|
Name |
Accession |
Description |
Interval |
E-value |
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-233 |
1.23e-127 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 361.33 E-value: 1.23e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAYVPQ 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSDIDWDFPITVLDVVLIGTYPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFF 160
Cdd:COG1121 83 RAEVDWDFPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446425376 161 LDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLIHYGEVRQVLEPTVMSKAY 233
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENLSRAY 235
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-218 |
4.71e-108 |
|
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: 310.62 E-value: 4.71e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAYVPQRSDIDW 86
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 87 DFPITVLDVVLIGTYPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFV 166
Cdd:cd03235 82 DFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446425376 167 GIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLIHYG 218
Cdd:cd03235 162 GVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-233 |
2.21e-81 |
|
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: 244.18 E-value: 2.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS-----VRKSVAYV 78
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlsrreLARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 79 PQRSDIDwdFPITVLDVVLIGTYPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEI 158
Cdd:COG1120 81 PQEPPAP--FGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446425376 159 FFLDEPFVGIDVTSEETIIKILREL-RKEGKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVLEPTVMSKAY 233
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDgRIVAQGPPEEVLTPELLEEVY 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-209 |
5.19e-67 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 205.55 E-value: 5.19e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 13 SYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQilgediRSVRKSVAYVPQRSDIDWDFPITV 92
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------RAGGARVAYVPQRSEVPDSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 93 LDVVLIGTYPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTS 172
Cdd:NF040873 75 RDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 446425376 173 EETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLL 209
Cdd:NF040873 155 RERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-225 |
2.34e-66 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 205.30 E-value: 2.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS----VRKSVAYVPQ 80
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARdpaeVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSDIDWDFpiTVLD-VVLIGtypslGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIF 159
Cdd:COG1131 81 EPALYPDL--TVREnLRFFA-----RLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVLE 225
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKgRIVADGTPDELKA 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-233 |
3.71e-66 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 206.27 E-value: 3.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIVKDLFVSYQ-GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR-SVRKS-VAY 77
Cdd:PRK15056 3 QQAGIVVNDVTVTWRnGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqALQKNlVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSDIDWDFPITVLDVVLIGTYPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAE 157
Cdd:PRK15056 83 VPQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 158 IFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLIHYGEVRQVLEPTVMSKAY 233
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLELAF 238
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
25-226 |
4.51e-65 |
|
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: 201.62 E-value: 4.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 25 FDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAYVPQRSDIDWDFPITVLDVVLIGTYPSL 104
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQRHEFAWDFPISVAHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 105 GMMKRPKKEhrDWAF--DCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRE 182
Cdd:TIGR03771 81 GWLRRPCVA--DFAAvrDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446425376 183 LRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLIHYGEVRQVLEP 226
Cdd:TIGR03771 159 LAGAGTAILMTTHDLAQAMATCDRVVLLNGRVIADGTPQQLQDP 202
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-218 |
2.05e-61 |
|
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: 190.72 E-value: 2.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS-----VRKSVAYVPQr 81
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlspkeLARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 82 sdidwdfpitvldvvligtypslgmmkrpkkehrdwafdCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFL 161
Cdd:cd03214 81 ---------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 162 DEPFVGIDVTSEETIIKILREL-RKEGKTIVVVHHDLSKAESYFDKLLLM-NKSLIHYG 218
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLkDGRIVAQG 180
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-225 |
9.27e-58 |
|
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: 183.30 E-value: 9.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQ-GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI-----RSVRKSVAYV 78
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItkknlRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 79 PQRSD--IdwdFPITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKA 156
Cdd:COG1122 81 FQNPDdqL---FAPTVEEDVAFG----PENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 157 EIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVLE 225
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDgRIVADGTPREVFS 223
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-205 |
1.72e-56 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 180.64 E-value: 1.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGN-QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI--------RSVRKS 74
Cdd:COG3638 2 MLELRNLSKRYPGGtPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalrgralRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 75 VAYVPQrsdidwDFPI----TVLDVVLIGTYPSLG----MMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRV 146
Cdd:COG3638 82 IGMIFQ------QFNLvprlSVLTNVLAGRLGRTStwrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 147 FLARALAQKAEIFFLDEPFVGIDVTSEETIIKILREL-RKEGKTIVVVHHDLSKAESYFD 205
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYAD 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-246 |
3.48e-55 |
|
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: 176.97 E-value: 3.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS----VRKSVAYVPQ 80
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKepreARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSDIdWDFpITVLDVVLIgtypsLGM-MKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIF 159
Cdd:COG4555 82 ERGL-YDR-LTVRENIRY-----FAElYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLM-NKSLIHYGEVRQVLEPTVMS---KAYVN 235
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILhKGKVVAQGSLDELREEIGEEnleDAFVA 234
|
250
....*....|.
gi 446425376 236 qgILFNNAAEV 246
Cdd:COG4555 235 --LIGSEEGEA 243
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-233 |
1.25e-54 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 176.07 E-value: 1.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVR-----KSVAYVP 79
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSpwelaRRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 QRSDIdwDFPITVLDVVLIGTYPSLgmmkRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAE-- 157
Cdd:COG4559 82 QHSSL--AFPFTVEEVVALGRAPHG----SSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQLWEpv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 158 -----IFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVLEPTVMSK 231
Cdd:COG4559 156 dggprWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQgRLVAQGTPEEVLTDELLER 235
|
..
gi 446425376 232 AY 233
Cdd:COG4559 236 VY 237
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-215 |
3.32e-54 |
|
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: 172.20 E-value: 3.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS----VRKSVAYVPQ 80
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKepeeVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSDIDWDFpiTVLDVVligtypslgmmkrpkkehrdwafdclkkvgmeefknrqigELSGGQQQRVFLARALAQKAEIFF 160
Cdd:cd03230 81 EPSLYENL--TVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 161 LDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLI 215
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-212 |
2.18e-53 |
|
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: 171.50 E-value: 2.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQG--NQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS-----VRKSVAYVP 79
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlslkeLRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 QRSDiDWDFPITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIF 159
Cdd:cd03225 82 QNPD-DQFFGPTVEEEVAFG----LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNK 212
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-233 |
6.26e-53 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 171.88 E-value: 6.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 3 EAIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVR-----KSVAY 77
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpaelaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSDIdwDFPITVLDVVLIGTYPslgmMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAE 157
Cdd:PRK13548 81 LPQHSSL--SFPFTVEEVVAMGRAP----HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 158 ------IFFLDEPFVGIDVTSEETIIKILREL-RKEGKTIVVVHHDLSKAESYFDKLLLMNKSLIH-YGEVRQVLEPTVM 229
Cdd:PRK13548 155 pdgpprWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVaDGTPAEVLTPETL 234
|
....
gi 446425376 230 SKAY 233
Cdd:PRK13548 235 RRVY 238
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-211 |
2.61e-51 |
|
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: 166.97 E-value: 2.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSY-QGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI--------RSVRKSV 75
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgkalRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 76 AYVPQrsdidwDFPI----TVLDVVLIGTYPSL----GMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVF 147
Cdd:cd03256 81 GMIFQ------QFNLierlSVLENVLSGRLGRRstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 148 LARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMN 211
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLK 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-223 |
4.10e-51 |
|
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: 165.77 E-value: 4.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV---RKSVAYVPQr 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVppeRRNIGMVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 82 sdiDWD-FP-ITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIF 159
Cdd:cd03259 80 ---DYAlFPhLTVAENIAFG----LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNKslihyGEVRQV 223
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNE-----GRIVQV 212
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-210 |
7.02e-51 |
|
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: 165.36 E-value: 7.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGN----QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS---------V 71
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekelaafR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 72 RKSVAYVPQrsdidwDF---P-ITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVF 147
Cdd:cd03255 81 RRHIGFVFQ------SFnllPdLTALENVELP----LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446425376 148 LARALAQKAEIFFLDEPFVGIDVTSEETIIKILREL-RKEGKTIVVVHHDLSKAEsYFDKLLLM 210
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELAE-YADRIIEL 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-220 |
1.84e-50 |
|
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: 164.92 E-value: 1.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI------RSVRKSVAYVPQ 80
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglpphEIARLGIGRTFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSDIdwdFP-ITVLDVVLIG------TYPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALA 153
Cdd:cd03219 83 IPRL---FPeLTVLENVMVAaqartgSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446425376 154 QKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMnksliHYGEV 220
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVL-----DQGRV 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-233 |
4.57e-50 |
|
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: 164.10 E-value: 4.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 3 EAIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVL-DLIPNDKGYVQILG-----EDIRSVRKSVA 76
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgDLPPTYGNDVRLFGerrggEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 77 YVpqRSDIDWDFP--ITVLDVVLIGTYPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQ 154
Cdd:COG1119 82 LV--SPALQLRFPrdETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 155 KAEIFFLDEPFVGIDVTSEETIIKILRELRKEG-KTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVLEPTVMSKA 232
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDgRVVAAGPKEEVLTSENLSEA 239
|
.
gi 446425376 233 Y 233
Cdd:COG1119 240 F 240
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-247 |
1.94e-49 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 162.88 E-value: 1.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI-----RSVRKSVAYVP 79
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsmlssRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 QRSDIdwdfP--ITVLDVVLIGTYPSL---GMMKRPKKEHRDWAfdcLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQ 154
Cdd:PRK11231 83 QHHLT----PegITVRELVAYGRSPWLslwGRLSAEDNARVNQA---MEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 155 KAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVLEPTVMSKay 233
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANgHVMAQGTPEEVMTPGLLRT-- 233
|
250
....*....|....
gi 446425376 234 vnqgiLFNNAAEVH 247
Cdd:PRK11231 234 -----VFDVEAEIH 242
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-212 |
8.70e-49 |
|
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: 159.94 E-value: 8.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQ----VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAYVPQ 80
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSDIdwdFP-ITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIF 159
Cdd:cd03293 81 QDAL---LPwLTVLDNVALG----LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446425376 160 FLDEPFVGID-VTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNK 212
Cdd:cd03293 154 LLDEPFSALDaLTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-200 |
2.21e-48 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 160.26 E-value: 2.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIVKDLFVSYQ----GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVA 76
Cdd:COG1116 4 AAPALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 77 YVPQRSDIdwdFP-ITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQK 155
Cdd:COG1116 84 VVFQEPAL---LPwLTVLDNVALG----LELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446425376 156 AEIFFLDEPFVGIDvtsEETIIK----ILRELRKEGKTIVVVHHDLSKA 200
Cdd:COG1116 157 PEVLLMDEPFGALD---ALTRERlqdeLLRLWQETGKTVLFVTHDVDEA 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
9.90e-48 |
|
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: 164.69 E-value: 9.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAII-VKDLFVSYQGN-----QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI------ 68
Cdd:COG1123 256 AAEPLLeVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtklsrr 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 69 --RSVRKSVAYVPQrsdidwD-----FP-ITVLDVVligTYP--SLGMMkrPKKEHRDWAFDCLKKVGM-EEFKNRQIGE 137
Cdd:COG1123 336 slRELRRRVQMVFQ------DpysslNPrMTVGDII---AEPlrLHGLL--SRAERRERVAELLERVGLpPDLADRYPHE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 138 LSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNK-SLI 215
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDgRIV 484
|
250
....*....|
gi 446425376 216 HYGEVRQVLE 225
Cdd:COG1123 485 EDGPTEEVFA 494
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-233 |
1.24e-47 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 157.94 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVR-----KSVAYVP 79
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPsrelaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 QRSDIdwDFPITVLDVVLIGTYP-SLGmmkRPKKEhrDWAF--DCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKA 156
Cdd:COG4604 82 QENHI--NSRLTVRELVAFGRFPySKG---RLTAE--DREIidEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 157 EIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLM-NKSLIHYGEVRQVLEPTVMSKAY 233
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMkDGRVVAQGTPEEIITPEVLSDIY 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
2.72e-47 |
|
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: 163.54 E-value: 2.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIVKDLFVSYQG--NQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPND---KGYVQILGEDIRSVR--- 72
Cdd:COG1123 1 MTPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSeal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 73 --KSVAYVPQRSDIDWDfPITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLAR 150
Cdd:COG1123 81 rgRRIGMVFQDPMTQLN-PVTVGDQIAEA----LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446425376 151 ALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVLE 225
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDgRIVEDGPPEEILA 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-233 |
3.20e-47 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 161.16 E-value: 3.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI-----RSVRKSVAYVP 79
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaRAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 QRSDIDWDFpiTVLDVVLIGTYPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIF 159
Cdd:PRK09536 84 QDTSLSFEF--DVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLIH-YGEVRQVLEPTVMSKAY 233
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRaAGPPADVLTADTLRAAF 236
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-212 |
1.47e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.82 E-value: 1.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV-----RKSVAYVPQR 81
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMpppewRRQVAYVPQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 82 SDIdwdFPITVLDVVLigtYPSLGMMKRPKKEH-RDWafdcLKKVGM-EEFKNRQIGELSGGQQQRVFLARALAQKAEIF 159
Cdd:COG4619 83 PAL---WGGTVRDNLP---FPFQLRERKFDRERaLEL----LERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNK 212
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-233 |
1.05e-45 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 152.84 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSY-QGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI--------RSVRKSV 75
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklrgkklRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 76 AYVPQRSD-IDwdfPITVLDVVLIG---TYPSL-GMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLAR 150
Cdd:TIGR02315 82 GMIFQHYNlIE---RLTVLENVLHGrlgYKPTWrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 151 ALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNKSLIHYGEVRQVLEPTVM 229
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVL 238
|
....
gi 446425376 230 SKAY 233
Cdd:TIGR02315 239 RHIY 242
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
16-233 |
1.47e-45 |
|
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: 153.05 E-value: 1.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 16 GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKS-----VAYVPQrsDIDWDFPI 90
Cdd:TIGR03873 13 GRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRararrVALVEQ--DSDTAVPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 91 TVLDVVLIGTYPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDV 170
Cdd:TIGR03873 91 TVRDVVALGRIPHRSLWAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446425376 171 TSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKS-LIHYGEVRQVLEPTVMSKAY 233
Cdd:TIGR03873 171 RAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGrVVAAGPPREVLTPALIRAVY 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-223 |
2.00e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 155.26 E-value: 2.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAII-VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV---RKSVA 76
Cdd:COG3842 1 MAMPALeLENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLppeKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 77 YVPQRSDIdwdFP-ITVLDVVligTYPsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQK 155
Cdd:COG3842 81 MVFQDYAL---FPhLTVAENV---AFG-LRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 156 AEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNKslihyGEVRQV 223
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMND-----GRIEQV 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
7-210 |
2.71e-45 |
|
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: 151.12 E-value: 2.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQG----NQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI--------RSVRKS 74
Cdd:cd03257 4 VKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsrrlrKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 75 VAYVPQrsdidwDfPITVLDVVL-IG-----TYPSLGMMKRPKKEhRDWAFDCLKKVGM-EEFKNRQIGELSGGQQQRVF 147
Cdd:cd03257 84 IQMVFQ------D-PMSSLNPRMtIGeqiaePLRIHGKLSKKEAR-KEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446425376 148 LARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLM 210
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVM 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-210 |
4.08e-45 |
|
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: 150.66 E-value: 4.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS------VRKSVAYVPQ 80
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlppherARAGIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSDIdwdFP-ITVLDVVLIGTYPSLgmmKRPKKEHRDWAFDC---LKkvgmeEFKNRQIGELSGGQQQRVFLARALAQKA 156
Cdd:cd03224 83 GRRI---FPeLTVEENLLLGAYARR---RAKRKARLERVYELfprLK-----ERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446425376 157 EIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLM 210
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVL 205
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-215 |
7.06e-45 |
|
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: 158.00 E-value: 7.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSY-QGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV-----RKSVAY 77
Cdd:COG4988 336 SIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLdpaswRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSDIdwdFPITVLDVVLIGtypslgmmkRPKKEhRDWAFDCLKKVGMEEFKNR-------QIGE----LSGGQQQRV 146
Cdd:COG4988 416 VPQNPYL---FAGTIRENLRLG---------RPDAS-DEELEAALEAAGLDEFVAAlpdgldtPLGEggrgLSGGQAQRL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 147 FLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKeGKTIVVVHHDLSKAESYfDKLLLMNKSLI 215
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQA-DRILVLDDGRI 549
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-218 |
1.61e-44 |
|
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: 148.58 E-value: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR-SVRKSVAYVPQRSDID 85
Cdd:cd03269 3 VENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiAARNRIGYLPEERGLY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 86 WDfpITVLDVVLigtYpsLGMMK-RPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEP 164
Cdd:cd03269 83 PK--MKVIDQLV---Y--LAQLKgLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 165 FVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKS-LIHYG 218
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGrAVLYG 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-223 |
4.86e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 150.26 E-value: 4.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI-RSVRKSVAYVP------ 79
Cdd:COG4152 4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLdPEDRRRIGYLPeergly 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 QRsdidwdfpITVLDVVLigtYpsLGMMK-RPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEI 158
Cdd:COG4152 84 PK--------MKVGEQLV---Y--LARLKgLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 159 FFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKS-LIHYGEVRQV 223
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGrKVLSGSVDEI 216
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-212 |
7.14e-44 |
|
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: 145.47 E-value: 7.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS-----VRKSVAYVPQr 81
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlpleeLRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 82 sdidwdfpitvldvvligtypslgmmkrpkkehrdwafdclkkvgmeefknrqigeLSGGQQQRVFLARALAQKAEIFFL 161
Cdd:cd00267 81 --------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446425376 162 DEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNK 212
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-228 |
7.71e-44 |
|
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: 147.82 E-value: 7.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAII-VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI--------RSV 71
Cdd:COG1127 1 MSEPMIeVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsekelYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 72 RKSVAYVPQRSDIdWDFpITVLDVVLigtYPsLGMMKR-PKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLAR 150
Cdd:COG1127 81 RRRIGMLFQGGAL-FDS-LTVFENVA---FP-LREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 151 ALAQKAEIFFLDEPFVGID-VTSEEtIIKILRELRKE-GKTIVVVHHDLSKAESYFDKL-LLMNKSLIHYG---EVRQVL 224
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDpITSAV-IDELIRELRDElGLTSVVVTHDLDSAFAIADRVaVLADGKIIAEGtpeELLASD 233
|
....
