|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
5-273 |
6.34e-131 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 373.06 E-value: 6.34e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 5 STSIWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNLVAYV 84
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSEEVDWQFPVSVYDVVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:PRK15056 84 PQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 165 ILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRTVIAAGKTEDTFNQHNLEIVFGGVLR 244
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLELAFSGVLR 243
|
250 260
....*....|....*....|....*....
gi 1169664 245 HIKLLGENLHndedkrsvtVLTDDEKAVV 273
Cdd:PRK15056 244 HVALNGSEES---------IITDDERPFI 263
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-247 |
8.42e-129 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 366.72 E-value: 8.42e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQAlkRNLVAYVPQSEE 89
Cdd:COG1121 9 LENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA--RRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 90 VDWQFPVSVYDVVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDE 169
Cdd:COG1121 86 VDWDFPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 170 PFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRTVIAAGKTEDTFNQHNLEIVFGGVLRHIK 247
Cdd:COG1121 166 PFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENLSRAYGGPVALLA 243
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-224 |
4.54e-118 |
|
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: 338.35 E-value: 4.54e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 9 WVNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQalKRNLVAYVPQSE 88
Cdd:cd03235 1 EVEDLTVSYGG-HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK--ERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 89 EVDWQFPVSVYDVVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLD 168
Cdd:cd03235 78 SIDRDFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 169 EPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRTVIAAG 224
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
10-240 |
5.28e-85 |
|
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: 255.74 E-value: 5.28e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISqALKRN----LVAYVP 85
Cdd:COG1120 4 AENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA-SLSRRelarRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEEVDwqFPVSVYDVVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPII 165
Cdd:COG1120 82 QEPPAP--FGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169664 166 LLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFNQHNLEIVFG 240
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDgRIVAQGPPEEVLTPELLEEVYG 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-254 |
9.29e-66 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 206.07 E-value: 9.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPI---SQALKRNlVAYV 84
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVardPAEVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSEEVDWQFpvSVYD-VVMMGR-YGymnflrIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQS 162
Cdd:COG1131 79 PQEPALYPDL--TVREnLRFFARlYG------LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 163 PIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTEDtFNQHNLEIVFgg 241
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKgRIVADGTPDE-LKARLLEDVF-- 227
|
250
....*....|...
gi 1169664 242 vlrhIKLLGENLH 254
Cdd:COG1131 228 ----LELTGEEAR 236
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
10-235 |
1.01e-65 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 205.64 E-value: 1.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL---VAYVPQ 86
Cdd:COG1122 3 LENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELrrkVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 87 SeeVDWQF--PvSVYDVVMmgrYGYMNfLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:COG1122 83 N--PDDQLfaP-TVEEDVA---FGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169664 165 ILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTEDTFNQHNL 235
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRViVLDDGRIVADGTPREVFSDYEL 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-224 |
7.39e-65 |
|
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: 201.90 E-value: 7.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 9 WVNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL---VAYVP 85
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELarkIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QseevdwqfpvsvydvvmmgrygymnflripkaidkqkvqeAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPII 165
Cdd:cd03214 80 Q----------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 166 LLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVVMI-NRTVIAAG 224
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLkDGRIVAQG 180
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-206 |
1.06e-60 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 191.68 E-value: 1.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 16 RYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIklcdlpiSQALKRNlVAYVPQSEEVDWQFP 95
Cdd:NF040873 1 GYG-GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------RRAGGAR-VAYVPQRSEVPDSLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 96 VSVYDVVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVD 175
Cdd:NF040873 72 LTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|.
gi 1169664 176 VKTENAIVDLLQQLREEGHLILVSTHNLGSV 206
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
10-217 |
1.29e-56 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 182.95 E-value: 1.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL------VAY 83
Cdd:COG3638 5 LRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlrrrIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 VPQseevdwQFPV----SVYDVVMMGRYGYMNFLR-----IPKAiDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFL 154
Cdd:COG3638 85 IFQ------QFNLvprlSVLTNVLAGRLGRTSTWRsllglFPPE-DRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169664 155 ARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVVMIN 217
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLR 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-218 |
3.01e-56 |
|
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: 180.74 E-value: 3.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 9 WVNDVTVRYNNGHT-AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL---VAYV 84
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSeeVDWQF-PVSVYDVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSP 163
Cdd:cd03225 81 FQN--PDDQFfGPTVEEEVAFG----LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1169664 164 IILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINR 218
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-245 |
3.75e-55 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 179.54 E-value: 3.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ------ALKRnlvAY 83
Cdd:COG4559 4 AENLSVRLG-GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwspwelARRR---AV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 VPQSEEVdwQFPVSVYDVVMMGRYGYmnflRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQ--- 160
Cdd:COG4559 80 LPQHSSL--AFPFTVEEVVALGRAPH----GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwe 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 161 ----QSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTH--NLGSVpdFCDQVVMINR-TVIAAGKTEDTFNQH 233
Cdd:COG4559 154 pvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHdlNLAAQ--YADRILLLHQgRLVAQGTPEEVLTDE 231
|
250
....*....|....*
gi 1169664 234 NLEIVFG---GVLRH 245
Cdd:COG4559 232 LLERVYGadlRVLAH 246
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-252 |
2.81e-54 |
|
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: 2.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHtAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK--RNLVAYVP 85
Cdd:COG4555 2 IEVENLSKKYGKVP-ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReaRRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEEVDWQFpvSVYDVVmmgRYgYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPII 165
Cdd:COG4555 81 DERGLYDRL--TVRENI---RY-FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 166 LLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRTVIAAGKTEDTFNQH----NLEIVFgg 241
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEigeeNLEDAF-- 232
|
250
....*....|.
gi 1169664 242 vlrhIKLLGEN 252
Cdd:COG4555 233 ----VALIGSE 239
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-234 |
1.87e-52 |
|
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: 180.34 E-value: 1.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 7 SIWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLP---ISQALKRNLVAY 83
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDlsdLDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 VPQSEEVdwqFPVSVYDVVMMGRygymnflriPKAiDKQKVQEAMQRVNIEHLAHR-------QIGE----LSGGQKKRV 152
Cdd:COG4988 416 VPQNPYL---FAGTIRENLRLGR---------PDA-SDEELEAALEAAGLDEFVAAlpdgldtPLGEggrgLSGGQAQRL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 153 FLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLReEGHLILVSTHNLGSVpDFCDQVVMINRTVIAAGKTEDTFNQ 232
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLA 560
|
..
gi 1169664 233 HN 234
Cdd:COG4988 561 KN 562
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-240 |
2.23e-52 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 172.51 E-value: 2.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 6 TSIWVNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL---VA 82
Cdd:PRK11231 1 MTLRTENLTVGYGT-KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLarrLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 83 YVPQSEEVdwqfP--VSVYDVVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQ 160
Cdd:PRK11231 80 LLPQHHLT----PegITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 161 QSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQ-VVMINRTVIAAGKTEDTFNQHNLEIVF 239
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHlVVLANGHVMAQGTPEEVMTPGLLRTVF 235
|
.
gi 1169664 240 G 240
Cdd:PRK11231 236 D 236
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-214 |
9.66e-52 |
|
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: 170.44 E-value: 9.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL------V 81
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 82 AYVPQseevdwQFP----VSVYDVVMMGRYGYMNFLR----IPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVF 153
Cdd:cd03256 81 GMIFQ------QFNlierLSVLENVLSGRLGRRSTWRslfgLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169664 154 LARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVV 214
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIV 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-233 |
9.15e-51 |
|
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: 175.09 E-value: 9.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYN----NGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL----- 80
Cdd:COG1123 263 VRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLrelrr 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 81 -VAYVPQSeevdwqfPVS-------VYDVVMmgrYGYMNFLRIPKAIDKQKVQEAMQRVNI-EHLAHRQIGELSGGQKKR 151
Cdd:COG1123 343 rVQMVFQD-------PYSslnprmtVGDIIA---EPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 152 VFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL-ILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTEDT 229
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLtYLFISHDLAVVRYIADRVAVMYDgRIVEDGPTEEV 492
|
....*.
gi 1169664 230 FN--QH 233
Cdd:COG1123 493 FAnpQH 498
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
10-218 |
4.91e-49 |
|
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: 161.03 E-value: 4.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK--RNLVAYVPQS 87
Cdd:cd03230 3 VRNLSKRYGK-KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEevKRRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 88 EEVDWQFpvSVYdvvmmgrygymnflripkaidkqkvqeamqrvniEHLahrqigELSGGQKKRVFLARALAQQSPIILL 167
Cdd:cd03230 82 PSLYENL--TVR----------------------------------ENL------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1169664 168 DEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINR 218
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNN 170
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
10-216 |
3.76e-48 |
|
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: 160.35 E-value: 3.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHT---AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ-------ALKRN 79
Cdd:cd03255 3 LKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekelaAFRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 80 LVAYVPQseevdwQF---PV-SVYDVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLA 155
Cdd:cd03255 83 HIGFVFQ------SFnllPDlTALENVELP----LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169664 156 RALAQQSPIILLDEPfTG-VDVKTENAIVDLLQQL-REEGHLILVSTHNLgSVPDFCDQVVMI 216
Cdd:cd03255 153 RALANDPKIILADEP-TGnLDSETGKEVMELLRELnKEAGTTIVVVTHDP-ELAEYADRIIEL 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-245 |
5.55e-48 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 161.09 E-value: 5.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 6 TSIWVNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ----ALKRNLv 81
Cdd:PRK13548 1 AMLEARNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspaELARRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 82 AYVPQSEEVDwqFPVSVYDVVMMGRYGymnfLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQ- 160
Cdd:PRK13548 79 AVLPQHSSLS--FPFTVEEVVAMGRAP----HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 161 -----QSPIILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFNQH 233
Cdd:PRK13548 153 wepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQgRLVADGTPAEVLTPE 232
|
250
....*....|....*
gi 1169664 234 NLEIVFG---GVLRH 245
Cdd:PRK13548 233 TLRRVYGadvLVQPH 247
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-240 |
7.86e-48 |
|
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: 160.16 E-value: 7.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL------V 81
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklrrrI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 82 AYVPQseevdwQF----PVSVYDVVMMGRYGYMNFLR-----IPKAiDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRV 152
Cdd:TIGR02315 82 GMIFQ------HYnlieRLTVLENVLHGRLGYKPTWRsllgrFSEE-DKERALSALERVGLADKAYQRADQLSGGQQQRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 153 FLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVVMINRTVIAAGKTEDTFN 231
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234
|
....*....
gi 1169664 232 QHNLEIVFG 240
Cdd:TIGR02315 235 DEVLRHIYG 243
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-233 |
6.09e-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: 164.69 E-value: 6.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNG-HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQ---QGEIKLCDLPI---SQALKRNL 80
Cdd:COG1123 5 LEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLlelSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 81 VAYVPQseEVDWQF-PVSVYDVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALA 159
Cdd:COG1123 85 IGMVFQ--DPMTQLnPVTVGDQIAEA----LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 160 QQSPIILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTEDTFNQH 233
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVvVMDDGRIVEDGPPEEILAAP 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
10-228 |
1.38e-46 |
|
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: 156.83 E-value: 1.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQaLKRNLVA------- 82
Cdd:cd03219 3 VRGLTKRFG-GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG-LPPHEIArlgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 83 -YVPQSeevdwqFP-VSVYDVVMMGRY----GYMNFLRIPKAIDK--QKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFL 154
Cdd:cd03219 81 fQIPRL------FPeLTVLENVMVAAQartgSGLLLARARREEREarERAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169664 155 ARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTED 228
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQgRVIAEGTPDE 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
10-201 |
4.48e-46 |
|
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: 154.56 E-value: 4.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK--RNLVAYVPQS 87
Cdd:COG4133 5 AENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdyRRRLAYLGHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 88 EEVdwqFPV-SVYDvvmmgrygYMNFLR--IPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:COG4133 84 DGL---KPElTVRE--------NLRFWAalYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1169664 165 ILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTH 201
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
8-216 |
5.05e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.82 E-value: 5.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNG---HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ-------ALK 77
Cdd:COG1136 5 LELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserelaRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 78 RNLVAYVPQseevdwQF---PV-SVYDVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVF 153
Cdd:COG1136 85 RRHIGFVFQ------FFnllPElTALENVALP----LLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169664 154 LARALAQQSPIILLDEPfTG-VDVKTENAIVDLLQQL-REEGHLILVSTHNLgSVPDFCDQVVMI 216
Cdd:COG1136 155 IARALVNRPKLILADEP-TGnLDSKTGEEVLELLRELnRELGTTIVMVTHDP-ELAARADRVIRL 217
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-271 |
1.04e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 156.42 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQAlKRNLVAYVPqsEE 89
Cdd:COG4152 4 LKGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE-DRRRIGYLP--EE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 90 ------VdwqfpvSVYDVVM-MGRygymnfLR-IPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQ 161
Cdd:COG4152 80 rglypkM------KVGEQLVyLAR------LKgLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 162 SPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTED---TFNQHNLEI 237
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKgRKVLSGSVDEirrQFGRNTLRL 227
|
250 260 270
....*....|....*....|....*....|....*
gi 1169664 238 VFGGVLRHIKLLGENLHNDEDKRSVTV-LTDDEKA 271
Cdd:COG4152 228 EADGDAGWLRALPGVTVVEEDGDGAELkLEDGADA 262
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-218 |
8.84e-45 |
|
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: 149.70 E-value: 8.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK---RNLVAYVPQ 86
Cdd:cd00267 2 IENLSFRYG-GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeelRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 87 seevdwqfpvsvydvvmmgrygymnflripkaidkqkvqeamqrvniehlahrqigeLSGGQKKRVFLARALAQQSPIIL 166
Cdd:cd00267 81 ---------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1169664 167 LDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINR 218
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
11-240 |
1.84e-44 |
|
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: 151.78 E-value: 1.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 11 NDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQG-EIKLCDLPISQA----LKRNLvAYVp 85
Cdd:COG1119 7 RNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEdvweLRKRI-GLV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 qSEEVDWQFPV--SVYDVVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSP 163
Cdd:COG1119 84 -SPALQLRFPRdeTVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 164 IILLDEPFTGVDVKTENAIVDLLQQLREEG--HLILVsTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFNQHNLEIVFG 240
Cdd:COG1119 163 LLILDEPTAGLDLGARELLLALLDKLAAEGapTLVLV-THHVEEIPPGITHVLLLKDgRVVAAGPKEEVLTSENLSEAFG 241
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
10-203 |
5.93e-44 |
|
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: 149.54 E-value: 5.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRY---NNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRnlVAYVPQ 86
Cdd:cd03293 3 VRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD--RGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 87 SEEVdwqFP-VSVYDVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPII 165
Cdd:cd03293 81 QDAL---LPwLTVLDNVALG----LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1169664 166 LLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNL 203
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDI 192
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-274 |
6.49e-44 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 152.99 E-value: 6.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 7 SIWVNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKL--CDLPISQ-ALKRNlVAY 83
Cdd:COG1118 2 SIEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLngRDLFTNLpPRERR-VGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 VPQseevDWQ-FP-VSVYDVVMMGrygymnfLRI---PKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARAL 158
Cdd:COG1118 80 VFQ----HYAlFPhMTVAENIAFG-------LRVrppSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 159 AQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL--ILVsTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFNQHNL 235
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGttVFV-THDQEEALELADRVVVMNQgRIEQVGTPDEVYDRPAT 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1169664 236 EIVF---GGVLR-HIKLLGENLHNDEDKRSVTVLTDDEKAVVF 274
Cdd:COG1118 228 PFVArflGCVNVlRGRVIGGQLEADGLTLPVAEPLPDGPAVAG 270
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-234 |
7.35e-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: 149.74 E-value: 7.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIK-----LCDLPISQALK-RNLVAY 83
Cdd:COG1127 8 VRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvdgqdITGLSEKELYElRRRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 VPQ------SeevdwqfpVSVYDVVMmgrYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARA 157
Cdd:COG1127 87 LFQggalfdS--------LTVFENVA---FPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 158 LAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL--ILVsTHNLGSVPDFCDQVVMI-NRTVIAAGKTEDTFNQHN 234
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLtsVVV-THDLDSAFAIADRVAVLaDGKIIAEGTPEELLASDD 234
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-228 |
9.02e-44 |
|
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: 157.24 E-value: 9.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 5 STSIWVNDVTVRY-NNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ----ALkRN 79
Cdd:COG4987 331 GPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDldedDL-RR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 80 LVAYVPQSEEVdwqFPVSVYDVVMMGRygymnflriPKAIDKQkVQEAMQRVNIEHLAHRQ-------IGE----LSGGQ 148
Cdd:COG4987 410 RIAVVPQRPHL---FDTTLRENLRLAR---------PDATDEE-LWAALERVGLGDWLAALpdgldtwLGEggrrLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 149 KKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVsTHNLgSVPDFCDQVVMINR-TVIAAGKTE 227
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLI-THRL-AGLERMDRILVLEDgRIVEQGTHE 554
|
.
gi 1169664 228 D 228
Cdd:COG4987 555 E 555
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
8-271 |
2.92e-43 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 152.69 E-value: 2.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL---VAYV 84
Cdd:PRK09536 4 IDVSDLSVEFG-DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAsrrVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSEEVDWQFpvSVYDVVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:PRK09536 83 PQDTSLSFEF--DVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 165 ILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMI-NRTVIAAGKTEDTFNQHNLEIVFGGVL 243
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLaDGRVRAAGPPADVLTADTLRAAFDART 240
|
250 260
....*....|....*....|....*...
gi 1169664 244 rhikLLGENLHNDEDkrSVTVLTDDEKA 271
Cdd:PRK09536 241 ----AVGTDPATGAP--TVTPLPDPDRT 262
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-217 |
4.13e-43 |
|
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: 145.60 E-value: 4.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRY-NNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPI---SQALKRNLVAY 83
Cdd:cd03228 1 IEFKNVSFSYpGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLrdlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 VPQSeevDWQFPVSVYDvvmmgrygymnflripkaidkqkvqeamqrvNIehlahrqigeLSGGQKKRVFLARALAQQSP 163
Cdd:cd03228 81 VPQD---PFLFSGTIRE-------------------------------NI----------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1169664 164 IILLDEPFTGVDVKTENAIVDLLQQLReEGHLILVSTHNLGSVpDFCDQVVMIN 217
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTI-RDADRIIVLD 168
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-223 |
9.35e-43 |
|
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: 155.76 E-value: 9.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYN-NGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ----ALkRNLVAYV 84
Cdd:COG2274 476 LENVSFRYPgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQidpaSL-RRQIGVV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSEEVdwqFPVSVYDVVMMGRygymnflripKAIDKQKVQEAMQRVN----IEHLA---HRQIGE----LSGGQKKRVF 153
Cdd:COG2274 555 LQDVFL---FSGTIRENITLGD----------PDATDEEIIEAARLAGlhdfIEALPmgyDTVVGEggsnLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 154 LARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLReEGHLILVSTHNLgSVPDFCDQVVMINRTVIAA 223
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRL-STIRLADRIIVLDKGRIVE 689
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
10-223 |
9.83e-43 |
|
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: 146.13 E-value: 9.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ--ALKRNlVAYVPQS 87
Cdd:cd03259 3 LKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvpPERRN-IGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 88 EEVdwqFP-VSVYDVVmmgRYGyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIIL 166
Cdd:cd03259 81 YAL---FPhLTVAENI---AFG-LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 167 LDEPFTGVDVKTENAIVDLLQQLREEGHLILVS-THNLGSVPDFCDQVVMINRTVIAA 223
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGITTIYvTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-217 |
1.06e-42 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 145.86 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNLVAYVPQseE 89
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQ--D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 90 VDWQ-FPVSVYDVVmmgRYGYMNflripKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLD 168
Cdd:cd03226 80 VDYQlFTDSVREEL---LLGLKE-----LDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1169664 169 EPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMIN 217
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-172 |
3.35e-42 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 142.79 E-value: 3.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 24 IHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS----QALKRNlVAYVPQSeevDWQFP-VSV 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdderKSLRKE-IGYVFQD---PQLFPrLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 99 YDVVMMGRYGYMNFlripKAIDKQKVQEAMQRVNIEHLAHR----QIGELSGGQKKRVFLARALAQQSPIILLDEPFT 172
Cdd:pfam00005 77 RENLRLGLLLKGLS----KREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-215 |
3.49e-42 |
|
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: 144.96 E-value: 3.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNG---HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCD---LPISQALK---RNL 80
Cdd:cd03257 4 VKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRkirRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 81 VAYVPQSeevdwqfPVSVYDVVMmgRYGY-----MNFLRIPKAIDKQKVQEAMQRVNI---EHLAHRQIGELSGGQKKRV 152
Cdd:cd03257 84 IQMVFQD-------PMSSLNPRM--TIGEqiaepLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169664 153 FLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL-ILVSTHNLGSVPDFCDQV-VM 215
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLtLLFITHDLGVVAKIADRVaVM 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-203 |
4.87e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 145.62 E-value: 4.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 1 MDSFSTSIWVNDVTVRY---NNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK 77
Cdd:COG1116 1 MSAAAPALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 78 RnlVAYVPQSeevD----WQfpvSVYDVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVF 153
Cdd:COG1116 81 D--RGVVFQE---PallpWL---TVLDNVALG----LELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1169664 154 LARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL--ILVsTHNL 203
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKtvLFV-THDV 199
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-218 |
1.15e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 143.65 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQaLKRNLVAY---- 83
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSR-LKRREIPYlrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 ---VPQseevDWQF-P-VSVYDVVMMGrygymnfLRI---PKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLA 155
Cdd:COG2884 81 igvVFQ----DFRLlPdRTVYENVALP-------LRVtgkSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169664 156 RALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINR 218
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELED 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-228 |
5.02e-41 |
|
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: 142.87 E-value: 5.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISqALKRNLVAY------ 83
Cdd:COG0411 7 VRGLTKRFG-GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT-GLPPHRIARlgiart 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 --VPQSeevdwqFP-VSVYDVVMMGRYGYMN------FLRIPKAIDK-----QKVQEAMQRVNIEHLAHRQIGELSGGQK 149
Cdd:COG0411 85 fqNPRL------FPeLTVLENVLVAAHARLGrgllaaLLRLPRARREerearERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 150 KRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREE-GHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTE 227
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFgRVIAEGTPA 238
|
.
