEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLsPSEGTITLQGKAIADY 69
Cdd:PRK15134 275 LLDVEQLQVAFpirkgilkrtvDHNV-VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 70 HSKEL---AQKMAVLPQTADTTFAYK--VKEVVALGRYPHQKGwlASESQEDERVIrEAMEQT----DTwkfRNKPLQTL 140
Cdd:PRK15134 353 NRRQLlpvRHRIQVVFQDPNSSLNPRlnVLQIIEEGLRVHQPT--LSAAQREQQVI-AVMEEVgldpET---RHRYPAEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 141 SGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVD 220
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
250 260
....*....|....*....|.
gi 1599980197 221 -------LNSPRQVMTEHQLA 234
Cdd:PRK15134 507 qgdcervFAAPQQEYTRQLLA 527
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-219 |
1.40e-26 |
|
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: 105.20 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEkTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIAdYHSKELAQKMAVl 81
Cdd:cd03216 1 LELRGITKRFGG-VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS-FASPRDARRAGI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 pqtadttfaykvkEVValgrypHQkgwlasesqedervireameqtdtwkfrnkplqtLSGGERQRALLARALCQEPDLL 161
Cdd:cd03216 78 -------------AMV------YQ----------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 162 LLDEPTNHLDISHQMQLLDALKDwTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRR-LRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
20-219 |
1.54e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 107.36 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 20 QLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKaiaDYHSKELAQK-MAVLPQTaDTTFAY-KVKEVV 97
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ---DHTTTPPSRRpVSMLFQE-NNLFSHlTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 98 ALGRYPHQKgwLASESQEDERVIREAMEQTDTwkFRNKPLQtLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQ 177
Cdd:PRK10771 93 GLGLNPGLK--LNAAQREKLHAIARQMGIEDL--LARLPGQ-LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1599980197 178 LLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-219 |
1.70e-26 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 106.97 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 17 IIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLL---SPSEGTITLQGKAIadyhSKELAQK-MAVLPQ--------T 84
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPR----KPDQFQKcVAYVRQddillpglT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 85 ADTTFAYKVkeVVALGRyphqkgwLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLD 164
Cdd:cd03234 98 VRETLTYTA--ILRLPR-------KSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 165 EPTNHLDISHQMQLLDALKDWTRtRQLTVVAILHD--LNMASLYcDRVLLLNEGRMV 219
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIHQprSDLFRLF-DRILLLSSGEIV 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-219 |
1.72e-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: 106.57 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE--LA---QKMA 79
Cdd:cd03301 4 ENVTKRFGNVT-ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDrdIAmvfQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 80 VLPQtadttfaYKVKEVVALGRYPHQkgwlASESQEDERViREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPD 159
Cdd:cd03301 83 LYPH-------MTVYDNIAFGLKLRK----VPKDEIDERV-REVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 160 LLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-237 |
2.22e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 107.29 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQK-MAV 80
Cdd:PRK10895 4 LTAKNLAKAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTADTTFAYKV-KEVVALGRYPHQkgwLASESQEDErvIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPD 159
Cdd:PRK10895 83 LPQEASIFRRLSVyDNLMAVLQIRDD---LSAEQREDR--ANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 160 LLLLDEPTNHLDishQMQLLDALK--DWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQLANVY 237
Cdd:PRK10895 158 FILLDEPFAGVD---PISVIDIKRiiEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-218 |
3.45e-26 |
|
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: 105.95 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA---QKMAVL 81
Cdd:cd03292 4 INVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADTTFAYKVKEVVALGRYPHQKGwlaseSQEDERVIREAMEQTD-TWKFRNKPLQtLSGGERQRALLARALCQEPDL 160
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVTGVP-----PREIRKRVPAALELVGlSHKHRALPAE-LSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 161 LLLDEPTNHLDISHQMQLLDALKDwTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRM 218
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-231 |
4.03e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 109.54 E-value: 4.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE-----LA 75
Cdd:PRK11607 19 LLEIRNLTKSFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQrpinmMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 QKMAVLPQ-TADTTFAYKVKEvvalGRYPhqKGWLASEsqedervIREAMEQTDTWKF-RNKPLQtLSGGERQRALLARA 153
Cdd:PRK11607 98 QSYALFPHmTVEQNIAFGLKQ----DKLP--KAEIASR-------VNEMLGLVHMQEFaKRKPHQ-LSGGQRQRVALARS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 154 LCQEPDLLLLDEPTNHLD--ISHQMQLldALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMtEH 231
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDkkLRDRMQL--EVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY-EH 240
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-230 |
6.10e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 111.74 E-value: 6.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEK--TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLP 82
Cdd:TIGR00958 482 QDVSFSYPNRpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVG 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 83 QTAdTTFAYKVKEVVALG--RYPHQKGWLASESQEDERVIREaMEQTDTWKFRNKPLQtLSGGERQRALLARALCQEPDL 160
Cdd:TIGR00958 562 QEP-VLFSGSVRENIAYGltDTPDEEIMAAAKAANAHDFIME-FPNGYDTEVGEKGSQ-LSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 161 LLLDEPTNHLDIshqmQLLDALKDWTRTRQLTVVAILHDLNMASlYCDRVLLLNEGRMVDLNSPRQVMTE 230
Cdd:TIGR00958 639 LILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLMED 703
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-235 |
8.22e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.12 E-value: 8.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 22 SFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE--------------LAQKMAVLpqtadt 87
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaialgigmvhqhfmLVPNLTVA------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 88 tfaykvkEVVALGRYPHQKGWLaSESQEDERvIREAMEQTDtwkFR---NKPLQTLSGGERQRALLARALCQEPDLLLLD 164
Cdd:COG3845 99 -------ENIVLGLEPTKGGRL-DRKAARAR-IRELSERYG---LDvdpDAKVEDLSVGEQQRVEILKALYRGARILILD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1599980197 165 EPTNHL---DISHQMQLLDALKDwtrtRQLTVVAILHDLN--MAslYCDRVLLLNEGRMVDLNSPRQVmTEHQLAN 235
Cdd:COG3845 167 EPTAVLtpqEADELFEILRRLAA----EGKSIIFITHKLRevMA--IADRVTVLRRGKVVGTVDTAET-SEEELAE 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
5-230 |
8.23e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.84 E-value: 8.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTPI----IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHS----KELAQ 76
Cdd:PRK13641 6 ENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 77 KMAVLPQTADTT-FAYKVKEVVALGryPHQKGwlASEsqederviREAMEQTDTW--------KFRNKPLQTLSGGERQR 147
Cdd:PRK13641 86 KVSLVFQFPEAQlFENTVLKDVEFG--PKNFG--FSE--------DEAKEKALKWlkkvglseDLISKSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 148 ALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQlTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQV 227
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
...
gi 1599980197 228 MTE 230
Cdd:PRK13641 233 FSD 235
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-230 |
9.44e-26 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 107.58 E-value: 9.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 33 ILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADY-----HSKELAQKMAVLPQ-TADTTFAYKVKevvalgryphQK 106
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVpphlrHINMVFQSYALFPHmTVEENVAFGLK----------MR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 107 GWLASESqeDERViREAMEQTDTWKF-RNKPLQtLSGGERQRALLARALCQEPDLLLLDEPTNHLD--ISHQMQLldALK 183
Cdd:TIGR01187 71 KVPRAEI--KPRV-LEALRLVQLEEFaDRKPHQ-LSGGQQQRVALARALVFKPKILLLDEPLSALDkkLRDQMQL--ELK 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1599980197 184 DWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTE 230
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-219 |
1.13e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 107.47 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTPIIQQL---SFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA-- 75
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALddvSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 -QKMAVLPQ-----TADTTF---AY--------------KVKEVVAL-------GRYPHQkgwlasesqedervireame 125
Cdd:COG1135 81 rRKIGMIFQhfnllSSRTVAenvALpleiagvpkaeirkRVAELLELvglsdkaDAYPSQ-------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 126 qtdtwkfrnkplqtLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASL 205
Cdd:COG1135 141 --------------LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRR 206
|
250
....*....|....
gi 1599980197 206 YCDRVLLLNEGRMV 219
Cdd:COG1135 207 ICDRVAVLENGRIV 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-237 |
1.19e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 104.96 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDeKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYH-SKELAQKMA 79
Cdd:PRK11614 5 MLSFDKVSAHYG-KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 80 VLPQTADTTFAYKVKEVVALGryphqkGWLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPD 159
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMG------GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 160 LLLLDEPTNHLDISHQMQLLDALKDwTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQLANVY 237
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQ-LREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| bifunc_CbiS |
NF038002 |
bifunctional adenosylcobinamide hydrolase/alpha-ribazole phosphatase CbiS; |
290-491 |
1.39e-25 |
|
bifunctional adenosylcobinamide hydrolase/alpha-ribazole phosphatase CbiS;
Pssm-ID: 468308 [Multi-domain] Cd Length: 333 Bit Score: 107.18 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 290 KTLSSAVLGAGFKWHQTFVNRHVSKDYYCDDVEREFQtflSNVGVD-GTDALGMMTAAILEDVAITEATYESFkvrVFVT 368
Cdd:NF038002 12 RALSSAPLNGGPPKVRAVAFMQVPKDFDGDYMEDARS---ARVGYGlPEDSVVFLTAAEVPKAFSVAEEGEVF---AAAT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 369 AGISNAVDPAKahlrKRNEATVGTINTWVFIEGTLPDAAYVQALMTATEAKgrALAEKEILDPVTGTLATGTSTDSVMIA 448
Cdd:NF038002 86 AGMTNASCVGN----TLDRWGEGTINVAVVVDRPLDDWGLVDLLRTAVEAK--CLAAVDLGLRCNGRRAGGTVTDAVAVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1599980197 449 SSQTGTYFPYAGTITPLGQAIGKLVYDATIQAVTDNEKRRLER 491
Cdd:NF038002 160 APEGDGESHFAGPATELGRRVSKLVYEAVRKGGSPDGYDLLRR 202
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-229 |
1.49e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 105.12 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGL--LSPS---EGTITLQGKAIadYHSK---- 72
Cdd:COG1117 12 IEVRNLNVYYGDK-QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDI--YDPDvdvv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 73 ELAQKMAVLPQTAdTTFAYKVKEVVALGryPHQKGWLaSESQEDERViREAMEQTDTW---KFR-NKPLQTLSGGERQRA 148
Cdd:COG1117 89 ELRRRVGMVFQKP-NPFPKSIYDNVAYG--LRLHGIK-SKSELDEIV-EESLRKAALWdevKDRlKKSALGLSGGQQQRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 149 LLARALCQEPDLLLLDEPTNHLD-ISHQM--QLLDALKDwtrtrQLTVVAILHdlNM--ASLYCDRVLLLNEGRMVDLNS 223
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDpISTAKieELILELKK-----DYTIVIVTH--NMqqAARVSDYTAFFYLGELVEFGP 236
|
....*.
gi 1599980197 224 PRQVMT 229
Cdd:COG1117 237 TEQIFT 242
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-231 |
1.76e-25 |
|
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: 104.54 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEK--TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLP 82
Cdd:cd03249 4 KNVSFRYPSRpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 83 QTAdTTFAYKVKEVVALGRYPhqkgwlaSESQEDERVIREA---------MEQTDTwKFRNKPLQtLSGGERQRALLARA 153
Cdd:cd03249 84 QEP-VLFDGTIAENIRYGKPD-------ATDEEVEEAAKKAnihdfimslPDGYDT-LVGERGSQ-LSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 154 LCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMASlYCDRVLLLNEGRMVDLNSPRQVMTEH 231
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAHRLSTIR-NADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-166 |
1.84e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 104.34 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDeKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQK-MA 79
Cdd:COG1137 3 TLEAENLVKSYG-KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 80 VLPQTA---------DTTFAykVKEVVALGRyphqkgwlasesQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALL 150
Cdd:COG1137 82 YLPQEAsifrkltveDNILA--VLELRKLSK------------KEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170
....*....|....*.
gi 1599980197 151 ARALCQEPDLLLLDEP 166
Cdd:COG1137 148 ARALATNPKFILLDEP 163
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-227 |
2.18e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 104.69 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 22 SFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVlpqtadTTFAY-------KVK 94
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVV------RTFQHvrlfremTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 95 EVVALGRYPHQK-----GWLASESQedERVIREAMEQTDTW-------KFRNKPLQTLSGGERQRALLARALCQEPDLLL 162
Cdd:PRK11300 99 ENLLVAQHQQLKtglfsGLLKTPAF--RRAESEALDRAATWlervgllEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1599980197 163 LDEP--------TNHLDishqmQLLDALKdwtRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQV 227
Cdd:PRK11300 177 LDEPaaglnpkeTKELD-----ELIAELR---NEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-220 |
2.23e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.96 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA------ 75
Cdd:COG3845 258 LEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrlgvay 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 -----QKMAVLPqtadttfAYKVKEVVALGRY---PHQKGWLasesqEDERVIRE-AMEQTDTWKFR----NKPLQTLSG 142
Cdd:COG3845 338 ipedrLGRGLVP-------DMSVAENLILGRYrrpPFSRGGF-----LDRKAIRAfAEELIEEFDVRtpgpDTPARSLSG 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 143 GERQRALLARALCQEPDLLLLDEPTNHLDIS-----HQmQLLDAlkdwtRTRQLTVVAILHDLN--MAslYCDRVLLLNE 215
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGaiefiHQ-RLLEL-----RDAGAAVLLISEDLDeiLA--LSDRIAVMYE 477
|
....*
gi 1599980197 216 GRMVD 220
Cdd:COG3845 478 GRIVG 482
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-228 |
2.35e-25 |
|
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: 106.73 E-value: 2.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 21 LSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADyhskelAQKMAVLP----------QTADTTFA 90
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD------SRKGIFLPpekrrigyvfQEARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 91 YKVKEVVALGRyphqkgwlaSESQEDERVIREA--MEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTN 168
Cdd:TIGR02142 90 LSVRGNLRYGM---------KRARPSERRISFErvIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 169 HLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVM 228
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-233 |
3.60e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.18 E-value: 3.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGydektPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE-LAQKMA 79
Cdd:COG1129 256 VLEVEGLSVG-----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 80 -----------VLPQTadttfaykVKEVVALGRYP-HQKGWLASESQEDERViREAMEQTDTwKFRN--KPLQTLSGGER 145
Cdd:COG1129 331 yvpedrkgeglVLDLS--------IRENITLASLDrLSRGGLLDRRRERALA-EEYIKRLRI-KTPSpeQPVGNLSGGNQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 146 QRALLARALCQEPDLLLLDEPTNHLDI-SHQ--MQLLDALKDwtrtRQLTVVAILHDL----NMaslyCDRVLLLNEGRM 218
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPTRGIDVgAKAeiYRLIRELAA----EGKAVIVISSELpellGL----SDRILVMREGRI 472
|
250
....*....|....*.
gi 1599980197 219 V-DLnsPRQVMTEHQL 233
Cdd:COG1129 473 VgEL--DREEATEEAI 486
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
9-220 |
3.71e-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: 3.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 9 VGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADY---HSKELAQKMAVLPQTA 85
Cdd:TIGR02769 18 FGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 86 DTTFAYKvKEVVALGRYPHQKGWLASESQEDERV--IREAMEQTDTwKFRNKPLQtLSGGERQRALLARALCQEPDLLLL 163
Cdd:TIGR02769 98 PSAVNPR-MTVRQIIGEPLRHLTSLDESEQKARIaeLLDMVGLRSE-DADKLPRQ-LSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 164 DEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVD 220
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
21-232 |
5.63e-25 |
|
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: 103.37 E-value: 5.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 21 LSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQTADTTFAYK-----VKE 95
Cdd:TIGR02323 22 VSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRRLMRTEWGFVHQnprdgLRM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 96 VVALGRYPHQKgwLASESQEDERVIREAME------QTDTWKFRNKPlQTLSGGERQRALLARALCQEPDLLLLDEPTNH 169
Cdd:TIGR02323 102 RVSAGANIGER--LMAIGARHYGNIRATAQdwleevEIDPTRIDDLP-RAFSGGMQQRLQIARNLVTRPRLVFMDEPTGG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1599980197 170 LDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQ 232
Cdd:TIGR02323 179 LDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQ 241
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-224 |
6.51e-25 |
|
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: 102.57 E-value: 6.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGY-DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQ 83
Cdd:cd03244 6 KNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 84 TAdTTFAYKVKEVVA-LGRYPhqkgwlasesqeDERvIREAMEQTDTWKFRNKP---LQT--------LSGGERQRALLA 151
Cdd:cd03244 86 DP-VLFSGTIRSNLDpFGEYS------------DEE-LWQALERVGLKEFVESLpggLDTvveeggenLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1599980197 152 RALCQEPDLLLLDEPTNHLDISHQMQLLDALKdwTRTRQLTVVAILHDLNmASLYCDRVLLLNEGRMVDLNSP 224
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLD-TIIDSDRILVLDKGRVVEFDSP 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-227 |
8.93e-25 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 102.38 E-value: 8.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDeKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADyHSKELA---QK 77
Cdd:COG1126 1 MIEIENLHKSFG-DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINklrRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 78 MAVLPQ--------TadttfaykVKEVVALGryP-HQKGWLASESQEdervirEAMEQ------TDtwKFRNKPLQtLSG 142
Cdd:COG1126 79 VGMVFQqfnlfphlT--------VLENVTLA--PiKVKKMSKAEAEE------RAMELlervglAD--KADAYPAQ-LSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 143 GERQRALLARALCQEPDLLLLDEPTNHLD---IShqmQLLDALKDWTRtRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAK-EGMTMVVVTHEMGFAREVADRVVFMDGGRIV 215
|
....*...