gi 446425376 225 EPTV 228
Cdd:COG1127 234 DPWV 237
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-210 |
2.68e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.96 E-value: 2.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIVKDLFVSYQ-GNQVVQ---NVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV----- 71
Cdd:COG1136 1 MSPLLELRNLTKSYGtGEGEVTalrGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLserel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 72 ----RKSVAYVPQrsdidwDF---P-ITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQ 143
Cdd:COG1136 81 arlrRRHIGFVFQ------FFnllPeLTALENVALP----LLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 144 QRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAeSYFDKLLLM 210
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELA-ARADRVIRL 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-223 |
3.59e-43 |
|
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: 145.79 E-value: 3.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAV---LDLIPN--DKGYVQILGEDIR-------SVRKS 74
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlNDLIPGapDEGEVLLDGKDIYdldvdvlELRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 75 VAYVPQRSDIdwdFPITVLDVVLIGtyPSLGMMKrPKKEHRDWAFDCLKKVGM-EEFKNRQIG-ELSGGQQQRVFLARAL 152
Cdd:cd03260 83 VGMVFQKPNP---FPGSIYDNVAYG--LRLHGIK-LKEELDERVEEALRKAALwDEVKDRLHAlGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446425376 153 AQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEgKTIVVVHHDLSKAESYFDKLLLMNKS-LIHYGEVRQV 223
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGrLVEFGPTEQI 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-226 |
4.12e-43 |
|
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: 146.29 E-value: 4.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 13 SYQGNQ-VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV-----RKSVAYVPQRSDIdw 86
Cdd:cd03295 9 RYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdpvelRRKIGYVIQQIGL-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 87 dFP-ITVLDVvlIGTYPSLGMMKRPKKEHRdwAFDCLKKVGME--EFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDE 163
Cdd:cd03295 87 -FPhMTVEEN--IALVPKLLKWPKEKIRER--ADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446425376 164 PFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNKslihyGEVRQVLEP 226
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKN-----GEIVQVGTP 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-215 |
6.99e-43 |
|
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: 144.59 E-value: 6.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGE-------DIRSVRKSVAY 77
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltddkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSDIdwdFP-ITVLDVVLIGTYPSLGMmkrPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKA 156
Cdd:cd03262 81 VFQQFNL---FPhLTVLENITLAPIKVKGM---SKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 157 EIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLI 215
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-200 |
1.17e-42 |
|
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: 144.74 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS------VRKSVAYVPQ 80
Cdd:COG0410 6 VENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlpphriARLGIGYVPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSDIdwdFP-ITVLDVVLIGTYPSLGmmKRPKKEHRDWAFDC---LKkvgmeEFKNRQIGELSGGQQQRVFLARALAQKA 156
Cdd:COG0410 86 GRRI---FPsLTVEENLLLGAYARRD--RAEVRADLERVYELfprLK-----ERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446425376 157 EIFFLDEPFVGI--DVTSEetIIKILRELRKEGKTIVVVHHDLSKA 200
Cdd:COG0410 156 KLLLLDEPSLGLapLIVEE--IFEIIRRLNREGVTILLVEQNARFA 199
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
7-198 |
1.47e-42 |
|
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: 145.18 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI------RSVRKSVAYVPQ 80
Cdd:COG0411 7 VRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglpphRIARLGIARTFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSDIdwdFP-ITVLDVVLIGTYPSLG-----------MMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFL 148
Cdd:COG0411 87 NPRL---FPeLTVLENVLVAAHARLGrgllaallrlpRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446425376 149 ARALAQKAEIFFLDEPFVGidVTSEET--IIKILRELRKE-GKTIVVVHHDLS 198
Cdd:COG0411 164 ARALATEPKLLLLDEPAAG--LNPEETeeLAELIRRLRDErGITILLIEHDMD 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-196 |
1.55e-42 |
|
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: 143.39 E-value: 1.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR----SVRKSVAYVPQ 80
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRdareDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSDIDWDFpiTVLDvvligtypSLGMMKR--PKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEI 158
Cdd:COG4133 83 ADGLKPEL--TVRE--------NLRFWAAlyGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 446425376 159 FFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHD 196
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-210 |
1.69e-42 |
|
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: 144.18 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI--------RSVRKSVA 76
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglseaelYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 77 YVPQRSDIdwdF-PITVLDVVligTYPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQK 155
Cdd:cd03261 81 MLFQSGAL---FdSLTVFENV---AFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446425376 156 AEIFFLDEPFVGID-VTSEEtIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLM 210
Cdd:cd03261 155 PELLLYDEPTAGLDpIASGV-IDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVL 210
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-212 |
5.16e-42 |
|
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: 140.98 E-value: 5.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGN--QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR-----SVRKSVAY 77
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRdldleSLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSDIdwdFPITVLDVVligtypslgmmkrpkkehrdwafdclkkvgmeefknrqigeLSGGQQQRVFLARALAQKAE 157
Cdd:cd03228 81 VPQDPFL---FSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 158 IFFLDEPFVGIDVTSEETIIKILRELRKeGKTIVVVHHDLSKAEsYFDKLLLMNK 212
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIR-DADRIIVLDD 169
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-198 |
1.99e-41 |
|
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: 149.98 E-value: 1.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQ--VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR-----SVRKSVA 76
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqidpaSLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 77 YVPQRSDIdwdFPITVLDVVLIGtYPSLGMmkrpkkehrDWAFDCLKKVGMEEFKNR-------QIGE----LSGGQQQR 145
Cdd:COG2274 553 VVLQDVFL---FSGTIRENITLG-DPDATD---------EEIIEAARLAGLHDFIEAlpmgydtVVGEggsnLSGGQRQR 619
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446425376 146 VFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKeGKTIVVVHHDLS 198
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLS 671
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-166 |
4.47e-41 |
|
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: 137.78 E-value: 4.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 20 VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI-----RSVRKSVAYVPQRsdiDWDFP-ITVL 93
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdderKSLRKEIGYVFQD---PQLFPrLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446425376 94 DVVLIGTYPsLGMMKRPKKEHRDWAfdcLKKVGMEEFKNR----QIGELSGGQQQRVFLARALAQKAEIFFLDEPFV 166
Cdd:pfam00005 78 ENLRLGLLL-KGLSKREKDARAEEA---LEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-210 |
1.13e-40 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 139.94 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSY----QGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI-----RSVRKS 74
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtrrrrKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 75 VAYVPQ--RSDIDwdfP-ITVLDVVLigtyPSLGMMKRPKKEHRDWAFdcLKKVGM-EEFKNRQIGELSGGQQQRVFLAR 150
Cdd:COG1124 81 VQMVFQdpYASLH---PrHTVDRILA----EPLRIHGLPDREERIAEL--LEQVGLpPSFLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446425376 151 ALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLM 210
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-211 |
2.09e-40 |
|
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: 2.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV-------RKSVAY 77
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedelpplRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSDIdwdFP-ITVLDVVLIGtypslgmmkrpkkehrdwafdclkkvgmeefknrqigeLSGGQQQRVFLARALAQKA 156
Cdd:cd03229 81 VFQDFAL---FPhLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 157 EIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMN 211
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-210 |
4.18e-40 |
|
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: 145.29 E-value: 4.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQ--VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR-----SVRKSVA 76
Cdd:COG4987 333 SLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdldedDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 77 YVPQRSDIdwdFPITVLDVVLIGtypslgmmkRPKKEHRD-WAfdCLKKVGMEEFKNRQ-------IGE----LSGGQQQ 144
Cdd:COG4987 413 VVPQRPHL---FDTTLRENLRLA---------RPDATDEElWA--ALERVGLGDWLAALpdgldtwLGEggrrLSGGERR 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 145 RVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKeGKTIVVVHHDLSKAEsYFDKLLLM 210
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLE-RMDRILVL 542
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-210 |
6.89e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 137.82 E-value: 6.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGE-------DIRSVRKSVAY 77
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEdltdskkDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSDIdwdFP-ITVLDVVLigtypsLGMM---KRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALA 153
Cdd:COG1126 82 VFQQFNL---FPhLTVLENVT------LAPIkvkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 154 QKAEIFFLDEPfvgidvTS--------EetIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLM 210
Cdd:COG1126 153 MEPKVMLFDEP------TSaldpelvgE--VLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFM 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-198 |
7.68e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 137.11 E-value: 7.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSY-QGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKS-VAY----- 77
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReIPYlrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 --VPQrsdidwDFPI----TVLDVVLIgtypSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARA 151
Cdd:COG2884 82 gvVFQ------DFRLlpdrTVYENVAL----PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446425376 152 LAQKAEIFFLDEPFVGID-VTSEEtIIKILRELRKEGKTIVVVHHDLS 198
Cdd:COG2884 152 LVNRPELLLADEPTGNLDpETSWE-IMELLEEINRRGTTVLIATHDLE 198
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-223 |
1.21e-39 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 139.90 E-value: 1.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI---RSVRKS-VAYVPQ 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLftnLPPRERrVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 rsdidwD---FP-ITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKA 156
Cdd:COG1118 83 ------HyalFPhMTVAENIAFG----LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 157 EIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNKslihyGEVRQV 223
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQ-----GRIEQV 215
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-228 |
7.55e-39 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 134.57 E-value: 7.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI------RSVRKSVAYVPQ 80
Cdd:TIGR03410 3 VSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItklpphERARAGIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSDIdwdFP-ITVLDVVLigtypsLGMMKRPKKEHR--DWAFDcLKKVgMEEFKNRQIGELSGGQQQRVFLARALAQKAE 157
Cdd:TIGR03410 83 GREI---FPrLTVEENLL------TGLAALPRRSRKipDEIYE-LFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446425376 158 IFFLDEPFVGIDVTSEETIIKILRELRKEGK-TIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVLEPTV 228
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERgRVVASGAGDELDEDKV 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-218 |
1.66e-38 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 133.40 E-value: 1.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQ--VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS----VRKSVAYV 78
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTdrkaARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 79 PQrSDIDWDFpITVLDVVLIgtYPSL-GMMKRPKKEHRDWAfdcLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAE 157
Cdd:cd03263 81 PQ-FDALFDE-LTVREHLRF--YARLkGLPKSEIKEEVELL---LRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446425376 158 IFFLDEPFVGIDVTSEETIIKILRELRKeGKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYG 218
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDgKLRCIG 214
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-201 |
2.26e-38 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 132.74 E-value: 2.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAYVPQRSDIDW 86
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 87 ---DFPI----TV---LDVVLIGTypslgmmKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKA 156
Cdd:TIGR03608 81 lfqNFALieneTVeenLDLGLKYK-------KLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446425376 157 EIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAE 201
Cdd:TIGR03608 154 PLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAK 198
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-215 |
2.68e-38 |
|
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: 132.88 E-value: 2.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI----RSVRKSVAYVPQ 80
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrepREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSDIDWDfpitvldvvLIGtYPSLGMMKR----PKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKA 156
Cdd:cd03265 81 DLSVDDE---------LTG-WENLYIHARlygvPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 157 EIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNKSLI 215
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-223 |
3.54e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 134.43 E-value: 3.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSY-QGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR-------SVRKSVAYV 78
Cdd:PRK13639 4 TRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkksllEVRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 79 PQRSDiDWDFPITVLDVVLIGTYPslgmMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEI 158
Cdd:PRK13639 84 FQNPD-DQLFAPTVEEDVAFGPLN----LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 159 FFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKS-LIHYGEVRQV 223
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGkIIKEGTPKEV 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-211 |
5.51e-38 |
|
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: 131.61 E-value: 5.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQ-VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI--RSVRKSVAYVPQRSD 83
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkaKERRKSIGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 iDWDFPITVLDVVLigtypsLGMMKRPKKEHRdwAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDE 163
Cdd:cd03226 82 -YQLFTDSVREELL------LGLKELDAGNEQ--AETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446425376 164 PFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMN 211
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
16-223 |
6.12e-38 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 134.45 E-value: 6.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 16 GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV-----RKSVAYVPQRSDIdwdFP- 89
Cdd:COG1125 14 GTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLdpvelRRRIGYVIQQIGL---FPh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 90 ITVLDVvlIGTYPSLgmMKRPKKEHRDWAFDCLKKVGM--EEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVG 167
Cdd:COG1125 91 MTVAEN--IATVPRL--LGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 168 ID-VTSE---ETIIKILRELrkeGKTIVVVHHDLSKAESYFDKLLLMNKslihyGEVRQV 223
Cdd:COG1125 167 LDpITREqlqDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMRE-----GRIVQY 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
16-225 |
7.37e-38 |
|
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: 132.46 E-value: 7.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 16 GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV---RKSVAYVPQRSDIdwdFP-IT 91
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLppeKRDISYVPQNYAL---FPhMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 92 VLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVT 171
Cdd:cd03299 88 VYKNIAYG----LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 172 SEETIIKILRELRKEGKTIVV-VHHDLSKAESYFDKL-LLMNKSLIHYGEVRQVLE 225
Cdd:cd03299 164 TKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVaIMLNGKLIQVGKPEEVFK 219
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-224 |
1.59e-37 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 132.58 E-value: 1.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGN-----QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKaVLD--LIPNdKGYVQILGEDI--------R 69
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQ-HLNglLKPT-SGTVTIDGRDItakkkkklK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 70 SVRKSVAYVPQrsdidwdFP------ITVLDVVLIGtyPSlgMMKRPKKEHRDWAFDCLKKVGM-EEFKNRQIGELSGGQ 142
Cdd:TIGR04521 79 DLRKKVGLVFQ-------FPehqlfeETVYKDIAFG--PK--NLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 143 QQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNKSLIHY-GEV 220
Cdd:TIGR04521 148 MRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLdGTP 227
|
....
gi 446425376 221 RQVL 224
Cdd:TIGR04521 228 REVF 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-210 |
1.85e-37 |
|
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: 137.42 E-value: 1.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQG-NQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR-----SVRKSVAY 77
Cdd:TIGR02857 321 SLEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdadadSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSDIdwdFPITVLDVVLIGT-YPSLGMMKRpkkehrdwafdCLKKVGMEEF-------KNRQIGE----LSGGQQQR 145
Cdd:TIGR02857 401 VPQHPFL---FAGTIAENIRLARpDASDAEIRE-----------ALERAGLDEFvaalpqgLDTPIGEggagLSGGQAQR 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 146 VFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRkEGKTIVVVHHDLSKAESYfDKLLLM 210
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-217 |
2.01e-37 |
|
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: 130.57 E-value: 2.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGN----QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI----RSVRKSVA 76
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVvkepAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 77 YVPQRSDI-DWdfpITVLDVVLIgtYPSLGMMKRPKKEHR-DWAFDCLkkvGMEEFKNRQIGELSGGQQQRVFLARALAQ 154
Cdd:cd03266 82 FVSDSTGLyDR---LTARENLEY--FAGLYGLKGDELTARlEELADRL---GMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446425376 155 KAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLIHY 217
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-217 |
2.31e-37 |
|
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: 130.39 E-value: 2.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGkLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS----VRKSVAYVPQ 80
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKqpqkLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 rsDIDWDFPITVLDVVligTYpsLGMMKR-PKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIF 159
Cdd:cd03264 80 --EFGVYPNFTVREFL---DY--IAWLKGiPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELrKEGKTIVVVHHDLSKAESYFDKLLLMNKSLIHY 217
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-200 |
2.79e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 131.31 E-value: 2.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAV---LDLIPNDK--GYVQILGEDIRS-------V 71
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIPGARveGEILLDGEDIYDpdvdvveL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 72 RKSVAYVPQRSDIdwdFPITVLDVVLIGtyPSLgMMKRPKKEHRDWAFDCLKKVGM-EEFKNR---QIGELSGGQQQRVF 147
Cdd:COG1117 91 RRRVGMVFQKPNP---FPKSIYDNVAYG--LRL-HGIKSKSELDEIVEESLRKAALwDEVKDRlkkSALGLSGGQQQRLC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446425376 148 LARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEgKTIVVVHHDLSKA 200
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQA 216
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-212 |
2.17e-36 |
|
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: 126.56 E-value: 2.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQ--VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV-----RKSVAY 77
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWdpnelGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRsdiDWDFPITVLDVVligtypslgmmkrpkkehrdwafdclkkvgmeefknrqigeLSGGQQQRVFLARALAQKAE 157
Cdd:cd03246 81 LPQD---DELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 158 IFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESyFDKLLLMNK 212
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLED 170
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-223 |
2.57e-36 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 131.35 E-value: 2.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEaIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI--RSVRK-SVAY 77
Cdd:COG3839 1 MAS-LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdLPPKDrNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSDIdwdFP-ITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKA 156
Cdd:COG3839 80 VFQSYAL---YPhMTVYENIAFP----LKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446425376 157 EIFFLDEPFVGID----VTSEETIIKILRELrkeGKTIVVVHHDLSKAESYFDKLLLMNKslihyGEVRQV 223
Cdd:COG3839 153 KVFLLDEPLSNLDaklrVEMRAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMND-----GRIQQV 215
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-225 |
3.36e-36 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 128.57 E-value: 3.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAV---LDLIPNDK--GYVQILGEDIRS-------V 71
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrmNDLVPGVRieGKVLFDGQDIYDkkidvveL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 72 RKSVAYVPQRSDidwDFPITVLDVVLIGtyPSLGMMKrPKKEHRDWAFDCLKKVGM-EEFKNR---QIGELSGGQQQRVF 147
Cdd:TIGR00972 81 RRRVGMVFQKPN---PFPMSIYDNIAYG--PRLHGIK-DKKELDEIVEESLKKAALwDEVKDRlhdSALGLSGGQQQRLC 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 148 LARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEgKTIVVVHHDLSKAESYFDKLLLM-NKSLIHYGEVRQVLE 225
Cdd:TIGR00972 155 IARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFyDGELVEYGPTEQIFT 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-217 |
4.88e-36 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 128.59 E-value: 4.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDK---GYVQILGE----------D 67
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRtvqregrlarD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 68 IRSVRKSVAYVPQRSDIDwdFPITVLDVVLIGTYPS-------LGMMKRPKKEHrdwAFDCLKKVGMEEFKNRQIGELSG 140
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLV--NRLSVLENVLIGALGStpfwrtcFSWFTREQKQR---ALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 141 GQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRK-EGKTIVVVHHDLSKAESYFDKLLLMNKSLIHY 217
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFY 233
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-215 |
7.95e-36 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 127.13 E-value: 7.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 13 SYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILG-------EDIRSVRKSVAYVPQRSDId 85
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpkVDERLIRQEAGMVFQQFYL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 86 wdFP-ITVLDVVLIGTYPSLGMmkrPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEP 164
Cdd:PRK09493 89 --FPhLTALENVMFGPLRVRGA---SKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446425376 165 FVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLI 215
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
1.44e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 127.54 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIVKDLFVSYQ-GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILG-----EDIRSVRKS 74
Cdd:PRK13647 1 MDNIIEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGrevnaENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 75 VAYVPQRSDiDWDFPITVLDVVLIGTYPslgmMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQ 154
Cdd:PRK13647 81 VGLVFQDPD-DQVFSSTVWDDVAFGPVN----MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 155 KAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKS-LIHYGEVRQVLEPTVMSKA 232
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGrVLAEGDKSLLTDEDIVEQA 234
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-212 |
2.87e-35 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 126.39 E-value: 2.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGN--QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS------VRKSVA 76
Cdd:TIGR04520 1 IEVENVSFSYPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDeenlweIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 77 YVPQRsdidwdfP------ITVLDVVLIGtyPSLGMMKRPKKEHR-DWAfdcLKKVGMEEFKNRQIGELSGGQQQRVFLA 149
Cdd:TIGR04520 81 MVFQN-------PdnqfvgATVEDDVAFG--LENLGVPREEMRKRvDEA---LKLVGMEDFRDREPHLLSGGQKQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446425376 150 RALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAEsYFDKLLLMNK 212
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAV-LADRVIVMNK 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-227 |
4.32e-35 |
|
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: 125.14 E-value: 4.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV---RKSVAYVPQ 80
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVpvqERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSDIdwdFP-ITVLDVVLIGtypsLGMMKR----PKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQK 155
Cdd:cd03296 82 HYAL---FRhMTVFDNVAFG----LRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446425376 156 AEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNKslihyGEVRQVLEPT 227
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNK-----GRIEQVGTPD 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-226 |
4.36e-35 |
|
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: 126.22 E-value: 4.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 20 VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV---------RKSVAYV-------PQRsd 83
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkelrelrRKKISMVfqsfallPHR-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 idwdfpiTVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDE 163
Cdd:cd03294 118 -------TVLENVAFG----LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446425376 164 PFVGIDVTseetiikILREL--------RKEGKTIVVVHHDLSKAESYFDKLLLMNKslihyGEVRQVLEP 226
Cdd:cd03294 187 AFSALDPL-------IRREMqdellrlqAELQKTIVFITHDLDEALRLGDRIAIMKD-----GRLVQVGTP 245
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-226 |
5.12e-35 |
|
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: 125.04 E-value: 5.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV---RKSVAYVPQR 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLpphKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 82 SDIdwdFP-ITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFF 160
Cdd:cd03300 81 YAL---FPhLTVFENIAFG----LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446425376 161 LDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNKslihyGEVRQVLEP 226
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNK-----GKIQQIGTP 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
10-233 |
6.23e-35 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 125.87 E-value: 6.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 10 LFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI-----RSVRKSVAYVPQRSDI 84
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyasKEVARRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 85 DWDfpITVLDVVLIGTYPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEP 164
Cdd:PRK10253 93 PGD--ITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446425376 165 FVGIDVTSEETIIKILREL-RKEGKTIVVVHHDLSKAESYFDKLL-LMNKSLIHYGEVRQVLEPTVMSKAY 233
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIaLREGKIVAQGAPKEIVTAELIERIY 241
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-198 |
1.47e-34 |
|
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: 125.94 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGN----QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPN---DKGYVQILGEDI--------RSV 71
Cdd:COG0444 4 VRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklsekelRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 72 R-KSVAYVPQrsDidwdfPITVLDVVL-IGTypSLGMM-----KRPKKEHRDWAFDCLKKVGM---EEFKNRQIGELSGG 141
Cdd:COG0444 84 RgREIQMIFQ--D-----PMTSLNPVMtVGD--QIAEPlrihgGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 142 QQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLS 198
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLG 212
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-216 |
2.34e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 124.36 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAII-VKDLFVSYQGNQ--VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILG-----EDIRSVR 72
Cdd:PRK13635 1 MKEEIIrVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 73 KSVAYVPQRSDIDWdFPITVLDVVLIGT----YPSLGMMKRPkkehrDWAfdcLKKVGMEEFKNRQIGELSGGQQQRVFL 148
Cdd:PRK13635 81 RQVGMVFQNPDNQF-VGATVQDDVAFGLenigVPREEMVERV-----DQA---LRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 149 ARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGK-TIVVVHHDLSKAESYfDKLLLMNKSLIH 216
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQA-DRVIVMNKGEIL 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-198 |
3.90e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 126.05 E-value: 3.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQ-VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR-----SVRKSVAY 77
Cdd:COG1132 339 EIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRdltleSLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSDIdwdFPITVLDVVLIGtypslgmmkRPkKEHRDWAFDCLKKVGMEEFKNR-------QIGE----LSGGQQQRV 146
Cdd:COG1132 419 VPQDTFL---FSGTIRENIRYG---------RP-DATDEEVEEAAKAAQAHEFIEAlpdgydtVVGErgvnLSGGQRQRI 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446425376 147 FLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKeGKTIVVVHHDLS 198
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLS 536
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
8-225 |
5.07e-33 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 126.13 E-value: 5.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 8 KDLFVSYQGNQ--VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS-----VRKSVAYVPQ 80
Cdd:TIGR03375 467 RNVSFAYPGQEtpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQidpadLRRNIGYVPQ 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 rsdidwdfpitvlDVVLIgtYPSLG---MMKRPKKEHRDwAFDCLKKVGMEEFKNR-------QIGE----LSGGQQQRV 146
Cdd:TIGR03375 547 -------------DPRLF--YGTLRdniALGAPYADDEE-ILRAAELAGVTEFVRRhpdgldmQIGErgrsLSGGQRQAV 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 147 FLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRkEGKTIVVVHHDLSkAESYFDKLLLMNKS-LIHYGEVRQVLE 225
Cdd:TIGR03375 611 ALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTS-LLDLVDRIIVMDNGrIVADGPKDQVLE 688
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-217 |
7.71e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 119.09 E-value: 7.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGnqvvQNVSFD--IEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKS---VAYVP 79
Cdd:COG3840 2 LRLDDLTYRYGD----FPLRFDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAerpVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 QRSDIdwdFP-ITVLDVVLIGTYPSLgmmkRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEI 158
Cdd:COG3840 78 QENNL---FPhLTVAQNIGLGLRPGL----KLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 159 FFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNKSLIHY 217
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAA 210
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-187 |
1.01e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 118.98 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI-------RSvRKSVAY 77
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkRA-RLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSDIDWDfpITVLDVVLIgtypSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAE 157
Cdd:COG1137 83 LPQEASIFRK--LTVEDNILA----VLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190
....*....|....*....|....*....|
gi 446425376 158 IFFLDEPFVGIDVTSEETIIKILRELRKEG 187
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKERG 186
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-224 |
1.39e-32 |
|
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: 118.45 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGN----QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI--------RSVR 72
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsgkelRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 73 KSVAYVPQRSDIDWDfpITVLDVVligTYPsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARAL 152
Cdd:cd03258 82 RRIGMIFQHFNLLSS--RTVFENV---ALP-LEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446425376 153 AQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVL 224
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKgEVVEEGTVEEVF 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-211 |
1.96e-32 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 118.68 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQilgediRSVRKSVAYVPQ 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSDIDWDFPITVldvvligtypSLGMMKRPKKEHRDwAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFF 160
Cdd:PRK09544 75 KLYLDTTLPLTV----------NRFLRLRPGTKKED-ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446425376 161 LDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMN 211
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLN 195
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-212 |
2.42e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 120.71 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI----RSVRKSVAYVP 79
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVparaRLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 QRSDIDWDFpiTVLDVVLI-GTYpsLGMMKRpkkEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEI 158
Cdd:PRK13536 121 QFDNLDLEF--TVRENLLVfGRY--FGMSTR---EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446425376 159 FFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNK 212
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEA 247
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-211 |
3.07e-32 |
|
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: 116.80 E-value: 3.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQ-----VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGedirsvrkSVAYVP 79
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------SIAYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 QRSdidWDFPITVLDVVLIGtypslgmmkrpKKEHRDWAFD-----CLKKvGMEEFKNR---QIGE----LSGGQQQRVF 147
Cdd:cd03250 73 QEP---WIQNGTIRENILFG-----------KPFDEERYEKvikacALEP-DLEILPDGdltEIGEkginLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 148 LARALAQKAEIFFLDEPFVGIDVTSEETII-KILRELRKEGKTIVVVHHDLSKAeSYFDKLLLMN 211
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLL-PHADQIVVLD 201
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-218 |
3.14e-32 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 117.81 E-value: 3.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKaVLDL--IPnDKGYVQILGE-----------DIRS 70
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLleTP-DSGQLNIAGHqfdfsqkpsekAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 71 VRKSVAYVPQRSDIdWdfP-ITVLDVVLIGTYPSLGMmkrPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLA 149
Cdd:COG4161 80 LRQKVGMVFQQYNL-W--PhLTVMENLIEAPCKVLGL---SKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446425376 150 RALAQKAEIFFLDEPFVGID--VTSEetIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKS-LIHYG 218
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDpeITAQ--VVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGrIIEQG 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-217 |
6.71e-32 |
|
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: 117.05 E-value: 6.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 14 YQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGED-----IRSVRKSVAYVPQRSDIDWDF 88
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrrKKFLRRIGVVFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 89 PitVLDvvligtypSLGMMKR----PKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEP 164
Cdd:cd03267 111 P--VID--------SFYLLAAiydlPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446425376 165 FVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNKSLIHY 217
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-226 |
8.86e-32 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 117.27 E-value: 8.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 3 EAIIVKDLFVSYQGN----QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR--SVRKSV- 75
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpGADRGVv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 76 ----AYVPqrsdidWdfpITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARA 151
Cdd:COG4525 82 fqkdALLP------W---LNVLDNVAFG----LRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 152 LAQKAEIFFLDEPFVGIDVTSEETIIKILREL-RKEGKTIVVVHHDLSKAesyfdklLLMNKSLI----HYGEVRQVLEP 226
Cdd:COG4525 149 LAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEA-------LFLATRLVvmspGPGRIVERLEL 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-212 |
1.08e-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: 115.39 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAYVPQRSDI 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 85 DWDFP-ITVLDVVLIGtypSLGMMKRPKKEHRdwafdCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDE 163
Cdd:cd03268 81 PGFYPnLTARENLRLL---ARLLGIRKKRIDE-----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446425376 164 PFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNK 212
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINK 201
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-212 |
1.67e-31 |
|
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: 115.79 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSY-QGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV-----RKSVAYV 78
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIsrkslRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 79 PQRsdiDWDFPITVLDVVLIGtypslgmmkRPKKEHRDWAfDCLKKVGMEEFKNR-------QIGE----LSGGQQQRVF 147
Cdd:cd03254 83 LQD---TFLFSGTIMENIRLG---------RPNATDEEVI-EAAKEAGAHDFIMKlpngydtVLGEnggnLSQGERQLLA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 148 LARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKeGKTIVVVHHDLSKAEsYFDKLLLMNK 212
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIK-NADKILVLDD 212
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-233 |
1.84e-31 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 116.09 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 20 VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNdKGYVQILGEDIRSVRKSV-----AYVPQRSDidwdfPITVLD 94
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAElarhrAYLSQQQS-----PPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 95 VvliGTYPSLGMMKRPKKEHRDWAFDCL-KKVGMEEFKNRQIGELSGGQQQRVFLARALAQ-------KAEIFFLDEPFV 166
Cdd:COG4138 86 V---FQYLALHQPAGASSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 167 GIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVLEPTVMSKAY 233
Cdd:COG4138 163 SLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQgKLVASGETAEVMTPENLSEVF 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-237 |
4.33e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 114.99 E-value: 4.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI------RSVRKSVAYV 78
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplhARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 79 PQRSDIdwdF-PITVLDVVLigtyPSLGMMKRPKKEHR-DWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKA 156
Cdd:PRK10895 84 PQEASI---FrRLSVYDNLM----AVLQIRDDLSAEQReDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 157 EIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVLEPTVMSKAYVN 235
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQgHLIAHGTPTEILQDEHVKRVYLG 236
|
..