gi 1169664 228 D 228
Cdd:COG0411 239 E 239
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-240 |
6.26e-41 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 142.53 E-value: 6.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFkSIMG-LVKPQQGEIKLCDLPISQALKRNL---VAY 83
Cdd:COG4604 2 IEIKNVSKRYGG-KVVLDDVSLTIPKGGITALIGPNGAGKSTLL-SMISrLLPPDSGEVLVDGLDVATTPSRELakrLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 VPQSEevdwQFPV--SVYDVVMMGRY----GymnflRiPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARA 157
Cdd:COG4604 80 LRQEN----HINSrlTVRELVAFGRFpyskG-----R-LTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 158 LAQQSPIILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTH--NLGSVpdFCDQVV-MINRTVIAAGKTEDTFNQH 233
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHdiNFASC--YADHIVaMKDGRVVAQGTPEEIITPE 227
|
....*..
gi 1169664 234 NLEIVFG 240
Cdd:COG4604 228 VLSDIYD 234
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-232 |
1.08e-40 |
|
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: 142.59 E-value: 1.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNG----HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL--- 80
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 81 ---VAYVpqseevdWQFP------VSVYDVVMmgrYGYMNFlRIPKAIDKQKVQEAMQRVNI-EHLAHRQIGELSGGQKK 150
Cdd:TIGR04521 81 rkkVGLV-------FQFPehqlfeETVYKDIA---FGPKNL-GLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 151 RVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTED 228
Cdd:TIGR04521 150 RVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKgKIVLDGTPRE 229
|
....
gi 1169664 229 TFNQ 232
Cdd:TIGR04521 230 VFSD 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
10-224 |
1.41e-40 |
|
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: 140.72 E-value: 1.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNG-HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK--RNLVAYVPQ 86
Cdd:cd03263 3 IRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKaaRQSLGYCPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 87 SEEVDWQFpvSVYDVVMmgrygYMNFLR-IPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPII 165
Cdd:cd03263 83 FDALFDEL--TVREHLR-----FYARLKgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 166 LLDEPFTGVDVKTENAIVDLLQQLReEGHLILVSTHNLGSVPDFCDQV-VMINRTVIAAG 224
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIaIMSDGKLRCIG 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-230 |
1.49e-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: 141.48 E-value: 1.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRY---NNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL---VAY 83
Cdd:COG1124 4 VRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFrrrVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 VPQSeevdwqfPvsvydvvmmgrYGYMN-FLRIPKAI-----------DKQKVQEAMQRVNI-EHLAHRQIGELSGGQKK 150
Cdd:COG1124 84 VFQD-------P-----------YASLHpRHTVDRILaeplrihglpdREERIAELLEQVGLpPSFLDRYPHQLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 151 RVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL--ILVStHNLGSVPDFCDQVVminrtVIAAGKTED 228
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLtyLFVS-HDLAVVAHLCDRVA-----VMQNGRIVE 219
|
..
gi 1169664 229 TF 230
Cdd:COG1124 220 EL 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
8-218 |
4.70e-40 |
|
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: 139.25 E-value: 4.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHtAIHNMTFSLNSGtICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK--RNLVAYVP 85
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQklRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QseEVDWQFPVSVYDVVmmgryGYMNFL-RIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:cd03264 79 Q--EFGVYPNFTVREFL-----DYIAWLkGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1169664 165 ILLDEPFTGVDVKTENAIVDLLQQLREEgHLILVSTHNLGSVPDFCDQVVMINR 218
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNK 204
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-231 |
7.18e-40 |
|
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: 139.17 E-value: 7.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKL-----CDL-PISQALKRNLV 81
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdgediSGLsEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 82 AYVPQSEEVdwqF-PVSVYDVVMMGRYgymNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQ 160
Cdd:cd03261 80 GMLFQSGAL---FdSLTVFENVAFPLR---EHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169664 161 QSPIILLDEPFTGVDVKTENAIVDLLQQLREE-GHLILVSTHNLGSVPDFCDQVVMI-NRTVIAAGKTEDTFN 231
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLyDGKIVAEGTPEELRA 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-221 |
3.18e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.87 E-value: 3.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ----ALkRNLVAYVP 85
Cdd:COG4619 3 LEGLSFRVG-GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmpppEW-RRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QseEVDWqFPVSVYDvvmmgrygymNFLRI----PKAIDKQKVQEAMQRVNI-EHLAHRQIGELSGGQKKRVFLARALAQ 160
Cdd:COG4619 81 Q--EPAL-WGGTVRD----------NLPFPfqlrERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169664 161 QSPIILLDEPFTGVDVKTENAIVDLLQQLR-EEGHLILVSTHNLGSVPDFCDQVVMINRTVI 221
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLaEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
10-224 |
3.56e-39 |
|
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: 136.64 E-value: 3.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIsQALKRNLVAYVPqsEE 89
Cdd:cd03269 3 VENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNRIGYLP--EE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 90 VDWQFPVSVYDVVMmgrygYMNFLR-IPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLD 168
Cdd:cd03269 79 RGLYPKMKVIDQLV-----YLAQLKgLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1169664 169 EPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRT-VIAAG 224
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGrAVLYG 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-223 |
9.01e-39 |
|
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: 135.96 E-value: 9.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHTAIH---NMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ---ALKRNLv 81
Cdd:cd03266 2 ITADALTKRFRDVKKTVQavdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepaEARRRL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 82 AYVPQSEEV-DWqfpVSVYDvvMMGRYGYMNFLRiPKAIdKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQ 160
Cdd:cd03266 81 GFVSDSTGLyDR---LTARE--NLEYFAGLYGLK-GDEL-TARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169664 161 QSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRTVIAA 223
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
10-224 |
1.84e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 142.61 E-value: 1.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ----ALkRNLVAYVP 85
Cdd:COG1132 342 FENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDltleSL-RRQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QseEVdWQFPVSVYDVVMMGRygymnflriPKAiDKQKVQEAMQRVNIEHLAHR-------QIGE----LSGGQKKRVFL 154
Cdd:COG1132 421 Q--DT-FLFSGTIRENIRYGR---------PDA-TDEEVEEAAKAAQAHEFIEAlpdgydtVVGErgvnLSGGQRQRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 155 ARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLReEGHLILVSTHNLGSVPDfCDQVVMINR-TVIAAG 224
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDgRIVEQG 556
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-234 |
2.17e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 135.27 E-value: 2.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNghtaiHNMTFSL--NSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCD-----LPISQalkR-- 78
Cdd:COG3840 2 LRLDDLTYRYGD-----FPLRFDLtiAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltaLPPAE---Rpv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 79 -------NLvayvpqseevdwqFP-VSVYDVVMMGrygymnfLRiPK----AIDKQKVQEAMQRVNIEHLAHRQIGELSG 146
Cdd:COG3840 74 smlfqenNL-------------FPhLTVAQNIGLG-------LR-PGlkltAEQRAQVEQALERVGLAGLLDRLPGQLSG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 147 GQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAG 224
Cdd:COG3840 133 GQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADgRIAADG 212
|
250
....*....|
gi 1169664 225 KTEDTFNQHN 234
Cdd:COG3840 213 PTAALLDGEP 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
10-232 |
4.42e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 137.92 E-value: 4.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKL-----CDLPISqalKRNlVAYV 84
Cdd:COG3842 8 LENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLdgrdvTGLPPE---KRN-VGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSEEVdwqFP-VSVYDVVmmgRYGyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSP 163
Cdd:COG3842 83 FQDYAL---FPhLTVAENV---AFG-LRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 164 IILLDEPFTGVDVKT-ENAIVDLLQQLREEG-HLILVsTHnlgsvpdfcDQ----------VVMINRTVIAAGKTEDTFN 231
Cdd:COG3842 156 VLLLDEPLSALDAKLrEEMREELRRLQRELGiTFIYV-TH---------DQeealaladriAVMNDGRIEQVGTPEEIYE 225
|
.
gi 1169664 232 Q 232
Cdd:COG3842 226 R 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
10-231 |
5.81e-38 |
|
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: 134.21 E-value: 5.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQA--LKRNL--VAYVP 85
Cdd:cd03218 3 AENLSKRYGK-RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmHKRARlgIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEEVdwqF-PVSVYDVVMmgryGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:cd03218 82 QEASI---FrKLTVEENIL----AVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 165 ILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTEDTFN 231
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAyIIYEGKVLAEGTPEEIAA 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
5-230 |
1.38e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 134.98 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 5 STSIWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK-----RN 79
Cdd:PRK13636 3 DYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmklRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 80 LVAYVPQSEevDWQ-FPVSVYDVVmmgRYGYMNfLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARAL 158
Cdd:PRK13636 83 SVGMVFQDP--DNQlFSASVYQDV---SFGAVN-LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169664 159 AQQSPIILLDEPFTGVDVKTENAIVDLLQQLREE-GHLILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTEDTF 230
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVfVMKEGRVILQGNPKEVF 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
26-238 |
1.56e-37 |
|
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: 133.23 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 26 NMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKL--CDLPISQALKRNlVAYVPQSEEVdwqFP-VSVYDVV 102
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLngKDITNLPPEKRD-ISYVPQNYAL---FPhMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 103 MMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAI 182
Cdd:cd03299 93 AYG----LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 183 VDLLQQLREEGHL-ILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTEDTFNQHNLEIV 238
Cdd:cd03299 169 REELKKIRKEFGVtVLHVTHDFEEAWALADKVaIMLNGKLIQVGKPEEVFKKPKNEFV 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-245 |
2.53e-37 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 133.76 E-value: 2.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 5 STSIWVNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPI----SQALKRNl 80
Cdd:PRK10575 9 DTTFALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsSKAFARK- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 81 VAYVPQseevdwQFP----VSVYDVVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLAR 156
Cdd:PRK10575 87 VAYLPQ------QLPaaegMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 157 ALAQQSPIILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFNQHN 234
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGgEMIAQGTPAELMRGET 240
|
250
....*....|....
gi 1169664 235 LEIVFG---GVLRH 245
Cdd:PRK10575 241 LEQIYGipmGILPH 254
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-228 |
9.12e-37 |
|
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: 131.02 E-value: 9.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHtAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPI----SQALKRNLVAYVP 85
Cdd:cd03224 3 VENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItglpPHERARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEEVdwqFP-VSVYDVVMMGRYgymnflripkAIDKQKVQEAMQRV-----NIEHLAHRQIGELSGGQKKRVFLARALA 159
Cdd:cd03224 82 EGRRI---FPeLTVEENLLLGAY----------ARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 160 QQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTED 228
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERgRVVLEGTAAE 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
10-259 |
1.95e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 131.74 E-value: 1.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK-----RNLVAYV 84
Cdd:PRK13639 4 TRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllevRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSEEvDWQFPVSVYDVVMmgrYGYMNfLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:PRK13639 84 FQNPD-DQLFAPTVEEDVA---FGPLN-LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 165 ILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTEDTFNqhNLEIVFGGVL 243
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVyVMSDGKIIKEGTPKEVFS--DIETIRKANL 236
|
250
....*....|....*...
gi 1169664 244 R--HIKLLGENLhNDEDK 259
Cdd:PRK13639 237 RlpRVAHLIEIL-NKEDN 253
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-216 |
2.62e-36 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 136.26 E-value: 2.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 5 STSIWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPI---SQALKRNLV 81
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLadaDADSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 82 AYVPQSEevdWQFPVSVYDVVMMGRygymnflriPKAIDKQkVQEAMQRVNIEHLA-------HRQIGE----LSGGQKK 150
Cdd:TIGR02857 399 AWVPQHP---FLFAGTIAENIRLAR---------PDASDAE-IREALERAGLDEFVaalpqglDTPIGEggagLSGGQAQ 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 151 RVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLReEGHLILVSTHNLGSVPDfCDQVVMI 216
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-202 |
1.69e-35 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 126.77 E-value: 1.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 17 YNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK-----RNLVAYVPQSEEvD 91
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKgllerRQRVGLVFQDPD-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 92 WQFPVSVYDVVmmgRYGYMNfLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPF 171
Cdd:TIGR01166 80 QLFAADVDQDV---AFGPLN-LGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|.
gi 1169664 172 TGVDVKTENAIVDLLQQLREEGHLILVSTHN 202
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVISTHD 186
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-217 |
1.78e-35 |
|
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: 126.95 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLcdlpisqalkrnlvayvpqs 87
Cdd:cd03268 1 LKTNDLTKTYG-KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF-------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 88 EEVDWQFPVSVYDVV-----MMGRYGYM----NFLRIPKA--IDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLAR 156
Cdd:cd03268 60 DGKSYQKNIEALRRIgalieAPGFYPNLtareNLRLLARLlgIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIAL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 157 ALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMIN 217
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIIN 200
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-223 |
6.49e-35 |
|
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: 126.16 E-value: 6.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 7 SIWVNDVTVRYNNG-HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ----ALKRNlV 81
Cdd:cd03245 2 RIEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQldpaDLRRN-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 82 AYVPQseEVdWQFPVSVYDVVMMGRygymnflripKAIDKQKVQEAMQRVNIEHLAHR-------QIGE----LSGGQKK 150
Cdd:cd03245 81 GYVPQ--DV-TLFYGTLRDNITLGA----------PLADDERILRAAELAGVTDFVNKhpngldlQIGErgrgLSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169664 151 RVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVsTHNLgSVPDFCDQVVMINRTVIAA 223
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIII-THRP-SLLDLVDRIIVMDSGRIVA 218
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
12-224 |
7.79e-35 |
|
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: 133.45 E-value: 7.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 12 DVTVRY-NNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ----ALKRNlVAYVPQ 86
Cdd:TIGR03375 468 NVSFAYpGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQidpaDLRRN-IGYVPQ 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 87 SEevdWQFPVSVYDVVMMGRygymnflripKAIDKQKVQEAMQRVNIEHLA--H-----RQIGE----LSGGQKKRVFLA 155
Cdd:TIGR03375 547 DP---RLFYGTLRDNIALGA----------PYADDEEILRAAELAGVTEFVrrHpdgldMQIGErgrsLSGGQRQAVALA 613
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 156 RALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVsTHNLgSVPDFCDQVVMINR-TVIAAG 224
Cdd:TIGR03375 614 RALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLV-THRT-SLLDLVDRIIVMDNgRIVADG 681
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
10-217 |
2.91e-34 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 123.07 E-value: 2.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEI-----KLCDLPISQALKRNLVAYV 84
Cdd:cd03229 3 LKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIlidgeDLTDLEDELPPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQseevDWQ-FP-VSVYDVVMMGrygymnflripkaidkqkvqeamqrvniehlahrqigeLSGGQKKRVFLARALAQQS 162
Cdd:cd03229 82 FQ----DFAlFPhLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 163 PIILLDEPFTGVDVKTENAIVDLLQQLREE-GHLILVSTHNLGSVPDFCDQVVMIN 217
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
8-228 |
3.14e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 124.76 E-value: 3.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCD-----LPISQ-AlkRNLV 81
Cdd:COG1137 4 LEAENLVKSYG-KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGedithLPMHKrA--RLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 82 AYVPQSEEVDWQfpVSVYDVVMMgrygYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQ 161
Cdd:COG1137 81 GYLPQEASIFRK--LTVEDNILA----VLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169664 162 SPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHN----LGsvpdFCDQV-VMINRTVIAAGKTED 228
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNvretLG----ICDRAyIISEGKVLAEGTPEE 222
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-218 |
3.55e-34 |
|
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: 124.26 E-value: 3.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ---ALKRNLVAYV 84
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDisrKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSeevDWQFPVSVYDVVMMGRygymnflripKAIDKQKVQEAMQRVN----IEHLA---HRQIGE----LSGGQKKRVF 153
Cdd:cd03254 83 LQD---TFLFSGTIMENIRLGR----------PNATDEEVIEAAKEAGahdfIMKLPngyDTVLGEnggnLSQGERQLLA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169664 154 LARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLReEGHLILVSTHNLGSVPDfCDQVVMINR 218
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKN-ADKILVLDD 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
12-202 |
3.60e-34 |
|
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: 124.06 E-value: 3.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 12 DVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQaLKRNLVAYVPQSEEVD 91
Cdd:cd03292 5 NVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSD-LRGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 92 WQ-----FPVSVYDVVMMGrygymnfLRI----PKAIDKqKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQS 162
Cdd:cd03292 84 FQdfrllPDRNVYENVAFA-------LEVtgvpPREIRK-RVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1169664 163 PIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHN 202
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHA 195
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-228 |
8.53e-34 |
|
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: 123.55 E-value: 8.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHtAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ----ALKRNLVAYVP 85
Cdd:COG0410 6 VENLHAGYGGIH-VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlpphRIARLGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEEVdwqFP-VSVYDVVMMGRYGymnflripkAIDKQKVQEAMQRV-----NIEHLAHRQIGELSGGQKKRVFLARALA 159
Cdd:COG0410 85 EGRRI---FPsLTVEENLLLGAYA---------RRDRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169664 160 QQSPIILLDEPFTG-----VDvktenAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTED 228
Cdd:COG0410 153 SRPKLLLLDEPSLGlapliVE-----EIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERgRIVLEGTAAE 222
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-227 |
1.04e-33 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 123.69 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 5 STSIWVNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLcdlpiSQALKrnlVAYV 84
Cdd:PRK09544 2 TSLVSLENVSVSFGQ-RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKR-----NGKLR---IGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSEEVDWQFPVSVydvvmmGRygymnFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:PRK09544 73 PQKLYLDTTLPLTV------NR-----FLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169664 165 ILLDEPFTGVDVKTENAIVDLLQQLREE-GHLILVSTHNLGSVPDFCDQVVMINRTVIAAGKTE 227
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPE 205
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
12-216 |
1.19e-33 |
|
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: 122.34 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 12 DVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCD---LPI----SQALKRNLVAYV 84
Cdd:TIGR03608 3 NISKKFGD-KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGqetPPLnskkASKFRREKLGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSEE-VDWQfpvSVYDVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSP 163
Cdd:TIGR03608 82 FQNFAlIENE---TVEENLDLG----LKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1169664 164 IILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLgSVPDFCDQVVMI 216
Cdd:TIGR03608 155 LILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-230 |
1.37e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 124.36 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRY-NNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK---RNLVAY 83
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwdvRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 VPQSEevDWQF-PVSVYDVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQS 162
Cdd:PRK13635 86 VFQNP--DNQFvGATVQDDVAFG----LENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 163 PIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVS-THNLGSVPdFCDQVVMINR-TVIAAGKTEDTF 230
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEAA-QADRVIVMNKgEILEEGTPEEIF 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-215 |
2.23e-33 |
|
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: 124.40 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRY--NNGH-TAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQ---QGEIKLCDLPISQALKRNL--- 80
Cdd:COG0444 4 VRNLKVYFptRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELrki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 81 ----VAYVPQSeevdwqfPVS-------VYDVVMMgryGYMNFLRIPKAIDKQKVQEAMQRVNI---EHLAHRQIGELSG 146
Cdd:COG0444 84 rgreIQMIFQD-------PMTslnpvmtVGDQIAE---PLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169664 147 GQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL--ILVsTHNLGSVPDFCDQV-VM 215
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLaiLFI-THDLGVVAEIADRVaVM 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-241 |
4.38e-33 |
|
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: 124.44 E-value: 4.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 29 FSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKL-----------CDLPisqALKRNLvAYVPQSEEVdwqFP-V 96
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqdsargIFLP---PHRRRI-GYVFQEARL---FPhL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 97 SVydvvmMG--RYGYMnflRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGV 174
Cdd:COG4148 93 SV-----RGnlLYGRK---RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169664 175 DVKTENAIVDLLQQLREEGHL-ILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFNQHNLEIVFGG 241
Cdd:COG4148 165 DLARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQgRVVASGPLAEVLSRPDLLPLAGG 233
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-213 |
4.67e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 124.42 E-value: 4.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 6 TSIWVNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKL-----CDLPISqalKRNl 80
Cdd:COG3839 2 ASLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIggrdvTDLPPK---DRN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 81 VAYVPQSEEVdwqFP-VSVYDVVMMGrygymnfLRI---PKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLAR 156
Cdd:COG3839 77 IAMVFQSYAL---YPhMTVYENIAFP-------LKLrkvPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169664 157 ALAQQSPIILLDEPFTGVDVK------TEnaIVDLLQQLreeGHLILVSTHnlgsvpdfcDQV 213
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDAKlrvemrAE--IKRLHRRL---GTTTIYVTH---------DQV 195
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-232 |
5.87e-33 |
|
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: 121.15 E-value: 5.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGH---TAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL---- 80
Cdd:cd03258 2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 81 --VAYVPQseevdwQFPV----SVYDVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFL 154
Cdd:cd03258 82 rrIGMIFQ------HFNLlssrTVFENVALP----LEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 155 ARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREE-GHLILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTEDTFNQ 232
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVaVMEKGEVVEEGTVEEVFAN 231
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-269 |
7.39e-33 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 121.77 E-value: 7.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHT-AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS--QALK--RNLVA 82
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdeENLWeiRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 83 YVPQSEevDWQFpVS--VYDVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQ 160
Cdd:TIGR04520 81 MVFQNP--DNQF-VGatVEDDVAFG----LENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 161 QSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVS-THNLGSVPDfCDQVVMINR-TVIAAGKTEDTFNQHNLeiv 238
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISiTHDMEEAVL-ADRVIVMNKgKIVAEGTPREIFSQVEL--- 229
|
250 260 270
....*....|....*....|....*....|....*...