gi 1599980197 220 DLNSPRQV 227
Cdd:COG1126 216 EEGPPEEF 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
9-225 |
9.41e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.10 E-value: 9.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 9 VGYD-EKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQTAdT 87
Cdd:PRK10247 13 VGYLaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTP-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 88 TFAYKVKEVVAlgrYPhqkgWLASESQEDERVIREAMEQ---TDTwkFRNKPLQTLSGGERQRALLARALCQEPDLLLLD 164
Cdd:PRK10247 92 LFGDTVYDNLI---FP----WQIRNQQPDPAIFLDDLERfalPDT--ILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1599980197 165 EPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASlYCDRVLLLNE--GRMVDLNSPR 225
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEIN-HADKVITLQPhaGEMQEARYEL 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
18-218 |
1.08e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 103.17 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 18 IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLL---SPSEGTITLQGKAI------ADYHSKELAQKMAVLPQTADTT 88
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVqregrlARDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 89 FAYKVKEVV--ALGRYPHQKGWLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEP 166
Cdd:PRK09984 100 RLSVLENVLigALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1599980197 167 TNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRM 218
Cdd:PRK09984 180 IASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-220 |
1.88e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 102.46 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 17 IIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADyhskelaqkmavLPQTADTTFAYKVKEV 96
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK------------LNRAQRKAFRRDIQMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 97 V--ALGRYPHQK--GWLASES-------QEDERVIR-----EAMEQTDTwkFRNKPLQTLSGGERQRALLARALCQEPDL 160
Cdd:PRK10419 95 FqdSISAVNPRKtvREIIREPlrhllslDKAERLARasemlRAVDLDDS--VLDKRPPQLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 161 LLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVD 220
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-216 |
2.43e-24 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 101.00 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 18 IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA--QKMAVLP-QTADTTFAYKVK 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVvfQNYSLLPwLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 95 EVVALGRYPhqkgwlasesqEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISH 174
Cdd:TIGR01184 81 RVLPDLSKS-----------ERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1599980197 175 QMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEG 216
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-227 |
2.79e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 103.27 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYdeKTP-----IIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPS---EGTITLQGKAIADYHSK 72
Cdd:PRK09473 12 LLDVKDLRVTF--STPdgdvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 73 EL----AQKMAVLPQTADTTF-AY-KVK----EVVALgryphQKGWLASESQEDERVIREAMEQTDTWKFRNKPLQTLSG 142
Cdd:PRK09473 90 ELnklrAEQISMIFQDPMTSLnPYmRVGeqlmEVLML-----HKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 143 GERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLN 222
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 244
|
....*
gi 1599980197 223 SPRQV 227
Cdd:PRK09473 245 NARDV 249
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
21-232 |
6.00e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.16 E-value: 6.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 21 LSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGK-------------------------AIADYHSKELA 75
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallelgagfhpeltgreniylngRLLGLSRKEID 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 QKMAvlpqtadttfaykvkEVVALgryphqkgwlaSEsqedervIREAMEQtdtwkfrnkPLQTLSGGERQRALLARALC 155
Cdd:COG1134 125 EKFD---------------EIVEF-----------AE-------LGDFIDQ---------PVKTYSSGMRARLAFAVATA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 156 QEPDLLLLDEPTNHLDISHQMQLLDALKD-WTRTRqlTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQ 232
Cdd:COG1134 163 VDPDILLVDEVLAVGDAAFQKKCLARIRElRESGR--TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAYE 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-232 |
6.67e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.79 E-value: 6.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGY---DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLL-SPS----EGTITLQGKAIADYHSK 72
Cdd:PRK15134 5 LLAIENLSVAFrqqQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpSPPvvypSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 73 ELAQ----KMAVLPQTADT------TFAYKVKEVVALGRYPHQKGWLASESQEDERV-IREAMEqtdtwKFRNKPLQtLS 141
Cdd:PRK15134 85 TLRGvrgnKIAMIFQEPMVslnplhTLEKQLYEVLSLHRGMRREAARGEILNCLDRVgIRQAAK-----RLTDYPHQ-LS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 142 GGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDL 221
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQ 238
|
250
....*....|.
gi 1599980197 222 NSPRQVMTEHQ 232
Cdd:PRK15134 239 NRAATLFSAPT 249
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-246 |
8.21e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 100.96 E-value: 8.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTPIIQQLSF----QVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLqGKAIADYHSKE--- 73
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFdidlEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQkei 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 74 --LAQKMAVLPQTADTT-FAYKVKEVVALGryPHQKGwlaSESQEDERVIREAMEQTDTWK-FRNKPLQTLSGGERQRAL 149
Cdd:PRK13643 80 kpVRKKVGVVFQFPESQlFEETVLKDVAFG--PQNFG---IPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 150 LARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQlTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMT 229
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
250
....*....|....*..
gi 1599980197 230 EHQLANVYETKIRRNEH 246
Cdd:PRK13643 234 EVDFLKAHELGVPKATH 250
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-239 |
1.31e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 99.60 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEkTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGL--LSPS---EGTITLQGKAIADYHSKELAQ 76
Cdd:PRK14247 4 IEIRDLKVSFGQ-VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 77 KMAVLPQTADTTFAYKVKEVVALGRYPHQkgwLASESQEDERVIREAMEQTDTW---KFR-NKPLQTLSGGERQRALLAR 152
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLKLNR---LVKSKKELQERVRWALEKAQLWdevKDRlDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 153 ALCQEPDLLLLDEPTNHLDISHQMQ---LLDALKdwtrtRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMT 229
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKiesLFLELK-----KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
250
....*....|..
gi 1599980197 230 --EHQLANVYET 239
Cdd:PRK14247 235 npRHELTEKYVT 246
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
22-219 |
1.60e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 99.62 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 22 SFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKaiaDYHSKELAQkmavLPQTadttfaykvkEVVALGR 101
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR---DGQLRDLYA----LSEA----------ERRRLLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 102 ----YPHQ------KGWLASESQEDERV----------IREA----MEQT--DTWKFRNKPlQTLSGGERQRALLARALC 155
Cdd:PRK11701 89 tewgFVHQhprdglRMQVSAGGNIGERLmavgarhygdIRATagdwLERVeiDAARIDDLP-TTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 156 QEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-232 |
1.80e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.78 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTPIIQ--QLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKM 78
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQlnGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 79 AVLPQTADTTF-AYKVKEVVALGryphqkgwLASESQEDERVIR---EAMEQTDTWKFRNKPLQTLSGGERQRALLARAL 154
Cdd:PRK13642 84 GMVFQNPDNQFvGATVEDDVAFG--------MENQGIPREEMIKrvdEALLAVNMLDFKTREPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 155 CQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASlYCDRVLLLNEGRMVDLNSPRQVMTEHQ 232
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-219 |
1.98e-23 |
|
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: 97.62 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKT-----PIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPS--EGTITLQGKAIadyHSKEL 74
Cdd:cd03213 4 LSFRNLTVTVKSSPsksgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPL---DKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 75 AQKMAVLPQtaDTTFaykvkevvalgrYPHQkgwlasesqederVIREAMEqtdtwkFRNKpLQTLSGGERQRALLARAL 154
Cdd:cd03213 81 RKIIGYVPQ--DDIL------------HPTL-------------TVRETLM------FAAK-LRGLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 155 CQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTrQLTVVAILHDLNmASLY--CDRVLLLNEGRMV 219
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPS-SEIFelFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-233 |
2.03e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 99.70 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIaDYHSK---ELAQK 77
Cdd:PRK13638 1 MLATSDLWFRYQDE-PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 78 MAVLPQTADTTFAYK-VKEVVALGRYPhqkgwLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQ 156
Cdd:PRK13638 79 VATVFQDPEQQIFYTdIDSDIAFSLRN-----LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 157 EPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAIlHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQL 233
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISS-HDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-235 |
2.03e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.79 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 22 SFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIAdYHSKELAQKM--AVLPQ--------Tadttfay 91
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-FRSPRDAQAAgiAIIHQelnlvpnlS------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 92 kVKEVVALGRYPHQKGWLasesqeDER-VIREAMEQTDTWKFR---NKPLQTLSGGERQRALLARALCQEPDLLLLDEPT 167
Cdd:COG1129 96 -VAENIFLGREPRRGGLI------DWRaMRRRARELLARLGLDidpDTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1599980197 168 ---NHLDISHQMQLLDALKDwtrtRQLTVVAILHDLN-MASLyCDRVLLLNEGRMVDlNSPRQVMTEHQLAN 235
Cdd:COG1129 169 aslTEREVERLFRIIRRLKA----QGVAIIYISHRLDeVFEI-ADRVTVLRDGRLVG-TGPVAELTEDELVR 234
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-227 |
2.06e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 101.31 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 14 KTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE-------------------- 73
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDrkvgfvfqhyalfrhmtvfd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 74 -LAQKMAVLPQTADTTFAYKVKEVVAL----------GRYPHQkgwlasesqedervireameqtdtwkfrnkplqtLSG 142
Cdd:PRK10851 94 nIAFGLTVLPRRERPNAAAIKAKVTQLlemvqlahlaDRYPAQ----------------------------------LSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 143 GERQRALLARALCQEPDLLLLDEPTNHLDishqMQLLDALKDWtrTRQL------TVVAILHDLNMASLYCDRVLLLNEG 216
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALD----AQVRKELRRW--LRQLheelkfTSVFVTHDQEEAMEVADRVVVMSQG 213
|
250
....*....|.
gi 1599980197 217 RMVDLNSPRQV 227
Cdd:PRK10851 214 NIEQAGTPDQV 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-216 |
3.27e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.96 E-value: 3.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTPIIQQLSFQVHKGEifGIL--GPNGSGKTTLLKAVSGLLSPSEGTITLQGKAiadyhskelaqKM 78
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-----------RV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 79 AVLPQTAdttfaY----KVKEVVAlgrYPHqkgwlaSESQEDERVIREAMEQ------------TDTWKfrnkplQTLSG 142
Cdd:COG4178 429 LFLPQRP-----YlplgTLREALL---YPA------TAEAFSDAELREALEAvglghlaerldeEADWD------QVLSL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1599980197 143 GERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDwtRTRQLTVVAILHDlnmASL--YCDRVLLLNEG 216
Cdd:COG4178 489 GEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHR---STLaaFHDRVLELTGD 559
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-220 |
3.76e-23 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 102.28 E-value: 3.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADY----HSKELAQK 77
Cdd:PRK15064 320 LEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYyaqdHAYDFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 78 MAVLPqtadttfaykvkevvalgryphqkgWLASESQE--DERVIREAM-----EQTDTwkfrNKPLQTLSGGERQRALL 150
Cdd:PRK15064 399 LTLFD-------------------------WMSQWRQEgdDEQAVRGTLgrllfSQDDI----KKSVKVLSGGEKGRMLF 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 151 ARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWtrtrQLTVVAILHDLNMASLYCDRVLLLNEGRMVD 220
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY----EGTLIFVSHDREFVSSLATRIIEITPDGVVD 515
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
20-218 |
4.37e-23 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 97.24 E-value: 4.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 20 QLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIAdyHSKELAQKMAVLPQTADTTFAYKVKEVVAL 99
Cdd:TIGR01277 16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHT--GLAPYQRPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 100 GRYPHQKgwLASESQEDervIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLL 179
Cdd:TIGR01277 94 GLHPGLK--LNAEQQEK---VVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1599980197 180 DALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRM 218
Cdd:TIGR01277 169 ALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-219 |
5.27e-23 |
|
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: 97.22 E-value: 5.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 8 SVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIAdyhskELAQKMAVLPQtadt 87
Cdd:cd03220 28 RKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS-----LLGLGGGFNPE---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 88 tfaYKVKE-VVALGRYphqKGWLASESQEderVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEP 166
Cdd:cd03220 99 ---LTGREnIYLNGRL---LGLSRKEIDE---KIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1599980197 167 TNHLDISHQMQLLDALKDWTRTRQlTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-199 |
7.45e-23 |
|
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: 101.55 E-value: 7.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYhskeLAQKmavlPQT 84
Cdd:TIGR03719 8 NRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGY----LPQE----PQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 85 ADTTfayKVKEVV---------ALGRYPHQKGWLASESQEDERVIRE------AMEQTDTWKFRNK-------------- 135
Cdd:TIGR03719 80 DPTK---TVRENVeegvaeikdALDRFNEISAKYAEPDADFDKLAAEqaelqeIIDAADAWDLDSQleiamdalrcppwd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 136 -PLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRtrqlTVVAILHD 199
Cdd:TIGR03719 157 aDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTHD 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-229 |
1.45e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 96.65 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 11 YDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIadYHSKE--------LAQKMAVLP 82
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVL--YFGKDifqidaikLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 83 QTADTTFAYKVKEVVAlgrYPHQKGWLaSESQEDERVIREAMEQTDTWK----FRNKPLQTLSGGERQRALLARALCQEP 158
Cdd:PRK14246 97 QQPNPFPHLSIYDNIA---YPLKSHGI-KEKREIKKIVEECLRKVGLWKevydRLNSPASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 159 DLLLLDEPTNHLDISHQM---QLLDALKdwtrtRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMT 229
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQaieKLITELK-----NEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-211 |
1.54e-22 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 96.32 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 27 KGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIAdYHSKELAQKMavlPQTADTTFAYKVKEvvaLGRYPHQK 106
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKADY---EGTVRDLLSSITKD---FYTHPYFK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 107 GWLASESQedervIREAMEQTdtwkfrnkpLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWT 186
Cdd:cd03237 97 TEIAKPLQ-----IEQILDRE---------VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
170 180
....*....|....*....|....*
gi 1599980197 187 RTRQLTVVAILHDLNMASLYCDRVL 211
Cdd:cd03237 163 ENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-220 |
1.54e-22 |
|
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: 96.02 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTP-IIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQ 83
Cdd:cd03252 4 EHVRFRYKPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 84 TaDTTFAYKVKEVVALGRyphqkgwlasESQEDERVIrEAMEQTDTWKF-RNKPL----------QTLSGGERQRALLAR 152
Cdd:cd03252 84 E-NVLFNRSIRDNIALAD----------PGMSMERVI-EAAKLAGAHDFiSELPEgydtivgeqgAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 153 ALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNmASLYCDRVLLLNEGRMVD 220
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLS-TVKNADRIIVMEKGRIVE 216
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-234 |
1.55e-22 |
|
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: 98.63 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 20 QLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSK--------------------------- 72
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGiflpphrrrigyvfqearlfphlsvrg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 73 --ELAQKMAVLPQTADTtFAykvkEVVA-------LGRYPHQkgwlasesqedervireameqtdtwkfrnkplqtLSGG 143
Cdd:COG4148 97 nlLYGRKRAPRAERRIS-FD----EVVEllgighlLDRRPAT----------------------------------LSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 144 ERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLN-MASLyCDRVLLLNEGRMVDLN 222
Cdd:COG4148 138 ERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDeVARL-ADHVVLLEQGRVVASG 216
|
250
....*....|..