gi 446425376 236 QG 237
Cdd:PRK10895 237 ED 238
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-223 |
6.72e-31 |
|
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: 113.50 E-value: 6.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVR---KSVAYVPQR 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpkdRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 82 SDIdwdFP-ITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFF 160
Cdd:cd03301 81 YAL---YPhMTVYDNIAFG----LKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446425376 161 LDEPFVGID----VTSEETIIKILRELrkeGKTIVVVHHDLSKAESYFDKLLLMNKslihyGEVRQV 223
Cdd:cd03301 154 MDEPLSNLDaklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMND-----GQIQQI 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
15-215 |
1.32e-30 |
|
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: 113.07 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 15 QGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS-----VRKSVAYVPQrsdidwdfp 89
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQldpadLRRNIGYVPQ--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 90 itvlDVVLI-GTYPSLGMMKRPkkEHRDWA-FDCLKKVGMEEFKNR-------QIGE----LSGGQQQRVFLARALAQKA 156
Cdd:cd03245 86 ----DVTLFyGTLRDNITLGAP--LADDERiLRAAELAGVTDFVNKhpngldlQIGErgrgLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 157 EIFFLDEPFVGIDVTSEETIIKILRELRkEGKTIVVVHHDLSkAESYFDKLLLMNKSLI 215
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-207 |
2.09e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 114.90 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAII-VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI----RSVRKSV 75
Cdd:PRK13537 3 MSVAPIdFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpsraRHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 76 AYVPQRSDIDWDFpiTVLDVVLI-GTYpsLGMmkrPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQ 154
Cdd:PRK13537 83 GVVPQFDNLDPDF--TVRENLLVfGRY--FGL---SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446425376 155 KAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKL 207
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRL 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-195 |
3.07e-30 |
|
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: 112.25 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI------RSVRKSVAYV 78
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItklpmhKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 79 PQRSDIDWDfpITVLDVVLIgtypSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEI 158
Cdd:cd03218 81 PQEASIFRK--LTVEENILA----VLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 446425376 159 FFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHH 195
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-215 |
3.70e-30 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 112.41 E-value: 3.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKaVLDL--IPnDKGYVQILGE-----------DIRS 70
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLleMP-RSGTLNIAGNhfdfsktpsdkAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 71 VRKSVAYVPQRSDIdWdfP-ITVLDVVLIGTYPSLGMMKRPKKEHrdwAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLA 149
Cdd:PRK11124 80 LRRNVGMVFQQYNL-W--PhLTVQQNLIEAPCRVLGLSKDQALAR---AEKLLERLRLKPYADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 150 RALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLI 215
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-225 |
3.85e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.16 E-value: 3.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQG--NQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILG-----EDIRSVRKSVA 76
Cdd:PRK13632 7 MIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 77 YVPQRSDIDWdFPITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKA 156
Cdd:PRK13632 87 IIFQNPDNQF-IGATVEDDIAFG----LENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446425376 157 EIFFLDEPFVGIDVTSEETIIKILRELRKEG-KTIVVVHHDLSKAeSYFDKLLLMNK-SLIHYGEVRQVLE 225
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEA-ILADKVIVFSEgKLIAQGKPKEILN 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-210 |
4.08e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 112.87 E-value: 4.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS-------VRKSVAYVP 79
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGpgaergvVFQNEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 QRSdidwdfpitVLDVVLIGTypSLGMMKRPKKEHRdwAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIF 159
Cdd:PRK11248 84 WRN---------VQDNVAFGL--QLAGVEKMQRLEI--AHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446425376 160 FLDEPFVGIDV-TSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLM 210
Cdd:PRK11248 151 LLDEPFGALDAfTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLL 202
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-215 |
5.21e-30 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 112.54 E-value: 5.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQI----------LGED---IRS 70
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarsLSQQkglIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 71 VRKSVAYVPQRSDIdwdFP-ITVLDVVLIGtypSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLA 149
Cdd:PRK11264 83 LRQHVGFVFQNFNL---FPhRTVLENIIEG---PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 150 RALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLI 215
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-197 |
6.57e-30 |
|
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: 116.69 E-value: 6.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQ-VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS-----VRKSVAYV 78
Cdd:TIGR02868 335 LELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSldqdeVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 79 PQRSDIdwdFPITVLDVVLIGtypslgmmkRPKKEHRDwAFDCLKKVGMEEFKNR-------QIGE----LSGGQQQRVF 147
Cdd:TIGR02868 415 AQDAHL---FDTTVRENLRLA---------RPDATDEE-LWAALERVGLADWLRAlpdgldtVLGEggarLSGGERQRLA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446425376 148 LARALAQKAEIFFLDEPFVGIDVTSEEtiiKILRELRK--EGKTIVVVHHDL 197
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETAD---ELLEDLLAalSGRTVVLITHHL 530
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-225 |
7.95e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 113.64 E-value: 7.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFV-SYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIrsVRKSVAYVP------ 79
Cdd:COG4586 24 LKGLFRrEYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVP--FKRRKEFARrigvvf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 -QRSDIDWDFPitVLDvvligtypSLGMMKR----PKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQ 154
Cdd:COG4586 102 gQRSQLWWDLP--AID--------SFRLLKAiyriPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLH 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446425376 155 KAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVLE 225
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHgRIIYDGSLEELKE 244
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-225 |
9.02e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 112.62 E-value: 9.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 22 NVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI---------RSVRKSVAYVPQRSDIDWdFPITV 92
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgnknlKKLRKKVSLVFQFPEAQL-FENTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 93 LDVVLIGTYpSLGMmkrPKKEHRDWAFDCLKKVGM-EEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVT 171
Cdd:PRK13641 104 LKDVEFGPK-NFGF---SEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 172 SEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKS-LIHYGEVRQVLE 225
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGkLIKHASPKEIFS 234
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-239 |
1.01e-29 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 111.80 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 6 IVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYV----QILGE-DIRSVRKSVAYVPQ 80
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaQPLESwSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RsdidwdFP----ITVLDVVLIGTYPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKA 156
Cdd:PRK10575 93 Q------LPaaegMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 157 EIFFLDEPFVGIDVTSEETIIKILREL-RKEGKTIVVVHHDLSKAESYFDKLL-LMNKSLIHYGEVRQVLEPTVMSKAY- 233
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVaLRGGEMIAQGTPAELMRGETLEQIYg 246
|
....*.
gi 446425376 234 VNQGIL 239
Cdd:PRK10575 247 IPMGIL 252
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
13-210 |
1.17e-29 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 110.42 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 13 SYQGN-QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGED--------IRSVRKSVAYVPQrsd 83
Cdd:TIGR02673 10 AYPGGvAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDvnrlrgrqLPLLRRRIGVVFQ--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 idwDFPI----TVLDVVLIgtypSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIF 159
Cdd:TIGR02673 87 ---DFRLlpdrTVYENVAL----PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLM 210
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIIL 210
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-225 |
1.23e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 111.47 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKA---VLDLIPNDK--GYVQILGEDIRS----- 70
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEARveGEVRLFGRNIYSpdvdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 71 --VRKSVAYVPQRSDidwDFP-ITVLDVVLIGTypSLGMMKRPKKE---HRDWAfdcLKKVGM-EEFKNR---QIGELSG 140
Cdd:PRK14267 81 ieVRREVGMVFQYPN---PFPhLTIYDNVAIGV--KLNGLVKSKKEldeRVEWA---LKKAALwDEVKDRlndYPSNLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 141 GQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEgKTIVVVHHDLSKAESYFD--KLLLMNKsLIHYG 218
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDyvAFLYLGK-LIEVG 230
|
....*..
gi 446425376 219 EVRQVLE 225
Cdd:PRK14267 231 PTRKVFE 237
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-218 |
1.54e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 110.08 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 22 NVSFDIEkGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAYVPQRSDIDWDFP----ITVLDVVL 97
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQqyalFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 98 IGTYpslGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETII 177
Cdd:cd03297 95 NLAF---GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446425376 178 KILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYG 218
Cdd:cd03297 172 PELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDgRLQYIG 214
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-198 |
1.64e-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: 110.78 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQ-GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR-----SVRKSVAYV 78
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRevtldSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 79 PQRSDIdwdFPITVLDVVLIGTyPSLG---MMKRPKKEHRDwafdcLKKVGMEEFKNRQIGE----LSGGQQQRVFLARA 151
Cdd:cd03253 81 PQDTVL---FNDTIGYNIRYGR-PDATdeeVIEAAKAAQIH-----DKIMRFPDGYDTIVGErglkLSGGEKQRVAIARA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446425376 152 LAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKeGKTIVVVHHDLS 198
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLS 197
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-227 |
2.49e-29 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 112.82 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIrsvrksVAYVPQ 80
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI------TRLPPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSD--IDWD----FP-ITVLDVVLIGTYPSlgmmKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALA 153
Cdd:TIGR03265 75 KRDygIVFQsyalFPnLTVADNIAYGLKNR----GMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 154 QKAEIFFLDEPFVGIDVTSEETIIKILREL-RKEGKTIVVVHHDLSKAESYFDKLLLMNKslihyGEVRQVLEPT 227
Cdd:TIGR03265 151 TSPGLLLLDEPLSALDARVREHLRTEIRQLqRRLGVTTIMVTHDQEEALSMADRIVVMNH-----GVIEQVGTPQ 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-217 |
6.36e-29 |
|
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: 108.90 E-value: 6.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDK---GYVQILGE--DIRSVRKSVAYVPQrSDIDWDFpITV 92
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQprKPDQFQKCVAYVRQ-DDILLPG-LTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 93 LDVVligTYPSLGMMKRPKKEHRD---WAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGID 169
Cdd:cd03234 99 RETL---TYTAILRLPRKSSDAIRkkrVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446425376 170 VTSEETIIKILRELRKEGKTIVV-VHHDLSKAESYFDKLLLMNKSLIHY 217
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEIVY 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
13-215 |
8.31e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 111.96 E-value: 8.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 13 SYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV---RKSVAYVPQRSDIdwdFP 89
Cdd:PRK09452 23 SFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaeNRHVNTVFQSYAL---FP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 90 -ITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGI 168
Cdd:PRK09452 100 hMTVFENVAFG----LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446425376 169 DVTSEETIIKILREL-RKEGKTIVVVHHDLSKAESYFDKLLLMNKSLI 215
Cdd:PRK09452 176 DYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-225 |
1.53e-28 |
|
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: 112.92 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQ--VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRK-----SVAY 77
Cdd:COG4618 331 LSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDReelgrHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSDIdwdFPITVLDVVligtypslGMMKRPKKEHrdwAFDCLKKVGMEEFKNR-------QIGE----LSGGQQQRV 146
Cdd:COG4618 411 LPQDVEL---FDGTIAENI--------ARFGDADPEK---VVAAAKLAGVHEMILRlpdgydtRIGEggarLSGGQRQRI 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 147 FLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSkAESYFDKLLLMNKSLI-HYGEVRQVLE 225
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVqAFGPRDEVLA 555
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-201 |
2.57e-28 |
|
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: 107.52 E-value: 2.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGN----QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMK--AVLDLIpnDKGYVQILGEDIRSV------ 71
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGllAGLDRP--TSGTVRLAGQDLFALdedara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 72 ---RKSVAYVPQrsdidwDFPI----TVLDVVLIgtyP-SLGMMKRPKKEHRDWafdcLKKVGMEEFKNRQIGELSGGQQ 143
Cdd:COG4181 86 rlrARHVGFVFQ------SFQLlptlTALENVML---PlELAGRRDARARARAL----LERVGLGHRLDHYPAQLSGGEQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 144 QRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAE 201
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAA 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-215 |
2.60e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 110.19 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI--RSVR-KSVAYVPQR 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQqRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 82 SDIdwdFP-ITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFF 160
Cdd:PRK11432 87 YAL---FPhMSLGENVGYG----LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 161 LDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNKSLI 215
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-197 |
2.77e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.65 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 6 IVKdlfvSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGE--DIRSVRKS----VAYVP 79
Cdd:COG1129 10 ISK----SFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvRFRSPRDAqaagIAIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 QRSDIdwdFP-ITVLDVVLIGTYP-SLGMMKRpkKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAE 157
Cdd:COG1129 86 QELNL---VPnLSVAENIFLGREPrRGGLIDW--RAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446425376 158 IFFLDEPfvgidvTS----EETII--KILRELRKEGKTIVVVHHDL 197
Cdd:COG1129 161 VLILDEP------TAslteREVERlfRIIRRLKAQGVAIIYISHRL 200
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-215 |
4.48e-28 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 107.58 E-value: 4.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 3 EAIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDL-IPnDKGYVQILGEDIRSV---------- 71
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLeTP-DSGEIRVGGEEIRLKpdrdgelvpa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 72 -RKSVAYVpqRSDIDWDFP-------ITVLDVVLIGtyPsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQ 143
Cdd:COG4598 86 dRRQLQRI--RTRLGMVFQsfnlwshMTVLENVIEA--P-VHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446425376 144 QRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLI 215
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
18-226 |
5.71e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.02 E-value: 5.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVR---KSVAYVPQRSDIdwdFP-ITVL 93
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHardRKVGFVFQHYAL---FRhMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 94 DVVLIGtypsLGMM---KRP-KKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGID 169
Cdd:PRK10851 93 DNIAFG----LTVLprrERPnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 170 VTSEETIIKILRELRKEGK-TIVVVHHDLSKAESYFDKLLLMNKslihyGEVRQVLEP 226
Cdd:PRK10851 169 AQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQ-----GNIEQAGTP 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-215 |
8.49e-28 |
|
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: 106.16 E-value: 8.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQG--NQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMkavlDLIPN----DKGYVQILGEDIR-----SVRK 73
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLV----NLIPRfydvDSGRILIDGHDVRdytlaSLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 74 SVAYVPQRSDIdwdFPITVLDVVLIGTypslgmmkrpKKEHRDWAFDCLKKVGMEEFKNR-------QIGE----LSGGQ 142
Cdd:cd03251 77 QIGLVSQDVFL---FNDTVAENIAYGR----------PGATREEVEEAARAANAHEFIMElpegydtVIGErgvkLSGGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446425376 143 QQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKeGKTIVVVHHDLSKAESYfDKLLLMNKSLI 215
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIENA-DRIVVLEDGKI 214
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-218 |
2.76e-27 |
|
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: 104.50 E-value: 2.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQ--VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV-----RKSVAY 77
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIglhdlRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQ---------RSDIDwdfpitvldvvligtypslgmmkrPKKEHRDWA-FDCLKKVGMEEFKNRQIGEL--------- 138
Cdd:cd03244 83 IPQdpvlfsgtiRSNLD------------------------PFGEYSDEElWQALERVGLKEFVESLPGGLdtvveegge 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 139 --SGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKeGKTIVVVHHDLSKAESYfDKLLLMNK-SLI 215
Cdd:cd03244 139 nlSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK-DCTVLTIAHRLDTIIDS-DRILVLDKgRVV 216
|
...
gi 446425376 216 HYG 218
Cdd:cd03244 217 EFD 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-218 |
2.77e-27 |
|
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: 103.78 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPN--DKGYVQILG--EDIRSVRKSVAYVPQRsdidwdfpitvl 93
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGrpLDKRSFRKIIGYVPQD------------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 94 DVVligtYPSLGMmkrpkKEHRDWAfDCLKKvgmeefknrqigeLSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSE 173
Cdd:cd03213 91 DIL----HPTLTV-----RETLMFA-AKLRG-------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446425376 174 ETIIKILRELRKEGKTIVVVHHDLS-KAESYFDKLLLMNK-SLIHYG 218
Cdd:cd03213 148 LQVMSLLRRLADTGRTIICSIHQPSsEIFELFDKLLLLSQgRVIYFG 194
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-224 |
3.07e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 106.70 E-value: 3.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGN----QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI--------RSVR 72
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalserelRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 73 KSVAYVPQ-------RsdidwdfpiTVLDVVLigtYPsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQR 145
Cdd:COG1135 82 RKIGMIFQhfnllssR---------TVAENVA---LP-LEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 146 VFLARALAQKAEIFFLDEPfvgidvTS----EET--IIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNKS-LIHY 217
Cdd:COG1135 149 VGIARALANNPKVLLCDEA------TSaldpETTrsILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGrIVEQ 222
|
....*..
gi 446425376 218 GEVRQVL 224
Cdd:COG1135 223 GPVLDVF 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-226 |
3.23e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 105.24 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAII-VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVL---DLIPN--DKGYVQILGEDIRS---- 70
Cdd:PRK14239 1 MTEPILqVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNPEvtITGSIVYNGHNIYSprtd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 71 ---VRKSVAYVPQRSDidwDFPITVLDVVLIGtypsLGMMKRPKKEHRDWAFD-CLKKVGM-EEFKNR----QIGeLSGG 141
Cdd:PRK14239 81 tvdLRKEIGMVFQQPN---PFPMSIYENVVYG----LRLKGIKDKQVLDEAVEkSLKGASIwDEVKDRlhdsALG-LSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 142 QQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEgKTIVVVHHDLSKAESYFDKL-LLMNKSLIHYGEV 220
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTgFFLDGDLIEYNDT 231
|
....*..
gi 446425376 221 RQV-LEP 226
Cdd:PRK14239 232 KQMfMNP 238
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-196 |
4.17e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.61 E-value: 4.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQIlGEDIRsvrksVAYVPQrsDIDW 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGLR-----IGYLPQ--EPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 87 DFPITVLDVVLIGTYPSLGMMKRPKK----------------------EHRD-WAFD-----CLKKVGM-EEFKNRQIGE 137
Cdd:COG0488 73 DDDLTVLDTVLDGDAELRALEAELEEleaklaepdedlerlaelqeefEALGgWEAEaraeeILSGLGFpEEDLDRPVSE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 138 LSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVtseETIIKILRELRKEGKTIVVVHHD 196
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDL---ESIEWLEEFLKNYPGTVLVVSHD 208
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-215 |
4.89e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.78 E-value: 4.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFV-SYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNdKGYVQILGEDIRSV-----RKSVAYV 78
Cdd:PRK11174 350 IEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELdpeswRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 79 PQRSDIdwdFPITVLDVVLIGTyPSLGmmkrpkkEHRDWAfdCLKKVGMEEFKNRQ-------IGE----LSGGQQQRVF 147
Cdd:PRK11174 429 GQNPQL---PHGTLRDNVLLGN-PDAS-------DEQLQQ--ALENAWVSEFLPLLpqgldtpIGDqaagLSVGQAQRLA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 148 LARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKeGKTIVVVHHDLSKAESYfDKLLLMNKSLI 215
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR-RQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-212 |
7.00e-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: 102.13 E-value: 7.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQgnqvVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR------SVRKSVAYVPq 80
Cdd:cd03215 7 VRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrsprdAIRAGIAYVP- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 rsdidwdfpitvldvvligtypslgmmkrpkkEHRdwafdclKKVGMeeFKNRQIGE-------LSGGQQQRVFLARALA 153
Cdd:cd03215 82 --------------------------------EDR-------KREGL--VLDLSVAEnialsslLSGGNQQKVVLARWLA 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 154 QKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNK 212
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYE 179
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-193 |
9.35e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.41 E-value: 9.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 2 GEAII-VKDLfvsyQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGE--DIRSVRKS---- 74
Cdd:COG1129 253 GEVVLeVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDAirag 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 75 VAYVP---------QRSDIDWDFPITVLDvvligTYPSLGMMkRPKKEhRDWAFDCLKKVGMeefK----NRQIGELSGG 141
Cdd:COG1129 329 IAYVPedrkgeglvLDLSIRENITLASLD-----RLSRGGLL-DRRRE-RALAEEYIKRLRI---KtpspEQPVGNLSGG 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446425376 142 QQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVV 193
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI 450
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-198 |
1.09e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 105.20 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 20 VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI--------RSVRKSVAYV---PQRS------ 82
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglsgrelRPLRRRMQMVfqdPYASlnprmt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 83 --DIdWDFPITVLDVVligtypslgmmkrPKKEHRDWAFDCLKKVGM-EEFKNRQIGELSGGQQQRVFLARALAQKAEIF 159
Cdd:COG4608 114 vgDI-IAEPLRIHGLA-------------SKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLS 198
Cdd:COG4608 180 VCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLS 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-215 |
1.59e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 103.51 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKS------------ 74
Cdd:PRK10619 8 VIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknql 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 75 ------VAYVPQRSDIdWDFpITVLDVVLIGTYPSLGMmkrPKKEHRDWAFDCLKKVGMEE-FKNRQIGELSGGQQQRVF 147
Cdd:PRK10619 88 rllrtrLTMVFQHFNL-WSH-MTVLENVMEAPIQVLGL---SKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 148 LARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLI 215
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-231 |
2.01e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 103.19 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAV-----LDLIPNDKGYVQILGEDI--RSV----- 71
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNQNIyeRRVnlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 72 RKSVAYVPQRSDIdwdFPITVLDVVLIGTyPSLGMmkRPKKEHRDWAFDCLKKVGM-EEFKNR---QIGELSGGQQQRVF 147
Cdd:PRK14258 87 RRQVSMVHPKPNL---FPMSVYDNVAYGV-KIVGW--RPKLEIDDIVESALKDADLwDEIKHKihkSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 148 LARALAQKAEIFFLDEPFVGIDVTSE---ETIIKILReLRKEgKTIVVVHHDLSKAE--SYFDKLLLMNKS----LIHYG 218
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASmkvESLIQSLR-LRSE-LTMVIVSHNLHQVSrlSDFTAFFKGNENrigqLVEFG 238
|
250
....*....|...
gi 446425376 219 EVRQVLEPTVMSK 231
Cdd:PRK14258 239 LTKKIFNSPHDSR 251
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-225 |
2.49e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 104.01 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGN-----QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGED------------ 67
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 68 -----------------IRSVRKSVAYVPQRSDIDWdFPITVLDVVLIGTYpSLGMmkrPKKEHRDWAFDCLKKVGM-EE 129
Cdd:PRK13651 83 vleklviqktrfkkikkIKEIRRRVGVVFQFAEYQL-FEQTIEKDIIFGPV-SMGV---SKEEAKKRAAKYIELVGLdES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 130 FKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLL 209
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIF 237
|
250
....*....|....*..
gi 446425376 210 MNKS-LIHYGEVRQVLE 225
Cdd:PRK13651 238 FKDGkIIKDGDTYDILS 254
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-239 |
2.57e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 103.34 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGN-QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGE-----DIRSVRKSVAYV 78
Cdd:PRK13652 4 IETRDLCYSYSGSkEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkeNIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 79 PQRSDiDWDFPITVLDVVLIGTYpSLGMmKRPKKEHRdwAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEI 158
Cdd:PRK13652 84 FQNPD-DQIFSPTVEQDIAFGPI-NLGL-DEETVAHR--VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 159 FFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQV-LEPTVMSKAYVN 235
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKgRIVAYGTVEEIfLQPDLLARVHLD 238
|
....
gi 446425376 236 QGIL 239
Cdd:PRK13652 239 LPSL 242
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-226 |
2.69e-26 |
|
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: 101.33 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGN--QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV-----RKSVAY 77
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIpledlRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSdidwdfpitvldVVLIGTYPSlgmMKRPKKEHRDwafdclkkvgMEEFKNRQIGE----LSGGQQQRVFLARALA 153
Cdd:cd03369 87 IPQDP------------TLFSGTIRS---NLDPFDEYSD----------EEIYGALRVSEgglnLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446425376 154 QKAEIFFLDEPFVGIDVTSEETIIKILRELRKeGKTIVVVHHDLSKAESYfDKLLLMNKslihyGEVRQVLEP 226
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDA-----GEVKEYDHP 207
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-197 |
5.09e-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: 99.43 E-value: 5.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGE--DIRSVRKS----VAYVPQ 80
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASPRDArragIAMVYQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 rsdidwdfpitvldvvligtypslgmmkrpkkehrdwafdclkkvgmeefknrqigeLSGGQQQRVFLARALAQKAEIFF 160
Cdd:cd03216 83 ---------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190
....*....|....*....|....*....|....*..