gi 1169664 239 fggvLRHIKL-------LGENLHNDEDKRSVTVLTDDE 269
Cdd:TIGR04520 230 ----LKEIGLdvpfiteLAKALKKRGIPLPPDILTEEE 263
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
12-234 |
1.28e-32 |
|
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: 120.48 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 12 DVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ----ALKRNLvAYVPQS 87
Cdd:cd03295 5 NVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqdpvELRRKI-GYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 88 EEVdwqFP-VSVYDVVMMgrygYMNFLRIPKAIDKQKVQEAMQRVNIE--HLAHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:cd03295 84 IGL---FPhMTVEENIAL----VPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169664 165 ILLDEPFTGVDVKTENAIVDLLQQLREE-GHLILVSTHNLGSVPDFCDQVVMINRTVIAAGKTEDTF--NQHN 234
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIlrSPAN 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-228 |
2.50e-32 |
|
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: 119.40 E-value: 2.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK--RNLVAYVP 85
Cdd:cd03265 1 IEVENLVKKYG-DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRevRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEEVD-----WQfpvsvyDVVMMGR-YGYmnflriPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALA 159
Cdd:cd03265 80 QDLSVDdeltgWE------NLYIHARlYGV------PGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 160 QQSPIILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTED 228
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHgRIIAEGTPEE 218
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-253 |
4.58e-32 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 119.17 E-value: 4.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 28 TFSLNSGTICALVGVNGSGKSTLFKSIMGLVkPQQGEIKLCDLPISQ------ALKRnlvAYVPQSeevdwQFPVSvydv 101
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwsaaelARHR---AYLSQQ-----QSPPF---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 102 vMMGRYGYMNfLRIPKAIDKQKVQEAM----QRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSP-------IILLDEP 170
Cdd:COG4138 83 -AMPVFQYLA-LHQPAGASSEAVEQLLaqlaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPtinpegqLLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 171 FTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFNQHNLEIVFGGVLRHIKLL 249
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQgKLVASGETAEVMTPENLSEVFGVKFRRLEVE 240
|
....
gi 1169664 250 GENL 253
Cdd:COG4138 241 GHRW 244
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
8-231 |
5.24e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.71 E-value: 5.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHT-AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQA-LK--RNLVAY 83
Cdd:PRK13632 8 IKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKeiRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 VPQSEevDWQF-PVSVYDVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQS 162
Cdd:PRK13632 88 IFQNP--DNQFiGATVEDDIAFG----LENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 163 PIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVS-THNLGSVPDfCDQV-VMINRTVIAAGKTEDTFN 231
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAIL-ADKViVFSEGKLIAQGKPKEILN 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-240 |
8.58e-32 |
|
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: 118.21 E-value: 8.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 7 SIWVNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ--ALKRNlVAYV 84
Cdd:cd03296 2 SIEVRNVSKRFGD-FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDvpVQERN-VGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSEEVdwqFP-VSVYDVVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSP 163
Cdd:cd03296 80 FQHYAL---FRhMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169664 164 IILLDEPFTGVDVKTENAIVDLLQQLREEGHLILV-STHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFNQHNLEIVFG 240
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVfVTHDQEEALEVADRVVVMNKgRIEQVGTPDEVYDHPASPFVYS 235
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
20-241 |
1.23e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 118.07 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 20 GHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS----QALKRNLVAYVPQSEEVDWQfp 95
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHARARRGIGYLPQEASIFRR-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 96 VSVYDvvmmgryGYMNFLRIPKAIDKQ----KVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPF 171
Cdd:PRK10895 93 LSVYD-------NLMAVLQIRDDLSAEqredRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 172 TGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFNQHNLEIVFGG 241
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQgHLIAHGTPTEILQDEHVKRVYLG 236
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-216 |
2.70e-31 |
|
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: 116.24 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 26 NMTFSLNSGTIcALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPI-SQALKRNL------VAYVPQSEEVdwqFP-VS 97
Cdd:cd03297 16 KIDFDLNEEVT-GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfDSRKKINLppqqrkIGLVFQQYAL---FPhLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 98 VYDVVMmgrYGYMnflRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVK 177
Cdd:cd03297 92 VRENLA---FGLK---RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1169664 178 TENAIVDLLQQLREE--GHLILVsTHNLGSVPDFCDQVVMI 216
Cdd:cd03297 166 LRLQLLPELKQIKKNlnIPVIFV-THDLSEAEYLADRIVVM 205
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-218 |
3.45e-31 |
|
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: 114.62 E-value: 3.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRY-NNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ---ALKRNLVAY 83
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwdpNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 VPQSEEVdwqFPVSVYDvvmmgrygymnflripkaidkqkvqeamqrvNIehlahrqigeLSGGQKKRVFLARALAQQSP 163
Cdd:cd03246 81 LPQDDEL---FSGSIAE-------------------------------NI----------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1169664 164 IILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLgSVPDFCDQVVMINR 218
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLED 170
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
8-250 |
5.22e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.14 E-value: 5.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK---RNLVAYV 84
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkwvRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSEEvDWQFPVSVYDVVMmgrYGYMNfLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:PRK13647 85 FQDPD-DQVFSSTVWDDVA---FGPVN-MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 165 ILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMIN--RTVIAAGKT----EDTFNQHNLEI- 237
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKegRVLAEGDKSlltdEDIVEQAGLRLp 239
|
250
....*....|...
gi 1169664 238 VFGGVLRHIKLLG 250
Cdd:PRK13647 240 LVAQIFEDLPELG 252
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-225 |
5.83e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 117.98 E-value: 5.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK--RNLVAYVP 85
Cdd:PRK13537 8 IDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARhaRQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEEVDWQFPVSvYDVVMMGRYgymnfLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPII 165
Cdd:PRK13537 87 QFDNLDPDFTVR-ENLLVFGRY-----FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 166 LLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMI-NRTVIAAGK 225
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIeEGRKIAEGA 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-253 |
1.71e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 117.24 E-value: 1.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 5 STSIWVNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPI-SQA-LKRNLVA 82
Cdd:PRK13536 39 TVAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARArLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 83 YVPQSEEVDWQFPVSvYDVVMMGRYGYMNFLRIPKAIdkqkvQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQS 162
Cdd:PRK13536 118 VVPQFDNLDLEFTVR-ENLLVFGRYFGMSTREIEAVI-----PSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 163 PIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRTV-IAAGKTEDTFNQH-------- 233
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRkIAEGRPHALIDEHigcqviei 271
|
250 260
....*....|....*....|....*.
gi 1169664 234 ------NLEIVFGGVLRHIKLLGENL 253
Cdd:PRK13536 272 yggdphELSSLVKPYARRIEVSGETL 297
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-217 |
2.56e-30 |
|
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: 114.35 E-value: 2.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 22 TAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDL-PISQ--ALKRNLVAYVPQSEEVDWQFPVSv 98
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKRrkKFLRRIGVVFGQKTQLWWDLPVI- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 99 yDVVMMGRYGYmnflRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKT 178
Cdd:cd03267 114 -DSFYLLAAIY----DLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1169664 179 ENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVVMIN 217
Cdd:cd03267 189 QENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-221 |
2.58e-30 |
|
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: 113.78 E-value: 2.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK-----RNLVA 82
Cdd:cd03262 1 IEIKNLHKSFGD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKninelRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 83 YVPQSEEVdwqFP-VSVYDVVMMGRygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQ 161
Cdd:cd03262 80 MVFQQFNL---FPhLTVLENITLAP---IKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 162 SPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRTVI 221
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
10-218 |
3.47e-30 |
|
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: 112.95 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHT----AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCdlpisqalkrNLVAYVP 85
Cdd:cd03250 3 VEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP----------GSIAYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEevdWQFPVSVYDVVMMGrygymnflripKAIDKQKVQEAMQ----RVNIEHLAHR---QIGE----LSGGQKKRVFL 154
Cdd:cd03250 73 QEP---WIQNGTIRENILFG-----------KPFDEERYEKVIKacalEPDLEILPDGdltEIGEkginLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 155 ARALAQQSPIILLDEPFTGVDVKTENAIVD--LLQQLREEGHLILVsTHNLGSVPDfCDQVVMINR 218
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILV-THQLQLLPH-ADQIVVLDN 202
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-202 |
1.01e-29 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 111.89 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 19 NGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCD------LPISQ--------ALKRNL-VAy 83
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpDVAEAchylghrnAMKPALtVA- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 vpqsEEVD-WQfpvsvydvvmmgrygymNFLripkAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQS 162
Cdd:PRK13539 92 ----ENLEfWA-----------------AFL----GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1169664 163 PIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHN 202
Cdd:PRK13539 147 PIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
10-228 |
1.24e-29 |
|
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: 117.93 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHTAI-HNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL---VAYVP 85
Cdd:COG4618 333 VENLTVVPPGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELgrhIGYLP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEEVdwqFPVSVYDvvmmgrygymNFLRIPKAiDKQKVQEAMQRVN----IEHLAHR---QIGE----LSGGQKKRVFL 154
Cdd:COG4618 413 QDVEL---FDGTIAE----------NIARFGDA-DPEKVVAAAKLAGvhemILRLPDGydtRIGEggarLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169664 155 ARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLgSVPDFCDQV-VMINRTVIAAGKTED 228
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP-SLLAAVDKLlVLRDGRVQAFGPRDE 552
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-234 |
1.48e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 117.62 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 7 SIWVNDVTVRY-NNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS----QALkRNLV 81
Cdd:PRK11160 338 SLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdyseAAL-RQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 82 AYVPQSEEVdwqFPVSVYDVVMMGrygymnflrIPKAIDKQkVQEAMQRVNIEHLAHRQ------IGE----LSGGQKKR 151
Cdd:PRK11160 417 SVVSQRVHL---FSATLRDNLLLA---------APNASDEA-LIEVLQQVGLEKLLEDDkglnawLGEggrqLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 152 VFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVsTHNLGSVPDFcDQV-VMINRTVIAAGKTEDTF 230
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMI-THRLTGLEQF-DRIcVMDNGQIIEQGTHQELL 561
|
....
gi 1169664 231 NQHN 234
Cdd:PRK11160 562 AQQG 565
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
10-203 |
2.33e-29 |
|
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: 117.08 E-value: 2.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPI---SQALKRNLVAYVPQ 86
Cdd:TIGR02868 337 LRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVsslDQDEVRRRVSVCAQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 87 SEEVdwqFPVSVYDVVMMGRygymnflriPKAIDkQKVQEAMQRVNIEHL-------AHRQIGE----LSGGQKKRVFLA 155
Cdd:TIGR02868 417 DAHL---FDTTVRENLRLAR---------PDATD-EELWAALERVGLADWlralpdgLDTVLGEggarLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1169664 156 RALAQQSPIILLDEPFTGVDVKTENAIV-DLLQQLreEGHLILVSTHNL 203
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLeDLLAAL--SGRTVVLITHHL 530
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
8-223 |
3.16e-29 |
|
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: 110.66 E-value: 3.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYnnGHTaihNMTFSLN--SGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKL----------CDLPISQA 75
Cdd:cd03298 1 VRLDKIRFSY--GEQ---PMHFDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIngvdvtaappADRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 76 LKRNLVayvpqseevdwqFP-VSVYDVVMMGRYGYMNFlripKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFL 154
Cdd:cd03298 76 FQENNL------------FAhLTVEQNVGLGLSPGLKL----TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 155 ARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVVMINRTVIAA 223
Cdd:cd03298 140 ARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-203 |
3.74e-29 |
|
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: 111.97 E-value: 3.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 23 AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ-------ALKRNLVAYVPQSEEVdwqFP 95
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrkelrELRRKKISMVFQSFAL---LP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 96 -VSVYDVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGV 174
Cdd:cd03294 116 hRTVLENVAFG----LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190
....*....|....*....|....*....|
gi 1169664 175 DVKTENAIVDLLQQL-REEGHLILVSTHNL 203
Cdd:cd03294 192 DPLIRREMQDELLRLqAELQKTIVFITHDL 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-218 |
4.37e-29 |
|
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: 109.32 E-value: 4.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRY-NNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS--QALKRNLVAYV 84
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSdlEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSeevdwqfpVSVYDVVMMgrygymnflripkaidkqkvqeamqrvniEHLAHRqigeLSGGQKKRVFLARALAQQSPI 164
Cdd:cd03247 81 NQR--------PYLFDTTLR-----------------------------NNLGRR----FSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1169664 165 ILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVsTHNLGSVPDFcDQVVMINR 218
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWI-THHLTGIEHM-DKILFLEN 171
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
10-227 |
4.90e-29 |
|
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: 110.73 E-value: 4.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHtAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVK-----PQQGEIKLCDLPISQ------ALKR 78
Cdd:cd03260 3 LRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldvdvlELRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 79 NlVAYVPQSEEVdwqFPVSVYDVVmmgRYGymnfLRI----PKAIDKQKVQEAMQRVNIEHLAHRQIG--ELSGGQKKRV 152
Cdd:cd03260 82 R-VGMVFQKPNP---FPGSIYDNV---AYG----LRLhgikLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 153 FLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEgHLILVSTHNLGSVPDFCDQVVMINRT-VIAAGKTE 227
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGrLVEFGPTE 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-221 |
1.24e-28 |
|
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: 109.63 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGhTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ--ALKRNlVAYVP 85
Cdd:cd03300 1 IELENVSKFYGGF-VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpPHKRP-VNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEEVdwqFP-VSVYDVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:cd03300 79 QNYAL---FPhLTVFENIAFG----LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 165 ILLDEPFTGVDVK-TENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRTVI 221
Cdd:cd03300 152 LLLDEPLGALDLKlRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
10-228 |
1.29e-28 |
|
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: 109.54 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHtAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS----QALKRNLVAYVP 85
Cdd:TIGR03410 3 VSNLNVYYGQSH-ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITklppHERARAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEEVdwqFP-VSVYDVVMMGrygYMNFLRIPKAIDKQ-----KVQEAMQrvniehlaHRQIGELSGGQKKRVFLARALA 159
Cdd:TIGR03410 82 QGREI---FPrLTVEENLLTG---LAALPRRSRKIPDEiyelfPVLKEML--------GRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 160 QQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL-ILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTED 228
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMaILLVEQYLDFARELADRYYVMERgRVVASGAGDE 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
3.37e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.11 E-value: 3.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 1 MDsfstsIWVNDVTVRYNNG----HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS--- 73
Cdd:PRK13634 1 MD-----ITFQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 74 --QALK--RNLVAYVpqseevdWQFPVS-------VYDVVmmgrYGYMNFlRIPKAIDKQKVQEAMQRVNI-EHLAHRQI 141
Cdd:PRK13634 76 knKKLKplRKKVGIV-------FQFPEHqlfeetvEKDIC----FGPMNF-GVSEEDAKQKAREMIELVGLpEELLARSP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 142 GELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL--ILVsTHNLGSVPDFCDQ-VVMINR 218
Cdd:PRK13634 144 FELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLttVLV-THSMEDAARYADQiVVMHKG 222
|
250
....*....|..
gi 1169664 219 TVIAAGKTEDTF 230
Cdd:PRK13634 223 TVFLQGTPREIF 234
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-244 |
6.71e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 108.56 E-value: 6.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 19 NGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLV---KPQQGEIKLCDLPISQA--LKRNLVAYVPQSEEVDWQ 93
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREgrLARDIRKSRANTGYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 94 FPV----SVYDVVMMGRYGYMNF----LRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPII 165
Cdd:PRK09984 95 FNLvnrlSVLENVLIGALGSTPFwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 166 LLDEPFTGVDVKTENAIVDLLQQLRE-EGHLILVSTHNLGSVPDFCDQVVMINRTVIAAGKTEDTFNQHNLEIVFGGVLR 244
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNERFDHLYRSINR 254
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-230 |
1.03e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 108.56 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 12 DVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQAlKRNLVAYVPQSEEVd 91
Cdd:PRK13638 6 DLWFRYQD-EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYS-KRGLLALRQQVATV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 92 WQFP---VSVYDVVMMGRYGYMNfLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLD 168
Cdd:PRK13638 83 FQDPeqqIFYTDIDSDIAFSLRN-LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169664 169 EPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTF 230
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQgQILTHGAPGEVF 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-201 |
1.15e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 108.03 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNG---HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ-ALKRNLV---- 81
Cdd:COG4525 6 VRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGpGADRGVVfqkd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 82 AYVPqseevdWQfpvSVYDVVMMGrygymnfLRI---PKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARAL 158
Cdd:COG4525 86 ALLP------WL---NVLDNVAFG-------LRLrgvPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1169664 159 AQQSPIILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTH 201
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITH 193
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-221 |
1.29e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.79 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 7 SIWVNDVTVRYnnGHTAI-HNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL-VAYV 84
Cdd:PRK10851 2 SIEIANIKKSF--GRTQVlNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRkVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSEEVdwqFP-VSVYDVVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSP 163
Cdd:PRK10851 80 FQHYAL---FRhMTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1169664 164 IILLDEPFTGVDVKTENAIVDLLQQLREEGHLILV-STHNLGSVPDFCDQVVMINRTVI 221
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVfVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-220 |
1.37e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.70 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKlcdlpISQALKrnlVAYVPQseE 89
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS-----IPKGLR---IGYLPQ--E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 90 VDWQFPVSVYDVVMMG-----------RYGYMNFLRIPKAIDKQ-----------------KVQEAMQRVNI-EHLAHRQ 140
Cdd:COG0488 70 PPLDDDLTVLDTVLDGdaelraleaelEELEAKLAEPDEDLERLaelqeefealggweaeaRAEEILSGLGFpEEDLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 141 IGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVkteNAIVDLLQQLRE-EGHLILVStHnlgsvpD--FCDQVVmiN 217
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL---ESIEWLEEFLKNyPGTVLVVS-H------DryFLDRVA--T 217
|
...