gi 1599980197 223 SPRQVMTEHQLA 234
Cdd:COG4148 217 PLAEVLSRPDLL 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
1.78e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.18 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTAD-TTFAYKVKEVVALGryPHQKGwLASESQEDErvIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPD 159
Cdd:PRK13652 83 VFQNPDdQIFSPTVEQDIAFG--PINLG-LDEETVAHR--VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 160 LLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQL 233
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-211 |
2.01e-22 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 100.65 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 24 QVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITlqgkaiadyhskelaqkmavlpqtADTTFAYKVKEVvalgryp 103
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------------------------PELKISYKPQYI------- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 104 hqkgwlasESQEDERV---IREAMEQTDTWKFRN---KPLQ----------TLSGGERQRALLARALCQEPDLLLLDEPT 167
Cdd:PRK13409 410 --------KPDYDGTVedlLRSITDDLGSSYYKSeiiKPLQlerlldknvkDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1599980197 168 NHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVL 211
Cdd:PRK13409 482 AHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-219 |
2.02e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 95.33 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE---LAQK 77
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 78 MAVLPQTADTTFAYKVKEVVALGRYphqkgwLASESQED-ERVIREAMEQTDTW-KFRNKPLQtLSGGERQRALLARALC 155
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLI------IAGASGDDiRRRVSAALDKVGLLdKAKNFPIQ-LSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 156 QEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTrQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-239 |
4.28e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 95.29 E-value: 4.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLL-----SPSEGTITLQGKAI--ADYHSKEL 74
Cdd:PRK14267 5 IETVNLRVYYGSNH-VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIysPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 75 AQKMAVLPQTADTTFAYKVKEVVALGRypHQKGWLASESQEDERViREAMEQTDTW-----KFRNKPLQtLSGGERQRAL 149
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIGV--KLNGLVKSKKELDERV-EWALKKAALWdevkdRLNDYPSN-LSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 150 LARALCQEPDLLLLDEPTNHLD---ISHQMQLLDALKDwtrtrQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQ 226
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-----EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRK 234
|
250
....*....|....*
gi 1599980197 227 VMT--EHQLANVYET 239
Cdd:PRK14267 235 VFEnpEHELTEKYVT 249
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
14-225 |
4.88e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.10 E-value: 4.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 14 KTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE-----LAQKMAVLPQTA-DT 87
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQrdicmVFQSYALFPHMSlGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 88 TFAYKVKevvALGRyphqkgwlaSESQEDERViREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPT 167
Cdd:PRK11432 98 NVGYGLK---MLGV---------PKEERKQRV-KEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 168 NHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPR 225
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQ 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-228 |
5.16e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.80 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGydektpiIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQ---- 76
Cdd:PRK10070 34 ILEKTGLSLG-------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 77 KMAVLPQTADTTFAYKVKEVVALGRypHQKGWLASESQEDERvirEAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQ 156
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGM--ELAGINAEERREKAL---DALRQVGLENYAHSYPDELSGGMRQRVGLARALAI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1599980197 157 EPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVM 228
Cdd:PRK10070 182 NPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-220 |
7.51e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.88 E-value: 7.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQT 84
Cdd:PRK13657 338 DDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 85 AdTTFAYKVKEVVALGRyphqkgwlasESQEDERViREAMEQTDTWKF---RNKPLQT--------LSGGERQRALLARA 153
Cdd:PRK13657 418 A-GLFNRSIEDNIRVGR----------PDATDEEM-RAAAERAQAHDFierKPDGYDTvvgergrqLSGGERQRLAIARA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 154 LCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMASlYCDRVLLLNEGRMVD 220
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKGR--TTFIIAHRLSTVR-NADRILVFDNGRVVE 549
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-211 |
9.06e-22 |
|
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: 98.32 E-value: 9.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 24 QVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTItlqgkaiadyhskELAQKMAVLPQ--TADTTfaykvKEVVALGR 101
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQyiSPDYD-----GTVEEFLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 102 YPHQKGWlaSESQEDERVIRE-AMEqtdtwKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLD 180
Cdd:COG1245 424 SANTDDF--GSSYYKTEIIKPlGLE-----KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAK 496
|
170 180 190
....*....|....*....|....*....|.
gi 1599980197 181 ALKDWTRTRQLTVVAILHDLNMASLYCDRVL 211
Cdd:COG1245 497 AIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-203 |
9.09e-22 |
|
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: 92.81 E-value: 9.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEkTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADyHSKELAQKMAVL 81
Cdd:TIGR01189 1 LAARNLACSRGE-RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-QRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADTTFAYKVKEVVAlgryphqkgWLASESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLL 161
Cdd:TIGR01189 79 GHLPGLKPELSALENLH---------FWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1599980197 162 LLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMA 203
Cdd:TIGR01189 150 ILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
1.28e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 93.64 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEkTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA----- 75
Cdd:COG4674 10 ILYVEDLTVSFDG-FKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIArlgig 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 ---QKMAVLPQ-TadttfaykVKEVVALGrYPHQKGWLAS----ESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQR 147
Cdd:COG4674 89 rkfQKPTVFEElT--------VFENLELA-LKGDRGVFASlfarLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQW 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 148 ALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMASLYCDRVLLLNEGR 217
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKH--SVVVVEHDMEFVRQIARKVTVLHQGS 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-219 |
1.74e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 95.25 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTPIIQQL---SFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA-- 75
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALnnvSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 -QKMAVLPQ-----TADTTFaykvkEVVALgryPHQkgwLASESQED-ERVIREAMEQTDTWKFRNK-PLQtLSGGERQR 147
Cdd:PRK11153 81 rRQIGMIFQhfnllSSRTVF-----DNVAL---PLE---LAGTPKAEiKARVTELLELVGLSDKADRyPAQ-LSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1599980197 148 ALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
5-260 |
1.84e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 94.32 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTPIIQQLSFQVH----KGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIA----DYHSKELAQ 76
Cdd:PRK13634 6 QKVEHRYQYKTPFERRALYDVNvsipSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKPLRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 77 KMAVLPQTADTT-FAYKVKEVVALGryPHQKGwlASEsQEDERVIREAMEQTD-TWKFRNKPLQTLSGGERQRALLARAL 154
Cdd:PRK13634 86 KVGIVFQFPEHQlFEETVEKDICFG--PMNFG--VSE-EDAKQKAREMIELVGlPEELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 155 CQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQV------M 228
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIfadpdeL 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1599980197 229 TEHQLaNVYET-----KIRRNEHPTIPRPLVTFEPAA 260
Cdd:PRK13634 241 EAIGL-DLPETvkfkrALEEKFGISFPKPCLTLEELA 276
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-230 |
1.92e-21 |
|
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: 97.89 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVL 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTAdTTFAYKVKEVVALGRYPHqkgwlaSESQEDERVIREAMEQTDTWKFrnkPL----------QTLSGGERQRALLA 151
Cdd:TIGR01193 554 PQEP-YIFSGSILENLLLGAKEN------VSQDEIWAACEIAEIKDDIENM---PLgyqtelseegSSISGGQKQRIALA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 152 RALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTrqlTVVAILHDLNMASLyCDRVLLLNEGRMVDLNSPRQVMTE 230
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-199 |
2.41e-21 |
|
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: 96.93 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLqGKAIadyhskelaqKMAVL 81
Cdd:TIGR03719 323 IEAENLTKAFGDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADTTFAYK-VKEVVA-------LGRYphqkgwlasESQEDERVIREAMEQTDtwkfRNKPLQTLSGGERQRALLARA 153
Cdd:TIGR03719 391 DQSRDALDPNKtVWEEISggldiikLGKR---------EIPSRAYVGRFNFKGSD----QQKKVGQLSGGERNRVHLAKT 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1599980197 154 LCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRtrqlTVVAILHD 199
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRALEEALLNFAG----CAVVISHD 499
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-228 |
4.48e-21 |
|
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: 96.32 E-value: 4.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGY-DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:TIGR02203 331 VEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTAdTTFAYKVKEVVALGRyphqkgwlasESQEDERVIREAMEQTDTWKFRNK-P--LQT--------LSGGERQRAL 149
Cdd:TIGR02203 411 VSQDV-VLFNDTIANNIAYGR----------TEQADRAEIERALAAAYAQDFVDKlPlgLDTpigengvlLSGGQRQRLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 150 LARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAilHDLNMASlYCDRVLLLNEGRMVDLNSPRQVM 228
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIA--HRLSTIE-KADRIVVMDDGRIVERGTHNELL 555
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-237 |
4.59e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 95.75 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 19 QQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE-LAQKMAVLPQTADTTFAYKVKEVV 97
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQELHLVPEMTVAENL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 98 ALGRYPHQKGWLasesqeDER-VIREAMEQTDTWKFR---NKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHL--- 170
Cdd:PRK11288 101 YLGQLPHKGGIV------NRRlLNYEAREQLEHLGVDidpDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLsar 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 171 DISHQMQLLDALKDWTRtrqlTVVAILHdlNMASLY--CDRVLLLNEGR-------MVDLNSPRQV--MTEHQLANVY 237
Cdd:PRK11288 175 EIEQLFRVIRELRAEGR----VILYVSH--RMEEIFalCDAITVFKDGRyvatfddMAQVDRDQLVqaMVGREIGDIY 246
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-219 |
4.72e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 96.45 E-value: 4.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLsPSEGTITLQGKAIADYHSKELAQKMAVL 81
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTAdTTFAYKVKEVVALGRyPHqkgwlASESQedervIREAMEQTDTWKFRNKPLQ-----------TLSGGERQRALL 150
Cdd:PRK11174 429 GQNP-QLPHGTLRDNVLLGN-PD-----ASDEQ-----LQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLAL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 151 ARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDwtRTRQLTVVAILHDLNmaSLY-CDRVLLLNEGRMV 219
Cdd:PRK11174 497 ARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA--ASRRQTTLMVTHQLE--DLAqWDQIWVMQDGQIV 562
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-203 |
1.08e-20 |
|
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: 89.86 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIaDYHSKELAQKMAVL 81
Cdd:cd03231 1 LEADELTCERDGRA-LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADTTFAYKVKEVVALgryphqkgWLASESQEDervIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLL 161
Cdd:cd03231 79 GHAPGIKTTLSVLENLRF--------WHADHSDEQ---VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLW 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1599980197 162 LLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMA 203
Cdd:cd03231 148 ILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-243 |
1.34e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.86 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIA----DYHSKELaq 76
Cdd:PRK13538 1 MLEARNLACERDER-ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdEYHQDLL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 77 kmavlpqtadttfaYkvkevvaLGrypHQKG------------WLASESQE-DERVIREAMEQTDTWKFRNKPLQTLSGG 143
Cdd:PRK13538 78 --------------Y-------LG---HQPGikteltalenlrFYQRLHGPgDDEALWEALAQVGLAGFEDVPVRQLSAG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 144 ERQRALLARALCQEPDLLLLDEPTNHLDISHqmqlldalkdwtrtrqltvVAILHDLNMAslYCDRvlllneGRMVdlns 223
Cdd:PRK13538 134 QQRRVALARLWLTRAPLWILDEPFTAIDKQG-------------------VARLEALLAQ--HAEQ------GGMV---- 182
|
250 260
....*....|....*....|
gi 1599980197 224 prqVMTEHQLANVYETKIRR 243
Cdd:PRK13538 183 ---ILTTHQDLPVASDKVRK 199
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-230 |
1.77e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.34 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTPI----IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAI-ADYHSKELAQ--- 76
Cdd:PRK13649 6 QNVSYTYQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQirk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 77 KMAVLPQTADTT-FAYKVKEVVALGryPHQKGwlasESQED-ERVIRE--AMEQTDTWKFRNKPLQtLSGGERQRALLAR 152
Cdd:PRK13649 86 KVGLVFQFPESQlFEETVLKDVAFG--PQNFG----VSQEEaEALAREklALVGISESLFEKNPFE-LSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 153 ALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTrQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTE 230
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
1.96e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.84 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTP----IIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIAD-------- 68
Cdd:PRK13631 21 ILRVKNLYCVFDEKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDkknnheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 69 -YHS-------KELAQKMAVLPQTAD-TTFAYKVKEVVALGryPHQKGWLASESQEDERVIREAMEQTDTWKFRNkPLQt 139
Cdd:PRK13631 101 tNPYskkiknfKELRRRVSMVFQFPEyQLFKDTIEKDIMFG--PVALGVKKSEAKKLAKFYLNKMGLDDSYLERS-PFG- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 140 LSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDwTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
250
....*....|....*.
gi 1599980197 220 DLNSPRQVMTEHQLAN 235
Cdd:PRK13631 256 KTGTPYEIFTDQHIIN 271
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-251 |
2.05e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 90.51 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTItLQGKAI---ADYHSKELAQKM 78
Cdd:PRK11247 13 LLLNAVSKRYGERT-VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPlaeAREDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 79 AVLPQTadttfayKVKEVVALGryphQKG-WLASESQEDERVIREamEQTDTWKfrnkplQTLSGGERQRALLARALCQE 157
Cdd:PRK11247 91 RLLPWK-------KVIDNVGLG----LKGqWRDAALQALAAVGLA--DRANEWP------AALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 158 PDLLLLDEPTNHLD----ISHQmQLLDALkdWtRTRQLTVVAILHDLNMASLYCDRVLLLNEGRM-----VDLNSPRQVM 228
Cdd:PRK11247 152 PGLLLLDEPLGALDaltrIEMQ-DLIESL--W-QQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldltVDLPRPRRRG 227
|
250 260
....*....|....*....|....*..
gi 1599980197 229 TeHQLA----NVYETKIRRNEHPTIPR 251
Cdd:PRK11247 228 S-ARLAeleaEVLQRVMSRGESEPTRL 253
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-199 |
2.74e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 94.25 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 3 DAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGK---AIADYHSKELAQKMA 79
Cdd:PRK11147 321 EMENVNYQIDGKQ-LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlevAYFDQHRAELDPEKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 80 VLPQTADTTfaykvKEVVALGRYPHQKGWLasesQEDERVIREAMeqtdtwkfrnKPLQTLSGGERQRALLARALCQEPD 159
Cdd:PRK11147 400 VMDNLAEGK-----QEVMVNGRPRHVLGYL----QDFLFHPKRAM----------TPVKALSGGERNRLLLARLFLKPSN 460
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1599980197 160 LLLLDEPTNHLDIsHQMQLLDALKDwtrTRQLTVVAILHD 199
Cdd:PRK11147 461 LLILDEPTNDLDV-ETLELLEELLD---SYQGTVLLVSHD 496
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-245 |
2.97e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.15 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSV----GYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQ 76
Cdd:COG1101 1 MLELKNLSKtfnpGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 77 KMAVLPQ--TADTTFAYKVKEVVALGRYPHQKGWLA-SESQEDERVIREAMEQT--------DTwkfrnkPLQTLSGGER 145
Cdd:COG1101 81 YIGRVFQdpMMGTAPSMTIEENLALAYRRGKRRGLRrGLTKKRRELFRELLATLglglenrlDT------KVGLLSGGQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 146 QrAL-LARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMV-DLNS 223
Cdd:COG1101 155 Q-ALsLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIIlDVSG 233
|
250 260
....*....|....*....|...
gi 1599980197 224 P-RQVMTEHQLANVYEtKIRRNE 245
Cdd:COG1101 234 EeKKKLTVEDLLELFE-EIRGEE 255
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-217 |
3.49e-20 |
|
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: 88.68 E-value: 3.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEK----TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGkaiadyhskelaqKMAV 80
Cdd:cd03250 4 EDASFTWDSGeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTA----DTtfaykVKEVVALGrYPHQKGWLasesqedERVIR--------EAMEQTDtwkfrnkplQT--------L 140
Cdd:cd03250 71 VSQEPwiqnGT-----IRENILFG-KPFDEERY-------EKVIKacalepdlEILPDGD---------LTeigekginL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 141 SGGERQRALLARALCQEPDLLLLDEPTNHLDI---SHQMQ--LLDALKDwTRTRqltvvaIL--HDLNMASlYCDRVLLL 213
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAhvgRHIFEncILGLLLN-NKTR------ILvtHQLQLLP-HADQIVVL 200
|
....
gi 1599980197 214 NEGR 217
Cdd:cd03250 201 DNGR 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-200 |
3.69e-20 |
|
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: 93.70 E-value: 3.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 27 KGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTIT-----------LQGKAIADYHSKeLAQ---KMAVLPQTAD---TTF 89
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepswdevlkrFRGTELQDYFKK-LANgeiKVAHKPQYVDlipKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 90 AYKVKEVvaLGRYphqkgwlasesqeDER-VIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTN 168
Cdd:COG1245 177 KGTVREL--LEKV-------------DERgKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190
....*....|....*....|....*....|..
gi 1599980197 169 HLDISHQMQLLDALKDWTRTRQlTVVAILHDL 200
Cdd:COG1245 242 YLDIYQRLNVARLIRELAEEGK-YVLVVEHDL 272
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
6-227 |
3.80e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.61 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 6 NVSVGYDEKTPI----IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIA----DYHSKELAQK 77
Cdd:PRK13646 7 NVSYTYQKGTPYehqaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRPVRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 78 MAVLPQTADTT-FAYKVKEVVALGryPHQKGWLASESQEDERVI-------REAMEQTdtwkfrnkPLQtLSGGERQRAL 149
Cdd:PRK13646 87 IGMVFQFPESQlFEDTVEREIIFG--PKNFKMNLDEVKNYAHRLlmdlgfsRDVMSQS--------PFQ-MSGGQMRKIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 150 LARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQV 227
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-200 |
4.20e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 93.33 E-value: 4.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 27 KGEIFGILGPNGSGKTTLLKAVSGLLSP------SEGTIT-----LQGKAIADYHsKELAQ---KMAVLPQTAD---TTF 89
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPnlgdyeEEPSWDevlkrFRGTELQNYF-KKLYNgeiKVVHKPQYVDlipKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 90 AYKVKEVValgryphqkgwlaseSQEDER-VIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTN 168
Cdd:PRK13409 177 KGKVRELL---------------KKVDERgKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190
....*....|....*....|....*....|..