gi 446425376 161 LDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDL 197
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRL 142
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
10-215 |
7.04e-26 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 101.81 E-value: 7.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 10 LFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI--------RSVRKSVAYVPQ- 80
Cdd:TIGR02769 17 LFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldrkqrRAFRRDVQLVFQd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 -------RSDIDWdfpitvldvvLIGTyPSLGMMKRPKKEHRDWAFDCLKKVGME-EFKNRQIGELSGGQQQRVFLARAL 152
Cdd:TIGR02769 97 spsavnpRMTVRQ----------IIGE-PLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446425376 153 AQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKT-IVVVHHDLSKAESYFDKLLLMNKSLI 215
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
9-217 |
1.08e-25 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 99.87 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 9 DLFVSYQgnqvVQNVSFD--IEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV---RKSVAYVPQRSD 83
Cdd:cd03298 5 KIRFSYG----EQPMHFDltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAppaDRPVSMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 IdwdFP-ITVLDVVLIGTYPSLgmmkRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLD 162
Cdd:cd03298 81 L---FAhLTVEQNVGLGLSPGL----KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 163 EPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNKSLIHY 217
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-210 |
1.36e-25 |
|
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: 98.92 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGN--QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVL-DLIPNdKGYVQILGEDI----RSVRKSVAY 77
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTgDLKPQ-QGEITLDGVPVsdleKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSDIdwdFPITVLDvvligtypslgmmkrpkkehrdwafdclkkvgmeefknrQIGE-LSGGQQQRVFLARALAQKA 156
Cdd:cd03247 80 LNQRPYL---FDTTLRN---------------------------------------NLGRrFSGGERQRLALARILLQDA 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446425376 157 EIFFLDEPFVGIDVTSEETIIKILRELRKEgKTIVVVHHDLSKAEsYFDKLLLM 210
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIE-HMDKILFL 169
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-226 |
1.84e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.61 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV---RKSVAYVPQRSD 83
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVppyQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 IdwdFP-ITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLD 162
Cdd:PRK11607 102 L---FPhMTVEQNIAFG----LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 163 EPFVGIDVTSEETI-IKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKslihyGEVRQVLEP 226
Cdd:PRK11607 175 EPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNR-----GKFVQIGEP 234
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-196 |
1.91e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 100.19 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV-----------RK-- 73
Cdd:COG4674 13 VEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLdeheiarlgigRKfq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 74 --SVayvpqrsdidwdFP-ITVLDVVLI------GTYPSLgmMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQ 144
Cdd:COG4674 93 kpTV------------FEeLTVFENLELalkgdrGVFASL--FARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446425376 145 RVFLARALAQKAEIFFLDEPFVGIdvTSEET--IIKILRELRKEgKTIVVVHHD 196
Cdd:COG4674 159 WLEIGMLLAQDPKLLLLDEPVAGM--TDAETerTAELLKSLAGK-HSVVVVEHD 209
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
7-210 |
3.64e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 101.32 E-value: 3.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQ---GNQ----------VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVrK 73
Cdd:PRK15079 11 VADLKVHFDikdGKQwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM-K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 74 SVAYVPQRSDIDWDF--PI-------TVLDVV---LIGTYPSLgmmkrPKKEHRDWAFDCLKKVGM-EEFKNRQIGELSG 140
Cdd:PRK15079 90 DDEWRAVRSDIQMIFqdPLaslnprmTIGEIIaepLRTYHPKL-----SRQEVKDRVKAMMLKVGLlPNLINRYPHEFSG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446425376 141 GQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLM 210
Cdd:PRK15079 165 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-224 |
7.31e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 102.60 E-value: 7.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSY--QGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLmkavLDLI-----PNdKGYVQILGEDIR-----SV 71
Cdd:PRK11160 338 SLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTL----LQLLtrawdPQ-QGEILLNGQPIAdyseaAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 72 RKSVAYVPQRSDIdwdFPITVLDVVLIGtypslgmmkrpKKEHRDWAF-DCLKKVGME------EFKNRQIGE----LSG 140
Cdd:PRK11160 413 RQAISVVSQRVHL---FSATLRDNLLLA-----------APNASDEALiEVLQQVGLEklleddKGLNAWLGEggrqLSG 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 141 GQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKeGKTIVVVHHDLSKAESyFDKLLLM-NKSLIHYGE 219
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRLTGLEQ-FDRICVMdNGQIIEQGT 556
|
....*
gi 446425376 220 VRQVL 224
Cdd:PRK11160 557 HQELL 561
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-226 |
7.37e-25 |
|
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: 100.26 E-value: 7.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 35 IIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV---RKSVAYVPQRSDIdwdFP-ITVLDVVLIGtypsLGMMKRP 110
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVpphLRHINMVFQSYAL---FPhMTVEENVAFG----LKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 111 KKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILREL-RKEGKT 189
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIqEQLGIT 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 446425376 190 IVVVHHDLSKAESYFDKLLLMNKslihyGEVRQVLEP 226
Cdd:TIGR01187 154 FVFVTHDQEEAMTMSDRIAIMRK-----GKIAQIGTP 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-197 |
8.78e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.03 E-value: 8.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 21 QNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGE--DIRSVRKSVAY----VPQ-RSDIDwdfPITVL 93
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAIALgigmVHQhFMLVP---NLTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 94 DVVLIGTYPSLGMMKRPKKEHRDwafdcLKKVgMEEFK-----NRQIGELSGGQQQRVFLARALAQKAEIFFLDEPfvgi 168
Cdd:COG3845 99 ENIVLGLEPTKGGRLDRKAARAR-----IREL-SERYGldvdpDAKVEDLSVGEQQRVEILKALYRGARILILDEP---- 168
|
170 180 190
....*....|....*....|....*....|....*
gi 446425376 169 dvTS----EET--IIKILRELRKEGKTIVVVHHDL 197
Cdd:COG3845 169 --TAvltpQEAdeLFEILRRLAAEGKSIIFITHKL 201
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
18-210 |
1.38e-24 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 97.10 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKaVLDLIPN-DKGYVQILGEDIRSVRKSVAYVPQRSDIDWDFP------- 89
Cdd:NF038007 19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLN-IIGMFDSlDSGSLTLAGKEVTNLSYSQKIILRRELIGYIFQsfnliph 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 90 ITVLDVVligtypSLGMMKR--PKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVG 167
Cdd:NF038007 98 LSIFDNV------ALPLKYRgvAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446425376 168 IDVTSEETIIKILRELRKEGKTIVVVHHDlSKAESYFDKLLLM 210
Cdd:NF038007 172 LDSKNARAVLQQLKYINQKGTTIIMVTHS-DEASTYGNRIINM 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-202 |
1.69e-24 |
|
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: 96.66 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVR----KSVAYVPQRS 82
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRdephENILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 83 DIDWDfpITVLDvvligtypSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLD 162
Cdd:TIGR01189 83 GLKPE--LSALE--------NLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446425376 163 EPFVGIDVTSEETIIKILRE-LRKEGKTIVVVHHDLSKAES 202
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLRAhLARGGIVLLTTHQDLGLVEA 193
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-231 |
2.08e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 98.33 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQ--VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLI---PNDKGYVQILG-----EDIRSVRK 73
Cdd:PRK13640 5 IVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGitltaKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 74 SVAYVPQRSDIDWdFPITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALA 153
Cdd:PRK13640 85 KVGIVFQNPDNQF-VGATVGDDVAFG----LENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 154 QKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNKSLIHYGEVRQVLEPTVMSK 231
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-196 |
2.26e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVqILGEDIRsvrksVAYVPQ-RSD 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGETVK-----IGYFDQhQEE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 IDWDfpITVLDVVligtypSLGMMKRPKKEHRDW--AF-----DCLKKVgmeefknrqiGELSGGQQQRVFLARALAQKA 156
Cdd:COG0488 390 LDPD--KTVLDEL------RDGAPGGTEQEVRGYlgRFlfsgdDAFKPV----------GVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446425376 157 EIFFLDEPFVGIDVTSEETIIKILRELrkEGkTIVVVHHD 196
Cdd:COG0488 452 NVLLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHD 488
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-224 |
3.69e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 97.04 E-value: 3.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIP------NDKGYVQILGEDIRSV-----RKSV 75
Cdd:PRK14246 13 ISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIdaiklRKEV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 76 AYVPQRSDidwDFP-ITVLDVVligTYPSLGMMKRPKKEHRDWAFDCLKKVGM----EEFKNRQIGELSGGQQQRVFLAR 150
Cdd:PRK14246 93 GMVFQQPN---PFPhLSIYDNI---AYPLKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 151 ALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEgKTIVVVHHDLSKAESYFDKL-LLMNKSLIHYGEVRQVL 224
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVaFLYNGELVEWGSSNEIF 240
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-233 |
4.46e-24 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 96.54 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 23 VSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNdKGYVQILGEDIRSVRKSV-----AYVPQRSDidwdfPITVLDVvl 97
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAElarhrAYLSQQQT-----PPFAMPV-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 98 igtYPSLgMMKRPKKEHRDWAFDCLKKV----GMEEFKNRQIGELSGGQQQRVFLARALAQ-------KAEIFFLDEPFV 166
Cdd:PRK03695 87 ---FQYL-TLHQPDKTRTEAVASALNEVaealGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 167 GIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVLEPTVMSKAY 233
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQgKLLASGRRDEVLTPENLAQVF 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-208 |
4.55e-24 |
|
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: 96.71 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 26 DIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGyvqilgeDIRSVRKSVAYVPQRsdIDWDFPITVLDVvLIGTYPSLG 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-------DIEIELDTVSYKPQY--IKADYEGTVRDL-LSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 106 mmkrpkkEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILREL-R 184
Cdd:cd03237 91 -------THPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaE 163
|
170 180
....*....|....*....|....
gi 446425376 185 KEGKTIVVVHHDLSKAESYFDKLL 208
Cdd:cd03237 164 NNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-196 |
6.12e-24 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 95.55 E-value: 6.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQV-VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKS-VAYVPQRS 82
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 83 DIDW-DFPI----TVLDVVLIgtypSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAE 157
Cdd:cd03292 81 GVVFqDFRLlpdrNVYENVAF----ALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 446425376 158 IFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHD 196
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHA 195
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-232 |
6.25e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.08 E-value: 6.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIVKDLFVSYQGNQ------VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILG------EDI 68
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 69 RSVRKSVAYVPQRSDIDWDFPITVLDVVLigTYPSLGMmkrPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFL 148
Cdd:PRK13633 81 WDIRNKAGMVFQNPDNQIVATIVEEDVAF--GPENLGI---PPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 149 ARALAQKAEIFFLDEPFVGIDVTSEETIIKILREL-RKEGKTIVVVHHDLSKAESYfDKLLLMNK-SLIHYGEVRQVLEP 226
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVEA-DRIIVMDSgKVVMEGTPKEIFKE 234
|
....*.
gi 446425376 227 TVMSKA 232
Cdd:PRK13633 235 VEMMKK 240
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-225 |
7.06e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 99.76 E-value: 7.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQ-----------VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDkGYVQILGEDIRSVRKSv 75
Cdd:COG4172 278 ARDLKVWFPIKRglfrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRR- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 76 AYVPQRSDIDWDF--P-------ITVLDVV---LIGTYPSLGmmkrpKKEHRDWAFDCLKKVGM-EEFKNRQIGELSGGQ 142
Cdd:COG4172 356 ALRPLRRRMQVVFqdPfgslsprMTVGQIIaegLRVHGPGLS-----AAERRARVAEALEEVGLdPAARHRYPHEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 143 QQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILREL-RKEGKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEV 220
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDgKVVEQGPT 510
|
....*
gi 446425376 221 RQVLE 225
Cdd:COG4172 511 EQVFD 515
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-209 |
7.19e-24 |
|
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: 94.87 E-value: 7.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAyvpqrSDI 84
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIA-----RGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 85 DWdfpitvldvvlIGTYPSLGMMKRPKKEHRDWAFDC--------LKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKA 156
Cdd:cd03231 76 LY-----------LGHAPGIKTTLSVLENLRFWHADHsdeqveeaLARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446425376 157 EIFFLDEPFVGIDVTSEETIIKILR-ELRKEGKTIVVVHHDLSKAESYFDKLLL 209
Cdd:cd03231 145 PLWILDEPTTALDKAGVARFAEAMAgHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-195 |
8.16e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 99.22 E-value: 8.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 12 VSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKaVL--DLIPnDKGYVQILGEDIR--SVRKSVA----------- 76
Cdd:PRK11288 12 KTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLK-ILsgNYQP-DAGSILIDGQEMRfaSTTAALAagvaiiyqelh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 77 YVPQrsdidwdfpITVLDVVLIGTYPS-LGMMKRpkKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQK 155
Cdd:PRK11288 90 LVPE---------MTVAENLYLGQLPHkGGIVNR--RLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446425376 156 AEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHH 195
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-224 |
9.89e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 95.75 E-value: 9.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLI-----PNDKGYVQILGEDI-----RSVRKS 74
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfkmdvIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 75 VAYVPQRSDidwdfPITVLDV---VLIGtyPSLGMMKRPKKEHRDWAFDCLKKVGM-EEFKNR---QIGELSGGQQQRVF 147
Cdd:PRK14247 84 VQMVFQIPN-----PIPNLSIfenVALG--LKLNRLVKSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 148 LARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEgKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVL 224
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKgQIVEWGPTREVF 233
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
7-233 |
1.15e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.83 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVldlipndKGYVQILGEDIRSVRKSVAYVP----QRS 82
Cdd:PRK11300 8 VSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCL-------TGFYKPTGGTILLRGQHIEGLPghqiARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 83 DIDWDF-------PITVLDVVLIGTYPSL------GMMKRP-----KKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQ 144
Cdd:PRK11300 81 GVVRTFqhvrlfrEMTVIENLLVAQHQQLktglfsGLLKTPafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 145 RVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMN--KSLIHyG--- 218
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNqgTPLAN-Gtpe 239
|
250
....*....|....*
gi 446425376 219 EVRQvlEPTVMsKAY 233
Cdd:PRK11300 240 EIRN--NPDVI-KAY 251
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-212 |
1.22e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 96.34 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIVKDLFVSYQGNQ---VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILG-----EDIRSVR 72
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 73 KSVAYVPQRSDIDWdFPITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARAL 152
Cdd:PRK13650 81 HKIGMVFQNPDNQF-VGATVEDDVAFG----LENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446425376 153 AQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSK-AESyfDKLLLMNK 212
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEvALS--DRVLVMKN 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-198 |
1.31e-23 |
|
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: 95.30 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSY---QGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV-----RKSVA 76
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLnlrwlRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 77 YVPQRSDIdwdFPITVLDVVLIGTYPslgmmkrPKKEHRDWAfdcLKKVGMEEF-------KNRQIGE----LSGGQQQR 145
Cdd:cd03249 81 LVSQEPVL---FDGTIAENIRYGKPD-------ATDEEVEEA---AKKANIHDFimslpdgYDTLVGErgsqLSGGQKQR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446425376 146 VFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKeGKTIVVVHHDLS 198
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK-GRTTIVIAHRLS 199
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-225 |
1.54e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 98.94 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQG--NQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR-----SVRKSVAY 77
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdytlaSLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSDIdwdFPITVLDVVligTYPSLGMMKRPKKEHR---DWAFDCLKKvgMEEFKNRQIGE----LSGGQQQRVFLAR 150
Cdd:PRK11176 422 VSQNVHL---FNDTIANNI---AYARTEQYSREQIEEAarmAYAMDFINK--MDNGLDTVIGEngvlLSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 151 ALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEgKTIVVVHHDLSKAESYFDKLLLMNKSLIHYGEVRQVLE 225
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLA 567
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-225 |
2.13e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.76 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIVKDLFVSYQGNQ----------------------VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDK 58
Cdd:COG1134 1 MSSMIEVENVSKSYRLYHepsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 59 GYVQILGEdIRS-VRKSVAYVPQrsdidwdfpITVLD-VVLIGTYpsLGMMKRPKKEHRDwafDCLKKVGMEEFKNRQIG 136
Cdd:COG1134 81 GRVEVNGR-VSAlLELGAGFHPE---------LTGREnIYLNGRL--LGLSRKEIDEKFD---EIVEFAELGDFIDQPVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 137 ELSGGQQQRVFLARALAQKAEIFFLDEPF-VGiDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNK-SL 214
Cdd:COG1134 146 TYSSGMRARLAFAVATAVDPDILLVDEVLaVG-DAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKgRL 224
|
250
....*....|.
gi 446425376 215 IHYGEVRQVLE 225
Cdd:COG1134 225 VMDGDPEEVIA 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-196 |
2.23e-23 |
|
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: 92.13 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKgyvqilGEDIRSVRKSVAYVPQrsdi 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDE------GIVTWGSTVKIGYFEQ---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 85 dwdfpitvldvvligtypslgmmkrpkkehrdwafdclkkvgmeefknrqigeLSGGQQQRVFLARALAQKAEIFFLDEP 164
Cdd:cd03221 71 -----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190
....*....|....*....|....*....|..
gi 446425376 165 FVGIDVtseETIIKILRELRKEGKTIVVVHHD 196
Cdd:cd03221 98 TNHLDL---ESIEALEEALKEYPGTVILVSHD 126
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-223 |
3.13e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.11 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 22 NVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI-------RSVRKSVAYVPQRSDIDWdFPITVLD 94
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkkvklSDIRKKVGLVFQYPEYQL-FEETIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 95 VVLIGtyPS-LGMmkrPKKEHRDWAFDCLKKVGM--EEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVT 171
Cdd:PRK13637 104 DIAFG--PInLGL---SEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446425376 172 SEETIIKILRELRKEGK-TIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQV 223
Cdd:PRK13637 179 GRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKgKCELQGTPREV 232
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-215 |
3.49e-23 |
|
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: 94.09 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 16 GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV-----RKSVAYVPQRSDIdwdFPI 90
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdpawlRRQVGVVLQENVL---FNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 91 TVLD-VVLIGTYPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGID 169
Cdd:cd03252 91 SIRDnIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446425376 170 VTSEETIIKILRELRKeGKTIVVVHHDLSKAESYfDKLLLMNKSLI 215
Cdd:cd03252 171 YESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNA-DRIIVMEKGRI 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-196 |
4.05e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 97.87 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 13 SYQGNQ----VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV---------RKSVAYVP 79
Cdd:PRK10535 13 SYPSGEeqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadalaqlrREHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 QRSDIdwdfpITVL----DVVLIGTYPSLGmmkrpKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQK 155
Cdd:PRK10535 93 QRYHL-----LSHLtaaqNVEVPAVYAGLE-----RKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446425376 156 AEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHD 196
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-213 |
4.46e-23 |
|
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: 91.83 E-value: 4.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDL-FVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGedirsvRKSVAYVPQRSd 83
Cdd:cd03223 1 IELENLsLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE------GEDLLFLPQRP- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 idwDFPITVLDVVLIgtYPslgmmkrpkkehrdWafdclKKVgmeefknrqigeLSGGQQQRVFLARALAQKAEIFFLDE 163
Cdd:cd03223 74 ---YLPLGTLREQLI--YP--------------W-----DDV------------LSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446425376 164 PFVGIDVTSEEtiiKILRELRKEGKTIVVVHHDlSKAESYFDKLLLMNKS 213
Cdd:cd03223 118 ATSALDEESED---RLYQLLKELGITVISVGHR-PSLWKFHDRVLDLDGE 163
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
10-233 |
6.26e-23 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 94.12 E-value: 6.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 10 LFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPND--------KGYVQILGE-----DIRSVRKSVA 76
Cdd:PRK13547 7 LHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEplaaiDAPRLARLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 77 YVPQRSDIdwDFPITVLDVVLIGTYPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQ-- 154
Cdd:PRK13547 87 VLPQAAQP--AFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 155 -------KAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKT-IVVVHHDLSKAESYFDKL-LLMNKSLIHYGEVRQVLE 225
Cdd:PRK13547 165 pphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIaMLADGAIVAHGAPADVLT 244
|
....*...
gi 446425376 226 PTVMSKAY 233
Cdd:PRK13547 245 PAHIARCY 252
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-201 |
6.35e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 92.54 E-value: 6.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 6 IVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVL-DLIP--NDKGYVQILGEDIRSV---RKSVAYVP 79
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPafSASGEVLLNGRRLTALpaeQRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 QrsDiDWDFP-ITVLDVVLIGTYPSLGmmkrpKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEI 158
Cdd:COG4136 83 Q--D-DLLFPhLSVGENLAFALPPTIG-----RAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446425376 159 FFLDEPFVGIDVTseetiikiLR---------ELRKEGKTIVVVHHDLSKAE 201
Cdd:COG4136 155 LLLDEPFSKLDAA--------LRaqfrefvfeQIRQRGIPALLVTHDEEDAP 198
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
10-224 |
6.47e-23 |
|
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: 97.03 E-value: 6.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 10 LFVSYQGNQ-VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVR-----KSVAYVPQrsD 83
Cdd:TIGR01842 323 TIVPPGGKKpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDretfgKHIGYLPQ--D 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 IDWdFPITVLDVVligtyPSLGMMKRPKKehrdwAFDCLKKVGMEEFKNR-------QIGE----LSGGQQQRVFLARAL 152
Cdd:TIGR01842 401 VEL-FPGTVAENI-----ARFGENADPEK-----IIEAAKLAGVHELILRlpdgydtVIGPggatLSGGQRQRIALARAL 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446425376 153 AQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESyFDKLLLMNKSLIH-YGEVRQVL 224
Cdd:TIGR01842 470 YGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGC-VDKILVLQDGRIArFGERDEVL 541
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
7-197 |
6.62e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.63 E-value: 6.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR--SVRKSVAYVPQRsdi 84
Cdd:PRK13539 5 GEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdpDVAEACHYLGHR--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 85 dwDF---PITVLDvvligtypSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFL 161
Cdd:PRK13539 82 --NAmkpALTVAE--------NLEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 446425376 162 DEPFVGIDVTSEETIIKILRELRKEGKTIVVV-HHDL 197
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRAHLAQGGIVIAAtHIPL 188
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-217 |
8.14e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 92.72 E-value: 8.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 24 SFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV---RKSVAYVPQRSDIdwdFP-ITVLDVVLIG 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTppsRRPVSMLFQENNL---FShLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 100 TYPSLGMMKRPKKEHRDWAfdclKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKI 179
Cdd:PRK10771 96 LNPGLKLNAAQREKLHAIA----RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 446425376 180 LREL-RKEGKTIVVVHHDLSKAESYFDKLLLMNKSLIHY 217
Cdd:PRK10771 172 VSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAW 210
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-218 |
1.10e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 93.31 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 8 KDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKA---VLDLIPNDK--GYVQILGEDIRS-------VRKSV 75
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFRveGKVTFHGKNLYApdvdpveVRRRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 76 AYVPQRSDidwDFPITVLDVVLIGtyPSLGMMKRPKKEHRDWAfdcLKKVGM-EEFKN--RQIG-ELSGGQQQRVFLARA 151
Cdd:PRK14243 94 GMVFQKPN---PFPKSIYDNIAYG--ARINGYKGDMDELVERS---LRQAALwDEVKDklKQSGlSLSGGQQQRLCIARA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446425376 152 LAQKAEIFFLDEPFVGIDVTSEETIIKILRELrKEGKTIVVVHHDLSKAESYFDKLLLMNKSLIHYG 218
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGG 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-226 |
1.30e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 95.10 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 20 VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV---------RKSVAYVPQRSDIdwdFP- 89
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaelrevrRKKIAMVFQSFAL---MPh 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 90 ITVLDVVLIGtypsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGID 169
Cdd:PRK10070 121 MTVLDNTAFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 170 -VTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKslihyGEVRQVLEP 226
Cdd:PRK10070 197 pLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN-----GEVVQVGTP 249
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-217 |
1.70e-22 |
|
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: 91.83 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAYVPQrsdidwdfpITVLD-VV 96
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGGFNPE---------LTGREnIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 97 LIGTYpsLGMMKR--PKKEHRDWAFDclkkvGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPF-VGiDVTSE 173
Cdd:cd03220 107 LNGRL--LGLSRKeiDEKIDEIIEFS-----ELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLaVG-DAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446425376 174 ETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLIHY 217
Cdd:cd03220 179 EKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-211 |
2.46e-22 |
|
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: 91.34 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIVKDL---FVSY-QGN---QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLD---------LIPNDKGYV--- 61
Cdd:COG4778 1 MTTLLEVENLsktFTLHlQGGkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnylpdsgsiLVRHDGGWVdla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 62 -----QILgeDIRsvRKSVAYVPQrsdidwdF----P-ITVLDVV---LIgtypSLGMmkrPKKEHRDWAFDCLKKVGME 128
Cdd:COG4778 81 qasprEIL--ALR--RRTIGYVSQ-------FlrviPrVSALDVVaepLL----ERGV---DREEARARARELLARLNLP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 129 EfknrqigEL--------SGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKA 200
Cdd:COG4778 143 E-------RLwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVR 215
|
250
....*....|.