gi 1169664 218 RTV 220
Cdd:COG0488 218 RIL 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-240 |
3.01e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 106.99 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 11 NDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL---VAYVPQS 87
Cdd:PRK10253 11 EQLTLGYGK-YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVarrIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 88 EEVDWQfpVSVYDVVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILL 167
Cdd:PRK10253 90 ATTPGD--ITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169664 168 DEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFNQHNLEIVFG 240
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREgKIVAQGAPKEIVTAELIERIYG 242
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-218 |
3.74e-27 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 110.96 E-value: 3.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 5 STSIWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS----QALkRNL 80
Cdd:PRK10790 338 SGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSslshSVL-RQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 81 VAYVPQSeevdwqfPV----SVYDVVMMGRygymnflripkAIDKQKVQEAMQRVNIEHLA-------HRQIGE----LS 145
Cdd:PRK10790 417 VAMVQQD-------PVvladTFLANVTLGR-----------DISEEQVWQALETVQLAELArslpdglYTPLGEqgnnLS 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169664 146 GGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVStHNLGSVPDfCDQVVMINR 218
Cdd:PRK10790 479 VGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA-HRLSTIVE-ADTILVLHR 549
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-226 |
4.94e-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: 104.56 E-value: 4.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 7 SIWVNDVTV-----RYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQ--GEIKLCDLPISQALKRN 79
Cdd:cd03213 3 TLSFRNLTVtvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 80 LVAYVPQSeevdwqfpvsvyDVVmmgrygymnflripkaIDKQKVQEAMQrvnieHLAHRQigELSGGQKKRVFLARALA 159
Cdd:cd03213 83 IIGYVPQD------------DIL----------------HPTLTVRETLM-----FAAKLR--GLSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 160 QQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNL-GSVPDFCDQVVminrtVIAAGKT 226
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLL-----LLSQGRV 190
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-235 |
5.04e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.81 E-value: 5.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQA-LK--RNLVAYV 84
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnIRevRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSEEvDWQFPVSVYDVVMmgrYGYMNfLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:PRK13652 84 FQNPD-DQIFSPTVEQDIA---FGPIN-LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169664 165 ILLDEPFTGVDVKTENAIVDLLQQLREE-GHLILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTEDTFNQHNL 235
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIyVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
6.80e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.99 E-value: 6.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 1 MDSFSTSIWVNDVTVRYNNGHT-AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRN 79
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 80 L---VAYVPQSEEVdwQFPVSV--YDVVmmgrYGYMNFLrIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFL 154
Cdd:PRK13648 81 LrkhIGIVFQNPDN--QFVGSIvkYDVA----FGLENHA-VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169664 155 ARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVS-THNLGSVPDfCDQVVMINR-TVIAAGKTEDTFN 231
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISiTHDLSEAME-ADHVIVMNKgTVYKEGTPTEIFD 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
10-203 |
8.48e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 105.55 E-value: 8.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS-QALKRNLVAyvpQSE 88
Cdd:PRK11248 4 ISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgPGAERGVVF---QNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 89 EV-DWQfpvSVYDVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILL 167
Cdd:PRK11248 80 GLlPWR---NVQDNVAFG----LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1169664 168 DEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNL 203
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDI 189
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
10-232 |
9.15e-27 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 105.08 E-value: 9.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQAlKRNL------VAY 83
Cdd:COG1126 4 IENLHKSFGD-LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDS-KKDInklrrkVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 VPQSEEVdwqFP-VSVYDVVMMGRygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQS 162
Cdd:COG1126 82 VFQQFNL---FPhLTVLENVTLAP---IKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 163 PIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVV-MINRTVIAAGKTEDTFNQ 232
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVfMDGGRIVEEGPPEEFFEN 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-282 |
1.19e-26 |
|
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: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRY---NNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNLVAY- 83
Cdd:COG1135 2 IELENLSKTFptkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 -----VPQseevdwQFPV----SVYDVVMMGrygymnfLRI---PKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKR 151
Cdd:COG1135 82 rkigmIFQ------HFNLlssrTVAENVALP-------LEIagvPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 152 VFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL-ILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTEDT 229
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLtIVLITHEMDVVRRICDRVaVLENGRIVEQGPVLDV 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 230 FN--QHNLeivfggvLRhiKLLGENLHNDEDKRSVTVLTDDEKA-----VVFYGETKQDP 282
Cdd:COG1135 229 FAnpQSEL-------TR--RFLPTVLNDELPEELLARLREAAGGgrlvrLTFVGESADEP 279
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-216 |
1.83e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 105.30 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 26 NMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPI-----SQALK--RNLVAYVPQSEEVDWqFPVSV 98
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgNKNLKklRKKVSLVFQFPEAQL-FENTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 99 YDVVMmgrYGYMNF-LRIPKAidKQKVQEAMQRVNI-EHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDV 176
Cdd:PRK13641 104 LKDVE---FGPKNFgFSEDEA--KEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1169664 177 KTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMI 216
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVL 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
7-232 |
2.23e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 105.13 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 7 SIWVNDVTVRYNNG----HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPI-SQALK---- 77
Cdd:PRK13637 2 SIKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItDKKVKlsdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 78 RNLVAYVPQSEEvdWQ-FPVSVY-DVVmmgrYGYMNfLRIPKAIDKQKVQEAMQRVNI--EHLAHRQIGELSGGQKKRVF 153
Cdd:PRK13637 82 RKKVGLVFQYPE--YQlFEETIEkDIA----FGPIN-LGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 154 LARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL--ILVStHNLGSVPDFCDQVVMINR-TVIAAGKTEDTF 230
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMtiILVS-HSMEDVAKLADRIIVMNKgKCELQGTPREVF 233
|
..
gi 1169664 231 NQ 232
Cdd:PRK13637 234 KE 235
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-205 |
2.87e-26 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 103.50 E-value: 2.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 24 IHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLV---KPQQGEIKLCDLPISQALKRNLVAYVPQSEevDWQFPVSVYD 100
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKPDQFQKCVAYVRQDD--ILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 101 VVMmgrygYMNFLRIP----KAIDKQKV-QEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVD 175
Cdd:cd03234 101 TLT-----YTAILRLPrkssDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190
....*....|....*....|....*....|
gi 1169664 176 VKTENAIVDLLQQLREEGHLILVSTHNLGS 205
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIHQPRS 205
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
22-235 |
3.05e-26 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 104.15 E-value: 3.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 22 TAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIsqalkrnlvayvpqseevdwQFpvsvydv 101
Cdd:COG4167 27 EAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL--------------------EY------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 102 vmmGRYGY------MNF----------LRIPKAID--------------KQKVQEAMQRVNI--EHlAHRQIGELSGGQK 149
Cdd:COG4167 80 ---GDYKYrckhirMIFqdpntslnprLNIGQILEeplrlntdltaeerEERIFATLRLVGLlpEH-ANFYPHMLSSGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 150 KRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL--ILVStHNLGSVPDFCDQV-VMINRTVIAAGKT 226
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGIsyIYVS-QHLGIVKHISDKVlVMHQGEVVEYGKT 234
|
250
....*....|.
gi 1169664 227 EDTFN--QHNL 235
Cdd:COG4167 235 AEVFAnpQHEV 245
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-253 |
3.15e-26 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 103.86 E-value: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 28 TFSLNSGTICALVGVNGSGKSTLFKSIMGLVkPQQGEIKLCDLPISQ------ALKRnlvAYVPQSeevdwQFPVSVYDV 101
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsaaelARHR---AYLSQQ-----QTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 102 vmmgrYGYMNfLRIPKAIDKQKVQEAM----QRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPII-------LLDEP 170
Cdd:PRK03695 87 -----FQYLT-LHQPDKTRTEAVASALnevaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqllLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 171 FTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFNQHNLEIVFGGVLRHIKLL 249
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQgKLLASGRRDEVLTPENLAQVFGVNFRRLDVE 240
|
....
gi 1169664 250 GENL 253
Cdd:PRK03695 241 GHPM 244
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-229 |
3.61e-26 |
|
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: 103.28 E-value: 3.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 1 MDSFSTS-IWVNDVTVRYNNGH---TAIHNMTFSLNSGTICALVGVNGSGKSTLFkSIM-GLVKPQQGEIKLCDLPISQ- 74
Cdd:COG4181 1 MSSSSAPiIELRGLTKTVGTGAgelTILKGISLEVEAGESVAIVGASGSGKSTLL-GLLaGLDRPTSGTVRLAGQDLFAl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 75 ------ALKRNLVAYVPQSeevdwqFPV----SVYDVVMM-----GRygymnflriPKAidKQKVQEAMQRVNIEHLAHR 139
Cdd:COG4181 80 dedaraRLRARHVGFVFQS------FQLlptlTALENVMLplelaGR---------RDA--RARARALLERVGLGHRLDH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 140 QIGELSGGQKKRVFLARALAQQSPIILLDEPfTG-VDVKTENAIVDLLQQLREEGH--LILVsTHNLgSVPDFCDQVVmi 216
Cdd:COG4181 143 YPAQLSGGEQQRVALARAFATEPAILFADEP-TGnLDAATGEQIIDLLFELNRERGttLVLV-THDP-ALAARCDRVL-- 217
|
250
....*....|...
gi 1169664 217 nrtVIAAGKTEDT 229
Cdd:COG4181 218 ---RLRAGRLVED 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
10-217 |
3.72e-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: 104.12 E-value: 3.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNG--------HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQaLKRNLV 81
Cdd:TIGR02769 5 VRDVTHTYRTGglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQ-LDRKQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 82 AYVPQSEEVDWQFPVSVYDVVMMGRY----GYMNFLRIPKAIDKQKVQEAMQRVNIE-HLAHRQIGELSGGQKKRVFLAR 156
Cdd:TIGR02769 84 RAFRRDVQLVFQDSPSAVNPRMTVRQiigePLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169664 157 ALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL-ILVSTHNLGSVPDFCDQVVMIN 217
Cdd:TIGR02769 164 ALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMD 225
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-232 |
4.35e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.43 E-value: 4.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 23 AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNLVAYVPQSEEVDWQFPVS-VYDV 101
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESqLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 102 VMMG--RYGYMNFlRIPKAIDKQKVQEAMQRVNI-EHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKT 178
Cdd:PRK13643 101 TVLKdvAFGPQNF-GIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1169664 179 ENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRT-VIAAGKTEDTFNQ 232
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGhIISCGTPSDVFQE 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-229 |
5.02e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.03 E-value: 5.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS-----QALKRNlVAYV 84
Cdd:COG1129 7 MRGISKSFG-GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrsprDAQAAG-IAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQseEVDwQFP-VSVYDVVMMGRYgYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSP 163
Cdd:COG1129 85 HQ--ELN-LVPnLSVAENIFLGRE-PRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 164 IILLDEP---FTGVDVKtenAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTEDT 229
Cdd:COG1129 161 VLILDEPtasLTEREVE---RLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVtVLRDGRLVGTGPVAEL 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-233 |
5.71e-26 |
|
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: 107.08 E-value: 5.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRY----------NNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVkPQQGEIKLCDLPIS------ 73
Cdd:COG4172 278 ARDLKVWFpikrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDglsrra 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 74 -QALKRNLvayvpQseeVDWQFPVS-------VYDVVMMGrygyMNFLRIP--KAIDKQKVQEAMQRVNI-EHLAHRQIG 142
Cdd:COG4172 357 lRPLRRRM-----Q---VVFQDPFGslsprmtVGQIIAEG----LRVHGPGlsAAERRARVAEALEEVGLdPAARHRYPH 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 143 ELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL--ILVStHNLGSVPDFCDQV-VMINRT 219
Cdd:COG4172 425 EFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLayLFIS-HDLAVVRALAHRVmVMKDGK 503
|
250
....*....|....*.
gi 1169664 220 VIAAGKTEDTFN--QH 233
Cdd:COG4172 504 VVEQGPTEQVFDapQH 519
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
10-208 |
1.78e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 100.63 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQ---QGEIKLCDLPIS--QALKRNlVAYV 84
Cdd:COG4136 4 LENLTITLG-GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTalPAEQRR-IGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSeevDWQFP-VSVYDVVMMGrygymnfL--RIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQ 161
Cdd:COG4136 82 FQD---DLLFPhLSVGENLAFA-------LppTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1169664 162 SPIILLDEPFTGVDVKTENAIVDL-LQQLREEGHLILVSTHNLGSVPD 208
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTHDEEDAPA 199
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-203 |
2.30e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 101.05 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 16 RYNNG--HT-AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ-------ALKRNLVAYVP 85
Cdd:PRK11629 14 RYQEGsvQTdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakaELRNQKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEEVDWQFpVSVYDVVMMGRYGYMNflriPKAIdKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPII 165
Cdd:PRK11629 94 QFHHLLPDF-TALENVAMPLLIGKKK----PAEI-NSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 1169664 166 LLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNL 203
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL 206
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
8-222 |
2.38e-25 |
|
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: 100.71 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYnngHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ-ALKRNLVAYVPQ 86
Cdd:TIGR01277 1 LALDKVRYEY---EHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGlAPYQRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 87 SEEVdwqFP-VSVYDVVMMGRYGYMNFlripKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPII 165
Cdd:TIGR01277 78 ENNL---FAhLTVRQNIGLGLHPGLKL----NAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 166 LLDEPFTGVDVKTENAIVDLLQQLREEGHL-ILVSTHNLGSVPDFCDQVVMINRTVIA 222
Cdd:TIGR01277 151 LLDEPFSALDPLLREEMLALVKQLCSERQRtLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
23-218 |
2.74e-25 |
|
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: 100.59 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 23 AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCD----LPISQA-------LKRNLVAYVpqSeevd 91
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwVDLAQAspreilaLRRRTIGYV--S---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 92 wQF----P-VSVYDVVM-----MGrygymnflrIPKAIDKQKVQEAMQRVNI-EHLAHRQIGELSGGQKKRVFLARALAQ 160
Cdd:COG4778 100 -QFlrviPrVSALDVVAeplleRG---------VDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVNIARGFIA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 161 QSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINR 218
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-223 |
3.29e-25 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 98.65 E-value: 3.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS----QALKRNLVAYVP 85
Cdd:cd03216 3 LRGITKRFG-GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfaspRDARRAGIAMVY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QseevdwqfpvsvydvvmmgrygymnflripkaidkqkvqeamqrvniehlahrqigeLSGGQKKRVFLARALAQQSPII 165
Cdd:cd03216 82 Q---------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 166 LLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRTVIAA 223
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-199 |
3.38e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.15 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKlcdlpISQALKrnlVAYVPQSEE 89
Cdd:COG0488 318 LEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-----LGETVK---IGYFDQHQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 90 vdwQFPV--SVYDVVMMGRygymnflripkaiDKQKVQEAMQRVniEHL------AHRQIGELSGGQKKRVFLARALAQQ 161
Cdd:COG0488 389 ---ELDPdkTVLDELRDGA-------------PGGTEQEVRGYL--GRFlfsgddAFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190
....*....|....*....|....*....|....*...
gi 1169664 162 SPIILLDEPFTGVDVKTENAIVDLLQQLreEGHLILVS 199
Cdd:COG0488 451 PNVLLLDEPTNHLDIETLEALEEALDDF--PGTVLLVS 486
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
12-221 |
5.29e-25 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 99.64 E-value: 5.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 12 DVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEI-----KLCDLPisqALKRNlVAYVPQ 86
Cdd:cd03301 5 NVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrDVTDLP---PKDRD-IAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 87 SEEVdwqFP-VSVYDVVMMGrygymnfLRI---PKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQS 162
Cdd:cd03301 80 NYAL---YPhMTVYDNIAFG-------LKLrkvPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169664 163 PIILLDEPFTGVD----VKTENAIVDLLQQLreeGHLILVSTHNLGSVPDFCDQVVMINRTVI 221
Cdd:cd03301 150 KVFLMDEPLSNLDaklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-231 |
2.64e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.41 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS-----QALKRNlVAYV 84
Cdd:COG3845 8 LRGITKRFG-GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprDAIALG-IGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQseevdwQF----PVSVYDVVMMGRYGyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQ 160
Cdd:COG3845 86 HQ------HFmlvpNLTVAENIVLGLEP-TKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169664 161 QSPIILLDEPfTGvdVKTENAIVDL---LQQLREEGHLILVSTHNLGSVPDFCDQVvminrTVIAAGKTEDTFN 231
Cdd:COG3845 159 GARILILDEP-TA--VLTPQEADELfeiLRRLAAEGKSIIFITHKLREVMAIADRV-----TVLRRGKVVGTVD 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
29-228 |
2.94e-24 |
|
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: 100.57 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 29 FSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKL-----------CDLPIsqalKRNLVAYVPQSEEVdwqFPVs 97
Cdd:TIGR02142 18 FTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtlfdsrkgIFLPP----EKRRIGYVFQEARL---FPH- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 98 vYDVVMMGRYGyMNFLRIPkaiDKQKVQEAMQRV-NIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDV 176
Cdd:TIGR02142 90 -LSVRGNLRYG-MKRARPS---ERRISFERVIELlGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1169664 177 KTENAIVDLLQQLREEGHL-ILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTED 228
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIpILYVSHSLQEVLRLADRVvVLEDGRVAAAGPIAE 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-207 |
3.47e-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: 97.04 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 19 NGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQA---LKRNLvAYVPQSEEVdwQFP 95
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQrdePHENI-LYLGHLPGL--KPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 96 VSVYDvvmmgrygYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVD 175
Cdd:TIGR01189 88 LSALE--------NLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180 190
....*....|....*....|....*....|...
gi 1169664 176 VKTENAIVDLLQQLREEGHLILVSTH-NLGSVP 207
Cdd:TIGR01189 160 KAGVALLAGLLRAHLARGGIVLLTTHqDLGLVE 192
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-230 |
5.93e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.92 E-value: 5.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSI--MGLVKPQ---QGEIKLCDLPIsqalkrnlvaYV 84
Cdd:PRK14239 8 VSDLSVYYNK-KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNI----------YS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSEEVDWQ------------FPVSVYDVVMMGrygymnfLRIPKAIDKQKVQEAMQR----VNI-----EHLAHRQIGe 143
Cdd:PRK14239 77 PRTDTVDLRkeigmvfqqpnpFPMSIYENVVYG-------LRLKGIKDKQVLDEAVEKslkgASIwdevkDRLHDSALG- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 144 LSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVsTHNLGSVPDFCDQV-VMINRTVIA 222
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLV-TRSMQQASRISDRTgFFLDGDLIE 227
|
....*...
gi 1169664 223 AGKTEDTF 230
Cdd:PRK14239 228 YNDTKQMF 235
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
7-234 |
6.77e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 98.31 E-value: 6.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 7 SIWVNDVTVRYNNG----HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNLVA 82
Cdd:PRK13646 2 TIRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 83 YVPQSEEVDWQFPVSVYDVVMMGR---YGYMNFlripkAIDKQKVQEAMQRVNIEHLAHRQIGEL-----SGGQKKRVFL 154
Cdd:PRK13646 82 PVRKRIGMVFQFPESQLFEDTVEReiiFGPKNF-----KMNLDEVKNYAHRLLMDLGFSRDVMSQspfqmSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 155 ARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLR-EEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFNQ 232
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEgSIVSQTSPKELFKD 236
|
..
gi 1169664 233 HN 234
Cdd:PRK13646 237 KK 238
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-232 |
1.15e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.51 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 23 AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNLVAYVPQSEEVDWQFPVS-VYD- 100
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPESqLFEe 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 101 -VVMMGRYGYMNFlRIPKAIDKQKVQEAMQRVNI-EHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKT 178
Cdd:PRK13649 102 tVLKDVAFGPQNF-GVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1169664 179 ENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTEDTFNQ 232
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVyVLEKGKLVLSGKPKDIFQD 235
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-218 |
1.62e-23 |
|
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: 94.81 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVrynngHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPI-----SQALKRNlVAYV 84
Cdd:cd03215 7 VRGLSV-----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrrspRDAIRAG-IAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PqsEE------VDWQfpvSVYDVVMMGRYgymnflripkaidkqkvqeamqrvniehlahrqigeLSGGQKKRVFLARAL 158
Cdd:cd03215 81 P--EDrkreglVLDL---SVAENIALSSL------------------------------------LSGGNQQKVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 159 AQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINR 218
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYE 179
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
10-236 |
1.75e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 98.00 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYN----NGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNLVAYVP 85
Cdd:PRK13631 24 VKNLYCVFDekqeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEEVD------------WQFP------VSVYDVVMMGRYGymnfLRIPKAIDKQKVQEAMQRVNI-EHLAHRQIGELSG 146
Cdd:PRK13631 104 YSKKIKnfkelrrrvsmvFQFPeyqlfkDTIEKDIMFGPVA----LGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 147 GQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGK 225
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKgKILKTGT 259
|
250
....*....|..
gi 1169664 226 TEDTF-NQHNLE 236
Cdd:PRK13631 260 PYEIFtDQHIIN 271
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-235 |
3.31e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.94 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRynnghTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS-----QALKRNlVAYV 84
Cdd:COG1129 259 VEGLSVG-----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprDAIRAG-IAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PqsEE-------VDWqfpvSVYD---VVMMGRYGYMNFLRIPKAidKQKVQEAMQRVNIE-HLAHRQIGELSGG--QKkr 151
Cdd:COG1129 333 P--EDrkgeglvLDL----SIREnitLASLDRLSRGGLLDRRRE--RALAEEYIKRLRIKtPSPEQPVGNLSGGnqQK-- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 152 VFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRTVIAAGKTEDTFN 231
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEAT 482
|
....
gi 1169664 232 QHNL 235
Cdd:COG1129 483 EEAI 486
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
10-214 |
3.38e-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: 92.90 E-value: 3.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLcdlpiSQALKrnlVAYVPQsee 89
Cdd:cd03221 3 LENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-----GSTVK---IGYFEQ--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 90 vdwqfpvsvydvvmmgrygymnflripkaidkqkvqeamqrvniehlahrqigeLSGGQKKRVFLARALAQQSPIILLDE 169
Cdd:cd03221 71 ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1169664 170 PFTGVDVKTENAIVDLLQQLreEGHLILVStHNlgsvPDFCDQVV 214
Cdd:cd03221 97 PTNHLDLESIEALEEALKEY--PGTVILVS-HD----RYFLDQVA 134
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-257 |
3.75e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.21 E-value: 3.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGE-----IKLCDLPISQALkRNLVA 82
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKvlvsgIDTGDFSKLQGI-RKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 83 YVPQSEEVdwQFpvsvydvvmMGR-------YGYMNFLRIPKAIDKqKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLA 155
Cdd:PRK13644 81 IVFQNPET--QF---------VGRtveedlaFGPENLCLPPIEIRK-RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 156 RALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDfCDQVVMINR-TVIAAGKTEDTFNQHN 234
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRgKIVLEGEPENVLSDVS 227
|
250 260
....*....|....*....|...
gi 1169664 235 LEiVFGGVLRHIKLLGENLHNDE 257
Cdd:PRK13644 228 LQ-TLGLTPPSLIELAENLKMHG 249
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-274 |
4.00e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.08 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 22 TAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDL-PI--SQALKRNLVAYVPQSEEVDWQFPVS- 97
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvPFkrRKEFARRIGVVFGQRSQLWWDLPAId 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 98 -------VYdvvmmgrygymnflRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEP 170
Cdd:COG4586 116 sfrllkaIY--------------RIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 171 FTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFNQHnleivfgGVLRHIKL 248
Cdd:COG4586 182 TIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHgRIIYDGSLEELKERF-------GPYKTIVL 254
|
250 260
....*....|....*....|....*..