gi 1599980197 169 HLDISHQMQLLDALKDWTRTRqlTVVAILHDL 200
Cdd:PRK13409 242 YLDIRQRLNVARLIRELAEGK--YVLVVEHDL 271
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-224 |
4.56e-20 |
|
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: 88.24 E-value: 4.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGY-DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:cd03369 7 IEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTAdTTFAYKVKEvvALGRYPHQkgwlasesqeDERVIREAMEQTDTWkfrnkplQTLSGGERQRALLARALCQEPDL 160
Cdd:cd03369 87 IPQDP-TLFSGTIRS--NLDPFDEY----------SDEEIYGALRVSEGG-------LNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 161 LLLDEPTNHLDISHQMQLLDALKdwTRTRQLTVVAILHDLNmASLYCDRVLLLNEGRMVDLNSP 224
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIR--EEFTNSTILTIAHRLR-TIIDYDKILVMDAGEVKEYDHP 207
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
5-219 |
9.40e-20 |
|
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: 92.19 E-value: 9.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQt 84
Cdd:COG5265 361 ENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQ- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 85 aDT-----TFAYKvkevVALGRyphqkgWLASEsQEDERVIREAmeQTDTwkF-RNKP--LQT--------LSGGERQRA 148
Cdd:COG5265 440 -DTvlfndTIAYN----IAYGR------PDASE-EEVEAAARAA--QIHD--FiESLPdgYDTrvgerglkLSGGEKQRV 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 149 LLARALCQEPDLLLLDEPTNHLDiSHQMQ-LLDALKDWTRTRqlTVVAILHDLnmaS--LYCDRVLLLNEGRMV 219
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALD-SRTERaIQAALREVARGR--TTLVIAHRL---StiVDADEILVLEAGRIV 571
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-199 |
1.00e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 92.10 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLqGKAIadyhskelaqKMAVL 81
Cdd:PRK11819 325 IEAENLSKSFGDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADTTFAYK-VKEVValgryphqkgwlaSESQEderVIReaMEQTDT--------WKFR----NKPLQTLSGGERQRA 148
Cdd:PRK11819 393 DQSRDALDPNKtVWEEI-------------SGGLD---IIK--VGNREIpsrayvgrFNFKggdqQKKVGVLSGGERNRL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1599980197 149 LLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRtrqlTVVAILHD 199
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPG----CAVVISHD 501
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-230 |
1.08e-19 |
|
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: 91.79 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 21 LSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQ-GKAIADYHSKELAQK------MAVLPQTADTtfaykv 93
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPDGRgrakryIGILHQEYDL------ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 94 kevvalgrYPHQ---KGWLASESQE--DERVIREAMEQTDTWKFR--------NKPLQTLSGGERQRALLARALCQEPDL 160
Cdd:TIGR03269 377 --------YPHRtvlDNLTEAIGLElpDELARMKAVITLKMVGFDeekaeeilDKYPDELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 161 LLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTE 230
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-227 |
1.51e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 89.38 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 22 SFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQK-----------MAVL--------- 81
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdiqmifqdpLASLnprmtigei 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 ---------PQTADTTFAYKVKEVVA--------LGRYPHQkgwlasesqedervireameqtdtwkfrnkplqtLSGGE 144
Cdd:PRK15079 121 iaeplrtyhPKLSRQEVKDRVKAMMLkvgllpnlINRYPHE----------------------------------FSGGQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 145 RQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSP 224
Cdd:PRK15079 167 CQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTY 246
|
...
gi 1599980197 225 RQV 227
Cdd:PRK15079 247 DEV 249
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-220 |
1.84e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.18 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDE---KTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGK--------AIADY 69
Cdd:PRK11629 5 LLQCDNLCKRYQEgsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsklssaAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 70 HSKELA---QKMAVLPqtaDTTFAYKVKEVVALGRYPhqkgwlASESQEDERVIREA--MEQtdtwKFRNKPLQtLSGGE 144
Cdd:PRK11629 85 RNQKLGfiyQFHHLLP---DFTALENVAMPLLIGKKK------PAEINSRALEMLAAvgLEH----RANHRPSE-LSGGE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1599980197 145 RQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASlYCDRVLLLNEGRMVD 220
Cdd:PRK11629 151 RQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAK-RMSRQLEMRDGRLTA 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-219 |
1.88e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.60 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 4 AQNVSVGYDEKTPI----IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHS-------- 71
Cdd:PRK13651 5 VKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkekekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 72 ----------------KELAQKMAVLPQTAD-TTFAYKVKEVVALGryPHQKGWLASESQEDERVIREaMEQTDTWKFRN 134
Cdd:PRK13651 85 eklviqktrfkkikkiKEIRRRVGVVFQFAEyQLFEQTIEKDIIFG--PVSMGVSKEEAKKRAAKYIE-LVGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 135 KPLQtLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQlTVVAILHDLNMASLYCDRVLLLN 214
Cdd:PRK13651 162 SPFE-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFK 239
|
....*
gi 1599980197 215 EGRMV 219
Cdd:PRK13651 240 DGKII 244
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-224 |
2.19e-19 |
|
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: 92.00 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 16 PIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIaDYHSKELAQKMAVLPQTADTTFAYKVKE 95
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 96 VVALgrYPHQKGwlasESQEDERVIREAM-EQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISH 174
Cdd:TIGR01257 1023 HILF--YAQLKG----RSWEEAQLEMEAMlEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1599980197 175 QMQLLDALKDWTRTRqlTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSP 224
Cdd:TIGR01257 1097 RRSIWDLLLKYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-199 |
2.85e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 90.56 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYhskeLAQKmavlPQ- 83
Cdd:PRK11819 10 NRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGY----LPQE----PQl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 84 TADTTfaykVKEVV---------ALGRYPHQKGWLASESQEDERVIRE------AMEQTDTWKFRNK------------- 135
Cdd:PRK11819 82 DPEKT----VRENVeegvaevkaALDRFNEIYAAYAEPDADFDALAAEqgelqeIIDAADAWDLDSQleiamdalrcppw 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1599980197 136 --PLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRtrqlTVVAILHD 199
Cdd:PRK11819 158 daKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG----TVVAVTHD 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-198 |
4.57e-19 |
|
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: 84.13 E-value: 4.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTItlqgkaiaDYHSKElaqKMAVLPQT 84
Cdd:cd03223 4 ENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGE---DLLFLPQR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 85 ---ADTTFaykvKEVVAlgrYPhqkgwlasesqedervireameqtdtWKfrnkplQTLSGGERQRALLARALCQEPDLL 161
Cdd:cd03223 73 pylPLGTL----REQLI---YP--------------------------WD------DVLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....*..
gi 1599980197 162 LLDEPTNHLDISHQMQLLDALKDwtrtRQLTVVAILH 198
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKE----LGITVISVGH 146
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-219 |
5.47e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 90.01 E-value: 5.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 15 TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIadyhskelaqkMAVLPQ-----TADTTF 89
Cdd:PRK11147 16 APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLI-----------VARLQQdpprnVEGTVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 90 AYkVKEVVA-----LGRYPHQKGWLASESQED-----ERViREAMEQTDTWKFRNK--------------PLQTLSGGER 145
Cdd:PRK11147 85 DF-VAEGIEeqaeyLKRYHDISHLVETDPSEKnlnelAKL-QEQLDHHNLWQLENRinevlaqlgldpdaALSSLSGGWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 146 QRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWtrtrQLTVVAILHDL----NMASlycdRVLLLNEGRMV 219
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF----QGSIIFISHDRsfirNMAT----RIVDLDRGKLV 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-229 |
9.20e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 85.86 E-value: 9.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSgLLSPSEGTITLQGKAiaDYHSKELAQ-------- 76
Cdd:PRK14258 11 NNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGRV--EFFNQNIYErrvnlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 77 ---------KMAVLPQTADTTFAYKVKEVvalgryphqkGWlaSESQEDERVIREAMEQTDTW-KFRNKPLQT---LSGG 143
Cdd:PRK14258 87 rrqvsmvhpKPNLFPMSVYDNVAYGVKIV----------GW--RPKLEIDDIVESALKDADLWdEIKHKIHKSaldLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 144 ERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLL--NEGR---M 218
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRigqL 234
|
250
....*....|.
gi 1599980197 219 VDLNSPRQVMT 229
Cdd:PRK14258 235 VEFGLTKKIFN 245
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
5-223 |
1.13e-18 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 88.79 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQT 84
Cdd:TIGR01192 338 RHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 85 ADTtFAYKVKEVVALGRyphqkgwlasESQEDERVIR--EAMEQTDTWKFRNKPLQT--------LSGGERQRALLARAL 154
Cdd:TIGR01192 418 AGL-FNRSIRENIRLGR----------EGATDEEVYEaaKAAAAHDFILKRSNGYDTlvgergnrLSGGERQRLAIARAI 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 155 CQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMASlYCDRVLLLNEGRMVDLNS 223
Cdd:TIGR01192 487 LKNAPILVLDEATSALDVETEARVKNAIDALRKNR--TTFIIAHRLSTVR-NADLVLFLDQGRLIEKGS 552
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-229 |
1.61e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 84.76 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDeKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE------- 73
Cdd:PRK09493 1 MIEFKNVSKHFG-PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 74 --LAQKMAVLPQ-TAdttfaykvKEVVALGryP-HQKGwlaSESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRAL 149
Cdd:PRK09493 80 gmVFQQFYLFPHlTA--------LENVMFG--PlRVRG---ASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 150 LARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTrTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMT 229
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
17-228 |
1.69e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 85.02 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 17 IIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAI-----ADYHSKELAQKMAVLPQTADT---- 87
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdKDGQLKVADKNQLRLLRTRLTmvfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 88 -----TFAYKVKEVValgRYPHQKGWLaSESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLL 162
Cdd:PRK10619 100 hfnlwSHMTVLENVM---EAPIQVLGL-SKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 163 LDEPTNHLD---ISHQMQLLDALKDWTRtrqlTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVM 228
Cdd:PRK10619 176 FDEPTSALDpelVGEVLRIMQQLAEEGK----TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-217 |
1.79e-18 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 84.41 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSvgydeKT-----------PIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQgkaiADY 69
Cdd:COG4778 4 LLEVENLS-----KTftlhlqggkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR----HDG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 70 HSKELAQkmavlpqtADttfaykVKEVVALGRypHQKGWLaseSQEdERVI-------------REAMEQTDTWKFRNKP 136
Cdd:COG4778 75 GWVDLAQ--------AS------PREILALRR--RTIGYV---SQF-LRVIprvsaldvvaeplLERGVDREEARARARE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 137 L---------------QTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQ---MQLLDALKDwtrtRQLTVVAILH 198
Cdd:COG4778 135 LlarlnlperlwdlppATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRavvVELIEEAKA----RGTAIIGIFH 210
|
250
....*....|....*....
gi 1599980197 199 DLNMASLYCDRVLLLNEGR 217
Cdd:COG4778 211 DEEVREAVADRVVDVTPFS 229
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-219 |
1.96e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 83.35 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLS--PSEGTITLQGKAIADYHSKELAQK-- 77
Cdd:cd03217 1 LEIKDLHVSVGGKE-ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERARLgi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 78 -MAvlpqtadttFAYKVK-EVVALGRYphqkgwlasesqedervIREAMEqtdtwkfrnkplqTLSGGERQRALLARALC 155
Cdd:cd03217 80 fLA---------FQYPPEiPGVKNADF-----------------LRYVNE-------------GFSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 156 QEPDLLLLDEPTNHLDISHQMQLLDALKDWtRTRQLTVVAILHDLNMASLY-CDRVLLLNEGRMV 219
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIV 184
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-216 |
2.60e-18 |
|
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: 88.43 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 15 TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAiaDYHSkelaQKMAVLPQTadttfaykVK 94
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRI--SFSP----QTSWIMPGT--------IK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 95 EVVALGryphqkgwLASESQEDERVIREAMEQTDTWKFRNK---PLQ----TLSGGERQRALLARALCQEPDLLLLDEPT 167
Cdd:TIGR01271 505 DNIIFG--------LSYDEYRYTSVIKACQLEEDIALFPEKdktVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1599980197 168 NHLDISHQMQLLDA--LKDWTRTRQLTVVAILHDLNMAslycDRVLLLNEG 216
Cdd:TIGR01271 577 THLDVVTEKEIFESclCKLMSNKTRILVTSKLEHLKKA----DKILLLHEG 623
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-216 |
5.13e-18 |
|
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: 84.14 E-value: 5.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 15 TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKaiADYHSkelaQKMAVLPQTadttfaykVK 94
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFSS----QFSWIMPGT--------IK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 95 EVVALGryphqkgwLASESQEDERVIREAMEQTDTWKFRNK---PLQ----TLSGGERQRALLARALCQEPDLLLLDEPT 167
Cdd:cd03291 116 ENIIFG--------VSYDEYRYKSVVKACQLEEDITKFPEKdntVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1599980197 168 NHLDISHQMQLLDA--LKDWTRTRQLTVVAILHDLNMAslycDRVLLLNEG 216
Cdd:cd03291 188 GYLDVFTEKEIFEScvCKLMANKTRILVTSKMEHLKKA----DKILILHEG 234
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
8-218 |
6.03e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.90 E-value: 6.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 8 SVGYDE-KTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA----------- 75
Cdd:PRK10584 15 SVGQGEhELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakhvgfvf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 QKMAVLPqtadTTFAYKVKEVVALGRYphqkgwlASESQEDERVIrEAMEQTDTWK-FRNKPLQtLSGGERQRALLARAL 154
Cdd:PRK10584 95 QSFMLIP----TLNALENVELPALLRG-------ESSRQSRNGAK-ALLEQLGLGKrLDHLPAQ-LSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 155 CQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASlYCDRVLLLNEGRM 218
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAA-RCDRRLRLVNGQL 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-233 |
6.81e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.12 E-value: 6.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSvGYDEKTPIiqqlSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE-LAQKMAV 80
Cdd:PRK11288 258 LRLDGLK-GPGLREPI----SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaIRAGIML 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQ--TADTTFA-YKVKEVVALGRYPHQK--GWLASESQEDE---RVIREAMEQTDTwkfRNKPLQTLSGGERQRALLAR 152
Cdd:PRK11288 333 CPEdrKAEGIIPvHSVADNINISARRHHLraGCLINNRWEAEnadRFIRSLNIKTPS---REQLIMNLSGGNQQKAILGR 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 153 ALCQEPDLLLLDEPTNHLDI---SHQMQLLDALKDwtrtRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDlNSPRQVMT 229
Cdd:PRK11288 410 WLSEDMKVILLDEPTRGIDVgakHEIYNVIYELAA----QGVAVLFVSSDLPEVLGVADRIVVMREGRIAG-ELAREQAT 484
|
....
gi 1599980197 230 EHQL 233
Cdd:PRK11288 485 ERQA 488
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-220 |
9.75e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.83 E-value: 9.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEktPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSP----SEGTITLQGKAIA--DYHSKELA 75
Cdd:PRK10418 5 IELRNIALQAAQ--PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVApcALRGRKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 QKMAVlPQTA----DTTFAYKVKEVVALGRyphqkgwlasesQEDERVIREAMEQT---DTWK-FRNKPLQtLSGGERQR 147
Cdd:PRK10418 83 TIMQN-PRSAfnplHTMHTHARETCLALGK------------PADDATLTAALEAVgleNAARvLKLYPFE-MSGGMLQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1599980197 148 ALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVD 220
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-219 |
1.09e-17 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 82.31 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGllSPS----EGTITLQGKAIADYHSKELAQK 77
Cdd:TIGR01978 1 LKIKDLHVSVEDK-EILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFKGQDLLELEPDERARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 78 -MAVLPQTADTTFAYKVKEVV--ALGRYPHQKGWLASESQEDERVIREAMEQTD-TWKFRNKPLQT-LSGGERQRALLAR 152
Cdd:TIGR01978 78 gLFLAFQYPEEIPGVSNLEFLrsALNARRSARGEEPLDLLDFEKLLKEKLALLDmDEEFLNRSVNEgFSGGEKKRNEILQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 153 ALCQEPDLLLLDEPTNHLDIshqmqllDALK-------DWtRTRQLTVVAILHDLNMA-SLYCDRVLLLNEGRMV 219
Cdd:TIGR01978 158 MALLEPKLAILDEIDSGLDI-------DALKivaeginRL-REPDRSFLIITHYQRLLnYIKPDYVHVLLDGRIV 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-230 |
1.19e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.91 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDeKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGL--LSPS---EGTITLQGKAIADYH--SKEL 74
Cdd:PRK14243 11 LRTENLNVYYG-SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLYAPDvdPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 75 AQKMAVLPQTADTtFAYKVKEVVALGryPHQKGWLASESQEDERVIREAM---EQTDtwKFRNKPLqTLSGGERQRALLA 151
Cdd:PRK14243 90 RRRIGMVFQKPNP-FPKSIYDNIAYG--ARINGYKGDMDELVERSLRQAAlwdEVKD--KLKQSGL-SLSGGQQQRLCIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 152 RALCQEPDLLLLDEPTNHLD-ISHQM--QLLDALKdwtrtRQLTVVAILHDLNMASLYCDRVLLLN---------EGRMV 219
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDpISTLRieELMHELK-----EQYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLV 238
|
250
....*....|....*...
gi 1599980197 220 D-------LNSPRQVMTE 230
Cdd:PRK14243 239 EfdrtekiFNSPQQQATR 256
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-236 |
1.33e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.84 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEG-----TITLQGKAIADYHSK-ELA 75
Cdd:PRK14271 22 MAAVNLTLGFAGKT-VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVlEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 QKMAVLPQTADTtFAYKVKEVVALGRYPHQkgwlASESQEDERVIREAMEQTDTW-----KFRNKPLQtLSGGERQRALL 150
Cdd:PRK14271 101 RRVGMLFQRPNP-FPMSIMDNVLAGVRAHK----LVPRKEFRGVAQARLTEVGLWdavkdRLSDSPFR-LSGGQQQLLCL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 151 ARALCQEPDLLLLDEPTNHLDISHQMQLLDALKdwTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVD-------LNS 223
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR--SLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEegpteqlFSS 252
|
250
....*....|...