gi 446425376 201 ESYFDKLLLMN 211
Cdd:COG4778 216 EAVADRVVDVT 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-215 |
3.24e-22 |
|
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: 91.08 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 24 SFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV---RKSVAYVPQRSDIdwdFP-ITVLDVVLIG 99
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLapyQRPVSMLFQENNL---FAhLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 100 TYPSLGMMKRPKKEHRDWAfdclKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKI 179
Cdd:TIGR01277 95 LHPGLKLNAEQQEKVVDAA----QQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 446425376 180 LRELRKEGK-TIVVVHHDLSKAESYFDKLLLMNKSLI 215
Cdd:TIGR01277 171 VKQLCSERQrTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-219 |
3.27e-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: 94.85 E-value: 3.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 28 EKGKLVGIIGPNGAGKSTLMKaVL--DLIPN----DKG-----------------YVQILGE-DIRSVRKS--VAYVPQR 81
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALK-ILsgELKPNlgdyDEEpswdevlkrfrgtelqdYFKKLANgEIKVAHKPqyVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 82 sdidwdFPITVLDvvLIGTYPSLGMMKrpkkehrdwafDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFL 161
Cdd:COG1245 176 ------FKGTVRE--LLEKVDERGKLD-----------ELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 162 DEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSkaesyfdkLLLMNKSLIH--YGE 219
Cdd:COG1245 237 DEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLA--------ILDYLADYVHilYGE 288
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-198 |
3.55e-22 |
|
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: 91.66 E-value: 3.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 30 GKLVGIIGPNGAGKSTLMKAVLD-LIPN----------------------DKGYVQILGEDIRSVRKsvayvPQRSD-ID 85
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGkLKPNlgkfddppdwdeildefrgselQNYFTKLLEGDVKVIVK-----PQYVDlIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 86 WDFPITVLDVVligtypslgmmkrPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPF 165
Cdd:cd03236 101 KAVKGKVGELL-------------KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|...
gi 446425376 166 VGIDVTSEETIIKILRELRKEGKTIVVVHHDLS 198
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-210 |
3.57e-22 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 93.25 E-value: 3.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 23 VSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAYVPQRSDIDWDFPITVLdvvligtYP 102
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARL-------FP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 103 SLGM-------MKRPKKEHRDWAFDCLKKV-GMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEE 174
Cdd:TIGR02142 89 HLSVrgnlrygMKRARPSERRISFERVIELlGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 446425376 175 TIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLM 210
Cdd:TIGR02142 169 EILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVL 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-225 |
3.69e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 94.75 E-value: 3.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGN----QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYV--QIL--GEDI--------RS 70
Cdd:COG4172 9 VEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPsgSILfdGQDLlglserelRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 71 VR-KSVAYVPQRsdidwdfPITVLDVVL-IGT--YPSL----GMmkrPKKEHRDWAFDCLKKVGMEEFKNRqIG----EL 138
Cdd:COG4172 89 IRgNRIAMIFQE-------PMTSLNPLHtIGKqiAEVLrlhrGL---SGAAARARALELLERVGIPDPERR-LDayphQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 139 SGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNK-SLIH 216
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQgEIVE 237
|
....*....
gi 446425376 217 YGEVRQVLE 225
Cdd:COG4172 238 QGPTAELFA 246
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
12-224 |
4.89e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.97 E-value: 4.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 12 VSY---QGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGED------IRSVRKSVAYVPQRS 82
Cdd:PRK13644 7 VSYsypDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDtgdfskLQGIRKLVGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 83 DIDWdFPITVLDVVLIGTyPSLGMmkrPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLD 162
Cdd:PRK13644 87 ETQF-VGRTVEEDLAFGP-ENLCL---PPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446425376 163 EPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYfDKLLLMNKSLIHY-GEVRQVL 224
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDA-DRIIVMDRGKIVLeGEPENVL 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-210 |
7.51e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 91.31 E-value: 7.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIVKDLFVSYQGNQVVQN---VSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGE-----DIRSVR 72
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaeNVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 73 KSVAYVPQRSDIDWdFPITVLDVVligtypSLGMMKR--PKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLAR 150
Cdd:PRK13642 81 RKIGMVFQNPDNQF-VGATVEDDV------AFGMENQgiPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446425376 151 ALAQKAEIFFLDEPFVGIDVTSEETIIKILRELR-KEGKTIVVVHHDLSKAESYfDKLLLM 210
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAASS-DRILVM 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-246 |
8.81e-22 |
|
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: 93.71 E-value: 8.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAV--LDLIPNDKG-------------YVQI---LGE 66
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGriiyhvalcekcgYVERpskVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 67 DI----------------------RSVRKSVAYVPQRSdidwdFPITVLDVVLIGTYPSLGMMKRPKKEHRDWAFDCLKK 124
Cdd:TIGR03269 81 PCpvcggtlepeevdfwnlsdklrRRIRKRIAIMLQRT-----FALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 125 VGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILREL-RKEGKTIVVVHHDLSKAESY 203
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446425376 204 FDKLLLMNKslihyGEVRQVLEPTVMSKAYVNQGILFNNAAEV 246
Cdd:TIGR03269 236 SDKAIWLEN-----GEIKEEGTPDEVVAVFMEGVSEVEKECEV 273
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
14-200 |
9.41e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 90.26 E-value: 9.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 14 YQGNQ----VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV---------RKSVAYVPQ 80
Cdd:PRK11629 15 YQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaelrNQKLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSDIDWDFpiTVLDVV----LIGtypslgmmKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKA 156
Cdd:PRK11629 95 FHHLLPDF--TALENVamplLIG--------KKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446425376 157 EIFFLDEPFVGIDVTSEETIIKILREL-RKEGKTIVVVHHDLSKA 200
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLA 209
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
7-224 |
1.46e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 90.68 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSY-QGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR-------SVRKSVAYV 78
Cdd:PRK13636 8 VEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkglmKLRESVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 79 PQRSDiDWDFPITVLDVVLIGTYPslgmMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEI 158
Cdd:PRK13636 88 FQDPD-NQLFSASVYQDVSFGAVN----LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 159 FFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVL 224
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEgRVILQGNPKEVF 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
5-215 |
1.99e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 90.46 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGN-----QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQIlGE----------DIR 69
Cdd:PRK13634 3 ITFQKVEHRYQYKtpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GErvitagkknkKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 70 SVRKSVAYVPQrsdidwdFP------ITVLDVVLIGtyPS-LGMmkrPKKEHRDWAFDCLKKVGM-EEFKNRQIGELSGG 141
Cdd:PRK13634 82 PLRKKVGIVFQ-------FPehqlfeETVEKDICFG--PMnFGV---SEEDAKQKAREMIELVGLpEELLARSPFELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 142 QQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNKSLI 215
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-225 |
2.11e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 92.54 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 20 VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR------SVRKSVAYVPQRSDIDWDFP---- 89
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldAVKKGMAYITESRRDNGFFPnfsi 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 90 ---ITVLDVVLIGTYPSLGMMKRPKKEHRdWAFDCLKKVGME-EFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPF 165
Cdd:PRK09700 359 aqnMAISRSLKDGGYKGAMGLFHEVDEQR-TAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 166 VGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKslihyGEVRQVLE 225
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCE-----GRLTQILT 492
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-215 |
2.26e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 90.68 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 2 GEAIIVKDLFVSYQGNQ-----VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQI----LGEDIRSVR 72
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 73 KSVAYVPQ----------RSDIDWDFPITVLDVVLIGTYPSLG--MMKRPKKEHRDWAFDCLKKVGMEE-FKNRQIGELS 139
Cdd:PRK13631 99 LITNPYSKkiknfkelrrRVSMVFQFPEYQLFKDTIEKDIMFGpvALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLS 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 140 GGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLI 215
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-205 |
2.40e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 89.82 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI----RS----VRKSVAYV 78
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSrlytVRKRMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 79 PQRSDIDWDfpITVLDVVligTYPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEI 158
Cdd:PRK11831 90 FQSGALFTD--MNVFDNV---AYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446425376 159 FFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFD 205
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIAD 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-197 |
2.51e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.01 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 2 GEAII-VKDLFV-SYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI-----RSVRKS 74
Cdd:COG3845 254 GEVVLeVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglspRERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 75 -VAYVP---QRSDIDWDFPITvlDVVLIGTYPSLGMMKRP---KKEHRDWAFDClkkvgMEEFK------NRQIGELSGG 141
Cdd:COG3845 334 gVAYIPedrLGRGLVPDMSVA--ENLILGRYRRPPFSRGGfldRKAIRAFAEEL-----IEEFDvrtpgpDTPARSLSGG 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 142 QQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDL 197
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDL 462
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
9-236 |
2.86e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.68 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 9 DLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR-------SVRKSVAYVPQr 81
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrgllALRQQVATVFQ- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 82 sDIDWDFPITVLDVVLIGTYPSLGMmkrPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFL 161
Cdd:PRK13638 85 -DPEQQIFYTDIDSDIAFSLRNLGV---PEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446425376 162 DEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVLEPT-VMSKAYVNQ 236
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQgQILTHGAPGEVFACTeAMEQAGLTQ 237
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-196 |
3.37e-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: 91.92 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQIlGEDIRsvrksVAYVPQ-RSD 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK-----LAYVDQsRDA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 ID-----WDFPITVLDVVLIGTYPslgMMKRpkkehrdwAFdclkkVGMEEFK----NRQIGELSGGQQQRVFLARALAQ 154
Cdd:TIGR03719 397 LDpnktvWEEISGGLDIIKLGKRE---IPSR--------AY-----VGRFNFKgsdqQKKVGQLSGGERNRVHLAKTLKS 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446425376 155 KAEIFFLDEPFVGIDVtseETiikiLRELRKE----GKTIVVVHHD 196
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDV---ET----LRALEEAllnfAGCAVVISHD 499
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-225 |
4.53e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.42 E-value: 4.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 22 NVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILG---------EDIRSVRKSVAYVPQ--RSDIdwdFPI 90
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknKDIKQIRKKVGLVFQfpESQL---FEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 91 TVLDVVLIGTyPSLGMmkrPKKEHRDWAFDCLKKVGM-EEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGID 169
Cdd:PRK13649 102 TVLKDVAFGP-QNFGV---SQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446425376 170 VTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVLE 225
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKgKLVLSGKPKDIFQ 234
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-196 |
4.60e-21 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 91.23 E-value: 4.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLmkavLDLIPND--KGYVQIL---------GEDIRSVRK 73
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTL----LSLITGDhpQGYSNDLtlfgrrrgsGETIWDIKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 74 SVAYVPQRSDIDWDFPITVLDVVLIGTYPSLGMMKRPKKEHRDWAFDCLKKVGM-EEFKNRQIGELSGGQQQRVFLARAL 152
Cdd:PRK10938 337 HIGYVSSSLHLDYRVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIdKRTADAPFHSLSWGQQRLALIVRAL 416
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446425376 153 AQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKT--IVVVHHD 196
Cdd:PRK10938 417 VKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqlLFVSHHA 462
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-209 |
5.42e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 87.31 E-value: 5.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR----SVRKSVAYVPQRS 82
Cdd:PRK13540 4 VIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkdlcTYQKQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 83 DIDWDfpITVLDVVLIGTYPSLGMMKrpkkehrdwAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLD 162
Cdd:PRK13540 84 GINPY--LTLRENCLYDIHFSPGAVG---------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446425376 163 EPFVGIDVTSEETIIKILRELRKEGKTIVVV-HHDLSKAESYFDKLLL 209
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRAKGGAVLLTsHQDLPLNKADYEEYHL 200
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
7-225 |
9.92e-21 |
|
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: 87.96 E-value: 9.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAYVPQRSDI-- 84
Cdd:TIGR02323 6 VSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRRLmr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 85 -DWDF----PITVLDVVL-----IGTYPsLGMMKRPKKEHRDWAFDCLKKVGMEEFK-NRQIGELSGGQQQRVFLARALA 153
Cdd:TIGR02323 86 tEWGFvhqnPRDGLRMRVsaganIGERL-MAIGARHYGNIRATAQDWLEEVEIDPTRiDDLPRAFSGGMQQRLQIARNLV 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446425376 154 QKAEIFFLDEPFVGIDVTSEETIIKILREL-RKEGKTIVVVHHDLSKAESYFDKLLLMNKS-LIHYGEVRQVLE 225
Cdd:TIGR02323 165 TRPRLVFMDEPTGGLDVSVQARLLDLLRGLvRDLGLAVIIVTHDLGVARLLAQRLLVMQQGrVVESGLTDQVLD 238
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-224 |
1.15e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.23 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLipNDK--GYVQ----ILG-------EDIRS 70
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRM--NDKvsGYRYsgdvLLGgrsifnyRDVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 71 VRKSVAYVPQRSDidwDFPITVLDVVLIGTYPSLGMmkrPKKEHRDWAFDCLKKVGMEEFKNRQIGE----LSGGQQQRV 146
Cdd:PRK14271 99 FRRRVGMLFQRPN---PFPMSIMDNVLAGVRAHKLV---PRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 147 FLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELrKEGKTIVVVHHDLSKAESYFDK-LLLMNKSLIHYGEVRQVL 224
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRaALFFDGRLVEEGPTEQLF 250
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-233 |
1.16e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 88.25 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 13 SYQGN-----QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQI---------LGEDIRSVRKSVAYV 78
Cdd:PRK13643 10 TYQPNspfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstsKQKEIKPVRKKVGVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 79 PQRSDIDWdFPITVLDVVLIGTyPSLGMmkrPKKEHRDWAFDCLKKVGM-EEFKNRQIGELSGGQQQRVFLARALAQKAE 157
Cdd:PRK13643 90 FQFPESQL-FEETVLKDVAFGP-QNFGI---PKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446425376 158 IFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKS-LIHYGEVRQVLEPTVMSKAY 233
Cdd:PRK13643 165 VLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGhIISCGTPSDVFQEVDFLKAH 241
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-223 |
1.71e-20 |
|
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: 86.75 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 20 VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAYVPQR-SDIDWdfpITVLDVVLI 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNySLLPW---LTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 99 GTypSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGID-VTSEETII 177
Cdd:TIGR01184 78 AV--DRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDaLTRGNLQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446425376 178 KILRELRKEGKTIVVVHHDLSKAESYFDKLLLM-NKSLIHYGEVRQV 223
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLtNGPAANIGQILEV 202
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-234 |
2.86e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.40 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 17 NQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR-----SVRKSVAYVPQRSDIdwdFPIT 91
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqydhhYLHRQVALVGQEPVL---FSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 92 VLDVVLIG--TYPSLGMMKRPKKEHrdwAFDCLKkvGMEEFKNRQIGE----LSGGQQQRVFLARALAQKAEIFFLDEPF 165
Cdd:TIGR00958 571 VRENIAYGltDTPDEEIMAAAKAAN---AHDFIM--EFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 166 VGIDVTSEETiikiLRELRK-EGKTIVVVHHDLSKAESYFDKLLLMNKSLIHYGEVRQVLEPTVMSKAYV 234
Cdd:TIGR00958 646 SALDAECEQL----LQESRSrASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-197 |
3.20e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 89.10 E-value: 3.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 27 IEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQIlgeDIRsvrksVAYVPQRsdIDWDFPITVLDVvligtypslgM 106
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---ELK-----ISYKPQY--IKPDYDGTVEDL----------L 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 107 MKRPKKEHRDWAF-DCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVtsEETII--KILREL 183
Cdd:PRK13409 422 RSITDDLGSSYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQRLAvaKAIRRI 499
|
170
....*....|....*
gi 446425376 184 -RKEGKTIVVVHHDL 197
Cdd:PRK13409 500 aEEREATALVVDHDI 514
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-223 |
3.93e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.69 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 13 SYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAY-------VPQRSDID 85
Cdd:PRK09700 14 SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAqlgigiiYQELSVID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 86 wdfPITVLDVVLIGTYPSLGMMKRPK---KEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLD 162
Cdd:PRK09700 94 ---ELTVLENLYIGRHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446425376 163 EPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLM-NKSLIHYGEVRQV 223
Cdd:PRK09700 171 EPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMkDGSSVCSGMVSDV 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-224 |
4.25e-20 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 87.85 E-value: 4.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 22 NVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGE---DIRSV------RKSVAYVPQrsdidwD---FP 89
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARGiflpphRRRIGYVFQ------EarlFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 90 -ITVLDVVLIGtypslgmMKRPKKEHRDWAFDCL-KKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVG 167
Cdd:COG4148 91 hLSVRGNLLYG-------RKRAPRAERRISFDEVvELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 168 IDVTSEETIIKILRELRKEGKT-IVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVL 224
Cdd:COG4148 164 LDLARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQgRVVASGPLAEVL 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
4.32e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 86.34 E-value: 4.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIV-KDLFVSYQGNQ--VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYV-----QILGEDIRSVR 72
Cdd:PRK13648 3 DKNSIIVfKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 73 KSVAYVPQRSDIDWDFPITVLDVVLigtypSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARAL 152
Cdd:PRK13648 83 KHIGIVFQNPDNQFVGSIVKYDVAF-----GLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446425376 153 AQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGK-TIVVVHHDLSKA-ESyfDKLLLMNKslihyGEVRQVLEPT 227
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAmEA--DHVIVMNK-----GTVYKEGTPT 227
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
7-224 |
5.40e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 86.04 E-value: 5.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGN---------QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGE-----DIRSVR 72
Cdd:COG4167 7 VRNLSKTFKYRtglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygDYKYRC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 73 KSVAYVPQRSDIDWDFPITV---LDVVLI-GTypSLGMMKRPKKehrdwAFDCLKKVGM-EEFKNRQIGELSGGQQQRVF 147
Cdd:COG4167 87 KHIRMIFQDPNTSLNPRLNIgqiLEEPLRlNT--DLTAEEREER-----IFATLRLVGLlPEHANFYPHMLSSGQKQRVA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 148 LARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVL 224
Cdd:COG4167 160 LARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQgEVVEYGKTAEVF 238
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-225 |
8.74e-20 |
|
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: 87.85 E-value: 8.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 16 GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKavldLIPN----DKGYVQILGEDI-----RSVRKSVAYVPQRSDIdw 86
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVN----LIPRfyepDSGQILLDGHDLadytlASLRRQVALVSQDVVL-- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 87 dFPITVLDVVLIGtypslgmmkRPKKEHRDWAFDCLKKVGMEEFKNR-------QIGE----LSGGQQQRVFLARALAQK 155
Cdd:TIGR02203 418 -FNDTIANNIAYG---------RTEQADRAEIERALAAAYAQDFVDKlplgldtPIGEngvlLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446425376 156 AEIFFLDEPFVGIDVTSEETIIKILRELrKEGKTIVVVHHDLSKAESYfDKLLLMNKS-LIHYGEVRQVLE 225
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTIEKA-DRIVVMDDGrIVERGTHNELLA 556
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-210 |
9.78e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.11 E-value: 9.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 2 GEAIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGyvQILG---------EDIRSVR 72
Cdd:PRK11247 10 GTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--ELLAgtaplaearEDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 73 KSVAYVPqrsdidWDfpiTVLDVVligtypSLGMmkrpKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARAL 152
Cdd:PRK11247 88 QDARLLP------WK---KVIDNV------GLGL----KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 153 AQKAEIFFLDEPFVGID-VTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLM 210
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDaLTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLI 207
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-215 |
9.96e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 85.60 E-value: 9.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILG---------EDIRSVRKSVAYVPQRSDIDWdF 88
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdKYIRPVRKRIGMVFQFPESQL-F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 89 PITVLDVVLIGTyPSLGMmkrPKKEHRDWAFDCLKKVGMEefknRQIGELS-----GGQQQRVFLARALAQKAEIFFLDE 163
Cdd:PRK13646 100 EDTVEREIIFGP-KNFKM---NLDEVKNYAHRLLMDLGFS----RDVMSQSpfqmsGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446425376 164 PFVGIDVTSEETIIKILRELR-KEGKTIVVVHHDLSKAESYFDKLLLMNKSLI 215
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-209 |
1.01e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.09 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 21 QNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAYvpqrsdidwdfpitvlDVVLIGT 100
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQ----------------DLLYLGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 101 YPSLgmmkrpKKE-----------------HRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDE 163
Cdd:PRK13538 82 QPGI------KTEltalenlrfyqrlhgpgDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446425376 164 PFVGIDVTSEETIIKILRE-LRKEGKTIVVVHHDLSKAESYFDKLLL 209
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQhAEQGGMVILTTHQDLPVASDKVRKLRL 202
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-197 |
1.07e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 87.56 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 27 IEKGKLVGIIGPNGAGKSTLMKAVLD-LIPN----------D------KG-----YVQILGE-DIRSVRKsvayvPQRSD 83
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGeLIPNlgdyeeepswDevlkrfRGtelqnYFKKLYNgEIKVVHK-----PQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 IdwdfpitvLDVVLIGTYPSLgMMKRPKKEHRDwafDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDE 163
Cdd:PRK13409 171 L--------IPKVFKGKVREL-LKKVDERGKLD---EVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....
gi 446425376 164 PFVGIDVTSEETIIKILRELrKEGKTIVVVHHDL 197
Cdd:PRK13409 239 PTSYLDIRQRLNVARLIREL-AEGKYVLVVEHDL 271
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-208 |
1.28e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.56 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 2 GEAIIVKDLFV-SYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQilgediRSVRKSVAYVPQ 80
Cdd:COG4178 360 DGALALEDLTLrTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA------RPAGARVLFLPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSDIdwdfPITVLDVVLigTYPSlgmmkrPKKEHRDWAF-DCLKKVGMEEFKNR--------QIgeLSGGQQQRVFLARA 151
Cdd:COG4178 434 RPYL----PLGTLREAL--LYPA------TAEAFSDAELrEALEAVGLGHLAERldeeadwdQV--LSLGEQQRLAFARL 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 152 LAQKAEIFFLDEPFVGIDVTSEETIIKILRElRKEGKTIVVV-HHdlSKAESYFDKLL 208
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVgHR--STLAAFHDRVL 554
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-230 |
1.30e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.12 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 10 LFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI--------RSVRKSVAYVPQ- 80
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnraqrKAFRRDIQMVFQd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 -------RSDIDWdfpitvldvvlIGTYP--SLGMMKRPKKEHRdwAFDCLKKVGM-EEFKNRQIGELSGGQQQRVFLAR 150
Cdd:PRK10419 98 sisavnpRKTVRE-----------IIREPlrHLLSLDKAERLAR--ASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 151 ALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKT-IVVVHHDLSKAESYFDKLLLMNKSLIHygEVRQVLEPTVM 229
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQIV--ETQPVGDKLTF 242
|
.
gi 446425376 230 S 230
Cdd:PRK10419 243 S 243
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-197 |
1.87e-19 |
|
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: 86.76 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 26 DIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQilgEDIRsvrksVAYVPQRsdIDWDFPITV---LDVVLIGTYP 102
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---EDLK-----ISYKPQY--ISPDYDGTVeefLRSANTDDFG 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 103 SlgmmkrpkkehrDWAF-DCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVtsEETII--KI 179
Cdd:COG1245 432 S------------SYYKtEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQRLAvaKA 497
|
170
....*....|....*....