gi 1169664 249 -LGENLHNDEDKRSVTVLTDDEKAVVF 274
Cdd:COG4586 255 eLAEPVPPLELPRGGEVIEREGNRVRL 281
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-208 |
4.25e-23 |
|
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: 94.10 E-value: 4.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 20 GHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ---ALKRNLvAYVPQSEEvdwqfpv 96
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFqrdSIARGL-LYLGHAPG------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 97 svydvvMMGRYGYMNFLRIPKAI-DKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVD 175
Cdd:cd03231 84 ------IKTTLSVLENLRFWHADhSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180 190
....*....|....*....|....*....|....
gi 1169664 176 VKTENAIVDLLQQLREEGHLILVSTH-NLGSVPD 208
Cdd:cd03231 158 KAGVARFAEAMAGHCARGGMVVLTTHqDLGLSEA 191
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
13-221 |
4.79e-23 |
|
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: 99.02 E-value: 4.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 13 VTVRY-NNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL---VAYVPQSE 88
Cdd:TIGR02203 336 VTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLrrqVALVSQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 89 EVdwqFPVSVYDVVMMGRygymnflriPKAIDKQKVQEAMQRVNIEHLA-------HRQIGE----LSGGQKKRVFLARA 157
Cdd:TIGR02203 416 VL---FNDTIANNIAYGR---------TEQADRAEIERALAAAYAQDFVdklplglDTPIGEngvlLSGGQRQRLAIARA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169664 158 LAQQSPIILLDEPFTGVDVKTENAIVDLLQQLReEGHLILVSTHNLGSVPDfCDQVVMINRTVI 221
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-184 |
8.35e-23 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 98.08 E-value: 8.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKlcdlpISQALKrnlVAYVPQS 87
Cdd:TIGR03719 323 IEAENLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE-----IGETVK---LAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 88 EE-VD-----WQFPVSVYDVVMMGRY--------GYMNFlripKAIDKQKvqeamqrvniehlahrQIGELSGGQKKRVF 153
Cdd:TIGR03719 394 RDaLDpnktvWEEISGGLDIIKLGKReipsrayvGRFNF----KGSDQQK----------------KVGQLSGGERNRVH 453
|
170 180 190
....*....|....*....|....*....|....*
gi 1169664 154 LARALAQQSPIILLDEPFTGVDVKT----ENAIVD 184
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVETlralEEALLN 488
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
21-216 |
9.37e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 94.75 E-value: 9.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 21 HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQaLKRNLVAYVPQSEEVDWQFPVSVYD 100
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK-LNRAQRKAFRRDIQMVFQDSISAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 101 ----VVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNI-EHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVD 175
Cdd:PRK10419 104 prktVREIIREPLRHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1169664 176 VKTENAIVDLLQQLREE-GHLILVSTHNLGSVPDFCDQVVMI 216
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVM 225
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-235 |
1.42e-22 |
|
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: 93.83 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ----ALKRNlVAY 83
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtldSLRRA-IGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 VPQseevdwqfpvsvyDVVMMG-------RYGYmnflriPKAIDKQkVQEAMQRVNIehlaHRQI-----------GE-- 143
Cdd:cd03253 80 VPQ-------------DTVLFNdtigyniRYGR------PDATDEE-VIEAAKAAQI----HDKImrfpdgydtivGErg 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 144 --LSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVsTHNLGSVPDfCDQV-VMINRTV 220
Cdd:cd03253 136 lkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVI-AHRLSTIVN-ADKIiVLKDGRI 213
|
250
....*....|....*
gi 1169664 221 IAAGKTEDTFNQHNL 235
Cdd:cd03253 214 VERGTHEELLAKGGL 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-233 |
1.77e-22 |
|
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: 93.45 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 11 NDVTVRYNN-GHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ-ALK--RNLVAYVPQ 86
Cdd:cd03251 4 KNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLAslRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 87 seEVdWQFPVSVYDVVMMGRYGymnflripkaIDKQKVQEAMQRVN----IEHLA---HRQIGE----LSGGQKKRVFLA 155
Cdd:cd03251 84 --DV-FLFNDTVAENIAYGRPG----------ATREEVEEAARAANahefIMELPegyDTVIGErgvkLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 156 RALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLrEEGHLILVSTHNLGSVPDFCDQVVMINRTVIAAGKTEDTFNQH 233
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-245 |
1.96e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.22 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 7 SIWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVkPQQGEIK-----LCDLPISQALKRnlV 81
Cdd:PRK11174 349 TIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKingieLRELDPESWRKH--L 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 82 AYVPQSEEVdwqFPVSVYDVVMMGRygymnflripKAIDKQKVQEAMQRVNI----EHLAH---RQIGE----LSGGQKK 150
Cdd:PRK11174 426 SWVGQNPQL---PHGTLRDNVLLGN----------PDASDEQLQQALENAWVseflPLLPQgldTPIGDqaagLSVGQAQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 151 RVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVsTHNLGSVPDfCDQV-VMINRTVIAAGKTEDT 229
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMV-THQLEDLAQ-WDQIwVMQDGQIVQQGDYAEL 570
|
250
....*....|....*.
gi 1169664 230 FNQHNLeivFGGVLRH 245
Cdd:PRK11174 571 SQAGGL---FATLLAH 583
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-216 |
2.28e-22 |
|
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: 92.91 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 24 IHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNLVAYVPQSeevdwQFP-VSVYDVV 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYS-----LLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 103 MMGRYGYMNFLriPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAI 182
Cdd:TIGR01184 76 ALAVDRVLPDL--SKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*
gi 1169664 183 VDLLQQLREEGHL-ILVSTHNLGSVPDFCDQVVMI 216
Cdd:TIGR01184 154 QEELMQIWEEHRVtVLMVTHDVDEALLLSDRVVML 188
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-221 |
2.32e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 93.66 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 6 TSIWVNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPI--------SQALK 77
Cdd:PRK11264 2 SAIEVKNLVKKFH-GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 78 RNL---VAYVPQSEEVdwqFP-VSVYDVVMMGrygymnflriPKAIDKQKVQEAMQRVNiEHLAhrQIG----------E 143
Cdd:PRK11264 81 RQLrqhVGFVFQNFNL---FPhRTVLENIIEG----------PVIVKGEPKEEATARAR-ELLA--KVGlagketsyprR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 144 LSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRTVI 221
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-232 |
2.48e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 95.25 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNG---HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEI--------KLCDLPISQAL 76
Cdd:PRK11153 2 IELKNISKVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgqdltALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 77 KR--------NLVAyvpqSEevdwqfpvSVYDVVMMGrygymnfLRI---PKAIDKQKVQEAMQRVNIEHLAHRQIGELS 145
Cdd:PRK11153 82 RQigmifqhfNLLS----SR--------TVFDNVALP-------LELagtPKAEIKARVTELLELVGLSDKADRYPAQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 146 GGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL-ILVSTHNLGSVPDFCDQV-VMINRTVIAA 223
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLtIVLITHEMDVVKRICDRVaVIDAGRLVEQ 222
|
....*....
gi 1169664 224 GKTEDTFNQ 232
Cdd:PRK11153 223 GTVSEVFSH 231
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
10-228 |
3.51e-22 |
|
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: 96.26 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNG-HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL---VAYVP 85
Cdd:TIGR01842 319 VENVTIVPPGGkKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFgkhIGYLP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEEVdwqFPVSVYDvvmmgrygymNFLRIPKAIDKQKVQEAMQRVNIEHLAHR-------QIGE----LSGGQKKRVFL 154
Cdd:TIGR01842 399 QDVEL---FPGTVAE----------NIARFGENADPEKIIEAAKLAGVHELILRlpdgydtVIGPggatLSGGQRQRIAL 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 155 ARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHN---LGSVpdfcDQVVMINRTVIAA-GKTED 228
Cdd:TIGR01842 466 ARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRpslLGCV----DKILVLQDGRIARfGERDE 539
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
12-216 |
4.96e-22 |
|
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: 92.15 E-value: 4.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 12 DVTVRYNN--GHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL---VAYVPQ 86
Cdd:cd03248 16 NVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLhskVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 87 SEEVdwqFPVSVYDVVMMGrYGYMNFLRIPKAIDKqkvqeAMQRVNIEHLAH---RQIGE----LSGGQKKRVFLARALA 159
Cdd:cd03248 96 EPVL---FARSLQDNIAYG-LQSCSFECVKEAAQK-----AHAHSFISELASgydTEVGEkgsqLSGGQKQRVAIARALI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1169664 160 QQSPIILLDEPFTGVDVKTENAIVDLLQQLREEgHLILVSTHNLGSVpDFCDQVVMI 216
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTV-ERADQILVL 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-231 |
7.51e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.54 E-value: 7.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 21 HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVkPQQGEIKLCDLPISQALKRNLVAYVPQSEEVdWQFPVS--- 97
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLLPVRHRIQVV-FQDPNSsln 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 98 ----VYDVVMMGrygymnfLRI-----PKAIDKQKVQEAMQRVNIE-HLAHRQIGELSGGQKKRVFLARALAQQSPIILL 167
Cdd:PRK15134 377 prlnVLQIIEEG-------LRVhqptlSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169664 168 DEPFTGVDVKTENAIVDLLQQLREEGHL--ILVStHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFN 231
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLayLFIS-HDLHVVRALCHQVIVLRQgEVVEQGDCERVFA 515
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-233 |
1.23e-21 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 94.75 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNG---HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQ----QGEIKLCDLPISQALKRNL-- 80
Cdd:COG4172 9 VEDLSVAFGQGggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSERELrr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 81 -----VAYVpqseevdWQFPVS-----------VYDVVMMGRygymnflRIPKAIDKQKVQEAMQRVNIEHlAHRQIG-- 142
Cdd:COG4172 89 irgnrIAMI-------FQEPMTslnplhtigkqIAEVLRLHR-------GLSGAAARARALELLERVGIPD-PERRLDay 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 143 --ELSGGQKKRVFLARALAQQsPIILL-DEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQV-VMIN 217
Cdd:COG4172 154 phQLSGGQRQRVMIAMALANE-PDLLIaDEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVaVMRQ 232
|
250
....*....|....*...
gi 1169664 218 RTVIAAGKTEDTFN--QH 233
Cdd:COG4172 233 GEIVEQGPTAELFAapQH 250
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
7-232 |
1.37e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 94.81 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 7 SIWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK---RNLVAY 83
Cdd:TIGR01193 473 DIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRhtlRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 VPQSEEVdwqFPVSVYDVVMMGRYGYMNFLRIPKAIDKQKVqeamqRVNIEHLA---HRQIGE----LSGGQKKRVFLAR 156
Cdd:TIGR01193 553 LPQEPYI---FSGSILENLLLGAKENVSQDEIWAACEIAEI-----KDDIENMPlgyQTELSEegssISGGQKQRIALAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169664 157 ALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGhLILVStHNLgSVPDFCDQVVMINR-TVIAAGKTEDTFNQ 232
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKT-IIFVA-HRL-SVAKQSDKIIVLDHgKIIEQGSHDELLDR 698
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
23-215 |
1.75e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 92.49 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 23 AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNLVAYVPQSEEVdWQFPVS----- 97
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMV-FQDPYAslnpr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 98 --VYDVVMMGrygymnfLRI----PKAIDKQKVQEAMQRV--NIEHlAHRQIGELSGGQKKRVFLARALAQQSPIILLDE 169
Cdd:COG4608 112 mtVGDIIAEP-------LRIhglaSKAERRERVAELLELVglRPEH-ADRYPHEFSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1169664 170 PFTGVDVKTENAIVDLLQQLREE-GHLILVSTHNLGSVPDFCDQV-VM 215
Cdd:COG4608 184 PVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVaVM 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
30-228 |
1.90e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 92.63 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 30 SLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCD-----------LPISqalKRNlVAYVPQSEEVdwqFPVsv 98
Cdd:PRK11144 20 TLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaekgicLPPE---KRR-IGYVFQDARL---FPH-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 99 YDVvmMG--RYGYmnflripKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDV 176
Cdd:PRK11144 91 YKV--RGnlRYGM-------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1169664 177 KTENAIVDLLQQLREEGHL-ILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTED 228
Cdd:PRK11144 162 PRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQgKVKAFGPLEE 215
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
24-202 |
3.14e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 90.13 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 24 IHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGL--VKPQQGEIKL-----CDLPISQALKRNL-VAYvpqseevdwQFP 95
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLdgediLELSPDERARAGIfLAF---------QYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 96 VSVYDVVMmgrygyMNFLRI---------PKAID-KQKVQEAMQRVNI-EHLAHRQIGE-LSGGQKKRVFLARALAQQSP 163
Cdd:COG0396 87 VEIPGVSV------SNFLRTalnarrgeeLSAREfLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1169664 164 IILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHN 202
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHY 199
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-232 |
3.39e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 90.48 E-value: 3.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 1 MDSFSTSIWVNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSI--MG-LVkPQQ---GEIKLCDLPISQ 74
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYGD-KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNdLI-PGArveGEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 75 ------ALKRNlVAYVPQseevdwQ---FPVSVYDVVMMGrygymnfLRI----PKAIDKQKVQEAMQRVNI-----EHL 136
Cdd:COG1117 83 pdvdvvELRRR-VGMVFQ------KpnpFPKSIYDNVAYG-------LRLhgikSKSELDEIVEESLRKAALwdevkDRL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 137 aHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEgHLILVSTHNL---GSVPDFCdqV 213
Cdd:COG1117 149 -KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMqqaARVSDYT--A 224
|
250
....*....|....*....
gi 1169664 214 VMINRTVIAAGKTEDTFNQ 232
Cdd:COG1117 225 FFYLGELVEFGPTEQIFTN 243
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-201 |
3.54e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.09 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 25 HNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ----------------ALKRNLVAYvpqsE 88
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRqrdeyhqdllylghqpGIKTELTAL----E 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 89 EVDWqfpvsvydvvmmgrygymnFLRIPKAIDKQKVQEAMQRVNI---EHLAHRQigeLSGGQKKRVFLARALAQQSPII 165
Cdd:PRK13538 94 NLRF-------------------YQRLHGPGDDEALWEALAQVGLagfEDVPVRQ---LSAGQQRRVALARLWLTRAPLW 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 1169664 166 LLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTH 201
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-184 |
3.78e-21 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 93.26 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 24 IHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKlcdlpISQALKrnlVAYVPQS-EEVD-----WQfPVS 97
Cdd:PRK11819 340 IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-----IGETVK---LAYVDQSrDALDpnktvWE-EIS 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 98 V-YDVVMMGRY--------GYMNFlripKAIDKQKvqeamqrvniehlahrQIGELSGGQKKRVFLARALAQQSPIILLD 168
Cdd:PRK11819 411 GgLDIIKVGNReipsrayvGRFNF----KGGDQQK----------------KVGVLSGGERNRLHLAKTLKQGGNVLLLD 470
|
170 180
....*....|....*....|
gi 1169664 169 EPFTGVDVKT----ENAIVD 184
Cdd:PRK11819 471 EPTNDLDVETlralEEALLE 490
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-231 |
4.43e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 90.14 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 24 IHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKP----QQGEIKLCDLPIS-QALKRNLVAYVPQSeevdwqfPVSV 98
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVApCALRGRKIATIMQN-------PRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 99 YD-VVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHlAHRQIG----ELSGGQKKRVFLARALAQQSPIILLDEPFTG 173
Cdd:PRK10418 92 FNpLHTMHTHARETCLALGKPADDATLTAALEAVGLEN-AARVLKlypfEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 174 VDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTEDTFN 231
Cdd:PRK10418 171 LDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVaVMSHGRIVEQGDVETLFN 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
8-221 |
4.99e-21 |
|
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: 89.52 E-value: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNN--GHTAIHNMTFSLNSGTICALVGVNGSGKSTlfksIMGLVK----PQQGEIKLCDLPISQ-ALK--R 78
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLErfydPTSGEILLDGVDIRDlNLRwlR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 79 NLVAYVPQsEEVdwQFPVSVYDVVMMGRygymnflriPKAIDKQkVQEAMQRVN----IEHLAHR---QIGE----LSGG 147
Cdd:cd03249 77 SQIGLVSQ-EPV--LFDGTIAENIRYGK---------PDATDEE-VEEAAKKANihdfIMSLPDGydtLVGErgsqLSGG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169664 148 QKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLReEGHLILVSTHNLGSVPDfCDQVVMINRTVI 221
Cdd:cd03249 144 QKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQV 215
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-235 |
5.81e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.45 E-value: 5.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 3 SFSTSIWVNDVTVRYNNG----HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKR 78
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKtpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 79 -NLVAYVPQSEEVDWQFPVsvYDVVMMGRYGYMNFLRIPKAIDKQ----KVQEAMQRVNI-EHLAHRQIGELSGGQKKRV 152
Cdd:PRK13645 82 iKEVKRLRKEIGLVFQFPE--YQLFQETIEKDIAFGPVNLGENKQeaykKVPELLKLVQLpEDYVKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 153 FLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTF 230
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEgKVISIGSPFEIF 239
|
....*
gi 1169664 231 NQHNL 235
Cdd:PRK13645 240 SNQEL 244
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-225 |
6.38e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 89.41 E-value: 6.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDlpisqalkRNLVAYvpqsEE 89
Cdd:COG4674 13 VEDLTVSFD-GFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGG--------TDLTGL----DE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 90 VD---------WQFPvSVY---------DVVMMGRYG-YMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKK 150
Cdd:COG4674 80 HEiarlgigrkFQKP-TVFeeltvfenlELALKGDRGvFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 151 RVFLARALAQQSPIILLDEPFTGV-DVKTENaIVDLLQQLREEgHLILVSTHNLGSVPDFCDQVvminrTVIAAGK 225
Cdd:COG4674 159 WLEIGMLLAQDPKLLLLDEPVAGMtDAETER-TAELLKSLAGK-HSVVVVEHDMEFVRQIARKV-----TVLHQGS 227
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-246 |
1.35e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 89.12 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 20 GHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMG-LVKPQ-------QGEIKLCDLPISQALKRNLV---AYVPQSE 88
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGaprgarvTGDVTLNGEPLAAIDAPRLArlrAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 89 EVdwQFPVSVYDVVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSP----- 163
Cdd:PRK13547 93 QP--AFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQLWPphdaa 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 164 ----IILLDEPFTGVDVKTENAIVDLLQQLREEGHL-ILVSTHNLGSVPDFCDQVVMI-NRTVIAAGKTEDTFNQHNLEI 237
Cdd:PRK13547 171 qpprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLaDGAIVAHGAPADVLTPAHIAR 250
|
....*....
gi 1169664 238 VFGGVLRHI 246
Cdd:PRK13547 251 CYGFAVRLV 259
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
10-231 |
1.58e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.51 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPI----SQALKRNLVAYVP 85
Cdd:PRK11300 8 VSGLMMRFG-GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpGHQIARMGVVRTF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEEVDWQFPVSVYDVVMMGRYGYMNFLR--IPKAIDKQKVQEAMQR-------VNIEHLAHRQIGELSGGQKKRVFLAR 156
Cdd:PRK11300 87 QHVRLFREMTVIENLLVAQHQQLKTGLFSglLKTPAFRRAESEALDRaatwlerVGLLEHANRQAGNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169664 157 ALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREE-GHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFN 231
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQgTPLANGTPEEIRN 243
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
10-219 |
1.66e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.41 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCD------LP-----ISQALkR 78
Cdd:COG4178 365 LEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAgarvlfLPqrpylPLGTL-R 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 79 NLVAYvPQSEEvdwqfpvsvydvvmmgrygymnflripkAIDKQKVQEAMQRVNIEHLAHR--------QIgeLSGGQKK 150
Cdd:COG4178 444 EALLY-PATAE----------------------------AFSDAELREALEAVGLGHLAERldeeadwdQV--LSLGEQQ 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 151 RVFLARALAQQSPIILLDEPFTGVDVKTENAivdLLQQLREE-GHLILVS-THNlGSVPDFCDQVVMINRT 219
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAA---LYQLLREElPGTTVISvGHR-STLAAFHDRVLELTGD 559
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-216 |
1.81e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.58 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 6 TSIWVNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQAlkRNLVAYVP 85
Cdd:PRK11247 11 TPLLLNAVSKRYGE-RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA--REDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEEV-DWQfpvSVYDVVMMGRYGYMnflripkaidKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:PRK11247 88 QDARLlPWK---KVIDNVGLGLKGQW----------RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1169664 165 ILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVVMI 216
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLI 207
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
8-203 |
2.26e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 87.72 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHtaihnMTFSL--NSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDlpisqalkRNLVAYVP 85
Cdd:PRK10771 2 LKLTDITWLYHHLP-----MRFDLtvERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG--------QDHTTTPP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QseevdwQFPVSvydvvmmgrygyMNF--------LRIPKAI-------------DKQKVQEAMQRVNIEHLAHRQIGEL 144
Cdd:PRK10771 69 S------RRPVS------------MLFqennlfshLTVAQNIglglnpglklnaaQREKLHAIARQMGIEDLLARLPGQL 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 145 SGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLIL--VStHNL 203
Cdd:PRK10771 131 SGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLlmVS-HSL 190
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
10-232 |
2.42e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.10 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQA-------------- 75
Cdd:PRK10619 8 VIDLHKRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 76 --LKRNLVAYVPQSEEVdWQFpVSVYDVVMMGRygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQI-GELSGGQKKRV 152
Cdd:PRK10619 87 lrLLRTRLTMVFQHFNL-WSH-MTVLENVMEAP---IQVLGLSKQEARERAVKYLAKVGIDERAQGKYpVHLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 153 FLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRTVI-AAGKTEDTFN 231
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIeEEGAPEQLFG 241
|
.