gi 1599980197 224 PRQVMTEHQLANV 236
Cdd:PRK14271 253 PKHAETARYVAGL 265
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-220 |
1.34e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 83.64 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGY-DEKTPI--IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLS-P---SEGTITLQGKAIADYHSKE 73
Cdd:PRK11022 3 LLNVDKLSVHFgDESAPFraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 74 LAQ----KMAVLPQTADT------TFAYKVKEVVALgrypHQKGwlaSESQEDERVIrEAMEQTD----TWKFRNKPLQt 139
Cdd:PRK11022 83 RRNlvgaEVAMIFQDPMTslnpcyTVGFQIMEAIKV----HQGG---NKKTRRQRAI-DLLNQVGipdpASRLDVYPHQ- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 140 LSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
.
gi 1599980197 220 D 220
Cdd:PRK11022 234 E 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-233 |
1.62e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.22 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSvGYDEKTpiIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQK-MA 79
Cdd:PRK09700 265 VFEVRNVT-SRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 80 VLPQT-ADTTF--AYKVKEVVALGRYPHQKGW-----LASESQEDerviREAMEQTDTWKFR----NKPLQTLSGGERQR 147
Cdd:PRK09700 342 YITESrRDNGFfpNFSIAQNMAISRSLKDGGYkgamgLFHEVDEQ----RTAENQRELLALKchsvNQNITELSGGNQQK 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 148 ALLARALCQEPDLLLLDEPTNHLDISHQMQLldalkdWTRTRQL-----TVVAILHDLNMASLYCDRVLLLNEGRMVDLN 222
Cdd:PRK09700 418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEI------YKVMRQLaddgkVILMVSSELPEIITVCDRIAVFCEGRLTQIL 491
|
250
....*....|.
gi 1599980197 223 SPRQVMTEHQL 233
Cdd:PRK09700 492 TNRDDMSEEEI 502
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-232 |
1.72e-17 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 85.22 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLqGKAIadyhskelaqKMAV 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRI-ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGI----------KLGY 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQtadttfaykvkevvalgrypHQKGWL-ASES--QEDERVIREAMEQtdtwKFRN-------------KPLQTLSGGE 144
Cdd:PRK10636 380 FAQ--------------------HQLEFLrADESplQHLARLAPQELEQ----KLRDylggfgfqgdkvtEETRRFSGGE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 145 RQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWtrtrQLTVVAILHDLNMASLYCDRVLLLNEGRMV----D 220
Cdd:PRK10636 436 KARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF----EGALVVVSHDRHLLRSTTDDLYLVHDGKVEpfdgD 511
|
250
....*....|..
gi 1599980197 221 LNSPRQVMTEHQ 232
Cdd:PRK10636 512 LEDYQQWLSDVQ 523
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-227 |
2.03e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 81.75 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTPIiQQLSFQVHKGEIFGILGPNGSGKTTLLKAVS--GLLSPS---EGTITLQGKAIadYHSK--- 72
Cdd:PRK14239 5 ILQVSDLSVYYNKKKAL-NSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNI--YSPRtdt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 73 -ELAQKMAVLPQTADTtFAYKVKEVVALGryphqkgwLASESQEDERVIREAME----QTDTWKFRNKPLQT----LSGG 143
Cdd:PRK14239 82 vDLRKEIGMVFQQPNP-FPMSIYENVVYG--------LRLKGIKDKQVLDEAVEkslkGASIWDEVKDRLHDsalgLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 144 ERQRALLARALCQEPDLLLLDEPTNHLD-ISHQM--QLLDALKDwtrtrQLTVVAILHDLNMASLYCDRVLLLNEGRMVD 220
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDpISAGKieETLLGLKD-----DYTMLLVTRSMQQASRISDRTGFFLDGDLIE 227
|
....*..
gi 1599980197 221 LNSPRQV 227
Cdd:PRK14239 228 YNDTKQM 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-227 |
2.30e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.91 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDE---KTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQG-------KAIADYH 70
Cdd:PRK10261 12 VLAVENLNIAFMQeqqKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 71 SKELAQ-------KMAVLPQTADTTF--AYKVKEVVALGRYPHQkGWLASESQEDERVIREAMEQTDTWKFRNKPLQTLS 141
Cdd:PRK10261 92 EQSAAQmrhvrgaDMAMIFQEPMTSLnpVFTVGEQIAESIRLHQ-GASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 142 GGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDL 221
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
|
....*.
gi 1599980197 222 NSPRQV 227
Cdd:PRK10261 251 GSVEQI 256
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-235 |
2.32e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.18 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 22 SFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIAdyhSKELAQKMAV--LPQtadtTFA-YK---VKE 95
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDIATRRRVgyMSQ----AFSlYGeltVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 96 VVALgrypHQKGWLASESQEDERvIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLD-ISH 174
Cdd:NF033858 359 NLEL----HARLFHLPAAEIAAR-VAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDpVAR 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1599980197 175 QM--QLLDALkdwTRTRQLTVVAILHDLNMAsLYCDRVLLLNEGRMVDLNSPRQVMTEHQLAN 235
Cdd:NF033858 434 DMfwRLLIEL---SREDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAALVAARGAAT 492
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-180 |
2.92e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.30 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE----LAQ 76
Cdd:PRK13539 2 MLEGEDLACVRGGRV-LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEachyLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 77 KMAVLPqtadttfAYKVKEVVALgryphqkgWLASESQeDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQ 156
Cdd:PRK13539 81 RNAMKP-------ALTVAENLEF--------WAAFLGG-EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVS 144
|
170 180
....*....|....*....|....
gi 1599980197 157 EPDLLLLDEPTNHLDISHQMQLLD 180
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAVALFAE 168
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-232 |
2.94e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 81.33 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITlqgkaIADYH---SKELAQK 77
Cdd:PRK11264 3 AIEVKNLVKKFHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIR-----VGDITidtARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 78 MAVLPQTADTT-FAYKvkevvALGRYPHQ-------KGWLASESQEDERVIREAME---------QTDTWKFRnkplqtL 140
Cdd:PRK11264 77 KGLIRQLRQHVgFVFQ-----NFNLFPHRtvleniiEGPVIVKGEPKEEATARAREllakvglagKETSYPRR------L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 141 SGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQlTVVAILHDLNMASLYCDRVLLLNEGRMVD 220
Cdd:PRK11264 146 SGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
250
....*....|..
gi 1599980197 221 LNSPRQVMTEHQ 232
Cdd:PRK11264 225 QGPAKALFADPQ 236
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-219 |
6.38e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 83.61 E-value: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 16 PIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQTAdTTFAYKVKE 95
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP-FLFSDTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 96 VVALGRyPhqkgwlASESQEDERVIREAMEQTDTWKFrNKPLQT--------LSGGERQRALLARALCQEPDLLLLDEPT 167
Cdd:PRK10789 408 NIALGR-P------DATQQEIEHVARLASVHDDILRL-PQGYDTevgergvmLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1599980197 168 NHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNmASLYCDRVLLLNEGRMV 219
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGR--TVIISAHRLS-ALTEASEILVMQHGHIA 528
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-220 |
7.14e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 80.06 E-value: 7.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 14 KTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIaDYHSKELAQKMAVLPQTADTTFA-YK 92
Cdd:COG4161 14 SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF-DFSQKPSEKAIRLLRQKVGMVFQqYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 93 VkevvalgrYPHQK---------GWLASESQEDERviREAMEQTDTWKFRNK----PLQtLSGGERQRALLARALCQEPD 159
Cdd:COG4161 93 L--------WPHLTvmenlieapCKVLGLSKEQAR--EKAMKLLARLRLTDKadrfPLH-LSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1599980197 160 LLLLDEPTNHLDISHQMQLLDALKDWTRTrQLTVVAILHDLNMASLYCDRVLLLNEGRMVD 220
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-220 |
8.80e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 79.67 E-value: 8.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 21 LSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIaDYHSKELAQKMAVLPQTADTTFA-YKVkevval 99
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHF-DFSKTPSDKAIRELRRNVGMVFQqYNL------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 100 grYPHQ-----------KGWLASESQEDERvireAMEQTDTWKFRNK----PLQtLSGGERQRALLARALCQEPDLLLLD 164
Cdd:PRK11124 94 --WPHLtvqqnlieapcRVLGLSKDQALAR----AEKLLERLRLKPYadrfPLH-LSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1599980197 165 EPTNHLDISHQMQLLDALKDWTRTrQLTVVAILHDLNMASLYCDRVLLLNEGRMVD 220
Cdd:PRK11124 167 EPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-229 |
1.27e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 83.10 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 16 PIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQTAdTTFAYKVK- 94
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSP-VLFSGTVRf 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 95 EVVALGRYPHQKGWLASESQEDERVIREAMEQTDTWKFRNKplQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISh 174
Cdd:PLN03232 1329 NIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGG--ENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR- 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 175 qmqlLDALKDWT---RTRQLTVVAILHDLNMAsLYCDRVLLLNEGRMVDLNSPRQVMT 229
Cdd:PLN03232 1406 ----TDSLIQRTireEFKSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
14-219 |
1.75e-16 |
|
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: 77.69 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 14 KTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPS---EGTITLQGKAIADYHSKelaqkmavlpqtadttfa 90
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEK------------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 91 ykvkevvalgrYPHQkgwLASESQEDERV----IREAMEqtdtwkFR-----NKPLQTLSGGERQRALLARALCQEPDLL 161
Cdd:cd03233 81 -----------YPGE---IIYVSEEDVHFptltVRETLD------FAlrckgNEFVRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 162 LLDEPTNHLDISHQMQLLDALKdwtrtrqlTVVAILHDLNMASLY---------CDRVLLLNEGRMV 219
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIR--------TMADVLKTTTFVSLYqasdeiydlFDKVLVLYEGRQI 199
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-202 |
2.27e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 81.48 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTItlqgkaiadyhSKELAQKMAV 80
Cdd:PRK15064 1 MLSTANITMQFGAK-PLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV-----------SLDPNERLGK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTadtTFAYK---VKEVVALGrypHQKGWLASesQEDERVIREA-MEQTDTWK------------------------- 131
Cdd:PRK15064 69 LRQD---QFAFEeftVLDTVIMG---HTELWEVK--QERDRIYALPeMSEEDGMKvadlevkfaemdgytaearagelll 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 132 -------FRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDwtrtRQLTVVAILHD---LN 201
Cdd:PRK15064 141 gvgipeeQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNE----RNSTMIIISHDrhfLN 216
|
.
gi 1599980197 202 M 202
Cdd:PRK15064 217 S 217
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-200 |
2.56e-16 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 78.56 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 22 SFQVHK------GEIFGILGPNGSGKTTLLKAVSGLLSPSEGTIT-----------LQGKAIADYHSKELAQKM--AVLP 82
Cdd:cd03236 14 SFKLHRlpvpreGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELQNYFTKLLEGDVkvIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 83 QTAD---TTFAYKVKEVValgryphqkgwlaseSQEDER-VIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEP 158
Cdd:cd03236 94 QYVDlipKAVKGKVGELL---------------KKKDERgKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1599980197 159 DLLLLDEPTNHLDISHQM---QLLDALKDWTRtrqlTVVAILHDL 200
Cdd:cd03236 159 DFYFFDEPSSYLDIKQRLnaaRLIRELAEDDN----YVLVVEHDL 199
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-217 |
3.18e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.89 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMav 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 lpqtadttfaykVKEVVALgrYPHQ--KGWLA--------SESQEDERV-----IREAMEQTDtwkfRnKPLQtLSGGER 145
Cdd:PRK11650 81 ------------VFQNYAL--YPHMsvRENMAyglkirgmPKAEIEERVaeaarILELEPLLD----R-KPRE-LSGGQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 146 QRALLARALCQEPDLLLLDEPTNHLD--ISHQMQLldALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGR 217
Cdd:PRK11650 141 QRVAMGRAIVREPAVFLFDEPLSNLDakLRVQMRL--EIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV 212
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-219 |
3.54e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.80 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLS--PSEGTITLQGKAIADYHSKELAQK-- 77
Cdd:COG0396 1 LEIKNLHVSVEGK-EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERARAgi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 78 -MAvlpqtadttFAYKVkEV----------VALGryphQKGWLASESQEDERVIREAMEQTD-TWKFRNKPL-QTLSGGE 144
Cdd:COG0396 80 fLA---------FQYPV-EIpgvsvsnflrTALN----ARRGEELSAREFLKLLKEKMKELGlDEDFLDRYVnEGFSGGE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 145 RQRALLARALCQEPDLLLLDEPTNHLDIshqmqllDALK------DWTRTRQLTVVAILHD---LNMasLYCDRVLLLNE 215
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLDI-------DALRivaegvNKLRSPDRGILIITHYqriLDY--IKPDFVHVLVD 216
|
....
gi 1599980197 216 GRMV 219
Cdd:COG0396 217 GRIV 220
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-227 |
3.68e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 79.24 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 22 SFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHS---KELAQKM------------------AV 80
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIqivfqnpygslnprkkvgQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 L--PQTADTTF-----AYKVKEVVAL--------GRYPHqkgwlasesqedervireaMeqtdtwkfrnkplqtLSGGER 145
Cdd:PRK11308 115 LeePLLINTSLsaaerREKALAMMAKvglrpehyDRYPH-------------------M---------------FSGGQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 146 QRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPR 225
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKE 240
|
..
gi 1599980197 226 QV 227
Cdd:PRK11308 241 QI 242
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-233 |
5.02e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.51 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 6 NVSVGYDEKTPI----IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLspsegtITLQGKAI-ADY----------H 70
Cdd:PRK13645 11 NVSYTYAKKTPFefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI------ISETGQTIvGDYaipanlkkikE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 71 SKELAQKMAVLPQTAD-TTFAYKVKEVVALGryPHQkgwLASESQEDERVIREAME--QTDTWKFRNKPLQtLSGGERQR 147
Cdd:PRK13645 85 VKRLRKEIGLVFQFPEyQLFQETIEKDIAFG--PVN---LGENKQEAYKKVPELLKlvQLPEDYVKRSPFE-LSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 148 ALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQV 227
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
....*.