gi 446425376 180 LREL-RKEGKTIVVVHHDL 197
Cdd:COG1245 498 IRRFaENRGKTAMVVDHDI 516
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-210 |
2.04e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.02 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPND---KGYVQILGE--DIRSVRKSVAYVPQRsdiDWDFP-IT 91
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMpiDAKEMRAISAYVQQD---DLFIPtLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 92 VLDVVligTYPSLGMMKR--PKKEHRDWAFDCLKKVGMEEFKNRQIGE------LSGGQQQRVFLARALAQKAEIFFLDE 163
Cdd:TIGR00955 116 VREHL---MFQAHLRMPRrvTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446425376 164 PFVGIDVTSEETIIKILRELRKEGKTIVV-VHHDLSKAESYFDKLLLM 210
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICtIHQPSSELFELFDKIILM 240
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-224 |
5.59e-19 |
|
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: 85.56 E-value: 5.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQ-GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV-----RKSVAYV 78
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIdrhtlRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 79 PQRSDIdwdFPITVLDVVLIGTypslgmmkRPKKEHRDWAFDCLKKVGMEEFKNRQIG----------ELSGGQQQRVFL 148
Cdd:TIGR01193 554 PQEPYI---FSGSILENLLLGA--------KENVSQDEIWAACEIAEIKDDIENMPLGyqtelseegsSISGGQKQRIAL 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446425376 149 ARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKegKTIVVVHHDLSKAESYfDKLLLMNK-SLIHYGEVRQVL 224
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQS-DKIIVLDHgKIIEQGSHDELL 696
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
15-210 |
6.04e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.35 E-value: 6.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 15 QGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGE--DIRS----VRKSVAYVPQRSDIDWDF 88
Cdd:PRK11288 264 KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSprdaIRAGIMLCPEDRKAEGII 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 89 PI-TVLDVVLIGT---YPSLGMMKRPKKEhRDWAFDCLKKVGMEEFKNRQ-IGELSGGQQQRVFLARALAQKAEIFFLDE 163
Cdd:PRK11288 344 PVhSVADNINISArrhHLRAGCLINNRWE-AENADRFIRSLNIKTPSREQlIMNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446425376 164 PFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLM 210
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVM 469
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-206 |
7.37e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.62 E-value: 7.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI------RSVRKSVAYVPQRSDIdwdFP-I 90
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwqtaKIMREAVAIVPEGRRV---FSrM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 91 TVLDVVLIGTYpslgMMKRPKKEHR-DWAFDCLKKvgMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGID 169
Cdd:PRK11614 96 TVEENLAMGGF----FAERDQFQERiKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLA 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 446425376 170 VTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDK 206
Cdd:PRK11614 170 PIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADR 206
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-198 |
8.05e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 85.15 E-value: 8.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQVV-QNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS-----VRKSVAY 77
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlshsvLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSdidwdfpitvldVVLIGTYPSLGMMKRPKKEHRDWafDCLKKV-------GMEEFKNRQIGE----LSGGQQQRV 146
Cdd:PRK10790 420 VQQDP------------VVLADTFLANVTLGRDISEEQVW--QALETVqlaelarSLPDGLYTPLGEqgnnLSVGQKQLL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446425376 147 FLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEgKTIVVVHHDLS 198
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLS 536
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-222 |
1.64e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 84.40 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQ---VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVL-DLIPNDKGYVQIlgedirsvRKSVAYVP 79
Cdd:PLN03130 614 AISIKNGYFSWDSKAerpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLgELPPRSDASVVI--------RGTVAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 QrsdIDWDFPITVLDVVLIGTypslgMMKRPKKE--------HRDwaFDCLKKVGMEEfknrqIGE----LSGGQQQRVF 147
Cdd:PLN03130 686 Q---VSWIFNATVRDNILFGS-----PFDPERYEraidvtalQHD--LDLLPGGDLTE-----IGErgvnISGGQKQRVS 750
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 148 LARALAQKAEIFFLDEPFVGID--VTSE--ETIIKilRELRkeGKTIVVVHHDLSKAeSYFDKLLlmnksLIHYGEVRQ 222
Cdd:PLN03130 751 MARAVYSNSDVYIFDDPLSALDahVGRQvfDKCIK--DELR--GKTRVLVTNQLHFL-SQVDRII-----LVHEGMIKE 819
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-197 |
2.69e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.44 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 6 IVKdlfvSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPND--KGYVQILGEDIR--SVRKS------- 74
Cdd:PRK13549 11 ITK----TFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQasNIRDTeragiai 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 75 ----VAYVPQrsdidwdfpITVLDVVLIGTYPS-LGMMKRPKKEHRdwAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLA 149
Cdd:PRK13549 87 ihqeLALVKE---------LSVLENIFLGNEITpGGIMDYDAMYLR--AQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446425376 150 RALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDL 197
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKL 203
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-212 |
2.87e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 81.29 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 17 NQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI-------RSvrKSVAYVPQrsDidwdfP 89
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpeykRA--KYIGRVFQ--D-----P 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 90 itvldvvLIGTYPSL----------------GMMKRPKKEHRDWAFDCLKKVGMeEFKNR---QIGELSGGQQQRVFLAR 150
Cdd:COG1101 90 -------MMGTAPSMtieenlalayrrgkrrGLRRGLTKKRRELFRELLATLGL-GLENRldtKVGLLSGGQRQALSLLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446425376 151 ALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGK-TIVVVHHDLSKAESYFDKLLLMNK 212
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRLIMMHE 224
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-196 |
5.09e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 82.86 E-value: 5.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQIlGEdirSVRksVAYVPQ-RSD 83
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE---TVK--LAYVDQsRDA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 IDWDfpITV-------LDVVLIGTY--PSlgmmkRpkkehrdwAFdclkkVGMEEFK----NRQIGELSGGQQQRVFLAR 150
Cdd:PRK11819 399 LDPN--KTVweeisggLDIIKVGNReiPS-----R--------AY-----VGRFNFKggdqQKKVGVLSGGERNRLHLAK 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446425376 151 ALAQKAEIFFLDEPFVGIDVtseETiikiLRELrkE------GKTIVVVHHD 196
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLDV---ET----LRAL--EeallefPGCAVVISHD 501
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-201 |
9.24e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 79.05 E-value: 9.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI-----RSVRKSVAYVPQRSDIdwdFPITV 92
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsqyehKYLHSKVSLVGQEPVL---FARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 93 LDVVLIG-TYPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVT 171
Cdd:cd03248 105 QDNIAYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190
....*....|....*....|....*....|
gi 446425376 172 SEETIIKILRElRKEGKTIVVVHHDLSKAE 201
Cdd:cd03248 185 SEQQVQQALYD-WPERRTVLVIAHRLSTVE 213
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
16-222 |
9.29e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.15 E-value: 9.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 16 GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSvaYVP-QRSDIDWDFP----- 89
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNR--EVPfLRRQIGMIFQdhhll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 90 --ITVLDVVLIgtypSLGMMKRPKKEHRDWAFDCLKKVGM-EEFKNRQIgELSGGQQQRVFLARALAQKAEIFFLDEPFV 166
Cdd:PRK10908 92 mdRTVYDNVAI----PLIIAGASGDDIRRRVSAALDKVGLlDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 167 GIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLIHYGEVRQ 222
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-198 |
1.17e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.55 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGN-QVVQNVSFDIEKGKLVGIIGPNGAGKST---LMKAVLDliPnDKGYVQILGEDIRSV-----RKS 74
Cdd:PRK13657 334 AVEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTlinLLQRVFD--P-QSGRILIDGTDIRTVtraslRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 75 VAYVPQRSDIdwdFPITVLDVVLIGtypslgmmkRPKKEHRDwAFDCLKKVGMEEFKNRQ-------IGE----LSGGQQ 143
Cdd:PRK13657 411 IAVVFQDAGL---FNRSIEDNIRVG---------RPDATDEE-MRAAAERAQAHDFIERKpdgydtvVGErgrqLSGGER 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 144 QRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKeGKTIVVVHHDLS 198
Cdd:PRK13657 478 QRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLS 531
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-198 |
1.35e-17 |
|
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: 81.40 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 13 SYQGN-QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR-----SVRKSVAYVPQrsdidw 86
Cdd:COG5265 366 GYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRdvtqaSLRAAIGIVPQ------ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 87 dfpitvlDVVL--------IGtYPslgmmkRP---KKEHRDWAfdclKKVGMEEFKNR-------QIGE----LSGGQQQ 144
Cdd:COG5265 440 -------DTVLfndtiaynIA-YG------RPdasEEEVEAAA----RAAQIHDFIESlpdgydtRVGErglkLSGGEKQ 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446425376 145 RVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKeGKTIVVVHHDLS 198
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHRLS 554
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
15-200 |
1.50e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.67 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 15 QGNQ---VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVR---------KSVAYVPQrs 82
Cdd:PRK10584 18 QGEHelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearaklraKHVGFVFQ-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 83 didwdfpitvlDVVLIGTYPSLGMMKRP-------KKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQK 155
Cdd:PRK10584 96 -----------SFMLIPTLNALENVELPallrgesSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446425376 156 AEIFFLDEPFVGIDVTSEETIIKILREL-RKEGKTIVVVHHDLSKA 200
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLA 210
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-195 |
1.64e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 80.23 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGN----QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI--------RSVR 72
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsekelRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 73 KSVAYVPQ-------RsdidwdfpiTVLDVVligTYPsLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQR 145
Cdd:PRK11153 82 RQIGMIFQhfnllssR---------TVFDNV---ALP-LELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446425376 146 VFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHH 195
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITH 199
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-231 |
1.94e-17 |
|
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: 81.50 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 13 SYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVL-DLIPNDkgyvqilGEDIRSVRksVAYVPQRSdidWDFPIT 91
Cdd:TIGR01271 435 SLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMgELEPSE-------GKIKHSGR--ISFSPQTS---WIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 92 VLDVVLIG-TYpslgmmkrpkKEHRdwAFDCLKKVGMEE----FKNRQ---IGE----LSGGQQQRVFLARALAQKAEIF 159
Cdd:TIGR01271 503 IKDNIIFGlSY----------DEYR--YTSVIKACQLEEdialFPEKDktvLGEggitLSGGQRARISLARAVYKDADLY 570
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLIHYGEVR--QVLEPTVMSK 231
Cdd:TIGR01271 571 LLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSelQAKRPDFSSL 644
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-207 |
2.52e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 80.64 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 6 IVKDlfvsYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPND--KGYVQILGEDIRSV------RKSVAY 77
Cdd:TIGR02633 7 IVKT----FGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASnirdteRAGIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSDIDWDfpITVLDVVLIG---TYPSlGMMKRPKKEHRdwAFDCLKKVGMEEFKN-RQIGELSGGQQQRVFLARALA 153
Cdd:TIGR02633 83 IHQELTLVPE--LSVAENIFLGneiTLPG-GRMAYNAMYLR--AKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446425376 154 QKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKL 207
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTI 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-198 |
2.66e-17 |
|
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: 81.15 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 20 VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGedirsvrkSVAYVPQRSDIDWDfpiTVLDVVLIG 99
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------SVAYVPQQAWIQND---SLRENILFG 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 100 TypslgMMKRPKKEHRDWAFDCLKKVGMEEFKNR-QIGE----LSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEE 174
Cdd:TIGR00957 723 K-----ALNEKYYQQVLEACALLPDLEILPSGDRtEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180
....*....|....*....|....*.
gi 446425376 175 TIIK--ILRELRKEGKTIVVVHHDLS 198
Cdd:TIGR00957 798 HIFEhvIGPEGVLKNKTRILVTHGIS 823
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
5-197 |
2.69e-17 |
|
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: 77.76 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGN-QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYV--------QILGEDIRSV-RKS 74
Cdd:cd03290 1 VQVTNGYFSWGSGlATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesEPSFEATRSRnRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 75 VAYVPQRSdidWDFPITVLDVVLIGTypslGMMKRPKKEHRDwAFDCLKKVGMEEFKNR-QIGE----LSGGQQQRVFLA 149
Cdd:cd03290 81 VAYAAQKP---WLLNATVEENITFGS----PFNKQRYKAVTD-ACSLQPDIDLLPFGDQtEIGErginLSGGQRQRICVA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446425376 150 RALAQKAEIFFLDEPFVGIDVTSEETIIK--ILRELRKEGKTIVVVHHDL 197
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKL 202
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-215 |
4.76e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.41 E-value: 4.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQG---NQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVL-DLIPNDKGYVQIlgedirsvRKSVAYVP 79
Cdd:PLN03232 614 AISIKNGYFSWDSktsKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLgELSHAETSSVVI--------RGSVAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 QrsdIDWDFPITVLDVVLIGT-YPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIgELSGGQQQRVFLARALAQKAEI 158
Cdd:PLN03232 686 Q---VSWIFNATVRENILFGSdFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGV-NISGGQKQRVSMARAVYSNSDI 761
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 159 FFLDEPFVGIDVTSEETIIK--ILRELRkeGKTIVVVHHDLSKAeSYFDKLLLMNKSLI 215
Cdd:PLN03232 762 YIFDDPLSALDAHVAHQVFDscMKDELK--GKTRVLVTNQLHFL-PLMDRIILVSEGMI 817
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-210 |
5.58e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 79.75 E-value: 5.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSY----QGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKgyVQILGEDIRSVRKSVAYVPQRS 82
Cdd:PRK15134 8 IENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPP--VVYPSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 83 -------DIDWDF--------PITVLDVVLigtYPSL----GMMKRPKkehRDWAFDCLKKVGMEEFKNRQIG---ELSG 140
Cdd:PRK15134 86 lrgvrgnKIAMIFqepmvslnPLHTLEKQL---YEVLslhrGMRREAA---RGEILNCLDRVGIRQAAKRLTDyphQLSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446425376 141 GQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLM 210
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVM 230
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-195 |
5.65e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.41 E-value: 5.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDlIPN---DKGYVQILGEDI-------RSvRKSVA 76
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HPKyevTSGSILLDGEDIlelspdeRA-RAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 77 YV---PQRsdidwdFP-ITVLDVVligtypSLGMMKRPKKEHRDWAF-----DCLKKVGM-EEFKNRQIGE-LSGGQQQR 145
Cdd:COG0396 81 LAfqyPVE------IPgVSVSNFL------RTALNARRGEELSAREFlkllkEKMKELGLdEDFLDRYVNEgFSGGEKKR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446425376 146 VFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHH 195
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH 198
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-182 |
7.12e-17 |
|
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: 79.57 E-value: 7.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 2 GEAIIVKDLFVSYQ--GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIpNDKGYVQILGEDIRSV-----RKS 74
Cdd:TIGR01271 1215 GGQMDVQGLTAKYTeaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVtlqtwRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 75 VAYVPQRSdidwdfpitvldVVLIGTYpslgmmKRPKKEHRDWAFDCLKKVGmEEFKNRQIGE----------------L 138
Cdd:TIGR01271 1294 FGVIPQKV------------FIFSGTF------RKNLDPYEQWSDEEIWKVA-EEVGLKSVIEqfpdkldfvlvdggyvL 1354
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446425376 139 SGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRE 182
Cdd:TIGR01271 1355 SNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-196 |
7.21e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.54 E-value: 7.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 3 EAIIVKDLF-VSYQGNQ--VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGyvqilgedirsvrKSVAYVP 79
Cdd:COG2401 26 RVAIVLEAFgVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV-------------AGCVDVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 qrsDIDWDFPITVLDVVLIgtypslgmmKRPKKEhrdwAFDCLKKVGMEE--FKNRQIGELSGGQQQRVFLARALAQKAE 157
Cdd:COG2401 93 ---DNQFGREASLIDAIGR---------KGDFKD----AVELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446425376 158 IFFLDEPFVGID-VTSEETIIKILRELRKEGKTIVVV-HHD 196
Cdd:COG2401 157 LLVIDEFCSHLDrQTAKRVARNLQKLARRAGITLVVAtHHY 197
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-221 |
7.37e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.10 E-value: 7.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 20 VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPND-KGYVQILGE--DIR----SVRKSVAYVPQRSDIDWDFPItv 92
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRnpaqAIRAGIAMVPEDRKRHGIVPI-- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 93 ldvVLIGTYPSLGMMKRPKKEHR-DWA--FDCLKKvGMEEFKNRQ------IGELSGGQQQRVFLARALAQKAEIFFLDE 163
Cdd:TIGR02633 354 ---LGVGKNITLSVLKSFCFKMRiDAAaeLQIIGS-AIQRLKVKTaspflpIGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 164 PFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMnksliHYGEVR 221
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVI-----GEGKLK 482
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-210 |
2.02e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.93 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGED--------IRSVRKSVAYVPQ--------R 81
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDllkadpeaQKLLRQKIQIVFQnpygslnpR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 82 SDIDwdfpiTVL-DVVLIGTypSLGmmkrpKKEHRDWAFDCLKKVGME-EFKNRQIGELSGGQQQRVFLARALAQKAEIF 159
Cdd:PRK11308 109 KKVG-----QILeEPLLINT--SLS-----AAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLM 210
Cdd:PRK11308 177 VADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVM 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-196 |
2.38e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.52 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 12 VSYQ--GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV-----RKSVAYVPQRSDI 84
Cdd:PRK10247 13 VGYLagDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLkpeiyRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 85 dwdFPITVLDvVLIGTYPSLGMMKRPKKEHRDwafdcLKKVGM-EEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDE 163
Cdd:PRK10247 93 ---FGDTVYD-NLIFPWQIRNQQPDPAIFLDD-----LERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190
....*....|....*....|....*....|....
gi 446425376 164 PFVGIDVTSEETIIKIL-RELRKEGKTIVVVHHD 196
Cdd:PRK10247 164 ITSALDESNKHNVNEIIhRYVREQNIAVLWVTHD 197
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-221 |
2.51e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.66 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 19 VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDK-GYVQILGE--DIRSVRKSV----AYVPQrsDIDWDFPIT 91
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKpvKIRNPQQAIaqgiAMVPE--DRKRDGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 92 VLDVVLIGTYPSLGMMKRPKKEHRDWAFDCLKKvGMEEFKNR------QIGELSGGQQQRVFLARALAQKAEIFFLDEPF 165
Cdd:PRK13549 355 VMGVGKNITLAALDRFTGGSRIDDAAELKTILE-SIQRLKVKtaspelAIARLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 166 VGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMnksliHYGEVR 221
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVM-----HEGKLK 484
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-230 |
2.77e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.40 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 22 NVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS------VRKSVAYVP---QRSDIDWDFPITV 92
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAlstaqrLARGLVYLPedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 93 LDVVLigTYPSLGMMKRPKKE-------HRDWAFDClkkvgmeEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPF 165
Cdd:PRK15439 361 NVCAL--THNRRGFWIKPAREnavleryRRALNIKF-------NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 166 VGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMnksliHYGEVRQVLEPTVMS 230
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVM-----HQGEISGALTGAAIN 491
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-198 |
3.29e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 76.32 E-value: 3.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 20 VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIpNDKGYV-----QILGEDIRSV-----RKSVAyvpqrSDIDWDF- 88
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLI-DYPGRVmaeklEFNGQDLQRIsekerRNLVG-----AEVAMIFq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 89 -PITVLDVVLIGTYPSLGMMKR----PKKEHRDWAFDCLKKVGMEEFKNR---QIGELSGGQQQRVFLARALAQKAEIFF 160
Cdd:PRK11022 97 dPMTSLNPCYTVGFQIMEAIKVhqggNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 446425376 161 LDEPFVGIDVTSEETIIKILREL-RKEGKTIVVVHHDLS 198
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLA 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-225 |
3.38e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.59 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 20 VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSvAYVPQRSDIDWDF--PITVLDVVL 97
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPG-KLQALRRDIQFIFqdPYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 98 IGTYPSLGMMK----RPKKEHRDWAFDCLKKVGME-EFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTS 172
Cdd:PRK10261 419 TVGDSIMEPLRvhglLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 173 EETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVLE 225
Cdd:PRK10261 499 RGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLgQIVEIGPRRAVFE 553
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-225 |
3.94e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.15 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 20 VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQIL-----------GEDIRS-VRKSVAYVPQRSDIdwd 87
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkpGPDGRGrAKRYIGILHQEYDL--- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 88 FP-ITVLDVVL--IG-TYP-SLGMMKrpkkehrdwAFDCLKKVGMEEFKNRQI-----GELSGGQQQRVFLARALAQKAE 157
Cdd:TIGR03269 377 YPhRTVLDNLTeaIGlELPdELARMK---------AVITLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVLIKEPR 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 158 IFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLM-NKSLIHYGEVRQVLE 225
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMrDGKIVKIGDPEEIVE 517
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-195 |
3.95e-16 |
|
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: 74.10 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDlIPN---DKGYVQILGEDIRsvrksvayvpqrsd 83
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKyevTEGEILFKGEDIT-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 idwDFPITvlDVVLIGtypsLGMM-KRPKKehrdwafdcLKKVGMEEFKnRQIGE-LSGGQQQRVFLARALAQKAEIFFL 161
Cdd:cd03217 68 ---DLPPE--ERARLG----IFLAfQYPPE---------IPGVKNADFL-RYVNEgFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190
....*....|....*....|....*....|....
gi 446425376 162 DEPFVGIDVTSEETIIKILRELRKEGKTIVVVHH 195
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-216 |
4.15e-16 |
|
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: 77.36 E-value: 4.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQ--GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS----VRKSVAY 77
Cdd:TIGR01257 928 GVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETnldaVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRSDIDwdFPITVLDVVLIgtYPSLgmMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAE 157
Cdd:TIGR01257 1008 CPQHNILF--HHLTVAEHILF--YAQL--KGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 158 IFFLDEPFVGIDVTSEETIIKILRELRkEGKTIVVVHHDLSKAESYFDKLLLMNKSLIH 216
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLY 1139
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-182 |
5.16e-16 |
|
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: 75.28 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQ--GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIpNDKGYVQILGEDIRSV-----RKSVAY 77
Cdd:cd03289 3 MTVKDLTAKYTegGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVplqkwRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRsdidwdfpitvldvVLIGTypslGMMKRPKKEHRDWAFDCLKKVGmEEFKNRQIGE----------------LSGG 141
Cdd:cd03289 82 IPQK--------------VFIFS----GTFRKNLDPYGKWSDEEIWKVA-EEVGLKSVIEqfpgqldfvlvdggcvLSHG 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446425376 142 QQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRE 182
Cdd:cd03289 143 HKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ 183
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
7-227 |
5.84e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 75.92 E-value: 5.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQ---GN-QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPND---KGYVQILGEDI-----RSVRKS 74
Cdd:PRK09473 15 VKDLRVTFStpdGDvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlnlpeKELNKL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 75 VAyvPQRSDIDWDfPITVLDvvligTYPSLG-------MMKR--PKKEHRDWAFDCLKKVGMEEFKNRqIG----ELSGG 141
Cdd:PRK09473 95 RA--EQISMIFQD-PMTSLN-----PYMRVGeqlmevlMLHKgmSKAEAFEESVRMLDAVKMPEARKR-MKmyphEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 142 QQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKT-IVVVHHDLSKAESYFDKLLLMNKS-LIHYGE 219
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGrTMEYGN 245
|
....*....