gi 1169664 232 Q 232
Cdd:PRK10619 242 N 242
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
11-202 |
2.48e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.94 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 11 NDVTVRYNNGHTAI---HNMTFSLNSGTICALVGVNGSGKSTLFkSIMG-LVKPQQGEIKLCDLPISQ-------ALKRN 79
Cdd:PRK10535 8 KDIRRSYPSGEEQVevlKGISLDIYAGEMVAIVGASGSGKSTLM-NILGcLDKPTSGTYRVAGQDVATldadalaQLRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 80 LVAYVPQseevdwqfpvsvydvvmmgRYGYMNFLR-------------IPKAIDKQKVQEAMQRVNIEHLAHRQIGELSG 146
Cdd:PRK10535 87 HFGFIFQ-------------------RYHLLSHLTaaqnvevpavyagLERKQRLLRAQELLQRLGLEDRVEYQPSQLSG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 147 GQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHN 202
Cdd:PRK10535 148 GQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
19-244 |
2.55e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.89 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 19 NGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQalkrnlvayVPQseevdWQFPVSv 98
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH---------VPP-----YQRPIN- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 99 ydvVMMGRYGYMNFL-------------RIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPII 165
Cdd:PRK11607 95 ---MMFQSYALFPHMtveqniafglkqdKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 166 LLDEPFTGVDVKTEN----AIVDLLQQLreeGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFNQHNLEI--- 237
Cdd:PRK11607 172 LLDEPMGALDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRgKFVQIGEPEEIYEHPTTRYsae 248
|
250
....*....|...
gi 1169664 238 ------VFGGVLR 244
Cdd:PRK11607 249 figsvnVFEGVLK 261
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-222 |
3.47e-20 |
|
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: 86.78 E-value: 3.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 7 SIWVNDVTVRYN-NGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ-ALK--RNLVA 82
Cdd:cd03244 2 DIEFKNVSLRYRpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHdlRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 83 YVPQseevdwqfpvsvyDVVMMG---R-----YGYMNFLRIPKAIDKQKVQEAMQRVNiEHLAHRQIGE---LSGGQKKR 151
Cdd:cd03244 82 IIPQ-------------DPVLFSgtiRsnldpFGEYSDEELWQALERVGLKEFVESLP-GGLDTVVEEGgenLSVGQRQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169664 152 VFLARALAQQSPIILLDEPFTGVDVKTENAIVDLlqqLREE--GHLILVSTHNLGSVPDfCDQVVMINRTVIA 222
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQKT---IREAfkDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-229 |
4.10e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 87.86 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 5 STSIWVNDVTVRYNNGHT--AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIklcdLPISQAL------ 76
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI----IIDGDLLteenvw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 77 -KRNLVAYVPQSEevDWQF-PVSVYDVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFL 154
Cdd:PRK13650 78 dIRHKIGMVFQNP--DNQFvGATVEDDVAFG----LENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169664 155 ARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVS-THNLgsvpdfcDQVVMINRT-VIAAGKTEDT 229
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISiTHDL-------DEVALSDRVlVMKNGQVEST 221
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-273 |
4.62e-20 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 88.70 E-value: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 39 LVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ-ALKRNLVAYVPQSEEVdwqFP-VSVYDVVMMGrygyMNFLRIP 116
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNvPPHLRHINMVFQSYAL---FPhMTVEENVAFG----LKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 117 KAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVK----TENAIVDLLQQLree 192
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlrdqMQLELKTIQEQL--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 193 GHLILVSTHNLGSVPDFCDQVVMINRTVIAAGKTEDT-------------------FNQHNLE-----IVFGGVLRHIKL 248
Cdd:TIGR01187 151 GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEiyeepanlfvarfigeinvFEATVIErkseqVVLAGVEGRRCD 230
|
250 260
....*....|....*....|....*
gi 1169664 249 LGENLhNDEDKRSVTVLTDDEKAVV 273
Cdd:TIGR01187 231 IYTDV-PVEKDQPLHVVLRPEKIVI 254
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
10-232 |
5.43e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 88.24 E-value: 5.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYN--NGH-TAIHNMTFSLNSGTICALVGVNGSGKS-TLFkSIMGLVKpQQGEIK---------LCDLPiSQAL 76
Cdd:PRK09473 15 VKDLRVTFStpDGDvTAVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLLA-ANGRIGgsatfngreILNLP-EKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 77 KRnlvayvPQSEEVD--WQFPVSVYDVVMmgRYG--YMNFLRIPKAIDKQ-------------KVQEAMQRVNIehLAHr 139
Cdd:PRK09473 92 NK------LRAEQISmiFQDPMTSLNPYM--RVGeqLMEVLMLHKGMSKAeafeesvrmldavKMPEARKRMKM--YPH- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 140 qigELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQV-VMIN 217
Cdd:PRK09473 161 ---EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVlVMYA 237
|
250
....*....|....*
gi 1169664 218 RTVIAAGKTEDTFNQ 232
Cdd:PRK09473 238 GRTMEYGNARDVFYQ 252
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-189 |
5.52e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 88.62 E-value: 5.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 12 DVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEI-----KLCDLPISQalkRNlVAYVPQ 86
Cdd:PRK11432 11 NITKRFGS-NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgeDVTHRSIQQ---RD-ICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 87 SEEVdwqFP-VSVYDVVmmgryGY-MNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:PRK11432 86 SYAL---FPhMSLGENV-----GYgLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180
....*....|....*....|....*....
gi 1169664 165 ILLDEPFTGVDVKTENA----IVDLLQQL 189
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSmrekIRELQQQF 186
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
20-177 |
6.94e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 88.47 E-value: 6.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 20 GHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ--ALKRNlVAYVPQSEEVdwqFP-V 96
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpAENRH-VNTVFQSYAL---FPhM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 97 SVYDVVMMGrygymnfLR---IPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTG 173
Cdd:PRK09452 102 TVFENVAFG-------LRmqkTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
....
gi 1169664 174 VDVK 177
Cdd:PRK09452 175 LDYK 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-218 |
9.05e-20 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 85.54 E-value: 9.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 7 SIWVNDVTVRYN-NGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS----QALKRNLv 81
Cdd:cd03369 6 EIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIStiplEDLRSSL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 82 AYVPQSEevdwqfpvsvydVVMMG-------RYGYMNFLRIPKAIdkqKVQEAmqrvniehlahrqiGE-LSGGQKKRVF 153
Cdd:cd03369 85 TIIPQDP------------TLFSGtirsnldPFDEYSDEEIYGAL---RVSEG--------------GLnLSQGQRQLLC 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169664 154 LARALAQQSPIILLDEPFTGVDVKTENAIVdllQQLREE--GHLILVSTHNLGSVPDfCDQVVMINR 218
Cdd:cd03369 136 LARALLKRPRVLVLDEATASIDYATDALIQ---KTIREEftNSTILTIAHRLRTIID-YDKILVMDA 198
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
23-202 |
1.07e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 86.09 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 23 AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ----ALKRNLVAYVPQSEEVDWQfpVSV 98
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtaKIMREAVAIVPEGRRVFSR--MTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 99 YDVVMMGryGYMnflripkaIDKQKVQEAMQRV-----NIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTG 173
Cdd:PRK11614 98 EENLAMG--GFF--------AERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180
....*....|....*....|....*....
gi 1169664 174 VDVKTENAIVDLLQQLREEGHLILVSTHN 202
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQGMTIFLVEQN 196
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-232 |
1.34e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 89.00 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 19 NGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQaLK----RNLVAYVPQSEevdWQF 94
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK-LQldswRSRLAVVSQTP---FLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 95 PVSVYDVVMMGRygymnflriPKAIdKQKVQEAMQRVNIEHLAHR-------QIGE----LSGGQKKRVFLARALAQQSP 163
Cdd:PRK10789 402 SDTVANNIALGR---------PDAT-QQEIEHVARLASVHDDILRlpqgydtEVGErgvmLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 164 IILLDEPFTGVDVKTENAIvdlLQQLRE--EGHLILVSTHNLGSVPDFCDQVVMINRTVIAAGKTEDTFNQ 232
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQI---LHNLRQwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-224 |
3.17e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 83.73 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHTaIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGL--VKPQQGEIKL-----CDLPISQALKRNLVa 82
Cdd:cd03217 3 IKDLHVSVGGKEI-LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFkgediTDLPPEERARLGIF- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 83 yvpqseeVDWQFPVSVYDVVMMgrygymNFLRipkaidkqkvqeamqRVNIEhlahrqigeLSGGQKKRVFLARALAQQS 162
Cdd:cd03217 81 -------LAFQYPPEIPGVKNA------DFLR---------------YVNEG---------FSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 163 PIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHN---LGSV-PDFCDqvVMINRTVIAAG 224
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYIkPDRVH--VLYDGRIVKSG 187
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-204 |
6.92e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.60 E-value: 6.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 12 DVTVRYnnGHTAI-HNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGE-----IKLCDLPISQALKRNLVAYVP 85
Cdd:PRK09493 6 NVSKHF--GPTQVlHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdgLKVNDPKVDERLIRQEAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEEVdwqFP-VSVYDVVMmgrYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:PRK09493 84 QQFYL---FPhLTALENVM---FGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1169664 165 ILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLG 204
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-215 |
9.84e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.99 E-value: 9.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTvRYNNGHtaIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS-----QALKRNLvAYV 84
Cdd:PRK09700 268 VRNVT-SRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprsplDAVKKGM-AYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSEEVDWQFP-------VSVYDVVMMGRYGYMNFLRIPKaiDKQKVQEAMQR-VNIE-HLAHRQIGELSGGQKKRVFLA 155
Cdd:PRK09700 344 TESRRDNGFFPnfsiaqnMAISRSLKDGGYKGAMGLFHEV--DEQRTAENQRElLALKcHSVNQNITELSGGNQQKVLIS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 156 RALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVM 215
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAV 481
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-200 |
1.11e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.85 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS----QALKRNLVAYVP 85
Cdd:COG3845 260 VENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITglspRERRRLGVAYIP 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 qsEE-------VDWqfpvSVYDVVMMGRYGYMNFLRIPkAIDKQKVQEAMQRVnIEHL------AHRQIGELSGG--QKk 150
Cdd:COG3845 340 --EDrlgrglvPDM----SVAENLILGRYRRPPFSRGG-FLDRKAIRAFAEEL-IEEFdvrtpgPDTPARSLSGGnqQK- 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1169664 151 rVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGH-LILVST 200
Cdd:COG3845 411 -VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAaVLLISE 460
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
24-201 |
1.26e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 82.31 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 24 IHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLcdlpISQALKRNLVAYVPQSEEVDWQFPVSVYDVVM 103
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILF----ERQSIKKDLCTYQKQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 104 MGRYGYMNFLRIPKAIDkqkvqEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIV 183
Cdd:PRK13540 93 ENCLYDIHFSPGAVGIT-----ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
|
170
....*....|....*...
gi 1169664 184 DLLQQLREEGHLILVSTH 201
Cdd:PRK13540 168 TKIQEHRAKGGAVLLTSH 185
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
14-228 |
2.59e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.53 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 14 TVRYNNG-----HT-AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPisqaLKRNLVAYVPQS 87
Cdd:PRK15112 13 TFRYRTGwfrrqTVeAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP----LHFGDYSYRSQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 88 EEVDWQFPVSVYDvvmmGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLahRQIG-----------ELSGGQKKRVFLAR 156
Cdd:PRK15112 89 IRMIFQDPSTSLN----PRQRISQILDFPLRLNTDLEPEQREKQIIETL--RQVGllpdhasyyphMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169664 157 ALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREE-GHLILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTED 228
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVlVMHQGEVVERGSTAD 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-221 |
4.34e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.52 E-value: 4.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 23 AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEI-----KLCDLPIS--QALKRNLvayvpqseEVDWQFP 95
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIifngqRIDTLSPGklQALRRDI--------QFIFQDP 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 96 VSVYDVVMMGRYGYMNFLRIPKAID----KQKVQEAMQRVNI--EHlAHRQIGELSGGQKKRVFLARALAQQSPIILLDE 169
Cdd:PRK10261 411 YASLDPRQTVGDSIMEPLRVHGLLPgkaaAARVAWLLERVGLlpEH-AWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1169664 170 PFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVVMINRTVI 221
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-231 |
4.98e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.54 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 23 AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ-------ALKRNLVAYVPQSeevdwqFP 95
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelrEVRRKKIAMVFQS------FA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 96 VSVYDVVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVD 175
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 176 VKTENAIVDLLQQLREEGHLILV-STHNLGSVPDFCDQV-VMINRTVIAAGKTEDTFN 231
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVfISHDLDEAMRIGDRIaIMQNGEVVQVGTPDEILN 254
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
23-235 |
5.57e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 82.16 E-value: 5.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 23 AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQG-EIKLCDLPISQALK-----RNLVAYVPQSEevDWQF-P 95
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNpNSKITVDGITLTAKtvwdiREKVGIVFQNP--DNQFvG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 96 VSVYDVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVD 175
Cdd:PRK13640 100 ATVGDDVAFG----LENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169664 176 VKTENAIVDLLQQLREEGHLILVS-THNLGSVpDFCDQVVMINR-TVIAAGKTEDTFNQHNL 235
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKNNLTVISiTHDIDEA-NMADQVLVLDDgKLLAQGSPVEIFSKVEM 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
26-218 |
8.71e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 83.62 E-value: 8.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 26 NMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL---VAYVPQseevdwqfpvsvyDVV 102
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLhrqVALVGQ-------------EPV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 103 MMGRYGYMNFLRIPKAIDKQKVQEAMQRVN-------IEHLAHRQIGE----LSGGQKKRVFLARALAQQSPIILLDEPF 171
Cdd:TIGR00958 566 LFSGSVRENIAYGLTDTPDEEIMAAAKAANahdfimeFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1169664 172 TGVDVKTENaivdLLQQLREEGHL-ILVSTHNLGSVPDfCDQVVMINR 218
Cdd:TIGR00958 646 SALDAECEQ----LLQESRSRASRtVLLIAHRLSTVER-ADQILVLKK 688
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
8-252 |
9.94e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.67 E-value: 9.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGH----TAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIK----------------- 66
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 67 -LCDLPISQALKRNL---------VAYVPQSEEvdWQ-FPVSVYDVVMMG--RYGymnflrIPKAIDKQKVQEAMQRVNI 133
Cdd:PRK13651 83 vLEKLVIQKTRFKKIkkikeirrrVGVVFQFAE--YQlFEQTIEKDIIFGpvSMG------VSKEEAKKRAAKYIELVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 134 -EHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQ 212
Cdd:PRK13651 155 dESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKR 234
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1169664 213 VVMI-NRTVIAAGKTEDtfnqhnleivfggVLRHIKLLGEN 252
Cdd:PRK13651 235 TIFFkDGKIIKDGDTYD-------------ILSDNKFLIEN 262
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-245 |
1.48e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 80.06 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 7 SIWVNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLC----DLP------ISQAL 76
Cdd:COG4161 2 SIQLKNINCFYGS-HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAghqfDFSqkpsekAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 77 KRNlVAYVPQSEEVdWqfP-VSVYDVVMMGRygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLA 155
Cdd:COG4161 81 RQK-VGMVFQQYNL-W--PhLTVMENLIEAP---CKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 156 RALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVV-MINRTVIAAGkTEDTFNQHN 234
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVyMEKGRIIEQG-DASHFTQPQ 232
|
250
....*....|.
gi 1169664 235 LEiVFGGVLRH 245
Cdd:COG4161 233 TE-AFAHYLSH 242
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
23-215 |
1.71e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 81.29 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 23 AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLcdlpisqaLKRNLVayvpQSEEVDW---------- 92
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW--------LGKDLL----GMKDDEWravrsdiqmi 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 93 -QFPV-------SVYDVVMMGRYGYmnFLRIPKAIDKQKVQEAMQRVNI-EHLAHRQIGELSGGQKKRVFLARALAQQSP 163
Cdd:PRK15079 104 fQDPLaslnprmTIGEIIAEPLRTY--HPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1169664 164 IILLDEPFTGVDVKTENAIVDLLQQLREEGHLILV-STHNLGSVPDFCDQV-VM 215
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIfIAHDLAVVKHISDRVlVM 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-245 |
1.91e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 79.67 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 7 SIWVNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCD--LPISQ--------AL 76
Cdd:PRK11124 2 SIQLNGINCFYGA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKtpsdkairEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 77 KRNlVAYVPQseevdwQFPVSVYDVVMMGRY-GYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLA 155
Cdd:PRK11124 81 RRN-VGMVFQ------QYNLWPHLTVQQNLIeAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 156 RALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVV-MINRTVIAAGkTEDTFNQHN 234
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVyMENGHIVEQG-DASCFTQPQ 232
|
250
....*....|.
gi 1169664 235 LEiVFGGVLRH 245
Cdd:PRK11124 233 TE-AFKNYLSH 242
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-215 |
2.14e-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: 82.18 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 12 DVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPI---SQALKRNLVAYVPQse 88
Cdd:COG5265 362 NVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIrdvTQASLRAAIGIVPQ-- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 89 evdwqfpvsvyDVVMMG-------RYGymnflRiPKAiDKQKVQEAMQRVNIEHLAHR-------QIGE----LSGGQKK 150
Cdd:COG5265 440 -----------DTVLFNdtiayniAYG-----R-PDA-SEEEVEAAARAAQIHDFIESlpdgydtRVGErglkLSGGEKQ 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 151 RVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLReEGHLILVSTHNLGSVPDfCDQ-VVM 215
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRLSTIVD-ADEiLVL 565
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-211 |
2.78e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.70 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 1 MDSFSTSIWVNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSI--MGLVKPQ---QGEIKLCDLPISQA 75
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDT-QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEvrvEGRVEFFNQNIYER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 76 ------LKRNLVAYVPQSEevdwQFPVSVYDVVMmgrYGYMNFLRIPKAIDKQKVQEAMQRVN----IEHLAHRQIGELS 145
Cdd:PRK14258 80 rvnlnrLRRQVSMVHPKPN----LFPMSVYDNVA---YGVKIVGWRPKLEIDDIVESALKDADlwdeIKHKIHKSALDLS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169664 146 GGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL-ILVSTHNLGSVPDFCD 211
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELtMVIVSHNLHQVSRLSD 219
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
32-232 |
2.79e-17 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 79.46 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 32 NSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNLVAYVPQSEEVD---------------WQFpV 96
Cdd:COG4598 32 RKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELVPADRRQLQrirtrlgmvfqsfnlWSH-M 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 97 SVYDVVMMGRygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDV 176
Cdd:COG4598 111 TVLENVIEAP---VHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1169664 177 KTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRTVI-AAGKTEDTFNQ 232
Cdd:COG4598 188 ELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIeEQGPPAEVFGN 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-235 |
2.82e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.88 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 28 TFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS-----QALKRNlVAYVPQSEEVDWQFPV-SVYDV 101
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprDAIRAG-IMLCPEDRKAEGIIPVhSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 102 VMMG--RygymNFLRIPKAIDKQK----VQEAMQRVNIEHLAHRQ-IGELSGGQKKRVFLARALAQQSPIILLDEPFTGV 174
Cdd:PRK11288 352 INISarR----HHLRAGCLINNRWeaenADRFIRSLNIKTPSREQlIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 175 DVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRTVIAAGKTEDTFNQHNL 235
Cdd:PRK11288 428 DVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQATERQA 488
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
12-177 |
3.09e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 81.04 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 12 DVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQaLK---RNlVAYVPQSE 88
Cdd:PRK11650 8 AVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE-LEpadRD-IAMVFQNY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 89 EVdwqFP-VSVYDvvMMGrYGymnfLRI---PKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:PRK11650 86 AL---YPhMSVRE--NMA-YG----LKIrgmPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170
....*....|...