gi 1599980197 228 MTEHQL 233
Cdd:PRK13645 239 FSNQEL 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-218 |
7.14e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 7.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 21 LSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE-LAQKMAVLPQTA-------DTTFAYK 92
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRqssglylDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 93 VKEVVAlgrypHQKGWLASESQEdeRVIREAMEQTDTWKFR--NKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHL 170
Cdd:PRK15439 362 VCALTH-----NRRGFWIKPARE--NAVLERYRRALNIKFNhaEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1599980197 171 DISHQMQLLDALKDWTRtRQLTVVAILHDLNMASLYCDRVLLLNEGRM 218
Cdd:PRK15439 435 DVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-231 |
7.89e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.15 E-value: 7.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVL 81
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQT----ADTTFAYkvkevVALGR-YPHQKGWLASESQEDERVIREAMEQTDTwkfrnkPL----QTLSGGERQRALLAR 152
Cdd:PRK10790 421 QQDpvvlADTFLAN-----VTLGRdISEEQVWQALETVQLAELARSLPDGLYT------PLgeqgNNLSVGQKQLLALAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 153 ALCQEPDLLLLDEPTNHLDISHQMQLLDALKdwTRTRQLTVVAILHDLNMAsLYCDRVLLLNEGRMVDLNSPRQVMTEH 231
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALA--AVREHTTLVVIAHRLSTI-VEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-219 |
9.47e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 9.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 18 IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQ-KMAVLPQTADTTFAYKVKEV 96
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlGIGIIYQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 97 VALGRYPHQKGWLASESQEDERVIREAM--EQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLdISH 174
Cdd:PRK09700 101 LYIGRHLTKKVCGVNIIDWREMRVRAAMmlLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL-TNK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1599980197 175 QMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:PRK09700 180 EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
16-218 |
9.99e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.66 E-value: 9.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 16 PIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE-LAQKMAVLPQ--TAD-TTFAY 91
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEdrKRDgLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 92 KVKE---VVALGRYPHQKGWL--ASESQEDERVIREAMEQTDTwkfRNKPLQTLSGGERQRALLARALCQEPDLLLLDEP 166
Cdd:PRK10762 346 SVKEnmsLTALRYFSRAGGSLkhADEQQAVSDFIRLFNIKTPS---MEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 167 TNHLDISHQ---MQLLDALKdwtrTRQLTVVAILHD----LNMAslycDRVLLLNEGRM 218
Cdd:PRK10762 423 TRGVDVGAKkeiYQLINQFK----AEGLSIILVSSEmpevLGMS----DRILVMHEGRI 473
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-233 |
1.87e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.82 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 22 SFQVHKGEIFGILGPNGSGKTTLLKAVSGLLsPS---EGTI-----TLQGKAIADYHSKELA---QKMAVLPQTAdttfa 90
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIifegeELQASNIRDTERAGIAiihQELALVKELS----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 91 ykVKEVVALGRYPHQKGWLasesqEDERVIREAMEQTDTWKFR---NKPLQTLSGGERQRALLARALCQEPDLLLLDEPT 167
Cdd:PRK13549 99 --VLENIFLGNEITPGGIM-----DYDAMYLRAQKLLAQLKLDinpATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1599980197 168 NHLDISHQMQLLDALKDwTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNsPRQVMTEHQL 233
Cdd:PRK13549 172 ASLTESETAVLLDIIRD-LKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTR-PAAGMTEDDI 235
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-231 |
1.95e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 78.78 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 18 IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLpqtadttfaykvkEVV 97
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI-------------ENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 98 ALgryphqKGWLASESQED-ERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQM 176
Cdd:PRK13545 107 EL------KGLMMGLTKEKiKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 177 QLLDALKDWtRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEH 231
Cdd:PRK13545 181 KCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHY 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-220 |
2.14e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 78.52 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 6 NVSVGYDEK-TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQT 84
Cdd:PRK11176 346 NVTFTYPGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 85 A----DT---TFAYKVKEvvalgRYphqkgwlaseSQEDervIREAMEQTDTWKFRNK---PLQT--------LSGGERQ 146
Cdd:PRK11176 426 VhlfnDTianNIAYARTE-----QY----------SREQ---IEEAARMAYAMDFINKmdnGLDTvigengvlLSGGQRQ 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 147 RALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRqlTVVAILHDLNMASlYCDRVLLLNEGRMVD 220
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIE-KADEILVVEDGEIVE 558
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-218 |
2.18e-15 |
|
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: 78.33 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVgYDEKTPIIQQL---SFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPS-EGTITLQGKAIADYH-SKELA 75
Cdd:TIGR02633 257 ILEARNLTC-WDVINPHRKRVddvSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 QKMAVLPQTADTTFAYKVKEV------VALGRYPhQKGWLASESQEDerVIREAMEQTDTWKFR-NKPLQTLSGGERQRA 148
Cdd:TIGR02633 336 AGIAMVPEDRKRHGIVPILGVgknitlSVLKSFC-FKMRIDAAAELQ--IIGSAIQRLKVKTASpFLPIGRLSGGNQQKA 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 149 LLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRtRQLTVVAILHDLNMASLYCDRVLLLNEGRM 218
Cdd:TIGR02633 413 VLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-166 |
3.58e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.57 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 16 PIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQ---KMAVLPQTADTTFAYK 92
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvrkRMSMLFQSGALFTDMN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 93 VKEVVAlgrYPhqkgwLASESQEDERVIREA-MEQTDTWKFRN----KPLQtLSGGERQRALLARALCQEPDLLLLDEP 166
Cdd:PRK11831 101 VFDNVA---YP-----LREHTQLPAPLLHSTvMMKLEAVGLRGaaklMPSE-LSGGMARRAALARAIALEPDLIMFDEP 170
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-228 |
4.12e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.00 E-value: 4.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 13 EKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPS--EGTITLQGKAIAdyhsKELAQKMAVLPQTaDTTFA 90
Cdd:PLN03211 80 ERT-ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT----KQILKRTGFVTQD-DILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 91 Y-KVKEV---VALGRYPH----QKGWLASESqederVIRE-AMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLL 161
Cdd:PLN03211 154 HlTVRETlvfCSLLRLPKsltkQEKILVAES-----VISElGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 162 LLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVM 228
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAM 295
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-250 |
6.69e-15 |
|
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: 77.75 E-value: 6.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 15 TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSkELAQKMAVLPQTADTTFAYKVK 94
Cdd:TIGR01257 1952 SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS-DVHQNMGYCPQFDAIDDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 95 EVVALgrYPHQKGwlaSESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISH 174
Cdd:TIGR01257 2031 EHLYL--YARLRG---VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1599980197 175 QMQLLDALKDWTRTRQlTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQLANVYETKIRRNEHPTIP 250
Cdd:TIGR01257 2106 RRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKDDLLP 2180
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-226 |
7.42e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.07 E-value: 7.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGY---DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELA-- 75
Cdd:PRK10535 4 LLELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 ---------QKMAVLPQtadTTFAYKVkEVVALgryphQKGWLASESQEDERVIREAMEQTDTWKFRnkPLQtLSGGERQ 146
Cdd:PRK10535 84 rrehfgfifQRYHLLSH---LTAAQNV-EVPAV-----YAGLERKQRLLRAQELLQRLGLEDRVEYQ--PSQ-LSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 147 RALLARALCQEPDLLLLDEPTNHLDiSHQ----MQLLDALKDwtrtRQLTVVAILHDLNMASlYCDRVLLLNEGRMVDlN 222
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALD-SHSgeevMAILHQLRD----RGHTVIIVTHDPQVAA-QAERVIEIRDGEIVR-N 224
|
....
gi 1599980197 223 SPRQ 226
Cdd:PRK10535 225 PPAQ 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-255 |
9.49e-15 |
|
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: 77.26 E-value: 9.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEK-TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSpSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:TIGR01271 1218 MDVQGLTAKYTEAgRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTADTTFAYKVKEVVALGRYPHQKGWLASEsqedERVIREAMEQ-TDTWKFRnkpLQ----TLSGGERQRALLARALC 155
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAE----EVGLKSVIEQfPDKLDFV---LVdggyVLSNGHKQLMCLARSIL 1369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 156 QEPDLLLLDEPTNHLD-ISHQMqLLDALKDwtRTRQLTVVAILHDLNmASLYCDRVLLLNEGRMVDLNSPRQVMTEHQL- 233
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDpVTLQI-IRKTLKQ--SFSNCTVILSEHRVE-ALLECQQFLVIEGSSVKQYDSIQKLLNETSLf 1445
|
250 260 270
....*....|....*....|....*....|.
gi 1599980197 234 ---------ANVYeTKIRRNEHPTIPRPLVT 255
Cdd:TIGR01271 1446 kqamsaadrLKLF-PLHRRNSSKRKPQPKIT 1475
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
4-198 |
9.72e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.45 E-value: 9.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 4 AQNVSVGYDE-KTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSpsegtiTLQGKAIADYHSKELAQKMAV-- 80
Cdd:COG2401 31 LEAFGVELRVvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK------GTPVAGCVDVPDNQFGREASLid 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 -LPQTADTTFAYKVKEVVALGryphqkgwlasesqedervireameqtDTWKFRNKPlQTLSGGERQRALLARALCQEPD 159
Cdd:COG2401 105 aIGRKGDFKDAVELLNAVGLS---------------------------DAVLWLRRF-KELSTGQKFRFRLALLLAERPK 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1599980197 160 LLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILH 198
Cdd:COG2401 157 LLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
30-219 |
9.77e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.30 E-value: 9.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 30 IFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE-LA---QKMAVLPQTADTTFAYKVK----------- 94
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIcLPpekRRIGYVFQDARLFPHYKVRgnlrygmaksm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 95 -----EVVA-------LGRYPHqkgwlasesqedervireameqtdtwkfrnkplqTLSGGERQRALLARALCQEPDLLL 162
Cdd:PRK11144 106 vaqfdKIVAllgieplLDRYPG----------------------------------SLSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 163 LDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMV 219
Cdd:PRK11144 152 MDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-218 |
1.06e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.12 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVgYDEKTP---IIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLL-SPSEGTITLQGKAIADYHSKE-LA 75
Cdd:PRK13549 259 ILEVRNLTA-WDPVNPhikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYpGRWEGEIFIDGKPVKIRNPQQaIA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 76 QKMAVLPQT-------------ADTTFAykvkevvALGRYphQKGWLASESQEdERVIREAMEqtdtwKFRNK------P 136
Cdd:PRK13549 338 QGIAMVPEDrkrdgivpvmgvgKNITLA-------ALDRF--TGGSRIDDAAE-LKTILESIQ-----RLKVKtaspelA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 137 LQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQM---QLLDALKDwtrtRQLTVVAILHDLNMASLYCDRVLLL 213
Cdd:PRK13549 403 IARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYeiyKLINQLVQ----QGVAIIVISSELPEVLGLSDRVLVM 478
|
....*
gi 1599980197 214 NEGRM 218
Cdd:PRK13549 479 HEGKL 483
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-227 |
1.07e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 76.38 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTpIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGL--LSPSEGTI-------------------- 59
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 60 --------TLQGKAI-----ADYHSKELAQKMAVLPQTadtTFA-YKVKEVVA-LGRYPHQKGWLASESqedervIREAM 124
Cdd:TIGR03269 80 epcpvcggTLEPEEVdfwnlSDKLRRRIRKRIAIMLQR---TFAlYGDDTVLDnVLEALEEIGYEGKEA------VGRAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 125 EQTDTWKFRNKPL---QTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLN 201
Cdd:TIGR03269 151 DLIEMVQLSHRIThiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*.
gi 1599980197 202 MASLYCDRVLLLNEGRMVDLNSPRQV 227
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-230 |
2.15e-14 |
|
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: 76.14 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTP-IIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQ 83
Cdd:TIGR00957 1288 RNYCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQ 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 84 -----------TADTTFAYKVKEVVALGRYPHQKGWLASESQEDERVIREAMEQtdtwkfrnkplqtLSGGERQRALLAR 152
Cdd:TIGR00957 1368 dpvlfsgslrmNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGEN-------------LSVGQRQLVCLAR 1434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 153 ALCQEPDLLLLDEPTNHLDISHQMQLLDALKdwTRTRQLTVVAILHDLNMASLYCdRVLLLNEGRMVDLNSPRQVMTE 230
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-250 |
3.77e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 74.48 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 18 IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPS--EGTITLQGKAIADYHSKELAQK-MAVLPQTADTTFAYKVK 94
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 95 EVVALGRYPHQKGWLASESQEDERViREAMEQTDTWKFRN-KPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDIS 173
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAYNAMYLRA-KNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEK 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 174 HQMQLLDALKDWTRtRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDlNSPRQVMTEHQLANVYETKIRRNEHPTIP 250
Cdd:TIGR02633 176 ETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHVA-TKDMSTMSEDDIITMMVGREITSLYPHEP 250
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-228 |
4.29e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.13 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 18 IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIA--DYHSKelAQKMAVLPQTADTTFAYKvKE 95
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYR--SQRIRMIFQDPSTSLNPR-QR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 96 VVALGRYPHQKGwLASESQEDERVIREAMEQTDTWK-FRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISH 174
Cdd:PRK15112 106 ISQILDFPLRLN-TDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 175 QMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVM 228
Cdd:PRK15112 185 RSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-226 |
4.37e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.70 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 28 GEIFGILGPNGSGKTTLLKAVSGLLSPS---EGTITLQGKAIadyHSKELAQKMAVLPQtaDTTF--AYKVKE---VVAL 99
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI---DAKEMRAISAYVQQ--DDLFipTLTVREhlmFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 100 GRYPHQkgwlASESQEDERViREAMEQTDTWKFRNKPLQT------LSGGERQRALLARALCQEPDLLLLDEPTNHLDIS 173
Cdd:TIGR00955 126 LRMPRR----VTKKEKRERV-DEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 174 HQMQLLDALKDWTrTRQLTVVAILHDLNmASLYC--DRVLLLNEGRMVDLNSPRQ 226
Cdd:TIGR00955 201 MAYSVVQVLKGLA-QKGKTIICTIHQPS-SELFElfDKIILMAEGRVAYLGSPDQ 253
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-210 |
5.95e-14 |
|
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: 69.91 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 25 VHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIAdyhskelaqkmaVLPQTADttfaykvkevvalgryph 104
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------YKPQYID------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 105 qkgwlasesqedervireameqtdtwkfrnkplqtLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKD 184
Cdd:cd03222 72 -----------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180
....*....|....*....|....*.
gi 1599980197 185 WTRTRQLTVVAILHDLNMASLYCDRV 210
Cdd:cd03222 117 LSEEGKKTALVVEHDLAVLDYLSDRI 142
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-237 |
6.24e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.00 E-value: 6.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSvgyDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQK-MA 79
Cdd:PRK10982 250 ILEVRNLT---SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHgFA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 80 VLPQTADTTFAYKVKEV------VALGRYPHQKGWLASES-QEDERVIREAME-QTDTWKfrnKPLQTLSGGERQRALLA 151
Cdd:PRK10982 327 LVTEERRSTGIYAYLDIgfnsliSNIRNYKNKVGLLDNSRmKSDTQWVIDSMRvKTPGHR---TQIGSLSGGNQQKVIIG 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 152 RALCQEPDLLLLDEPTNHLDIS-----HQMQLLDALKDWTrtrqltvvAILHDLNMASLY--CDRVLLLNEGRMVDLNSP 224
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGIDVGakfeiYQLIAELAKKDKG--------IIIISSEMPELLgiTDRILVMSNGLVAGIVDT 475
|
250
....*....|....*
gi 1599980197 225 RQVMTEH--QLANVY 237
Cdd:PRK10982 476 KTTTQNEilRLASLH 490
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-188 |
6.26e-14 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 74.51 E-value: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEktpIIQQLSFQVHKGEIFGILGPNGSGKTTLLK-----AVSGLlsPS-------------EGTITLQG 63
Cdd:PLN03073 180 MENFSISVGGRD---LIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGI--PKncqilhveqevvgDDTTALQC 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 64 KAIADYHSKELAQKMAVLPQtadttfayKVKEVVALGRYPHQKGWLASESQED---ERV--IREAMEQTD---------- 128
Cdd:PLN03073 255 VLNTDIERTQLLEEEAQLVA--------QQRELEFETETGKGKGANKDGVDKDavsQRLeeIYKRLELIDaytaearaas 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 129 -------TWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRT 188
Cdd:PLN03073 327 ilaglsfTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKT 393
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-232 |
1.30e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.35 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 18 IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAI---ADYHSKELAQKMAVLPQTA------DTT 88
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPyasldpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 89 FAYKVKEVVALGRYPHQKGWLASESQEDERVireAMEQTDTWKFRNKplqtLSGGERQRALLARALCQEPDLLLLDEPTN 168
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKAAAARVAWLLERV---GLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 169 HLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQ 232
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-220 |
1.36e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.84 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 25 VHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKE-LAQKMAVLPQTADTTFAYKVKEVVALGRYP 103
Cdd:PRK10982 21 VRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVLQRSVMDNMWLGRYP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 104 hQKGWLASESQ--EDERVIreaMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHL---DISHQMQL 178
Cdd:PRK10982 101 -TKGMFVDQDKmyRDTKAI---FDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtekEVNHLFTI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1599980197 179 LDALKDwtrtRQLTVVAILHDLNMASLYCDRVLLLNEGRMVD 220
Cdd:PRK10982 177 IRKLKE----RGCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-224 |
1.84e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.60 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 6 NVSVGYDEkTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMavlpqta 85
Cdd:PRK11000 8 NVTKAYGD-VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGM------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 86 dttfaykVKEVVALgrYPHQ----------KGWLASESQEDERVIREA-MEQTDTWKFRnKPlQTLSGGERQRALLARAL 154
Cdd:PRK11000 80 -------VFQSYAL--YPHLsvaenmsfglKLAGAKKEEINQRVNQVAeVLQLAHLLDR-KP-KALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 155 CQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSP 224
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-183 |
3.91e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.29 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEkTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGllSPS----EGTITLQGKAIADYHSKELAQ 76
Cdd:CHL00131 7 ILEIKNLHASVNE-NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 77 KMAVL--------PQTADTTF---AYKVKevvalgryphQKGWLASESQEDE--RVIRE-----AMEQTdtwkFRNKPL- 137
Cdd:CHL00131 84 LGIFLafqypieiPGVSNADFlrlAYNSK----------RKFQGLPELDPLEflEIINEklklvGMDPS----FLSRNVn 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1599980197 138 QTLSGGERQR-ALLARALCqEPDLLLLDEPTNHLDIshqmqllDALK 183
Cdd:CHL00131 150 EGFSGGEKKRnEILQMALL-DSELAILDETDSGLDI-------DALK 188
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-229 |
4.96e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 71.69 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGY-DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQ 83
Cdd:PLN03130 1241 EDVVLRYrPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQ 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 84 TAdTTFAYKVK-EVVALGRYPHQKGWLASESQEDERVIREAMEQTDTWKFRNKplQTLSGGERQRALLARALCQEPDLLL 162
Cdd:PLN03130 1321 AP-VLFSGTVRfNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAG--ENFSVGQRQLLSLARALLRRSKILV 1397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 163 LDEPTNHLDIShqmqlLDALKDWT---RTRQLTVVAILHDLNMAsLYCDRVLLLNEGRMVDLNSPRQVMT 229
Cdd:PLN03130 1398 LDEATAAVDVR-----TDALIQKTireEFKSCTMLIIAHRLNTI-IDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-218 |
6.55e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 71.04 E-value: 6.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 6 NVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAiadyhskelaqKMAVLPQTA 85
Cdd:PLN03073 513 DASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV-----------RMAVFSQHH 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 86 DTTFAYKVKEVVALGR----YPHQKgwlasesqedervIREAMEQTD-TWKFRNKPLQTLSGGERQRALLARALCQEPDL 160
Cdd:PLN03073 582 VDGLDLSSNPLLYMMRcfpgVPEQK-------------LRAHLGSFGvTGNLALQPMYTLSGGQKSRVAFAKITFKKPHI 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 161 LLLDEPTNHLDISHQMQLLDALKDWtrtrQLTVVAILHDLNMASLYCDRVLLLNEGRM 218
Cdd:PLN03073 649 LLLDEPSNHLDLDAVEALIQGLVLF----QGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-225 |
8.07e-13 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 70.60 E-value: 8.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 21 LSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAI----------------ADYHskeLAQKMAVLPQT 84
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtadnreayrqlfsavfSDFH---LFDRLLGLDGE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 85 ADTTFAYKvkevvalgryphqkgWLasesqedervirEAMEQTDTWKFRNKPLQT--LSGGERQR-ALLArALCQEPDLL 161
Cdd:COG4615 428 ADPARARE---------------LL------------ERLELDHKVSVEDGRFSTtdLSQGQRKRlALLV-ALLEDRPIL 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1599980197 162 LLDEPTnhldiSHQ---------MQLLDALKDwtrtRQLTVVAILHDLNMASLyCDRVLLLNEGRMVDLNSPR 225
Cdd:COG4615 480 VFDEWA-----ADQdpefrrvfyTELLPELKA----RGKTVIAISHDDRYFDL-ADRVLKMDYGKLVELTGPA 542
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-261 |
8.27e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.92 E-value: 8.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDeKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIAD-YHSKELAQKMAVLPQ 83
Cdd:NF033858 5 EGVSHRYG-KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADaRHRRAVCPRIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 84 tadttfaykvkevvALGR--YP----------------HQKgwlasesQEDERVIREAMEQTDTWKFRNKPLQTLSGGER 145
Cdd:NF033858 84 --------------GLGKnlYPtlsvfenldffgrlfgQDA-------AERRRRIDELLRATGLAPFADRPAGKLSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 146 QRALLARALCQEPDLLLLDEPTNHLD-ISHQM--QLLDALKdwTRTRQLTVVailhdlnMASLY------CDRVLLLNEG 216
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVDpLSRRQfwELIDRIR--AERPGMSVL-------VATAYmeeaerFDWLVAMDAG 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 217 RMVDLNSPRQVMTEHQLANVYETKI-------RRNEHPTI--PRPLVTFEPAAI 261
Cdd:NF033858 214 RVLATGTPAELLARTGADTLEAAFIallpeekRRGHQPVVipPRPADDDDEPAI 267
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-234 |
1.88e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 69.27 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 11 YDEKTPIIQQLSfqVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYhSKELAQKMA----------- 79
Cdd:PRK10938 14 SDTKTLQLPSLT--LNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRL-SFEQLQKLVsdewqrnntdm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 80 VLPQTADTtfAYKVKEVVALgryphqkgwlasESQEDERVIREAmEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPD 159
Cdd:PRK10938 91 LSPGEDDT--GRTTAEIIQD------------EVKDPARCEQLA-QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 160 LLLLDEPTNHLDISHQMQLLDALKDwTRTRQLTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTE---HQLA 234
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLAS-LHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQalvAQLA 232
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-230 |
2.80e-12 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 67.19 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGY-DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSpSEGTITLQGKAIADYHSKELAQKMAV 80
Cdd:cd03289 3 MTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQTADTTFAYKVKEVVALGRYPHQKGWLASESQEDERVIREAMEQTDTWKFRNKPLqtLSGGERQRALLARALCQEPDL 160
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCV--LSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 161 LLLDEPTNHLD-ISHQM---QLLDALKDwtrtrqLTVVAILHDLNmASLYCDRVLLLNEGRMVDLNSPRQVMTE 230
Cdd:cd03289 160 LLLDEPSAHLDpITYQVirkTLKQAFAD------CTVILSEHRIE-AMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
25-211 |
2.86e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 69.04 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 25 VHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGK-AIADYHSKELAQKMAVLPQTADTTFAYKVKEvvalgryp 103
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPALPQPALEYVIDGDREYRQLE-------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 104 hQKGWLASEsQEDERVIREAMEQTDT---WKFRNK-----------------PLQTLSGGERQRALLARALCQEPDLLLL 163
Cdd:PRK10636 96 -AQLHDANE-RNDGHAIATIHGKLDAidaWTIRSRaasllhglgfsneqlerPVSDFSGGWRMRLNLAQALICRSDLLLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1599980197 164 DEPTNHLDishqmqlLDA---LKDWTRTRQLTVVAILHDLNMASLYCDRVL 211
Cdd:PRK10636 174 DEPTNHLD-------LDAviwLEKWLKSYQGTLILISHDRDFLDPIVDKII 217
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-171 |
4.56e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.97 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIadyhSKELAqkmav 80
Cdd:PRK13540 1 MLDVIELDFDYHDQ-PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLC----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 lpqtadttfAYKvKEVVALGrypHQKG-----WLASESQEDERVIREAMEQTDTWK------FRNKPLQTLSGGERQRAL 149
Cdd:PRK13540 71 ---------TYQ-KQLCFVG---HRSGinpylTLRENCLYDIHFSPGAVGITELCRlfslehLIDYPCGLLSSGQKRQVA 137
|
170 180
....*....|....*....|..