gi 446425376 220 VRQVL-EPT 227
Cdd:PRK09473 246 ARDVFyQPS 254
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-225 |
8.48e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 76.29 E-value: 8.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 13 SYQGNQ--VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGyvQILGEDIR-------SVRKSVAYVPQRSD 83
Cdd:PRK10789 322 TYPQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG--DIRFHDIPltklqldSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 IdwdFPITVLDVVLIG----TYPSLGMMKRPKKEHRDwafdCLKkvgMEEFKNRQIGE----LSGGQQQRVFLARALAQK 155
Cdd:PRK10789 400 L---FSDTVANNIALGrpdaTQQEIEHVARLASVHDD----ILR---LPQGYDTEVGErgvmLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446425376 156 AEIFFLDEPFVGIDVTSEETIIKILRELRkEGKTIVVVHHDLSkAESYFDKLLLMNK-SLIHYGEVRQVLE 225
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLS-ALTEASEILVMQHgHIAQRGNHDQLAQ 538
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-210 |
9.40e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.81 E-value: 9.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 20 VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI--RS----VRKSVAYVPQ--RSD-------I 84
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtRSpqdgLANGIVYISEdrKRDglvlgmsV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 85 DWDFPITVLDvvligtYPSLGMMKRPKKEHRDWAFDC-----LKKVGMEEfknrQIGELSGGQQQRVFLARALAQKAEIF 159
Cdd:PRK10762 348 KENMSLTALR------YFSRAGGSLKHADEQQAVSDFirlfnIKTPSMEQ----AIGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLM 210
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVM 468
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-226 |
9.78e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.66 E-value: 9.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVqILGE-----------DIRSVRKSVAYVPQRSDIDW 86
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVGDyaipanlkkikEVKRLRKEIGLVFQFPEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 87 dFPITVLDVVLIGTYpSLGmmkRPKKEHRDWAFDCLKKVGM-EEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPF 165
Cdd:PRK13645 104 -FQETIEKDIAFGPV-NLG---ENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446425376 166 VGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMnksliHYGEVRQVLEP 226
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVM-----HEGKVISIGSP 235
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
13-218 |
1.50e-15 |
|
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: 74.12 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 13 SYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEdirsvrksVAYVPQRSdidWDFPITV 92
Cdd:cd03291 46 CLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------ISFSSQFS---WIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 93 LDVVLIGT----YPSLGMMKRPKKEHrdwafDCLKkvgMEEFKNRQIGE----LSGGQQQRVFLARALAQKAEIFFLDEP 164
Cdd:cd03291 115 KENIIFGVsydeYRYKSVVKACQLEE-----DITK---FPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 165 FVGIDVTSEETII-KILRELRKEGKTIVV---VHHdLSKAesyfDK-LLLMNKSLIHYG 218
Cdd:cd03291 187 FGYLDVFTEKEIFeSCVCKLMANKTRILVtskMEH-LKKA----DKiLILHEGSSYFYG 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-197 |
1.82e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.13 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSY---QG--------NQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIpNDKGYVQILGEDIRSVRKSv 75
Cdd:PRK15134 278 VEQLQVAFpirKGilkrtvdhNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRR- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 76 AYVPQRSDIDWDFP---------ITVLDVVLIGT---YPSLGMMKRpkkEHRdwAFDCLKKVGME-EFKNRQIGELSGGQ 142
Cdd:PRK15134 356 QLLPVRHRIQVVFQdpnsslnprLNVLQIIEEGLrvhQPTLSAAQR---EQQ--VIAVMEEVGLDpETRHRYPAEFSGGQ 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 143 QQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGK-TIVVVHHDL 197
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDL 486
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-198 |
4.46e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.22 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 21 QNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIrsvrksVAYVPQrsDIDWDFPITVLDVV---- 96
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLI------VARLQQ--DPPRNVEGTVYDFVaegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 97 ---------------LIGTYPSLGMMKRPKK-----EHRD-WAFD-----CLKKVGMEefKNRQIGELSGGQQQRVFLAR 150
Cdd:PRK11147 92 eeqaeylkryhdishLVETDPSEKNLNELAKlqeqlDHHNlWQLEnrineVLAQLGLD--PDAALSSLSGGWLRKAALGR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446425376 151 ALAQKAEIFFLDEPFVGIDVTSeetiIKILRELRKEGK-TIVVVHHDLS 198
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQgSIIFISHDRS 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-197 |
5.89e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 5.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAY------VPQ 80
Cdd:PRK15439 14 ARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHqlgiylVPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 81 RSDIdwdFP-ITVLDVVLigtypsLGMMKRPKKEHRDWAFdcLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIF 159
Cdd:PRK15439 94 EPLL---FPnLSVKENIL------FGLPKRQASMQKMKQL--LAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDL 197
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKL 200
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-218 |
6.00e-15 |
|
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: 70.74 E-value: 6.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLmkavLDLIPNDK------GYVQILGEDIR-SVRKSVAYVPQrSDIDWDFpI 90
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTL----LDVLAGRKtagvitGEILINGRPLDkNFQRSTGYVEQ-QDVHSPN-L 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 91 TVLDVVLIGTypslgmmkrpkkehrdwafdCLKkvgmeefknrqigELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDV 170
Cdd:cd03232 95 TVREALRFSA--------------------LLR-------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446425376 171 TSEETIIKILRELRKEGKTIVVVHHDLSKAE-SYFDKLLLMNKS--LIHYG 218
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQAILCTIHQPSASIfEKFDRLLLLKRGgkTVYFG 192
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-226 |
7.32e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.14 E-value: 7.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGE---DIRSVRKSVAYVPQR 81
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 82 SDIdwdFP-ITVLDVVligtypSLGM-MKRPKKEHRDwafdclKKVG-------MEEFKNRQIGELSGGQQQRVFLARAL 152
Cdd:PRK11000 84 YAL---YPhLSVAENM------SFGLkLAGAKKEEIN------QRVNqvaevlqLAHLLDRKPKALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 153 AQKAEIFFLDEPFVGIDVTSE-ETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKslihyGEVRQVLEP 226
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRvQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDA-----GRVAQVGKP 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
13-197 |
7.92e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 7.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 13 SYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGED-------------IRSVRKSVAYVP 79
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEvtfngpkssqeagIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 QrsdidwdfpITVLDVVLIGTYPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIF 159
Cdd:PRK10762 93 Q---------LTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDL 197
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRL 201
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-210 |
2.39e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.68 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 20 VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIR------SVRKSVAYVPQ--RS-------DI 84
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhnaneAINHGFALVTEerRStgiyaylDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 85 DWDFPITVLDVVLigtyPSLGMMKRPK-KEHRDWAFDCLKkVGMEEFKNrQIGELSGGQQQRVFLARALAQKAEIFFLDE 163
Cdd:PRK10982 344 GFNSLISNIRNYK----NKVGLLDNSRmKSDTQWVIDSMR-VKTPGHRT-QIGSLSGGNQQKVIIGRWLLTQPEILMLDE 417
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446425376 164 PFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLM 210
Cdd:PRK10982 418 PTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVM 464
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-224 |
2.53e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 70.34 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAYVPQRSDI-- 84
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRRLlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 85 -DWDFpitvldvvlIGTYPSLGM--------------M---KRPKKEHRDWAFDCLKKVgmeEFKNRQIGEL----SGGQ 142
Cdd:PRK11701 89 tEWGF---------VHQHPRDGLrmqvsaggnigerlMavgARHYGDIRATAGDWLERV---EIDAARIDDLpttfSGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 143 QQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNKS-LIHYGEV 220
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGrVVESGLT 236
|
....
gi 446425376 221 RQVL 224
Cdd:PRK11701 237 DQVL 240
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-169 |
9.55e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.15 E-value: 9.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 14 YQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLmkavLDLIPNDK----GYVQILGEDIRS--VRKSV----AYVPQrsd 83
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSL----LSLIAGARkiqqGRVEVLGGDMADarHRRAVcpriAYMPQ--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 idwdfpitvldvvliG----TYPSL-------------GMmkrPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRV 146
Cdd:NF033858 84 ---------------GlgknLYPTLsvfenldffgrlfGQ---DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKL 145
|
170 180
....*....|....*....|...
gi 446425376 147 FLARALAQKAEIFFLDEPFVGID 169
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVD 168
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
13-195 |
1.16e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.76 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 13 SYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI------RSVRKSVAYVPQrsDIDW 86
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskEALENGISMVHQ--ELNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 87 DFPITVLDVVLIGTYPSLGMMKRPKKEHRDwAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFV 166
Cdd:PRK10982 85 VLQRSVMDNMWLGRYPTKGMFVDQDKMYRD-TKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180
....*....|....*....|....*....
gi 446425376 167 GIDVTSEETIIKILRELRKEGKTIVVVHH 195
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKLKERGCGIVYISH 192
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
21-196 |
1.23e-13 |
|
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: 68.05 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 21 QNVSFDIEKGKLVGIIGPNGAGKSTLmkaVLDLI--PNDKGYVQILGEDIRSvrksvaYVPQRSDIDWDFpITVLDVVL- 97
Cdd:cd03270 12 KNVDVDIPRNKLVVITGVSGSGKSSL---AFDTIyaEGQRRYVESLSAYARQ------FLGQMDKPDVDS-IEGLSPAIa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 98 -------------IGT-----------YPSLGMMKRpkkehrdwaFDCLKKVGMEEFK-NRQIGELSGGQQQRVFLARAL 152
Cdd:cd03270 82 idqkttsrnprstVGTvteiydylrllFARVGIRER---------LGFLVDVGLGYLTlSRSAPTLSGGEAQRIRLATQI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446425376 153 AQKAE--IFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHD 196
Cdd:cd03270 153 GSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD 198
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-220 |
1.86e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.89 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGyvQILGEDIRSVRKSVAYVPQRSDIDWDFPIT------ 91
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSG--ELLIDDHPLHFGDYSYRSQRIRMIFQDPSTslnprq 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 92 ----VLDVVLIgTYPSLGMMKRPKKehrdwAFDCLKKVGM-EEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFV 166
Cdd:PRK15112 105 risqILDFPLR-LNTDLEPEQREKQ-----IIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 167 GIDVTSEETIIKILRELR-KEGKTIVVVHHDLSKAESYFDKLLLMnksliHYGEV 220
Cdd:PRK15112 179 SLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVM-----HQGEV 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-197 |
2.12e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.42 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 19 VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVqiLGEdirsvrKSVAYVPQRSdidWDFPITVLDVVLI 98
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--WAE------RSIAYVPQQA---WIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 99 GT---YPSLGMMKRPKKEHRDWAfdcLKKVGMEEfknrQIGE----LSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVT 171
Cdd:PTZ00243 744 FDeedAARLADAVRVSQLEADLA---QLGGGLET----EIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180
....*....|....*....|....*...
gi 446425376 172 SEETIIK--ILRELRkeGKTIVVVHHDL 197
Cdd:PTZ00243 817 VGERVVEecFLGALA--GKTRVLATHQV 842
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-218 |
2.44e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 66.52 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPndkGYVQILG----------EDIRS 70
Cdd:cd03233 4 LSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---GNVSVEGdihyngipykEFAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 71 VRKSVAYVPQRsdiDWDFP-ITVldvvligtypslgmmkrpkKEHRDWAFDCLKkvgmeefkNRQIGELSGGQQQRVFLA 149
Cdd:cd03233 81 YPGEIIYVSEE---DVHFPtLTV-------------------RETLDFALRCKG--------NEFVRGISGGERKRVSIA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446425376 150 RALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVhhDLSKA--ESY--FDKLLLMNKS-LIHYG 218
Cdd:cd03233 131 EALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFV--SLYQAsdEIYdlFDKVLVLYEGrQIYYG 202
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-198 |
2.63e-13 |
|
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: 66.19 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 20 VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDlipndkgyvqilgediRSVRKSVAYVPQRSDidwDFPITVLDvvlig 99
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----------------ASGKARLISFLPKFS---RNKLIFID----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 100 typSLGMmkrpkkehrdwafdcLKKVGMEEFK-NRQIGELSGGQQQRVFLARALAQKAE--IFFLDEPFVGIDVTSEETI 176
Cdd:cd03238 67 ---QLQF---------------LIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQL 128
|
170 180
....*....|....*....|..
gi 446425376 177 IKILRELRKEGKTIVVVHHDLS 198
Cdd:cd03238 129 LEVIKGLIDLGNTVILIEHNLD 150
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
7-222 |
2.72e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 68.76 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQ---VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGedirsvrkSVAYVPQRSD 83
Cdd:PRK13545 24 LKDLFFRSKDGEyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--------SAALIAISSG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 IDWDFpITVLDVVLIGTypslgMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDE 163
Cdd:PRK13545 96 LNGQL-TGIENIELKGL-----MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 164 PFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLlmnksLIHYGEVRQ 222
Cdd:PRK13545 170 ALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKAL-----WLHYGQVKE 223
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
9-212 |
5.81e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.98 E-value: 5.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 9 DLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGED---IRSVRKSVAYVPQRsdiD 85
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNrkpTKQILKRTGFVTQD---D 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 86 WDFP-ITVLDVVLIgtypsLGMMKRPKKEHRD----WAFDCLKKVGMEEFKNRQIGE-----LSGGQQQRVFLARALAQK 155
Cdd:PLN03211 150 ILYPhLTVRETLVF-----CSLLRLPKSLTKQekilVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLIN 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 156 AEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVV-VHHDLSKAESYFDKLLLMNK 212
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSE 282
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-207 |
5.91e-13 |
|
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: 65.29 E-value: 5.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 26 DIEKGKLVGIIGPNGAGKSTLMKAVL-DLIPNDkgyvqilgEDIRSVRKSVAYVPQRSDidwdfpitvldvvligtypsl 104
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAgQLIPNG--------DNDEWDGITPVYKPQYID--------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 105 gmmkrpkkehrdwafdclkkvgmeefknrqigeLSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELR 184
Cdd:cd03222 72 ---------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180
....*....|....*....|....
gi 446425376 185 KEG-KTIVVVHHDLSKAESYFDKL 207
Cdd:cd03222 119 EEGkKTALVVEHDLAVLDYLSDRI 142
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-222 |
5.96e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.21 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIpnDKGYVQilgEDIR---------SVRKSVAYVpQRSDIDWDf 88
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVIT---GGDRlvngrpldsSFQRSIGYV-QQQDLHLP- 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 89 PITVLDVVLIGTYpslgmMKRP----KKEHRDWAFDCLKKVGMEEFKNRQIGE----LSGGQQQRVFLARALAQKAE-IF 159
Cdd:TIGR00956 850 TSTVRESLRFSAY-----LRQPksvsKSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKlLL 924
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSK---AEsyFDKLLLMNK--SLIHYGEVRQ 222
Cdd:TIGR00956 925 FLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAilfEE--FDRLLLLQKggQTVYFGDLGE 990
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-194 |
6.37e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.08 E-value: 6.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 19 VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI-----RSVRKSVAYVPQRSdidwdfpitvl 93
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVakfglTDLRRVLSIIPQSP----------- 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 94 dVVLIGTypsLGMMKRPKKEHRD---WafDCLKKVGMEEFKNR-------QIGE----LSGGQQQRVFLARALAQKAEIF 159
Cdd:PLN03232 1320 -VLFSGT---VRFNIDPFSEHNDadlW--EALERAHIKDVIDRnpfgldaEVSEggenFSVGQRQLLSLARALLRRSKIL 1393
|
170 180 190
....*....|....*....|....*....|....*
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVH 194
Cdd:PLN03232 1394 VLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAH 1428
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-194 |
1.06e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.46 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGN--QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRS-----VRKSVA 76
Cdd:PLN03130 1237 SIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfglmdLRKVLG 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 77 YVPQRSDIdwdFPITV---LDvvligtypslgmmkrPKKEHRD---WafDCLKKVGMEEFKNR----------QIGE-LS 139
Cdd:PLN03130 1317 IIPQAPVL---FSGTVrfnLD---------------PFNEHNDadlW--ESLERAHLKDVIRRnslgldaevsEAGEnFS 1376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 140 GGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVH 194
Cdd:PLN03130 1377 VGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAH 1431
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-212 |
2.22e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.58 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 20 VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGE----DIRSVRKSVAYVPQrsdidwdfpITVLDV 95
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISDVHQNMGYCPQ---------FDAIDD 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 96 VLIGT---YPSLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTS 172
Cdd:TIGR01257 2026 LLTGRehlYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446425376 173 EETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNK 212
Cdd:TIGR01257 2106 RRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVK 2145
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-223 |
2.78e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 2 GEAIIVKDLFVSYQGNQ----VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAY 77
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 78 VPQRS----------DIDWDF--PITVLDVVL---------IGTYPSLGmmkrpKKEHRDWAFDCLKKVGMEEFK---NR 133
Cdd:PRK10261 90 LSEQSaaqmrhvrgaDMAMIFqePMTSLNPVFtvgeqiaesIRLHQGAS-----REEAMVEAKRMLDQVRIPEAQtilSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 134 QIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKE-GKTIVVVHHDLSKAESYFDKLLLMNK 212
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQ 244
|
250
....*....|..
gi 446425376 213 -SLIHYGEVRQV 223
Cdd:PRK10261 245 gEAVETGSVEQI 256
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-196 |
2.79e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.68 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQIlgedirSVRKSVAYVPQRSD 83
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW------SENANIGYYAQDHA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 IDWDFPITVLDvvligtypslgMMKRPKKEHRD-------------WAFDCLKKVgmeefKNrqigeLSGGQQQRVFLAR 150
Cdd:PRK15064 393 YDFENDLTLFD-----------WMSQWRQEGDDeqavrgtlgrllfSQDDIKKSV-----KV-----LSGGEKGRMLFGK 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446425376 151 ALAQKAEIFFLDEPFVGIDVTSEETIIKILRELrkEGkTIVVVHHD 196
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDMESIESLNMALEKY--EG-TLIFVSHD 494
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-196 |
5.00e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.96 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 16 GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLipnDKgyvQILGEDIRSVRKSVAYVPQRSDIDWDfpITVLDV 95
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DK---DFNGEARPQPGIKVGYLPQEPQLDPT--KTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 96 VLIGTYPSLGMMKR--------------------------PKKEHRD-WAFDCLKKVGMEEFK----NRQIGELSGGQQQ 144
Cdd:TIGR03719 89 VEEGVAEIKDALDRfneisakyaepdadfdklaaeqaelqEIIDAADaWDLDSQLEIAMDALRcppwDADVTKLSGGERR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446425376 145 RVFLARALAQKAEIFFLDEPFVGIDVtseETIIKILRELRKEGKTIVVVHHD 196
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLDA---ESVAWLERHLQEYPGTVVAVTHD 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2-193 |
5.34e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.81 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 2 GEAII-VKDLFV---SYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDlipndKGY-VQILGE--------DI 68
Cdd:NF040905 254 GEVVFeVKNWTVyhpLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG-----RSYgRNISGTvfkdgkevDV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 69 RSVRKSV----AYVPQ-RSdidwdfpitVLDVVLIG------TYPSLGMMKRPK--KEHRDwafdclKKVGmEEFKNR-- 133
Cdd:NF040905 329 STVSDAIdaglAYVTEdRK---------GYGLNLIDdikrniTLANLGKVSRRGviDENEE------IKVA-EEYRKKmn 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 134 --------QIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVV 193
Cdd:NF040905 393 iktpsvfqKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI 460
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-243 |
5.62e-12 |
|
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: 65.35 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 19 VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSV-----RKSVAYVPQrsdidwdfpitvl 93
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIglhdlRFKITIIPQ------------- 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 94 DVVLIGTypSLGMMKRPKKEHRD----WAFDCLKKVGME-------EFKNRQIGE-LSGGQQQRVFLARALAQKAEIFFL 161
Cdd:TIGR00957 1368 DPVLFSG--SLRMNLDPFSQYSDeevwWALELAHLKTFVsalpdklDHECAEGGEnLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 162 DEPFVGIDVTSEETIIKILRElRKEGKTIVVVHHDLSKAESYfDKLLLMNKslihyGEVRQVLEPTVMSKAyvnQGILFN 241
Cdd:TIGR00957 1446 DEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDK-----GEVAEFGAPSNLLQQ---RGIFYS 1515
|
..
gi 446425376 242 NA 243
Cdd:TIGR00957 1516 MA 1517
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-197 |
7.91e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.43 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 21 QNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQIL--GE-----DIR-SVRKSV-------AYVPQRSdid 85
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEILfdGEvcrfkDIRdSEALGIviihqelALIPYLS--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 86 wdfpitVLDVVLIGTYPS-LGMMKRPKKEHRdwAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEP 164
Cdd:NF040905 95 ------IAENIFLGNERAkRGVIDWNETNRR--ARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166
|
170 180 190
....*....|....*....|....*....|...
gi 446425376 165 FVGIDVTSEETIIKILRELRKEGKTIVVVHHDL 197
Cdd:NF040905 167 TAALNEEDSAALLDLLLELKAQGITSIIISHKL 199
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
7-195 |
1.09e-11 |
|
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: 62.66 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAvldLIPNDK-----GYVQILGEDIRSV------RKSV 75
Cdd:TIGR01978 3 IKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKT---IAGHPSyevtsGTILFKGQDLLELepderaRAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 76 AYVPQRSDidwDFP-ITVLDvvLIGTYPSLGMMKRPKKEHRDWAF-----DCLKKVGM-EEFKNRQIGE-LSGGQQQRVF 147
Cdd:TIGR01978 80 FLAFQYPE---EIPgVSNLE--FLRSALNARRSARGEEPLDLLDFekllkEKLALLDMdEEFLNRSVNEgFSGGEKKRNE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446425376 148 LARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHH 195
Cdd:TIGR01978 155 ILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITH 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-196 |
1.75e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.43 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 12 VSYQ--GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQIlgedirSVRKSVAYVPQ-RSDIDWDf 88
Cdd:PRK11147 325 VNYQidGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC------GTKLEVAYFDQhRAELDPE- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 89 pITVLDVVLIGTYPslgMMKRPKKEH-----RDWAFDclKKVGMEEFKnrqigELSGGQQQRVFLARALAQKAEIFFLDE 163
Cdd:PRK11147 398 -KTVMDNLAEGKQE---VMVNGRPRHvlgylQDFLFH--PKRAMTPVK-----ALSGGERNRLLLARLFLKPSNLLILDE 466
|
170 180 190
....*....|....*....|....*....|....
gi 446425376 164 PFVGIDVtseETiIKILRELRKEGK-TIVVVHHD 196
Cdd:PRK11147 467 PTNDLDV---ET-LELLEELLDSYQgTVLLVSHD 496
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-224 |
2.13e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.11 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 24 SFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQilGEDIRSVRKSVAYVPQRSDIDW-------------DFPI 90
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ--SQFSHITRLSFEQLQKLVSDEWqrnntdmlspgedDTGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 91 TVLDVVLIGTypslgmmkrpKKEHRdwafdCL---KKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVG 167
Cdd:PRK10938 101 TTAEIIQDEV----------KDPAR-----CEqlaQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 168 IDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKL-LLMNKSLIHYGEVRQVL 224
Cdd:PRK10938 166 LDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAgVLADCTLAETGEREEIL 223
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-194 |
2.65e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.40 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 25 FDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKS--VAYVPQRSDIDWDfpitvldvvlIGTYP 102
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSrfMAYLGHLPGLKAD----------LSTLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 103 SLGMM-----KRPKKEhrdwAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETII 177
Cdd:PRK13543 102 NLHFLcglhgRRAKQM----PGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVN 177
|
170
....*....|....*...
gi 446425376 178 KILR-ELRKEGKTIVVVH 194
Cdd:PRK13543 178 RMISaHLRGGGAALVTTH 195
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
13-223 |
4.27e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.78 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 13 SYQGN-QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRksvayvPQRSDIDWDFPIT 91
Cdd:PRK11650 12 SYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE------PADRDIAMVFQNY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 92 VLdvvligtYP----------SLGMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFL 161
Cdd:PRK11650 86 AL-------YPhmsvrenmayGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 162 DEPFVGID----VTSEETIIKILRELrkeGKTIVVVHHDLSKAESYFDKLLLMNKslihyGEVRQV 223
Cdd:PRK11650 159 DEPLSNLDaklrVQMRLEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNG-----GVAEQI 216
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
7-195 |
5.61e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.81 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKavldLIPNDKGYvQILGEDIRSVRKSVAYVP--QRSD- 83
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSK----VIAGHPAY-KILEGDILFKGESILDLEpeERAHl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 ---IDWDFPITVLDV----VLIGTYPSlGMMKRPKKEHRDWAF-----DCLKKVGMEE-FKNRQIGE-LSGGQQQRVFLA 149
Cdd:CHL00131 85 gifLAFQYPIEIPGVsnadFLRLAYNS-KRKFQGLPELDPLEFleiinEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEIL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446425376 150 RALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHH 195
Cdd:CHL00131 164 QMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-197 |
7.20e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.48 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 20 VQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIP----NDKGYVQILGEDI--RSVR-KSVAYVPQ--RSDIDwdfPI 90
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPVapCALRgRKIATIMQnpRSAFN---PL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 91 TVLDVVLIGTYPSLGmmkrpKKEHRDWAFDCLKKVGMEEFKnRQIG----ELSGGQQQRVFLARALAQKAEIFFLDEPFV 166
Cdd:PRK10418 96 HTMHTHARETCLALG-----KPADDATLTAALEAVGLENAA-RVLKlypfEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190
....*....|....*....|....*....|..