gi 1169664 165 ILLDEPFTGVDVK 177
Cdd:PRK11650 156 FLFDEPLSNLDAK 168
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-247 |
4.52e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 22 TAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQaLKRNLVAYVPQS---EEVDWQFPVSV 98
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNK-LDHKLAAQLGIGiiyQELSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 99 YDVVMMGRYGYMNFLRIPkAID----KQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGV 174
Cdd:PRK09700 98 LENLYIGRHLTKKVCGVN-IIDwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169664 175 DVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTEDTFNQhnlEIVFGGVLRHIK 247
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYtVMKDGSSVCSGMVSDVSND---DIVRLMVGRELQ 247
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-226 |
4.87e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.13 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 19 NGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGlVKPQ---QGEIKLCDLP----------------ISQALkrn 79
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEElqasnirdteragiaiIHQEL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 80 lvAYVPQseevdwqfpVSVYDVVMMG----RYGYMNFLRIpkaidKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLA 155
Cdd:PRK13549 92 --ALVKE---------LSVLENIFLGneitPGGIMDYDAM-----YLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169664 156 RALAQQSPIILLDEPfTGVDVKTENAIV-DLLQQLREEGHLILVSTHNLGSVPDFCDQVvminrTVIAAGKT 226
Cdd:PRK13549 156 KALNKQARLLILDEP-TASLTESETAVLlDIIRDLKAHGIACIYISHKLNEVKAISDTI-----CVIRDGRH 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-202 |
4.90e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.22 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 15 VRYNNGHTAI-HNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISqALK----RNLVAYVPQSEE 89
Cdd:PRK10247 13 VGYLAGDAKIlNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIS-TLKpeiyRQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 90 VdwqFPVSVYDvvmmgrygymNfLRIPKAIDKQKVQEA-----MQRVNI-EHLAHRQIGELSGGQKKRVFLARALAQQSP 163
Cdd:PRK10247 92 L---FGDTVYD----------N-LIFPWQIRNQQPDPAiflddLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1169664 164 IILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHN 202
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHD 197
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-225 |
6.98e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 6.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 20 GHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLP----------------ISQALkrNLVay 83
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEvtfngpkssqeagigiIHQEL--NLI-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 84 vPQseevdwqfpVSVYDVVMMGRygymNFLRIPKAIDKQKV-QEA---MQRVNIEHLAHRQIGELSGGQKKRVFLARALA 159
Cdd:PRK10762 92 -PQ---------LTIAENIFLGR----EFVNRFGRIDWKKMyAEAdklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169664 160 QQSPIILLDEPFTGV-DVKTEnAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVvminrTVIAAGK 225
Cdd:PRK10762 158 FESKVIIMDEPTDALtDTETE-SLFRVIRELKSQGRGIVYISHRLKEIFEICDDV-----TVFRDGQ 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-232 |
7.72e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.78 E-value: 7.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 11 NDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS----QALKRNLvAYVPQ 86
Cdd:PRK13657 338 DDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRtvtrASLRRNI-AVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 87 SEEVdwqFPVSVYDVVMMGRygymnflriPKAIDKQkVQEAMQRVNIEHLAHRQ-------IGE----LSGGQKKRVFLA 155
Cdd:PRK13657 417 DAGL---FNRSIEDNIRVGR---------PDATDEE-MRAAAERAQAHDFIERKpdgydtvVGErgrqLSGGERQRLAIA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 156 RALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLReEGHLILVSTHNLGSVPDfCDQV-VMINRTVIAAGktedTFNQ 232
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRN-ADRIlVFDNGRVVESG----SFDE 555
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-228 |
7.99e-17 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 77.91 E-value: 7.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 13 VTVRYN-NGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKL--CDLP-ISQALKRNLVAYVPQSE 88
Cdd:cd03252 6 VRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdgHDLAlADPAWLRRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 89 EVdwqFPVSVYDVVMMGRYGyMNFLRIpkaIDKQKVQEAMQRVNIEHLAHRQI-GE----LSGGQKKRVFLARALAQQSP 163
Cdd:cd03252 86 VL---FNRSIRDNIALADPG-MSMERV---IEAAKLAGAHDFISELPEGYDTIvGEqgagLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169664 164 IILLDEPFTGVDVKTENAIVDLLQQLReEGHLILVSTHNLGSVPDFCDQVVMINRTVIAAGKTED 228
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDE 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-204 |
8.29e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.61 E-value: 8.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQaLKRNLVAYVPQS 87
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITR-LKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 88 EEVDWQ-----FPVSVYDVVMMGrygymnfLRIPKAID---KQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALA 159
Cdd:PRK10908 81 IGMIFQdhhllMDRTVYDNVAIP-------LIIAGASGddiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1169664 160 QQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLG 204
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIG 198
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-176 |
9.85e-17 |
|
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: 77.83 E-value: 9.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 30 SLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLcdlpisqalKRNLVAYVPQSEEVDwqFPVSVYDVVM-----M 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI---------ELDTVSYKPQYIKAD--YEGTVRDLLSsitkdF 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169664 105 GRYGYMNflripkaidkqkvQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDV 176
Cdd:cd03237 90 YTHPYFK-------------TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
8-221 |
1.06e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 80.06 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHT-AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKL--CDLpisQALK----RNL 80
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdgHDL---RDYTlaslRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 81 VAYVPQSEEVdwqFPVSVYDVVMMGRYGYMNFLRIPKAidkQKVQEAMQRVN-IEHLAHRQIGE----LSGGQKKRVFLA 155
Cdd:PRK11176 419 VALVSQNVHL---FNDTIANNIAYARTEQYSREQIEEA---ARMAYAMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIA 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 156 RALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEgHLILVSTHNLGSVPDfCDQVVMINRTVI 221
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEK-ADEILVVEDGEI 556
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
29-228 |
1.27e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.71 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 29 FSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLP---ISQALKRNLVAY-VPQSEEVdwqFP-VSVYDVVM 103
Cdd:PRK15439 32 FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPcarLTPAKAHQLGIYlVPQEPLL---FPnLSVKENIL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 104 mgrygymnfLRIPK-AIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVD-VKTENa 181
Cdd:PRK15439 109 ---------FGLPKrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAETER- 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1169664 182 ivdLLQQLRE---EGHLILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTED 228
Cdd:PRK15439 179 ---LFSRIREllaQGVGIVFISHKLPEIRQLADRIsVMRDGTIALSGKTAD 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
29-232 |
1.94e-16 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 79.29 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 29 FSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEI-------------KLCDLpISQALKRNLVAYVPQSEEvdwQFP 95
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsqfshitrlsfeQLQKL-VSDEWQRNNTDMLSPGED---DTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 96 VSVYDVVMMGrygymnflripkAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVD 175
Cdd:PRK10938 100 RTTAEIIQDE------------VKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1169664 176 VKTENAIVDLLQQLREEGH-LILVSTHnLGSVPDFCDQV-VMINRTVIAAGKTEDTFNQ 232
Cdd:PRK10938 168 VASRQQLAELLASLHQSGItLVLVLNR-FDEIPDFVQFAgVLADCTLAETGEREEILQQ 225
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
23-232 |
2.32e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 78.02 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 23 AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQ---------GEIKLCDLPISQalKRNLV------------ 81
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWhvtadrfrwNGIDLLKLSPRE--RRKIIgreiamifqeps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 82 AYVPQSEEVDWQFPVSVYDVVMMGRygymnFLRIPKAiDKQKVQEAMQRVNIEHlaHRQI-----GELSGGQKKRVFLAR 156
Cdd:COG4170 100 SCLDPSAKIGDQLIEAIPSWTFKGK-----WWQRFKW-RKKRAIELLHRVGIKD--HKDImnsypHELTEGECQKVMIAM 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 157 ALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL-ILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTEDTFNQ 232
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTsILLISHDLESISQWADTItVLYCGQTVESGPTEQILKS 249
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-232 |
2.59e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.80 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 23 AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLP----------------ISQALKrnlvaYVPQ 86
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfasttaalaagvaiIYQELH-----LVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 87 seevdwqfpVSVYDVVMMG----RYGYMNflripKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQS 162
Cdd:PRK11288 94 ---------MTVAENLYLGqlphKGGIVN-----RRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 163 PIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVvminrTVIAAGKTEDTFNQ 232
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAI-----TVFKDGRYVATFDD 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-241 |
3.19e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.55 E-value: 3.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 26 NMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS-----QALKRNLVaYVPQSEEVDWQF---PVS 97
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINalstaQRLARGLV-YLPEDRQSSGLYldaPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 98 vYDVVMMgRYGYMNFLRIPKAiDKQKVQEAMQRVNIEhLAHRQ--IGELSGGQKKRVFLARALAQQSPIILLDEPFTGVD 175
Cdd:PRK15439 360 -WNVCAL-THNRRGFWIKPAR-ENAVLERYRRALNIK-FNHAEqaARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169664 176 VKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRTVIAAGKTEDTFNQHNL-EIVFGG 241
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTImRLAFGE 502
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
8-207 |
3.25e-16 |
|
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: 75.83 E-value: 3.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEI----KLCDLP---ISQALKRNL 80
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPsfeATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 81 VAYVPQSEevdWQFPVSVYDVVMMGryGYMNFLRIPKAIDKQKVQEamqrvNIEHLAH---RQIGE----LSGGQKKRVF 153
Cdd:cd03290 81 VAYAAQKP---WLLNATVEENITFG--SPFNKQRYKAVTDACSLQP-----DIDLLPFgdqTEIGErginLSGGQRQRIC 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 154 LARALAQQSPIILLDEPFTGVDVKTENAIVD--LLQQLREEGHLILVSTHNLGSVP 207
Cdd:cd03290 151 VARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLP 206
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-201 |
3.48e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.94 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 24 IHNMTFSLNSGTICALVGVNGSGKSTL-----FKSIMGLVKpqQGEIKLCDLPISQALKRNLVAYVPQseeVDWQFP-VS 97
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLmnalaFRSPKGVKG--SGSVLLNGMPIDAKEMRAISAYVQQ---DDLFIPtLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 98 VYDVVMmgrygYMNFLRIPKAIDK----QKVQEAMQRVNIEHLAHRQIGE------LSGGQKKRVFLARALAQQSPIILL 167
Cdd:TIGR00955 116 VREHLM-----FQAHLRMPRRVTKkekrERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190
....*....|....*....|....*....|....
gi 1169664 168 DEPFTGVDVKTENAIVDLLQQLREEGHLILVSTH 201
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-233 |
5.62e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.82 E-value: 5.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNG---HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGL-----VKPQQGEIKL-------CDLPISQ 74
Cdd:PRK15134 8 IENLSVAFRQQqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFhgesllhASEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 75 ALKRNLVAYVPQSEEVDWQfPV-----SVYDVVMMGRYgymnfLRIPKAidKQKVQEAMQRVNIEHLAHRQIG---ELSG 146
Cdd:PRK15134 88 GVRGNKIAMIFQEPMVSLN-PLhtlekQLYEVLSLHRG-----MRREAA--RGEILNCLDRVGIRQAAKRLTDyphQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 147 GQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL-ILVSTHNLGSVPDFCDQV-VMINRTVIAAG 224
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMgLLFITHNLSIVRKLADRVaVMQNGRCVEQN 239
|
250
....*....|.
gi 1169664 225 KTEDTFN--QH 233
Cdd:PRK15134 240 RAATLFSapTH 250
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
24-201 |
5.64e-16 |
|
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: 74.59 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 24 IHNMTFSLNSGTICALVGVNGSGKSTLF-----KSIMGLVKpqqGEIKLCDLPISQALKRNlVAYVPQseeVDWQFPvsv 98
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLdvlagRKTAGVIT---GEILINGRPLDKNFQRS-TGYVEQ---QDVHSP--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 99 ydvvmmgrygymnflripkaidKQKVQEAMqrvniehLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKT 178
Cdd:cd03232 93 ----------------------NLTVREAL-------RFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180
....*....|....*....|...
gi 1169664 179 ENAIVDLLQQLREEGHLILVSTH 201
Cdd:cd03232 144 AYNIVRFLKKLADSGQAILCTIH 166
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
12-201 |
5.75e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.09 E-value: 5.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 12 DVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQAlkrNLVAYVPQSEEV- 90
Cdd:PRK10522 327 NVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE---QPEDYRKLFSAVf 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 91 -D-WQFPvsvydvVMMGRYGymnflripKAIDKQKVQEAMQRVNIEHLAHRQIGE-----LSGGQKKRVFLARALAQQSP 163
Cdd:PRK10522 404 tDfHLFD------QLLGPEG--------KPANPALVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERD 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1169664 164 IILLDE------P-FTGVDVKtenaivDLLQQLREEGHLILVSTH 201
Cdd:PRK10522 470 ILLLDEwaadqdPhFRREFYQ------VLLPLLQEMGKTIFAISH 508
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-200 |
5.88e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.74 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 24 IHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS-----QALKrNLVAYVPQSEEVD-WQFPVS 97
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspqDGLA-NGIVYISEDRKRDgLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 98 VYDVVMMGRYGYMNFL--RIPKAIDKQKVQEAMQRVNIEHLAHRQ-IGELSGGQKKRVFLARALAQQSPIILLDEPFTGV 174
Cdd:PRK10762 347 VKENMSLTALRYFSRAggSLKHADEQQAVSDFIRLFNIKTPSMEQaIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180
....*....|....*....|....*..
gi 1169664 175 DVKTENAIVDLLQQLREEG-HLILVST 200
Cdd:PRK10762 427 DVGAKKEIYQLINQFKAEGlSIILVSS 453
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-232 |
6.47e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.48 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 26 NMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQgeiklcdlpISQALKRNLVAYVPQseeVDWQFPVSVYDVVMMG 105
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE---------TSSVVIRGSVAYVPQ---VSWIFNATVRENILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 106 ------RYGymnflripKAIDKQKVQEamqrvNIEHLAHR---QIGE----LSGGQKKRVFLARALAQQSPIILLDEPFT 172
Cdd:PLN03232 703 sdfeseRYW--------RAIDVTALQH-----DLDLLPGRdltEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 173 GVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPdFCDQVVMINRTVIaagKTEDTFNQ 232
Cdd:PLN03232 770 ALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLP-LMDRIILVSEGMI---KEEGTFAE 825
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
10-230 |
7.70e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 76.70 E-value: 7.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHT---AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGL------VKPQQGEIKLCDL-PISQALKRN 79
Cdd:PRK11022 6 VDKLSVHFGDESApfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypgrVMAEKLEFNGQDLqRISEKERRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 80 LVAyvpqsEEVD--WQFPVSVYDVVMMGRYGYMNFLRI----PKAIDKQKVQEAMQRVNIEHLAHR---QIGELSGGQKK 150
Cdd:PRK11022 86 LVG-----AEVAmiFQDPMTSLNPCYTVGFQIMEAIKVhqggNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 151 RVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQL--REEGHLILVsTHNLGSVPDFCDQV-VMINRTVIAAGKTE 227
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLI-THDLALVAEAAHKIiVMYAGQVVETGKAH 239
|
...
gi 1169664 228 DTF 230
Cdd:PRK11022 240 DIF 242
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-237 |
9.69e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.47 E-value: 9.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 17 YNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKL--------CDLPISQALK-RNLVAYVPQS 87
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdgkvlyfgKDIFQIDAIKlRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 88 EEvdwQFP-VSVYDVVM--MGRYGYMNFLRIpkaidKQKVQEAMQRVNIEHLAHRQI----GELSGGQKKRVFLARALAQ 160
Cdd:PRK14246 99 PN---PFPhLSIYDNIAypLKSHGIKEKREI-----KKIVEECLRKVGLWKEVYDRLnspaSQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 161 QSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVStHNLGSVPDFCDQVVMI-NRTVIAAGKTEDTFNQHNLEI 237
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVS-HNPQQVARVADYVAFLyNGELVEWGSSNEIFTSPKNEL 247
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-235 |
1.37e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 76.79 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 24 IHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQ-QGEIKLCDLPIS-----QALkRNLVAYVPQSEEVDWQFPVS 97
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDirnpaQAI-RAGIAMVPEDRKRHGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 98 V--YDVVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLA-HRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGV 174
Cdd:TIGR02633 355 GvgKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 175 DVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVminrtVIAAGKTEDTFNQHNL 235
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVL-----VIGEGKLKGDFVNHAL 490
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-201 |
1.72e-15 |
|
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: 76.38 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 6 TSIWVNDVTVRYNNGHT----AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQAlkrNLV 81
Cdd:COG4615 326 QTLELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD---NRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 82 AYvpQSeevdwQFPVsVY-DVVMMGR-YGymnflrIPKAIDKQKVQEAMQRVNIEHLAHRQIG-----ELSGGQKKRVFL 154
Cdd:COG4615 403 AY--RQ-----LFSA-VFsDFHLFDRlLG------LDGEADPARARELLERLELDHKVSVEDGrfsttDLSQGQRKRLAL 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 155 ARALAQQSPIILLDE------P-----FTgvdvkTEnaivdLLQQLREEGHLILVSTH 201
Cdd:COG4615 469 LVALLEDRPILVFDEwaadqdPefrrvFY-----TE-----LLPELKARGKTVIAISH 516
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-226 |
2.13e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.19 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHtAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEI-------KLCDL-PISQALKRNLV 81
Cdd:PRK11701 9 VRGLTKLYGPRK-GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgQLRDLyALSEAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 82 ----AYVPQSEEVDWQFPVSVYDVV---MMGrYGYMNFLRIpkaidKQKVQEAMQRVNIEhlAHRqIGEL----SGGQKK 150
Cdd:PRK11701 88 rtewGFVHQHPRDGLRMQVSAGGNIgerLMA-VGARHYGDI-----RATAGDWLERVEID--AAR-IDDLpttfSGGMQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 151 RVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQV-VMINRTVIAAGKT 226
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLlVMKQGRVVESGLT 236
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-201 |
3.03e-15 |
|
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: 75.74 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 11 NDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLcdlpiSQALKrnlVAYVPQSEEV 90
Cdd:TIGR03719 8 NRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-----QPGIK---VGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 91 DwqfP-VSVYDVVMMG---------RYG--YMNF----LRIPKAIDKQ-KVQEAMQRVNIEHLAHR-------------- 139
Cdd:TIGR03719 80 D---PtKTVRENVEEGvaeikdaldRFNeiSAKYaepdADFDKLAAEQaELQEIIDAADAWDLDSQleiamdalrcppwd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169664 140 -QIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTenaiVDLLQQ-LRE-EGHLILVsTH 201
Cdd:TIGR03719 157 aDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERhLQEyPGTVVAV-TH 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-182 |
3.11e-15 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 76.10 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 24 IHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKlcdlpisqalKRNLVAYVPQseeVDWQFPVSVYDVVM 103
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK----------HSGRISFSPQ---TSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 104 MGrYGYMNFlRIPKAIDKQKVQEamqrvNIEHLAHRQ---IGE----LSGGQKKRVFLARALAQQSPIILLDEPFTGVDV 176
Cdd:TIGR01271 509 FG-LSYDEY-RYTSVIKACQLEE-----DIALFPEKDktvLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
....*.
gi 1169664 177 KTENAI 182
Cdd:TIGR01271 582 VTEKEI 587
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
21-223 |
3.39e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 73.34 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 21 HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLC---DLPISQAlkrnlVAYVPQseevdwqfpVS 97
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRgrvSSLLGLG-----GGFNPE---------LT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 98 VYD-VVMMGRygymnFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDV 176
Cdd:cd03220 101 GREnIYLNGR-----LLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1169664 177 KTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINRTVIAA 223
Cdd:cd03220 176 AFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
8-232 |
3.61e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.97 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNG-----HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK----R 78
Cdd:PRK13633 5 IKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwdiR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 79 NLVAYVPQSEevDWQFPVSVY--DVVmmgrYGYMNFLRIPKAIdKQKVQEAMQRVNI----EHLAHRqigeLSGGQKKRV 152
Cdd:PRK13633 85 NKAGMVFQNP--DNQIVATIVeeDVA----FGPENLGIPPEEI-RERVDESLKKVGMyeyrRHAPHL----LSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 153 FLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQVVMINRTVIAAGKTEDTFN 231
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
.