gi 1599980197 150 LARALCQEPDLLLLDEPTNHLD 171
Cdd:PRK13540 138 LLRLWMSKAKLWLLDEPLVALD 159
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-230 |
7.41e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.47 E-value: 7.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDekTP-----IIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSeGTIT--------------- 60
Cdd:COG4170 3 LLDIRNLTIEID--TPqgrvkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN-WHVTadrfrwngidllkls 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 61 ------LQGKAIA----------DYHSKELAQKMAVLPqtaDTTFAykvkevvalGRYPHQKGWLASESQE--------D 116
Cdd:COG4170 80 prerrkIIGREIAmifqepssclDPSAKIGDQLIEAIP---SWTFK---------GKWWQRFKWRKKRAIEllhrvgikD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 117 ERVIREAMeqtdtwkfrnkPLQtLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAI 196
Cdd:COG4170 148 HKDIMNSY-----------PHE-LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLI 215
|
250 260 270
....*....|....*....|....*....|....
gi 1599980197 197 LHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTE 230
Cdd:COG4170 216 SHDLESISQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-229 |
7.88e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 66.36 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGY---DEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGL---------------------LSPSE 56
Cdd:PRK15093 3 LLDIRNLTIEFktsDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrvtadrmrfddidllrLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 57 ---------GTITLQGKAIADYHSKELAQKMAVLPqtadtTFAYKvkevvalGRYPHQKGWLASESQED-ERV----IRE 122
Cdd:PRK15093 83 rrklvghnvSMIFQEPQSCLDPSERVGRQLMQNIP-----GWTYK-------GRWWQRFGWRKRRAIELlHRVgikdHKD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 123 AMeqtdtwkfRNKPLQtLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHDLNM 202
Cdd:PRK15093 151 AM--------RSFPYE-LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQM 221
|
250 260
....*....|....*....|....*..
gi 1599980197 203 ASLYCDRVLLLNEGRMVDLNSPRQVMT 229
Cdd:PRK15093 222 LSQWADKINVLYCGQTVETAPSKELVT 248
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-170 |
2.01e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYdEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYhSKELAQKMAV 80
Cdd:PRK15439 11 LLCARSISKQY-SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL-TPAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 --LPQTADTTFAYKVKEVVALGRYPHQKgwlasESQEDERVIREAMEQTDTwkfrNKPLQTLSGGERQRALLARALCQEP 158
Cdd:PRK15439 89 ylVPQEPLLFPNLSVKENILFGLPKRQA-----SMQKMKQLLAALGCQLDL----DSSAGSLEVADRQIVEILRGLMRDS 159
|
170
....*....|..
gi 1599980197 159 DLLLLDEPTNHL 170
Cdd:PRK15439 160 RILILDEPTASL 171
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
5-232 |
3.30e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKTPII-QQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQ 83
Cdd:PTZ00243 1312 EGVQMRYREGLPLVlRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQ 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 84 TA---DTTFAYKV--------KEVVALGRYPHQKGWLASESQE-DERVIREAmeqtdtwkfrnkplQTLSGGERQRALLA 151
Cdd:PTZ00243 1392 DPvlfDGTVRQNVdpfleassAEVWAALELVGLRERVASESEGiDSRVLEGG--------------SNYSVGQRQLMCMA 1457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 152 RALCQE-PDLLLLDEPTNHLD--ISHQMQ--LLDALKDWtrtrqlTVVAILHDLNMASLYcDRVLLLNEGRMVDLNSPRQ 226
Cdd:PTZ00243 1458 RALLKKgSGFILMDEATANIDpaLDRQIQatVMSAFSAY------TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRE 1530
|
....*.
gi 1599980197 227 VMTEHQ 232
Cdd:PTZ00243 1531 LVMNRQ 1536
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-220 |
3.64e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.20 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 19 QQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLsPS---EGTITLQG-----KAIADyhSKELA-----QKMAVLPQTA 85
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfKDIRD--SEALGiviihQELALIPYLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 86 dttfaykVKEVVALGRYPHQKG---WlasesqedERVIREAMEQTDTWKFRNKPlQTLSG----GERQRALLARALCQEP 158
Cdd:NF040905 95 -------IAENIFLGNERAKRGvidW--------NETNRRARELLAKVGLDESP-DTLVTdigvGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 159 DLLLLDEPT---NHLDISHQMQLLDALKDwtrtRQLTVVAILHDLNMASLYCDRVLLLNEGRMVD 220
Cdd:NF040905 159 KLLILDEPTaalNEEDSAALLDLLLELKA----QGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-171 |
4.42e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.04 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 6 NVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSG-----------LLSPSEGTitlqGKAIAD------ 68
Cdd:PRK10938 265 NGVVSYNDR-PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRGS----GETIWDikkhig 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 69 YHSKELAQKMAVlpqtaDTTfaykVKEVV------ALGRYphqkgwlaseSQEDERVIREAMEQTD----TWKFRNKPLQ 138
Cdd:PRK10938 340 YVSSSLHLDYRV-----STS----VRNVIlsgffdSIGIY----------QAVSDRQQKLAQQWLDilgiDKRTADAPFH 400
|
170 180 190
....*....|....*....|....*....|...
gi 1599980197 139 TLSGGERQRALLARALCQEPDLLLLDEPTNHLD 171
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-183 |
1.43e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 61.35 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEKtPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGL--LSPSEGTITLQGKAIADYHSKELAQKM 78
Cdd:PRK09580 1 MLSIKDLHVSVEDK-AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 79 AVLpqtadtTFAYKVKEVVALGRYPHQKGWLASESQEDErvirEAMEQTDTWKFRNKPLQTL---------------SGG 143
Cdd:PRK09580 80 IFM------AFQYPVEIPGVSNQFFLQTALNAVRSYRGQ----EPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1599980197 144 ERQRALLARALCQEPDLLLLDEPTNHLDIshqmqllDALK 183
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDI-------DALK 182
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-216 |
3.99e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.69 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEKT--PIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGT-ITLQGKaiadyhskelaqkMAVL 81
Cdd:PLN03232 618 KNGYFSWDSKTskPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSsVVIRGS-------------VAYV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTAdTTFAYKVKEVVALG-RYPHQKGWlasesqedeRVIREAMEQTDTWKFRNKPLQ-------TLSGGERQRALLARA 153
Cdd:PLN03232 685 PQVS-WIFNATVRENILFGsDFESERYW---------RAIDVTALQHDLDLLPGRDLTeigergvNISGGQKQRVSMARA 754
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 154 LCQEPDLLLLDEPTNHLDISHQMQLLDA-LKDWTRTRqlTVVAILHDLNMASLYcDRVLLLNEG 216
Cdd:PLN03232 755 VYSNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGK--TRVLVTNQLHFLPLM-DRIILVSEG 815
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-172 |
5.37e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.09 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 1 MLDAQNVSVGYDEkTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIAdyhSKELAQKMAV 80
Cdd:PRK13543 11 LLAAHALAFSRNE-EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT---RGDRSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 81 LPQ----TADTTFAYKVKEVVAL-GRYPhqkgwlasesqedERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALC 155
Cdd:PRK13543 87 LGHlpglKADLSTLENLHFLCGLhGRRA-------------KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWL 153
|
170
....*....|....*..
gi 1599980197 156 QEPDLLLLDEPTNHLDI 172
Cdd:PRK13543 154 SPAPLWLLDEPYANLDL 170
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-221 |
7.47e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.14 E-value: 7.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 2 LDAQNVSVGYDEKTPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKaiadyhskelaqkmavl 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK----------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTADTTFAYK------VKEVVALGRYPHQKGWLASESQEDERVIREAME---QTDTWKFRNkpLQtLSGGERQRALLAR 152
Cdd:PRK10522 386 PVTAEQPEDYRklfsavFTDFHLFDQLLGPEGKPANPALVEKWLERLKMAhklELEDGRISN--LK-LSKGQKKRLALLL 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1599980197 153 ALCQEPDLLLLDEPTNHLD-----ISHQmQLLDALKDWTRtrqlTVVAILHD---LNMAslycDRVLLLNEGRMVDL 221
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDphfrrEFYQ-VLLPLLQEMGK----TIFAISHDdhyFIHA----DRLLEMRNGQLSEL 530
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-211 |
9.26e-10 |
|
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: 57.72 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 18 IQQLSFQVHKGEIFGILGPNGSGKTTLLKavsgllspsEGTITLQGKAIADYHSKELAQKMAVLPQtadttfaykVKEVV 97
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLISFLPKFSRNKLIFIDQ---------LQFLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 98 ALGRyphqkGWLASesqedervireameqtdtwkfrNKPLQTLSGGERQRALLARALCQEPD--LLLLDEPTNHLDISHQ 175
Cdd:cd03238 73 DVGL-----GYLTL----------------------GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125
|
170 180 190
....*....|....*....|....*....|....*...
gi 1599980197 176 MQLLDALKdwtRTRQL--TVVAILHDLNMASlYCDRVL 211
Cdd:cd03238 126 NQLLEVIK---GLIDLgnTVILIEHNLDVLS-SADWII 159
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-171 |
1.66e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.43 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEK--TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQ-GKAIADYHSKELAQKMAVL 81
Cdd:PTZ00265 386 KNVRFHYDTRkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVV 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 82 PQTA---------DTTFA-YKVKEVVALGRYPHQKGWLASESQEDERVIR--------------------------EAME 125
Cdd:PTZ00265 466 SQDPllfsnsiknNIKYSlYSLKDLEALSNYYNEDGNDSQENKNKRNSCRakcagdlndmsnttdsneliemrknyQTIK 545
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1599980197 126 QTDTWKFRNKPL--------------------QTLSGGERQRALLARALCQEPDLLLLDEPTNHLD 171
Cdd:PTZ00265 546 DSEVVDVSKKVLihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-232 |
2.50e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.90 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 18 IQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGK----AIADYHSKELAQ------KMAVLpqtadt 87
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvsviAISAGLSGQLTGieniefKMLCM------ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 88 tfAYKVKEVVALgryphqkgwlasesqedervIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPT 167
Cdd:PRK13546 114 --GFKRKEIKAM--------------------TPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 168 NHLDISHQMQLLDALKDWTRTRQlTVVAILHDLNMASLYCDRVLLLNEGRMVDLNSPRQVMTEHQ 232
Cdd:PRK13546 172 SVGDQTFAQKCLDKIYEFKEQNK-TIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYE 235
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-199 |
2.58e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.84 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 27 KGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTItlqgkaiadyhskelaqkmavlpqtadttfaykvkEVVALGRYPHQK 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-----------------------------------IYIDGEDILEEV 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 107 GWLASESQEDERVIreameqtdtwkfrnkplqTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLD-----A 181
Cdd:smart00382 46 LDQLLLIIVGGKKA------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrL 107
|
170
....*....|....*...
gi 1599980197 182 LKDWTRTRQLTVVAILHD 199
Cdd:smart00382 108 LLLLKSEKNLTVILTTND 125
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
30-199 |
4.86e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 56.08 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 30 IFGILGPNGSGKTTLLKAVS----GLLSPSegtitlqgkAIADYHSKELAQKMAVLPQtADTTFAYKVKEVVALGRYPHQ 105
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKyaltGELPPN---------SKGGAHDPKLIREGEVRAQ-VKLAFENANGKKYTITRSLAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 106 KGWLASESQEDERVIREAMeqtdtwkfrnkpLQTLSGGERQ------RALLARALCQEPDLLLLDEPTNHLDISH-QMQL 178
Cdd:cd03240 94 LENVIFCHQGESNWPLLDM------------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESL 161
|
170 180
....*....|....*....|.
gi 1599980197 179 LDALKDWTRTRQLTVVAILHD 199
Cdd:cd03240 162 AEIIEERKSQKNFQLIVITHD 182
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-174 |
7.36e-09 |
|
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: 58.42 E-value: 7.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 16 PIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGkaiadyhskelaqKMAVLPQTA----DTtfay 91
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAwiqnDS---- 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 92 kVKEVVALGRYPHQKGWLASESQEDERVIREAMEQTDTWKFRNKPLQtLSGGERQRALLARALCQEPDLLLLDEPTNHLD 171
Cdd:TIGR00957 715 -LRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
...