gi 446425376 167 GIDVTSEETIIKILREL-RKEGKTIVVVHHDL 197
Cdd:PRK10418 170 DLDVVAQARILDLLESIvQKRALGMLLVTHDM 201
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-212 |
1.10e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.14 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 23 VSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIrSVRKSVAYVPQRSDIDWDFPItvLDVVLigtyp 102
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV-TAEQPEDYRKLFSAVFTDFHL--FDQLL----- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 103 slgmmkRPKKEHRDWA--FDCLKKVGME---EFKNRQIG--ELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVT-SEE 174
Cdd:PRK10522 414 ------GPEGKPANPAlvEKWLERLKMAhklELEDGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfRRE 487
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446425376 175 TIIKILRELRKEGKTIVVVHHDlskaESYF---DKLLLMNK 212
Cdd:PRK10522 488 FYQVLLPLLQEMGKTIFAISHD----DHYFihaDRLLEMRN 524
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-215 |
1.99e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.05 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAG--KSTLMKAVLDLIPNDKGY-VQILGEDIRSVRKSVA-YVP 79
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWrF*TWCANRRALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 80 QRSDIDWDFPiTVLDVVLIGTYPSLGmmkrpKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIF 159
Cdd:NF000106 93 VR*GRRESFS-GRENLYMIGR*LDLS-----RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKSLI 215
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-223 |
2.14e-09 |
|
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: 57.12 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 23 VSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIrsvrksvayvpQRSDIDW----------DF---- 88
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV-----------TADNREAyrqlfsavfsDFhlfd 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 89 ----PITVLDVVLIGTYpslgmmkrpkkehrdwafdcLKKVGMEE---FKNRQIG--ELSGGQQQRVFLARALAQKAEIF 159
Cdd:COG4615 420 rllgLDGEADPARAREL--------------------LERLELDHkvsVEDGRFSttDLSQGQRKRLALLVALLEDRPIL 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 160 FLDE------P-----FVgidvtsEEtiikILRELRKEGKTIVVVHHDlskaESYF---DKLLLMnksliHYGEVRQV 223
Cdd:COG4615 480 VFDEwaadqdPefrrvFY------TE----LLPELKARGKTVIAISHD----DRYFdlaDRVLKM-----DYGKLVEL 538
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-219 |
3.05e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 56.68 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 16 GNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQIlgedirSVRKSVAYVPQRsdidwdfPI----T 91
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK------PAKGKLFYVPQR-------PYmtlgT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 92 VLDVVLigtYP-SLGMMKRpkKEHRDWAFD-CLKKVGMEEFKNRQIG---------ELSGGQQQRVFLARALAQKAEIFF 160
Cdd:TIGR00954 531 LRDQII---YPdSSEDMKR--RGLSDKDLEqILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 161 LDEPFVGIDVTSEEtiiKILRELRKEGKTIVVVHHdlskaesyfdklllmNKSLIHYGE 219
Cdd:TIGR00954 606 LDECTSAVSVDVEG---YMYRLCREFGITLFSVSH---------------RKSLWKYHE 646
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
132-196 |
4.79e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 56.38 E-value: 4.79e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 132 NRQIGELSGGQQQRVFLARALAqkAEIF----FLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHD 196
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLG--AELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD 537
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
11-213 |
7.67e-09 |
|
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: 54.20 E-value: 7.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 11 FVSYQGNQVVqnvSF-DIEKGKLVGIIGPNGAGKSTLMKAV-LDLIPNDKGYvqilgEDIRSVRKSVAYVPQRSDIDWDF 88
Cdd:cd03279 11 FGPFREEQVI---DFtGLDNNGLFLICGPTGAGKSTILDAItYALYGKTPRY-----GRQENLRSVFAPGEDTAEVSFTF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 89 PITvldvvlIGTYPslgMMKRPKKEHRDW---AFdcLKKVGMEEFKNRQIGELSGGQQQRVFLARALA-----QKA---- 156
Cdd:cd03279 83 QLG------GKKYR---VERSRGLDYDQFtriVL--LPQGEFDRFLARPVSTLSGGETFLASLSLALAlsevlQNRggar 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 157 -EIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESyFDKLLLMNKS 213
Cdd:cd03279 152 lEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKER-IPQRLEVIKT 208
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-229 |
9.61e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.88 E-value: 9.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 35 IIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVRKSVAYVPQRSDIDWDFPitvlDVVLIGTYPSLGM----MKRP 110
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQ----DARLFPHYKVRGNlrygMAKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 111 KKEHRDwafDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKT- 189
Cdd:PRK11144 105 MVAQFD---KIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIp 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446425376 190 IVVVHHDLSKAESYFDKLLLMNK-SLIHYGEVRQVLEPTVM 229
Cdd:PRK11144 182 ILYVSHSLDEILRLADRVVVLEQgKVKAFGPLEEVWASSAM 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-220 |
1.06e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 4 AIIVKDL------FVSyqgnqvVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGE-----DIrSVR 72
Cdd:NF033858 266 AIEARGLtmrfgdFTA------VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvdagDI-ATR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 73 KSVAYVPQrsdidwDFP----ITV-----LDVVLIGTypslgmmkrPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQ 143
Cdd:NF033858 339 RRVGYMSQ------AFSlygeLTVrqnleLHARLFHL---------PAAEIAARVAEMLERFDLADVADALPDSLPLGIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 144 QRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILREL-RKEGKTIVVVHHdlskaesyFdklllMNK-------SLI 215
Cdd:NF033858 404 QRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELsREDGVTIFISTH--------F-----MNEaercdriSLM 470
|
....*
gi 446425376 216 HYGEV 220
Cdd:NF033858 471 HAGRV 475
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
138-211 |
2.02e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 2.02e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 138 LSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELR-KEGKTIVVVHHDLSKAESYfDKLLLMN 211
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASIKRS-DKIVVFN 1432
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
35-204 |
2.04e-08 |
|
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: 52.99 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 35 IIGPNGAGKSTLMKAVL-----DLIPNDKGyVQILGEDIRSVRKSvAYVPQRSDIDWDFPITVldvvligtypslgmmkr 109
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyaltgELPPNSKG-GAHDPKLIREGEVR-AQVKLAFENANGKKYTI----------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 110 pkkeHRDwaFDCLKKVGM---EEFKN---RQIGELSGGQQQ------RVFLARALAQKAEIFFLDEPFVGIDVTS-EETI 176
Cdd:cd03240 88 ----TRS--LAILENVIFchqGESNWpllDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESL 161
|
170 180 190
....*....|....*....|....*....|..
gi 446425376 177 IKILRELRKEG--KTIVVVHHD--LSKAESYF 204
Cdd:cd03240 162 AEIIEERKSQKnfQLIVITHDEelVDAADHIY 193
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-212 |
5.29e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMkavlDLIPNDK--GYVQilgEDIR-----SVRKSVAYVP---QRSDIDwD 87
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLM----DVLAGRKtgGYIE---GDIRisgfpKKQETFARISgycEQNDIH-S 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 88 FPITVLDVVLIGTYpsLGMMKRPKKEHRDWAFD-CLKKVGMEEFKNRQIG-----ELSGGQQQRVFLARALAQKAEIFFL 161
Cdd:PLN03140 966 PQVTVRESLIYSAF--LRLPKEVSKEEKMMFVDeVMELVELDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446425376 162 DEPFVGIDVTSEETIIKILRELRKEGKTIVVVHH----DLSKAesyFDKLLLMNK 212
Cdd:PLN03140 1044 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpsiDIFEA---FDELLLMKR 1095
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
122-196 |
6.47e-08 |
|
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: 53.09 E-value: 6.47e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 122 LKKVGMEEFK-NRQIGELSGGQQQRVFLARALAQK--AEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHD 196
Cdd:TIGR00630 472 LIDVGLDYLSlSRAAGTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD 549
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
122-197 |
8.93e-08 |
|
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: 51.46 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 122 LKKVGMEEFK-NRQIGELSGGQQQRVFLARALAQKAE---IFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDL 197
Cdd:cd03271 153 LCDVGLGYIKlGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL 232
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1-198 |
1.36e-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: 51.06 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 1 MGEAIIVKDLFVSYQGN--QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDIRSVrkSVAYV 78
Cdd:cd03288 16 LGGEIKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL--PLHTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 79 PQRSDIDWDFPITVLDVVLIGTYPslgmmKRPKKEHRDW-----------------AFDCLKKVGMEEFknrqigelSGG 141
Cdd:cd03288 94 RSRLSIILQDPILFSGSIRFNLDP-----ECKCTDDRLWealeiaqlknmvkslpgGLDAVVTEGGENF--------SVG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446425376 142 QQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEgKTIVVVHHDLS 198
Cdd:cd03288 161 QRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVS 216
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-196 |
1.50e-07 |
|
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: 49.68 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 29 KGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGyvqilgedirsvrksvayvpqrsdidwdfpitvlDVVLIGTypslgmmk 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG----------------------------------GVIYIDG-------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 109 rpkkehrDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILR------E 182
Cdd:smart00382 39 -------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllllL 111
|
170
....*....|....
gi 446425376 183 LRKEGKTIVVVHHD 196
Cdd:smart00382 112 KSEKNLTVILTTND 125
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-210 |
1.62e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 51.06 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIP------------NDKGYVQILGEDIRS-VRKSVAYVPQ--RS 82
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhvtadrfrwNGIDLLKLSPRERRKiIGREIAMIFQepSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 83 DIDwdfPITVLDVVLIGTYPSL---GMMKRPKKEHRDWAFDCLKKVG-------MEEFKNrqigELSGGQQQRVFLARAL 152
Cdd:COG4170 101 CLD---PSAKIGDQLIEAIPSWtfkGKWWQRFKWRKKRAIELLHRVGikdhkdiMNSYPH----ELTEGECQKVMIAMAI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 153 AQKAEIFFLDEPFVGIDVTSEETIIKILRELRK-EGKTIVVVHHDLSKAESYFDKLLLM 210
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVL 232
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
19-197 |
1.95e-07 |
|
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: 49.28 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 19 VVQNVSFDieKGKLVGIIGPNGAGKSTLMKAVldlipndkGYV---QILGEDIRSVRKSVAYVPQRSdidwdfpitvldV 95
Cdd:cd03227 12 VPNDVTFG--EGSLTIITGPNGSGKSTILDAI--------GLAlggAQSATRRRSGVKAGCIVAAVS------------A 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 96 VLIGTypslgmmkrpkkehrdwafdclkkvgmeefknrqIGELSGGQQQRVFLARALA----QKAEIFFLDEPFVGIDVT 171
Cdd:cd03227 70 ELIFT----------------------------------RLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPR 115
|
170 180
....*....|....*....|....*.
gi 446425376 172 SEETIIKILRELRKEGKTIVVVHHDL 197
Cdd:cd03227 116 DGQALAEAILEHLVKGAQVIVITHLP 141
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-225 |
2.04e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVL-DLIPNDKG------YVQILGEDI-RSVRKSVAYVpqrSDIDWDFP 89
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsNTDGFHIGvegvitYDGITPEEIkKHYRGDVVYN---AETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 90 -ITV---LDVVLIGTYPSLGMMKRPKKEHRDWAFD-CLKKVGMEEFKNRQIGE-----LSGGQQQRVFLARALAQKAEIF 159
Cdd:TIGR00956 152 hLTVgetLDFAARCKTPQNRPDGVSREEYAKHIADvYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446425376 160 FLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESY--FDKLLLMNKS-LIHYGEVRQVLE 225
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYelFDKVIVLYEGyQIYFGPADKAKQ 300
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-210 |
2.56e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.57 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDL------IPNDK---GYVQILGEDIRSVRKSVAY-------VPQr 81
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrVTADRmrfDDIDLLRLSPRERRKLVGHnvsmifqEPQ- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 82 SDIDwdfPITVLDVVLIGTYPSLGM----MKRPKKEHRDwAFDCLKKVGMEEFKNRQIG---ELSGGQQQRVFLARALAQ 154
Cdd:PRK15093 100 SCLD---PSERVGRQLMQNIPGWTYkgrwWQRFGWRKRR-AIELLHRVGIKDHKDAMRSfpyELTEGECQKVMIAIALAN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446425376 155 KAEIFFLDEPFVGIDVTSEETIIKILRELRK-EGKTIVVVHHDLSKAESYFDKLLLM 210
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVL 232
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-197 |
4.29e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.41 E-value: 4.29e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 138 LSGGQQQRVFLARALAQKAE---IFFLDEPFVGI---DVtseETIIKILRELRKEGKTIVVVHHDL 197
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhDI---RKLLEVLHRLVDKGNTVVVIEHNL 889
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
18-196 |
4.76e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 18 QVVQNVSFDIEKGKLVGIIGPNGAGKSTLMK--AVLDlipndkgyVQILGEDIRSVRKSVAYVPQRSDIDWDFpiTVLDV 95
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRimAGVD--------KEFEGEARPAPGIKVGYLPQEPQLDPEK--TVREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 96 VLIGTYPSLGMMKR----------PkkehrDWAFDCLkkvgMEEFKNRQ------------------------------I 135
Cdd:PRK11819 91 VEEGVAEVKAALDRfneiyaayaeP-----DADFDAL----AAEQGELQeiidaadawdldsqleiamdalrcppwdakV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446425376 136 GELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVtseETIIKILRELRKEGKTIVVVHHD 196
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-197 |
1.53e-06 |
|
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: 48.86 E-value: 1.53e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446425376 138 LSGGQQQRVFLARALAQKAE---IFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDL 197
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-211 |
2.87e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 19 VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEDI-----RSVRKSVAYVPQ---------RSDI 84
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIgayglRELRRQFSMIPQdpvlfdgtvRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 85 DWDFPITVLDVvligtypslgmmkrpkkehrdWAfdCLKKVGMEEfknRQIGELSG--------------GQQQRVFLAR 150
Cdd:PTZ00243 1405 DPFLEASSAEV---------------------WA--ALELVGLRE---RVASESEGidsrvleggsnysvGQRQLMCMAR 1458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446425376 151 ALAQKAEIFFL-DEPFVGIDVTSEETIIKILRELRkEGKTIVVVHHDLSKAESYfDKLLLMN 211
Cdd:PTZ00243 1459 ALLKKGSGFILmDEATANIDPALDRQIQATVMSAF-SAYTVITIAHRLHTVAQY-DKIIVMD 1518
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
137-198 |
2.95e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 2.95e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446425376 137 ELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIKILRELR-KEGKTIVVVHHDLS 198
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLS 641
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-196 |
2.98e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 5 IIVKDLFVSYQGNQVV-QNVSFDIEKGKLVGIIGPNGAGKSTLMKAVL-DLIPndkgyvqILGEDIRSVRKSVAYVPQRS 82
Cdd:PLN03073 509 ISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISgELQP-------SSGTVFRSAKVRMAVFSQHH 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 83 DIDWDFPITVLdVVLIGTYPslGMMKRPKKEHrdwafdcLKKVGME-EFKNRQIGELSGGQQQRVFLARALAQKAEIFFL 161
Cdd:PLN03073 582 VDGLDLSSNPL-LYMMRCFP--GVPEQKLRAH-------LGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLL 651
|
170 180 190
....*....|....*....|....*....|....*
gi 446425376 162 DEPFVGIDVTSEETIIKILrELRKEGktIVVVHHD 196
Cdd:PLN03073 652 DEPSNHLDLDAVEALIQGL-VLFQGG--VLMVSHD 683
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
138-197 |
6.44e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 6.44e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 138 LSGGQQQRVFLARALAQKA---EIFFLDEPFVGI---DVtseETIIKILRELRKEGKTIVVVHHDL 197
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfeDI---RKLLEVLHRLVDKGNTVVVIEHNL 893
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
132-196 |
9.82e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.17 E-value: 9.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446425376 132 NRQIGELSGGQQQRVFLARALAqkAE----IFFLDEPFVGI---DVtseETIIKILRELRKEGKTIVVVHHD 196
Cdd:COG0178 480 DRSAGTLSGGEAQRIRLATQIG--SGlvgvLYVLDEPSIGLhqrDN---DRLIETLKRLRDLGNTVIVVEHD 546
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-197 |
3.20e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 3.20e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446425376 133 RQIGELSGGQQQRVFLARAL---AQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDL 197
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM 872
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
115-182 |
4.53e-05 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 41.07 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 115 RDW-AFDCLK--KVGMEEFKNRQIGELSGGQQQRVF---LARALAQKAE----------IFFLDEPFVGIDVTSEETIIK 178
Cdd:pfam13558 7 RNWlSFEVEVrdEDGSEVETYRRSGGLSGGEKQLLAylpLAAALAAQYGsaegrppaprLVFLDEAFAKLDEENIRTALE 86
|
....
gi 446425376 179 ILRE 182
Cdd:pfam13558 87 LLRA 90
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-196 |
5.09e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 21 QNVSFDIEKGKLVGIIGPNGAGKSTLMKaVL--DLIPNdKGYVQI-LGEDIRSVRK-SVAYVPQRsdidwdfpitVLDVV 96
Cdd:PRK15064 18 ENISVKFGGGNRYGLIGANGCGKSTFMK-ILggDLEPS-AGNVSLdPNERLGKLRQdQFAFEEFT----------VLDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 97 LIGTypslGMMKRPKKEhRDW---------------------------------AFDCLKKVGM-EEFKNRQIGELSGGQ 142
Cdd:PRK15064 86 IMGH----TELWEVKQE-RDRiyalpemseedgmkvadlevkfaemdgytaearAGELLLGVGIpEEQHYGLMSEVAPGW 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446425376 143 QQRVFLARALAQKAEIFFLDEPFVGIDVtseETIIKILRELRKEGKTIVVVHHD 196
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDI---NTIRWLEDVLNERNSTMIIISHD 211
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
7-46 |
5.44e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.24 E-value: 5.44e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTL 46
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTL 43
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-217 |
1.60e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 2 GEAIIVKDLF-----VSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAV----LDLIP--------------NDK 58
Cdd:PLN03073 170 GGGPAIKDIHmenfsISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMamhaIDGIPkncqilhveqevvgDDT 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 59 GYVQ-ILGEDIRSVR---KSVAYVPQRSDIDWDFPITVLDVVLIGT-------------YPSLGMMKRPKKEHRdwAFDC 121
Cdd:PLN03073 250 TALQcVLNTDIERTQlleEEAQLVAQQRELEFETETGKGKGANKDGvdkdavsqrleeiYKRLELIDAYTAEAR--AASI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 122 LKKVGME-EFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDEPFVGIDVtseETIIKILRELRKEGKTIVVVHHdlskA 200
Cdd:PLN03073 328 LAGLSFTpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL---HAVLWLETYLLKWPKTFIVVSH----A 400
|
250 260
....*....|....*....|..
gi 446425376 201 ESYF-----DKLLLMNKSLIHY 217
Cdd:PLN03073 401 REFLntvvtDILHLHGQKLVTY 422
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
11-50 |
3.28e-04 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 41.02 E-value: 3.28e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446425376 11 FVSYQGNQVVQnvSFDiekgKLVGIIGPNGAGKSTLMKAV 50
Cdd:cd03275 9 FKSYKGRHVIG--PFD----RFTCIIGPNGSGKSNLMDAI 42
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
20-67 |
5.16e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 40.76 E-value: 5.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 446425376 20 VQNVSFDIEKGKLVgIIGPNGAGKSTLMKAvLDLIPNDKGYVQILGED 67
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEA-LRLLLGPSSSRKFDEED 59
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
7-224 |
6.74e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.18 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 7 VKDLFVSYQGNQ---VVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQILGEdIRSVRKSVAYVPQRSD 83
Cdd:PRK13546 24 MKDALIPKHKNKtffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-VSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 84 IDwDFPITVLdvvligtypslgMMKRPKKEHRDWAFDCLKKVGMEEFKNRQIGELSGGQQQRVFLARALAQKAEIFFLDE 163
Cdd:PRK13546 103 IE-NIEFKML------------CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446425376 164 PFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLSKAESYFDKLLLMNKS-LIHYGEVRQVL 224
Cdd:PRK13546 170 ALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGkLKDYGELDDVL 231
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
11-197 |
7.72e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 11 FVSYQGNQVVqnvsfDIEKGkLVGIIGPNGAGKSTLMKAVL---------------DLI--PNDKGYVQIL----GEDIR 69
Cdd:COG0419 10 FRSYRDTETI-----DFDDG-LNLIVGPNGAGKSTILEAIRyalygkarsrsklrsDLInvGSEEASVELEfehgGKRYR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 70 SVRksvayvPQrSDIDWDF---PITVLDVV--LIGTYPSLGMMKRPKK-----EHRDWAFDCLKKVGMEEFKN----RQI 135
Cdd:COG0419 84 IER------RQ-GEFAEFLeakPSERKEALkrLLGLEIYEELKERLKEleealESALEELAELQKLKQEILAQlsglDPI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446425376 136 GELSGGQQQRVFLARALAqkaeiFFLDepFVGIDVTSEETIIKILRELRkegktivVVHHDL 197
Cdd:COG0419 157 ETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA-------IITHVI 204
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
29-56 |
9.43e-04 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 38.90 E-value: 9.43e-04
10 20
....*....|....*....|....*...
gi 446425376 29 KGKLVGIIGPNGAGKSTLMKAVLDLIPN 56
Cdd:COG0194 1 RGKLIVLSGPSGAGKTTLVKALLERDPD 28
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
133-195 |
1.09e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 1.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446425376 133 RQIGELSGGQQQRVFLARALA----------QKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHH 195
Cdd:TIGR00618 946 RPSATLSGGETFLASLSLALAladllstsggTVLDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISH 1018
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
138-195 |
1.19e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 39.78 E-value: 1.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446425376 138 LSGGQQQRVFLARALA------QKAEI--FFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHH 195
Cdd:PRK10246 950 LSGGESFLVSLALALAlsdlvsHKTRIdsLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISH 1015
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
21-50 |
1.26e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.63 E-value: 1.26e-03
10 20 30
....*....|....*....|....*....|
gi 446425376 21 QNVSFDIEKGkLVGIIGPNGAGKSTLMKAV 50
Cdd:pfam13476 10 RDQTIDFSKG-LTLITGPNGSGKTTILDAI 38
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
32-218 |
1.30e-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: 39.30 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 32 LVGIIGPNGAGKSTLMKAvLDLIPNDKGYVQILGEDIRSvrksvayvpqRSDIDWDFPITVLDVVLIGTYPSLGMMKRPK 111
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEA-LRFLADFDALVIGLTDERSR----------NGGIGGIPSLLNGIDPKEPIEFEISEFLEDG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425376 112 KEHRDWAFDCLKKVGMEEFKNRQIGELsggqqqRVFLARALAQKAEIFFLDEPFVGIDVTSEETIIK--ILRELRKEGKT 189
Cdd:pfam13304 70 VRYRYGLDLEREDVEEKLSSKPTLLEK------RLLLREDSEEREPKFPPEAEELRLGLDVEERIELslSELSDLISGLL 143
|
170 180
....*....|....*....|....*....
gi 446425376 190 IVVVHHDLSKAESYFDKLLLMNKSLIHYG 218
Cdd:pfam13304 144 LLSIISPLSFLLLLDEGLLLEDWAVLDLA 172
|
|
| VirB11 |
COG0630 |
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ... |
27-72 |
1.33e-03 |
|
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440395 [Multi-domain] Cd Length: 462 Bit Score: 39.68 E-value: 1.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446425376 27 IEKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQIlgEDIRSVR 72
Cdd:COG0630 287 LENGKSVLVAGGTASGKTTLLNALLSFIPPDAKIVTI--EDTRELN 330
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
20-51 |
2.66e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 37.83 E-value: 2.66e-03
10 20 30
....*....|....*....|....*....|..
gi 446425376 20 VQNVSFDIEKGkLVGIIGPNGAGKSTLMKAVL 51
Cdd:cd03278 13 ADKTTIPFPPG-LTAIVGPNGSGKSNIIDAIR 43
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
131-198 |
3.01e-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: 38.14 E-value: 3.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446425376 131 KNRQIGELSGGQQQRVFLARAL---AQKAEIFFLDEPFVGIDVTSEETIIKILRELRKEGKTIVVVHHDLS 198
Cdd:pfam13304 230 GELPAFELSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
28-61 |
3.50e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 37.48 E-value: 3.50e-03
10 20 30
....*....|....*....|....*....|....
gi 446425376 28 EKGKLVGIIGPNGAGKSTLMKAVLDLIPNDKGYV 61
Cdd:COG3709 3 GPGRLIYVVGPSGAGKDSLLAAARARLAADPRLV 36
|
|
| PRK09270 |
PRK09270 |
nucleoside triphosphate hydrolase domain-containing protein; Reviewed |
32-63 |
4.29e-03 |
|
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
Pssm-ID: 236442 Cd Length: 229 Bit Score: 37.22 E-value: 4.29e-03
10 20 30
....*....|....*....|....*....|..
gi 446425376 32 LVGIIGPNGAGKSTLMKAVLDLIPNDKGYVQI 63
Cdd:PRK09270 35 IVGIAGPPGAGKSTLAEFLEALLQQDGELPAI 66
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
24-51 |
6.16e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 37.26 E-value: 6.16e-03
10 20
....*....|....*....|....*...
gi 446425376 24 SFDIEKGKLVGIIGPNGAGKSTLMKAVL 51
Cdd:COG4938 14 EAELELKPLTLLIGPNGSGKSTLIQALL 41
|
|
| AAA_27 |
pfam13514 |
AAA domain; This domain is found in a number of double-strand DNA break proteins. This domain ... |
35-53 |
7.30e-03 |
|
AAA domain; This domain is found in a number of double-strand DNA break proteins. This domain contains a P-loop motif.
Pssm-ID: 433272 [Multi-domain] Cd Length: 207 Bit Score: 36.38 E-value: 7.30e-03
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
21-54 |
7.67e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 37.44 E-value: 7.67e-03
10 20 30
....*....|....*....|....*....|....
gi 446425376 21 QNVSFDIEKGkLVGIIGPNGAGKSTLMKAVLDLI 54
Cdd:COG4717 15 RDRTIEFSPG-LNVIYGPNEAGKSTLLAFIRAML 47
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
11-50 |
8.36e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 36.95 E-value: 8.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446425376 11 FVSYQGNQVVQNVSFDIEKGKLVGIIGPNGAGKSTLMKAV 50
Cdd:COG1106 10 FRSFKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEAL 49
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
35-54 |
9.25e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 33.73 E-value: 9.25e-03
|
| |