gi 1599980197 172 iSH 174
Cdd:TIGR00957 793 -AH 794
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-216 |
1.03e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 55.41 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 16 PIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSpsegtiTLQGKAiadYHSKELAQKMAVLPQTADTTFAykvke 95
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ------TLEGKV---HWSNKNESEPSFEATRSRNRYS----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 96 vVAlgrYPHQKGWLASESQEDE------------RVIREA---MEQTDTWKFRNkplQT--------LSGGERQRALLAR 152
Cdd:cd03290 81 -VA---YAAQKPWLLNATVEENitfgspfnkqryKAVTDAcslQPDIDLLPFGD---QTeigerginLSGGQRQRICVAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 153 ALCQEPDLLLLDEPTNHLDI---SHQMQ--LLDALKDWTRtrqlTVVAILHDLNMASlYCDRVLLLNEG 216
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIhlsDHLMQegILKFLQDDKR----TLVLVTHKLQYLP-HADWIIAMKDG 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-233 |
1.53e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 10 GYDEKTPIIQQLS---FQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADY---HSKE-----LAQKM 78
Cdd:PRK10762 9 GIDKAFPGVKALSgaaLNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpkSSQEagigiIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 79 AVLPQtadTTFAykvkEVVALGRYPHQK----GWLASESQEDERVIREAMeqtdtwKFRNK-PLQTLSGGERQRALLARA 153
Cdd:PRK10762 89 NLIPQ---LTIA----ENIFLGREFVNRfgriDWKKMYAEADKLLARLNL------RFSSDkLVGELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 154 LCQEPDLLLLDEPTnhldishqmqllDALKDwTRTRQL------------TVVAILHDLNMASLYCDRVLLLNEGRMVDl 221
Cdd:PRK10762 156 LSFESKVIIMDEPT------------DALTD-TETESLfrvirelksqgrGIVYISHRLKEIFEICDDVTVFRDGQFIA- 221
|
250
....*....|..
gi 1599980197 222 NSPRQVMTEHQL 233
Cdd:PRK10762 222 EREVADLTEDSL 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-293 |
1.96e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 16 PIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSP-SEGTITLQGKaiadyhskelaqkMAVLPQTAdTTFAYKVK 94
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGT-------------VAYVPQVS-WIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 95 EVVALGryphqkgwLASESQEDERVIREAMEQTDTWKFRNKPLQ-------TLSGGERQRALLARALCQEPDLLLLDEPT 167
Cdd:PLN03130 697 DNILFG--------SPFDPERYERAIDVTALQHDLDLLPGGDLTeigergvNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 168 NHLDISHQMQLLDA-LKDWTR--TRQLtVVAILHDLNmaslYCDRVLLLNEGrMV-------DL--NSP--RQVMTEH-Q 232
Cdd:PLN03130 769 SALDAHVGRQVFDKcIKDELRgkTRVL-VTNQLHFLS----QVDRIILVHEG-MIkeegtyeELsnNGPlfQKLMENAgK 842
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 233 LANVYETKIRRNEHPTIPRPLVTFEPAAIRSKPSSPISELEvfTSEQLIKV----TSSIRWKTLS 293
Cdd:PLN03130 843 MEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKE--GKSVLIKQeereTGVVSWKVLE 905
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-214 |
1.97e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.96 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 55 SEGTITLQGKAIADYHSKELAQKMAVLPQTAdTTFAYKVKEVVALGRyphqkgwlASESQED-ERVIREAMEQTDTWKFR 133
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNLFSIVSQEP-MLFNMSIYENIKFGK--------EDATREDvKRACKFAAIDEFIESLP 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 134 NK------PL-QTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQLTVVAILHdlNMASL- 205
Cdd:PTZ00265 1346 NKydtnvgPYgKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH--RIASIk 1423
|
....*....
gi 1599980197 206 YCDRVLLLN 214
Cdd:PTZ00265 1424 RSDKIVVFN 1432
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
33-185 |
6.60e-08 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 53.85 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 33 ILGPNGSGKTTLLKAVSGLLSPSEGTITL---------------QGKAIADY------HSKELAQKMAVLPQTADTTFAY 91
Cdd:COG3950 30 LVGENGSGKTTLLEAIALALSGLLSRLDDvkfrkllirngefgdSAKLILYYgtsrllLDGPLKKLERLKEEYFSRLDGY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 92 K--VKEVVALGRYphqKGWLAsESQED----------------ERVIREAMEQTDTWKFRNK--------------PLQT 139
Cdd:COG3950 110 DslLDEDSNLREF---LEWLR-EYLEDlenklsdeldekleavREALNKLLPDFKDIRIDRDpgrlvildkngeelPLNQ 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 140 LSGGERQR----ALLARALCQE-PDL---------LLLDEPTNHLDISHQMQLLDALKDW 185
Cdd:COG3950 186 LSDGERSLlalvGDLARRLAELnPALenplegegiVLIDEIDLHLHPKWQRRILPDLRKI 245
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-219 |
7.48e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 28 GEIFGILGPNGSGKTTLLKAVS----GLLSPSEGTITLQGKAIADYhSKELAQKMAVLPQTaDTTFAY-KVKEV---VAL 99
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAET-DVHFPHlTVGETldfAAR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 100 GRYPHQKGWLASESQEDERVIREAM-----EQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISH 174
Cdd:TIGR00956 165 CKTPQNRPDGVSREEYAKHIADVYMatyglSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 175 QMQLLDALKdwtrtrqlTVVAILHDLNMASLY-C--------DRVLLLNEGRMV 219
Cdd:TIGR00956 245 ALEFIRALK--------TSANILDTTPLVAIYqCsqdayelfDKVIVLYEGYQI 290
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
5-230 |
1.53e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 52.60 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 5 QNVSVGYDEK-TPIIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELAQKMAVLPQ 83
Cdd:cd03288 23 HDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 84 TAdTTFAYKVKevvaLGRYPHQKG-----WLASESQEDERVIREAMEQTDTwkFRNKPLQTLSGGERQRALLARALCQEP 158
Cdd:cd03288 103 DP-ILFSGSIR----FNLDPECKCtddrlWEALEIAQLKNMVKSLPGGLDA--VVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1599980197 159 DLLLLDEPTNHLDISH----QMQLLDALKDwtrtrqLTVVAILHDLNmASLYCDRVLLLNEGRMVDLNSPRQVMTE 230
Cdd:cd03288 176 SILIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVS-TILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
18-154 |
3.44e-07 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 50.73 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 18 IQQLSF-QVHKGEIFGILGPNGSGKTTLLKAVsgllspsegTITLQGKAIADYHSKELAQKMAVLPQTADTTFA------ 90
Cdd:cd03279 17 EQVIDFtGLDNNGLFLICGPTGAGKSTILDAI---------TYALYGKTPRYGRQENLRSVFAPGEDTAEVSFTfqlggk 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1599980197 91 -YKVKevvalgRYPHqkgwlasesQEDERVIREAM-EQTDTWKFRNKPLQTLSGGERQRALLARAL 154
Cdd:cd03279 88 kYRVE------RSRG---------LDYDQFTRIVLlPQGEFDRFLARPVSTLSGGETFLASLSLAL 138
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
25-216 |
8.87e-07 |
|
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: 49.16 E-value: 8.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 25 VHKGEIFGILGPNGSGKTTLLKAVSGLLSPS--EGTITLQGKAIADYHSKEL--AQKMAVLpqtadttfaykvkevvalg 100
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNFQRSTgyVEQQDVH------------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 101 ryphqkgwlasesqEDERVIREAMEqtdtwkFRNKpLQTLSGGERQRALLARALCQEPDLLLLDEPTNHLDISHQMQLLD 180
Cdd:cd03232 91 --------------SPNLTVREALR------FSAL-LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 1599980197 181 ALKDWTRTRQlTVVAILHDLNmASL--YCDRVLLLNEG 216
Cdd:cd03232 150 FLKKLADSGQ-AILCTIHQPS-ASIfeKFDRLLLLKRG 185
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
17-184 |
2.39e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.08 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 17 IIQQLS---FQVHKGE--------IFGILGPNGSGKTTLLKAVS-GLLSPSEGTITLQGKAIADYHSK-------ELAQK 77
Cdd:COG0419 1 KLLRLRlenFRSYRDTetidfddgLNLIVGPNGAGKSTILEAIRyALYGKARSRSKLRSDLINVGSEEasvelefEHGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 78 MAVL--PQTADTTFAYK--------VKEVVALGRYPHQKGWLASESQEDERVIREAMEQTDTWKFR------NKPLQTLS 141
Cdd:COG0419 81 RYRIerRQGEFAEFLEAkpserkeaLKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEIlaqlsgLDPIETLS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1599980197 142 GGERQRALLARALcqepdLLLLDepTNHLDISHQMQLLDALKD 184
Cdd:COG0419 161 GGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEE 196
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
136-200 |
2.82e-06 |
|
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: 48.76 E-value: 2.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1599980197 136 PLQTLSGGERQRALLARALcQEPD----LLLLDEPTNHL---DISHQMQLLDALKDwtrtRQLTVVAILHDL 200
Cdd:cd03271 166 PATTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLhfhDVKKLLEVLQRLVD----KGNTVVVIEHNL 232
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-184 |
2.85e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 49.75 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 17 IIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPSEGTITlqgkaiadyhsKELAQKMAVLPQtadttfaykvKEV 96
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLT-----------KPAKGKLFYVPQ----------RPY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 97 VALGRYPHQKGWLASESQEDERVIREA--------------MEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLL 162
Cdd:TIGR00954 526 MTLGTLRDQIIYPDSSEDMKRRGLSDKdleqildnvqlthiLEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180
....*....|....*....|..
gi 1599980197 163 LDEPTNHLDISHQMQLLDALKD 184
Cdd:TIGR00954 606 LDECTSAVSVDVEGYMYRLCRE 627
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-219 |
3.08e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 17 IIQQLSFQVHKGEIFGILGPNGSGKTTLLKAVSGllsPS-----EGTITLQGKAIaDYH--SKELAQKMA---------- 79
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG---RSygrniSGTVFKDGKEV-DVStvSDAIDAGLAyvtedrkgyg 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 80 -VLPQT--ADTTFAykvkevvALGRYPHqKGWLasesqEDERVIREAMEqtdtwkFRNK----------PLQTLSGGERQ 146
Cdd:NF040905 351 lNLIDDikRNITLA-------NLGKVSR-RGVI-----DENEEIKVAEE------YRKKmniktpsvfqKVGNLSGGNQQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 147 RALLARALCQEPDLLLLDEPTNHLDISHQM-------QLLDALKdwtrtrqlTVVAILHD----LNMaslyCDRVLLLNE 215
Cdd:NF040905 412 KVVLSKWLFTDPDVLILDEPTRGIDVGAKYeiytiinELAAEGK--------GVIVISSElpelLGM----CDRIYVMNE 479
|
....
gi 1599980197 216 GRMV 219
Cdd:NF040905 480 GRIT 483
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-206 |
4.53e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.58 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 26 HKGEIFGILGPNGSGKTTLLKAVSgllspsegtitlqgkaiadyhskelaqkmavlpqtadttfaykvkeVVALGRYPHq 105
Cdd:cd03227 19 GEGSLTIITGPNGSGKSTILDAIG----------------------------------------------LALGGAQSA- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 106 kgwLASESQEDERVIREAMEQTdtwkfRNKPLQTLSGGERQRA----LLARALCQEPDLLLLDEPTNHLDISHQMQLLDA 181
Cdd:cd03227 52 ---TRRRSGVKAGCIVAAVSAE-----LIFTRLQLSGGEKELSalalILALASLKPRPLYILDEIDRGLDPRDGQALAEA 123
|
170 180
....*....|....*....|....*
gi 1599980197 182 LKDwTRTRQLTVVAILHDLNMASLY 206
Cdd:cd03227 124 ILE-HLVKGAQVIVITHLPELAELA 147
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
18-184 |
9.59e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 47.69 E-value: 9.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 18 IQQLSFQVHKGeIFGILGPNGSGKTTLLKAVSGLLSPSEG---------------------TITLQ---GKAIADYHSKE 73
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSrkfdeedfylgddpdlpeieiELTFGsllSRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 74 LAQKMAVLPQTADTTFAYKVKEVVA-LGRYPHQKGWLASESQEDERVIREAMEQTDTWKFRNK---PLQTLSGGERQRAL 149
Cdd:COG3593 93 DKEELEEALEELNEELKEALKALNElLSEYLKELLDGLDLELELSLDELEDLLKSLSLRIEDGkelPLDRLGSGFQRLIL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1599980197 150 LA--RALCQ-----EPDLLLLDEPTNHLDISHQMQLLDALKD 184
Cdd:COG3593 173 LAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKE 214
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-200 |
1.11e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.09 E-value: 1.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1599980197 136 PLQTLSGGERQRALLARALCQE---PDLLLLDEPTNHL---DISHQMQLLDALKDwtrtRQLTVVAILHDL 200
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIKKLLEVLQRLVD----KGNTVVVIEHNL 892
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
139-200 |
1.55e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.71 E-value: 1.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1599980197 139 TLSGGERQRALLARALcQEPD----LLLLDEPTNHL---DISHqmqLLDALkdwtrtRQL-----TVVAILHDL 200
Cdd:COG0178 826 TLSGGEAQRVKLASEL-SKRStgktLYILDEPTTGLhfhDIRK---LLEVL------HRLvdkgnTVVVIEHNL 889
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-213 |
2.48e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 135 KPLQTLSGGERQRALLARAL---CQEPDLLLLDEPTNHLDISHQMQLLDALKDWTRTRQlTVVAILHDLNMASLyCDRVL 211
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH-TVVIIEHNMHVVKV-ADYVL 882
|
..
gi 1599980197 212 LL 213
Cdd:PRK00635 883 EL 884
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-287 |
1.04e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 134 NKPLQTLSGGERQRALLARALCQEPD--LLLLDEPTNHL---DISHQMQLLDALKDWTRtrqlTVVAILHDLNMASLyCD 208
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLhpqDTHKLINVIKKLRDQGN----TVLLVEHDEQMISL-AD 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 209 RVLLLNE------GRMVDLNSPRQ-VMTEHQLANVYetkiRRNEHpTIPRPlvtfepaAIRSKPSSPISeLEVFTSEQLI 281
Cdd:PRK00635 546 RIIDIGPgagifgGEVLFNGSPREfLAKSDSLTAKY----LRQEL-TIPIP-------EKRTNSLGTLT-LSKATKHNLK 612
|
....*.
gi 1599980197 282 KVTSSI 287
Cdd:PRK00635 613 DLTISL 618
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
18-171 |
1.37e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 18 IQQLSFQVHKGEIFG------------ILGPNGSGKTTLLKAVSGLLSPSEGTITLQGKAIADYHSKELaqkmavlpqta 85
Cdd:PRK13541 4 LHQLQFNIEQKNLFDlsitflpsaityIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1599980197 86 dTTFAYKVKEVVALGRYPHQKGWlaSESQEDERVIREAMEQTDTWKFRNKPLQTLSGGERQRALLARALCQEPDLLLLDE 165
Cdd:PRK13541 73 -TYIGHNLGLKLEMTVFENLKFW--SEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
....*.
gi 1599980197 166 PTNHLD 171
Cdd:PRK13541 150 VETNLS 155
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
22-55 |
6.98e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.96 E-value: 6.98e-04
10 20 30
....*....|....*....|....*....|....
gi 1599980197 22 SFQVHKGEIFGILGPNGSGKTTLLKAVSGLLSPS 55
Cdd:pfam13555 16 TIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPA 49
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
18-48 |
1.28e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.79 E-value: 1.28e-03
10 20 30
....*....|....*....|....*....|.
gi 1599980197 18 IQQLSFQVHKGeIFGILGPNGSGKTTLLKAV 48
Cdd:pfam13476 9 FRDQTIDFSKG-LTLITGPNGSGKTTILDAI 38
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
139-200 |
1.44e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 1.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1599980197 139 TLSGGERQRALLARALcQEPD----LLLLDEPTNHL---DISHQMQLLDALKDwtrtRQLTVVAILHDL 200
Cdd:PRK00349 830 TLSGGEAQRVKLAKEL-SKRStgktLYILDEPTTGLhfeDIRKLLEVLHRLVD----KGNTVVVIEHNL 893
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
30-53 |
1.64e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.45 E-value: 1.64e-03
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
139-202 |
2.33e-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: 39.55 E-value: 2.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1599980197 139 TLSGGERQRALLARALCQEPD--LLLLDEPTNHLDISHQMQLLDALKdwtRTRQL--TVVAILHDLNM 202
Cdd:cd03270 137 TLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLK---RLRDLgnTVLVVEHDEDT 201
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
140-184 |
4.05e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 39.37 E-value: 4.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 140 LSGGErQRALL-------ARALCQ---EPDLLLLDEPTNHLDISHQMQLLDALKD 184
Cdd:PRK00064 274 GSTGQ-QKLLLlalklaeAELLKEetgEAPILLLDDVASELDDGRRAALLERLKG 327
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
31-80 |
8.42e-03 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 37.96 E-value: 8.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1599980197 31 FGILGPNGSGKTTLLKAvsgLLSPSeGTITLQGK-----AIADYHSKELAQKMAV 80
Cdd:cd04170 2 IALVGHSGSGKTTLAEA---LLYAT-GAIDRLGRvedgnTVSDYDPEEKKRKMSI 52
|
|
| |