gi 1169664 232 Q 232
Cdd:PRK13633 234 E 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
24-203 |
4.20e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.97 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 24 IHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNL---VAYVPQSEevDWQF-PVSVY 99
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLrrkIGMVFQNP--DNQFvGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 100 DVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTE 179
Cdd:PRK13642 101 DDVAFG----MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180
....*....|....*....|....*
gi 1169664 180 NAIVDLLQQLREEGHLILVS-THNL 203
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSiTHDL 201
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-235 |
4.99e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.97 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 24 IHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQ-QGEIKLCDLPIS-----QALkRNLVAYVPQSEEVDWQFPV- 96
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKirnpqQAI-AQGIAMVPEDRKRDGIVPVm 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 97 --------SVYDvvmmgryGYMNFLRIPKAIDKQKVQEAMQRVNIE----HLAhrqIGELSGGQKKRVFLARALAQQSPI 164
Cdd:PRK13549 357 gvgknitlAALD-------RFTGGSRIDDAAELKTILESIQRLKVKtaspELA---IARLSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 165 ILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVminrtVIAAGKTEDTFNQHNL 235
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVL-----VMHEGKLKGDLINHNL 492
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-216 |
5.62e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 74.86 E-value: 5.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 20 GHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGlVKPQ---QGEIKLCDLPISQALKRNL----VAYVPQseEVDW 92
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASNIRDTeragIVIIHQ--ELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 93 QFPVSVYDVVMMGRYGYMNFLRIPKAIDKQKVQEAMQRVNIEHL-AHRQIGELSGGQKKRVFLARALAQQSPIILLDEPF 171
Cdd:TIGR02633 90 VPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1169664 172 TGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMI 216
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVI 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-235 |
7.01e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 72.64 E-value: 7.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 24 IHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVK--PQ---QGEIKL-----CDLPISQALKR-NLVAYVPQSeevdw 92
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLdgqdiFKMDVIELRRRvQMVFQIPNP----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 93 qFP-VSVYDVVMMGRYgyMNFLRIPKAIDKQKVQEAMQRVNI-EHLAHR---QIGELSGGQKKRVFLARALAQQSPIILL 167
Cdd:PRK14247 94 -IPnLSIFENVALGLK--LNRLVKSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 168 DEPFTGVDVKTENAIVDLLQQLREEGHLILVsTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFN--QHNL 235
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLV-THFPQQAARISDYVAFLYKgQIVEWGPTREVFTnpRHEL 240
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-234 |
8.90e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.42 E-value: 8.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 5 STSIWVNDVTVRYNNGH---------------------TAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQG 63
Cdd:COG1134 2 SSMIEVENVSKSYRLYHepsrslkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 64 EIKLcdlpisqalkrnlvayvpqSEEVDWQFPV--------SVYD-VVMMGR-YGYmnflripkaiDKQKVQEAMQRV-- 131
Cdd:COG1134 82 RVEV-------------------NGRVSALLELgagfhpelTGREnIYLNGRlLGL----------SRKEIDEKFDEIve 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 132 --NIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDV----KTENAIvdllQQLREEGHLILVSTHNLGS 205
Cdd:COG1134 133 faELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLARI----RELRESGRTVIFVSHSMGA 208
|
250 260 270
....*....|....*....|....*....|
gi 1169664 206 VPDFCDQVVMINR-TVIAAGKTEDTFNQHN 234
Cdd:COG1134 209 VRRLCDRAIWLEKgRLVMDGDPEEVIAAYE 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-233 |
9.46e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.51 E-value: 9.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 23 AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKlCDLPISQALKRNLVAYVPQSEE-----------VD 91
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ-CDKMLLRRRSRQVIELSEQSAAqmrhvrgadmaMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 92 WQFPVSVYDVVMMGRYGYMNFLRIPKAIDKQKVQEAMQR----VNI---EHLAHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:PRK10261 110 FQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRmldqVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169664 165 ILLDEPFTGVDVKTENAIVDLLQQLREEGHL-ILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTEDTFN--QH 233
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVlVMYQGEAVETGSVEQIFHapQH 262
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
23-232 |
9.84e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 73.46 E-value: 9.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 23 AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKL--CDL----PISQALKRNLVAYVPQSeevdwqfPv 96
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqgQDLlkadPEAQKLLRQKIQIVFQN-------P- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 97 svydvvmmgrYGYMN-------FLRIPKAID--------KQKVQEAMQRVNI--EHlAHRQIGELSGGQKKRVFLARALA 159
Cdd:PRK11308 102 ----------YGSLNprkkvgqILEEPLLINtslsaaerREKALAMMAKVGLrpEH-YDRYPHMFSGGQRQRIAIARALM 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169664 160 QQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILV-STHNLGSVPDFCDQV-VMINRTVIAAGKTEDTFNQ 232
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVfISHDLSVVEHIADEVmVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
26-228 |
1.18e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.49 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 26 NMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISqALKRNLVAYVPQSEEVDWQ----FP-VSVYD 100
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIP-AMSRSRLYTVRKRMSMLFQsgalFTdMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 101 VVMmgrYGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTEN 180
Cdd:PRK11831 104 NVA---YPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1169664 181 AIVDLLQQLREE-GHLILVSTHNLGSVPDFCDQVVMI-NRTVIAAGKTED 228
Cdd:PRK11831 181 VLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVaDKKIVAHGSAQA 230
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
11-184 |
1.44e-14 |
|
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: 72.58 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 11 NDVTVRYNN----GHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKlcdlpisqalKRNLVAYVPQ 86
Cdd:cd03291 36 DDNNLFFSNlclvGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK----------HSGRISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 87 seeVDWQFPVSVYDVVMMG-RYGYMNFLRIPKAIDKQKvqeamqrvNIEHLAHRQ---IGE----LSGGQKKRVFLARAL 158
Cdd:cd03291 106 ---FSWIMPGTIKENIIFGvSYDEYRYKSVVKACQLEE--------DITKFPEKDntvLGEggitLSGGQRARISLARAV 174
|
170 180
....*....|....*....|....*.
gi 1169664 159 AQQSPIILLDEPFTGVDVKTENAIVD 184
Cdd:cd03291 175 YKDADLYLLDSPFGYLDVFTEKEIFE 200
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-222 |
1.55e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.14 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 6 TSIWVNDVTVRYnnGHTAI-HNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEI-----KLCDLPISqalKRN 79
Cdd:PRK11000 2 ASVTLRNVTKAY--GDVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigekRMNDVPPA---ERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 80 lVAYVPQSEEVdwqFP-VSVYDVVMMGrygyMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARAL 158
Cdd:PRK11000 77 -VGMVFQSYAL---YPhLSVAENMSFG----LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 159 AQQSPIILLDEPFTGVD----VKTENAIVDLLQQLREEghLILVsTHNLGSVPDFCDQVVMINRTVIA 222
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRLGRT--MIYV-THDQVEAMTLADKIVVLDAGRVA 213
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
8-208 |
2.29e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 73.13 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGlVKPQ--------------QGEiKLCDLpis 73
Cdd:PRK10938 261 IVLNNGVVSYND-RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgysndltlfgrrrgSGE-TIWDI--- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 74 qalKRNlVAYVPQSEEVDWQFPVSVYDVVMMGrygYMNFLRIPKAI-DKQKvQEAMQRVNIEHLAHRQ----IGELSGGQ 148
Cdd:PRK10938 335 ---KKH-IGYVSSSLHLDYRVSTSVRNVILSG---FFDSIGIYQAVsDRQQ-KLAQQWLDILGIDKRTadapFHSLSWGQ 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169664 149 KKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGH--LILVS----------THNLGSVPD 208
Cdd:PRK10938 407 QRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGEtqLLFVShhaedapaciTHRLEFVPD 478
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
12-176 |
2.45e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.30 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 12 DVTVRYNNghtaihnmtFSLNS-------GTICALVGVNGSGKSTLFKSIMGLVKPQQGEIklcdlpiSQALKrnlVAYV 84
Cdd:PRK13409 345 DLTKKLGD---------FSLEVeggeiyeGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-------DPELK---ISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 85 PQSEEVDwqFPVSVYDvvmmgrygymnFLR-IPKAIDKQKVQ-EAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQS 162
Cdd:PRK13409 406 PQYIKPD--YDGTVED-----------LLRsITDDLGSSYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDA 472
|
170
....*....|....
gi 1169664 163 PIILLDEPFTGVDV 176
Cdd:PRK13409 473 DLYLLDEPSAHLDV 486
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-203 |
3.22e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.89 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNG----HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ--ALKR-NLVA 82
Cdd:COG1101 4 LKNLSKTFNPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlpEYKRaKYIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 83 YVpqseevdWQFPvsvydvvMMGRYGYM----NF-----------LRIpkAIDKQKVQEAMQRVNIEH--LAHR---QIG 142
Cdd:COG1101 84 RV-------FQDP-------MMGTAPSMtieeNLalayrrgkrrgLRR--GLTKKRRELFRELLATLGlgLENRldtKVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169664 143 ELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLI-LVSTHNL 203
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTtLMVTHNM 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-232 |
4.36e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.53 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 23 AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIklcdlpisqalkrnlvaYVPQSEEvdWqfpVSVYDVV 102
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV-----------------NVRVGDE--W---VDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 103 MMGR---YGYMNFL----------------------RIPKAIDKQKVQEAMQRVNIEHLAHRQI-----GELSGGQKKRV 152
Cdd:TIGR03269 357 PDGRgraKRYIGILhqeydlyphrtvldnlteaiglELPDELARMKAVITLKMVGFDEEKAEEIldkypDELSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 153 FLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREE-GHLILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTEDTF 230
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAaLMRDGKIVKIGDPEEIV 516
|
..
gi 1169664 231 NQ 232
Cdd:TIGR03269 517 EE 518
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-209 |
4.79e-14 |
|
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: 70.47 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 11 NDVTVRYNNGHTAIHNMTfSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGeiKLCDLPISQALKRN-----LVAYVP 85
Cdd:cd03236 4 DEPVHRYGPNSFKLHRLP-VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLG--KFDDPPDWDEILDEfrgseLQNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QSEEVDwqfpvsvYDVVMMGRYgymnFLRIPKAI------------DKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVF 153
Cdd:cd03236 81 KLLEGD-------VKVIVKPQY----VDLIPKAVkgkvgellkkkdERGKLDELVDQLELRHVLDRNIDQLSGGELQRVA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 154 LARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLgSVPDF 209
Cdd:cd03236 150 IAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL-AVLDY 204
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-225 |
5.23e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 72.67 E-value: 5.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 24 IHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLcdlpisqalkRNLVAYVPQSEevdWQFPVSVYDVVM 103
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM----------KGSVAYVPQQA---WIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 104 MGrygymnflripKAIDKQKVQEAMQRV----NIEHLA---HRQIGE----LSGGQKKRVFLARALAQQSPIILLDEPFT 172
Cdd:TIGR00957 721 FG-----------KALNEKYYQQVLEACallpDLEILPsgdRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 173 GVDVKTENAIVDllQQLREEGHL-----ILVsTHNLGSVPdfcdQVVMInrTVIAAGK 225
Cdd:TIGR00957 790 AVDAHVGKHIFE--HVIGPEGVLknktrILV-THGISYLP----QVDVI--IVMSGGK 838
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-235 |
6.95e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 69.87 E-value: 6.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 12 DVTVRYNNGHTaIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQ-----GEIKLCDL--------PISQALKR 78
Cdd:PRK14267 9 NLRVYYGSNHV-IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRniyspdvdPIEVRREV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 79 NLVAYVPQSeevdwqFP-VSVYDVVMMGrYGYMNFLRIPKAIDKqKVQEAMQRVNI-EHLAHR---QIGELSGGQKKRVF 153
Cdd:PRK14267 88 GMVFQYPNP------FPhLTIYDNVAIG-VKLNGLVKSKKELDE-RVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 154 LARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVsTHNLGSVPDFCDQVVMINR-TVIAAGKTEDTFN- 231
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLV-THSPAQAARVSDYVAFLYLgKLIEVGPTRKVFEn 238
|
....*
gi 1169664 232 -QHNL 235
Cdd:PRK14267 239 pEHEL 243
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-216 |
1.12e-13 |
|
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: 71.58 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHT-AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK--RNLVAYVPQ 86
Cdd:TIGR01257 1940 LNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISdvHQNMGYCPQ 2019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 87 SEEVDwqfpvsvydVVMMGR---YGYMNFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSP 163
Cdd:TIGR01257 2020 FDAID---------DLLTGRehlYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1169664 164 IILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMI 216
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-199 |
1.93e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 15 VRYN-NGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKlCDLPISqalkrnlVAYVPQ-SEEVDW 92
Cdd:PRK11147 325 VNYQiDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKLE-------VAYFDQhRAELDP 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 93 QFPV------SVYDVVMMGR----YGYM-NFLRIPKaidkqkvqEAMQRVNiehlahrqigELSGGQKKRVFLARALAQQ 161
Cdd:PRK11147 397 EKTVmdnlaeGKQEVMVNGRprhvLGYLqDFLFHPK--------RAMTPVK----------ALSGGERNRLLLARLFLKP 458
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1169664 162 SPIILLDEPFTGVDVKTenaiVDLLQQLREE--GHLILVS 199
Cdd:PRK11147 459 SNLLILDEPTNDLDVET----LELLEELLDSyqGTVLLVS 494
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
38-202 |
2.06e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 68.27 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 38 ALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ-------ALKRNLVAYVPQSeevdwqfpvsvydvvmmgrygym 110
Cdd:PRK10584 40 ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeearaKLRAKHVGFVFQS----------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 111 nFLRIPKAIDKQKVQ-EAMQRVNIEHLAH-------RQIG----------ELSGGQKKRVFLARALAQQSPIILLDEPFT 172
Cdd:PRK10584 97 -FMLIPTLNALENVElPALLRGESSRQSRngakallEQLGlgkrldhlpaQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190
....*....|....*....|....*....|.
gi 1169664 173 GVDVKTENAIVDLLQQL-REEGHLILVSTHN 202
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLnREHGTTLILVTHD 206
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-229 |
2.68e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.76 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 20 GHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPIS-----QALKrNLVAYVPQseEVDWQF 94
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksskEALE-NGISMVHQ--ELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 95 PVSVYDVVMMGRYGYMNFLripkaIDKQKVQEAMQRV----NIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEP 170
Cdd:PRK10982 87 QRSVMDNMWLGRYPTKGMF-----VDQDKMYRDTKAIfdelDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1169664 171 FTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVvminrTVIAAGKTEDT 229
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEI-----TILRDGQWIAT 215
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-217 |
2.71e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.39 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 5 STSIWVNDVTVRYNNG-HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ----ALKRN 79
Cdd:PLN03232 1232 RGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgltDLRRV 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 80 LvAYVPQSeevdwqfPVSVYDVVmmgRYGYMNFLRIPKAidkqKVQEAMQRVNIEHLAHR-------QIGE----LSGGQ 148
Cdd:PLN03232 1312 L-SIIPQS-------PVLFSGTV---RFNIDPFSEHNDA----DLWEALERAHIKDVIDRnpfgldaEVSEggenFSVGQ 1376
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 149 KKRVFLARALAQQSPIILLDEPFTGVDVKTENAIvdlLQQLREE--GHLILVSTHNLGSVPDfCDQVVMIN 217
Cdd:PLN03232 1377 RQLLSLARALLRRSKILVLDEATASVDVRTDSLI---QRTIREEfkSCTMLVIAHRLNTIID-CDKILVLS 1443
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-230 |
2.74e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.54 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 26 NMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGeiklcdlpiSQALKRNLVAYVPQseeVDWQFPVSVYDVVMMG 105
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD---------ASVVIRGTVAYVPQ---VSWIFNATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 106 ryGYMNFLRIPKAIDKQkvqeAMQRvNIEHLA---HRQIGE----LSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKT 178
Cdd:PLN03130 703 --SPFDPERYERAIDVT----ALQH-DLDLLPggdLTEIGErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 179 ENAIVD--LLQQLREEGHlILVST--HNLGSVpdfcDQVVMINRTVIaagKTEDTF 230
Cdd:PLN03130 776 GRQVFDkcIKDELRGKTR-VLVTNqlHFLSQV----DRIILVHEGMI---KEEGTY 823
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-218 |
2.75e-13 |
|
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: 70.43 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 11 NDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALK--RNLVAYVPQSE 88
Cdd:TIGR01257 933 NLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDavRQSLGMCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 89 EVDWQFPVSVYDVVMMGRYGymnflripKAIDKQKVQ-EAM-QRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIIL 166
Cdd:TIGR01257 1013 ILFHHLTVAEHILFYAQLKG--------RSWEEAQLEmEAMlEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1169664 167 LDEPFTGVDVKTENAIVDLLQQLReEGHLILVSTHNLGSVPDFCDQVVMINR 218
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQ 1135
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
12-231 |
4.36e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.88 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 12 DVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTL---FKSIMGLVKPQQGEIK-------LCDLPISQALKRNLV 81
Cdd:PRK14243 15 NLNVYYGS-FLAVKNVWLDIPKNQITAFIGPSGCGKSTIlrcFNRLNDLIPGFRVEGKvtfhgknLYAPDVDPVEVRRRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 82 AYVPQSEEvdwQFPVSVYDVVMMGRY--GYMNFLriPKAIDKQKVQEAMQRVNIEHLahRQIG-ELSGGQKKRVFLARAL 158
Cdd:PRK14243 94 GMVFQKPN---PFPKSIYDNIAYGARinGYKGDM--DELVERSLRQAALWDEVKDKL--KQSGlSLSGGQQQRLCIARAI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 159 AQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVsTHNLGSVPDFCDQVVMINRTVIAAG----------KTED 228
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIV-THNMQQAARVSDMTAFFNVELTEGGgrygylvefdRTEK 245
|
...
gi 1169664 229 TFN 231
Cdd:PRK14243 246 IFN 248
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-176 |
5.02e-13 |
|
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: 69.04 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 30 SLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLcdlpisqALKrnlVAYVPQSEEVDwqFPVSVYDvvmmgrygy 109
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-------DLK---ISYKPQYISPD--YDGTVEE--------- 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 110 mnFLR--IPKAIDKQKVQ-EAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDV 176
Cdd:COG1245 421 --FLRsaNTDDFGSSYYKtEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
29-201 |
6.57e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.41 E-value: 6.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 29 FSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNLVAYVPQseevdwqFPVSVYDVVMMGRYG 108
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGH-------LPGLKADLSTLENLH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 109 YMNFLRIPKAidKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQ 188
Cdd:PRK13543 105 FLCGLHGRRA--KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISA 182
|
170
....*....|...
gi 1169664 189 LREEGHLILVSTH 201
Cdd:PRK13543 183 HLRGGGAALVTTH 195
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
39-201 |
7.67e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.61 E-value: 7.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 39 LVGVNGSGKSTLFKsIM-GLVKPQQGEIKLcdlpiSQALKrnlVAYVPQSEEVDWQFpvSVYDVVMMG---------RYG 108
Cdd:PRK11819 38 VLGLNGAGKSTLLR-IMaGVDKEFEGEARP-----APGIK---VGYLPQEPQLDPEK--TVRENVEEGvaevkaaldRFN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 109 --YMNFLRiPKA-----IDKQ-KVQEAMQRVNIEHLAHR---------------QIGELSGGQKKRVFLARALAQQSPII 165
Cdd:PRK11819 107 eiYAAYAE-PDAdfdalAAEQgELQEIIDAADAWDLDSQleiamdalrcppwdaKVTKLSGGERRRVALCRLLLEKPDML 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 1169664 166 LLDEPFTGVDVKTenaiVDLLQQ-LRE-EGHLILVsTH 201
Cdd:PRK11819 186 LLDEPTNHLDAES----VAWLEQfLHDyPGTVVAV-TH 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-251 |
1.43e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.23 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNgHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNLV----AYVP 85
Cdd:NF033858 4 LEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVcpriAYMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 Q------------SEEVDwqFpvsvydvvmMGR-YGymnflrIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRV 152
Cdd:NF033858 83 QglgknlyptlsvFENLD--F---------FGRlFG------QDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 153 FLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREE--GHLILVSTHNLGSVPDFcDQVVMIN--RtVIAAGKTED 228
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAERF-DWLVAMDagR-VLATGTPAE 223
|
250 260
....*....|....*....|....*.
gi 1169664 229 TFNQ---HNLEIVFggvlrhIKLLGE 251
Cdd:NF033858 224 LLARtgaDTLEAAF------IALLPE 243
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-201 |
1.92e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.36 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 21 HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVK--PQQGEIKLCDLPISQalKRNLVAYVPQSEEvdwqFPVSV 98
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGR--EASLIDAIGRKGD----FKDAV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 99 YDVVMMGRYGYMNFLRIPKaidkqkvqeamqrvniehlahrqigELSGGQKKRVFLARALAQQSPIILLDEpFT-GVDVK 177
Cdd:COG2401 117 ELLNAVGLSDAVLWLRRFK-------------------------ELSTGQKFRFRLALLLAERPKLLVIDE-FCsHLDRQ 170
|
170 180
....*....|....*....|....*
gi 1169664 178 TENAIVDLLQQL-REEGHLILVSTH 201
Cdd:COG2401 171 TAKRVARNLQKLaRRAGITLVVATH 195
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-261 |
3.07e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.11 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 24 IHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIklcdlpisqaLKRNLVAYVPQSEevdWQFPVSVYDVVM 103
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV----------WAERSIAYVPQQA---WIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 104 mgrygymnFLRIPKAIDKQKVQEAMQ-RVNIEHLA---HRQIGE----LSGGQKKRVFLARALAQQSPIILLDEPFTGVD 175
Cdd:PTZ00243 743 --------FFDEEDAARLADAVRVSQlEADLAQLGgglETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 176 VKTENAIVD--LLQQLReeGHLILVSTHNLGSVPdFCDQVVMINR-TVIAAGKTEDtFNQHNLEIVFGGVLRHIKLLGEN 252
Cdd:PTZ00243 815 AHVGERVVEecFLGALA--GKTRVLATHQVHVVP-RADYVVALGDgRVEFSGSSAD-FMRTSLYATLAAELKENKDSKEG 890
|
....*....
gi 1169664 253 LHNDEDKRS 261
Cdd:PTZ00243 891 DADAEVAEV 899
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-238 |
4.31e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 66.36 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNnGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGL--VKPQQGEI----KLC------DLPISQA 75
Cdd:TIGR03269 1 IEVKNLTKKFD-GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvALCekcgyvERPSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 76 LKRNLVAYVPQSEEVDWQFPVSVYDVVMMGRYGYM---------------NFLRIPKAID---KQKVQEAMQRVNIEHLA 137
Cdd:TIGR03269 80 EPCPVCGGTLEPEEVDFWNLSDKLRRRIRKRIAIMlqrtfalygddtvldNVLEALEEIGyegKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 138 HRQIG---ELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQL-REEGHLILVSTHNLGSVPDFCDQV 213
Cdd:TIGR03269 160 HRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLSDKA 239
|
250 260
....*....|....*....|....*
gi 1169664 214 VMINRTVIAAGKTEDTFNQHNLEIV 238
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVVAVFMEGV 264
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-225 |
5.96e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.30 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 5 STSIWVNDVTVRYN-NGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQ---ALKRNL 80
Cdd:PLN03130 1235 SGSIKFEDVVLRYRpELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfglMDLRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 81 VAYVPQSeevdwqfPVSVYDVVmmgRYGYMNFLRIPKAidkqKVQEAMQRVNIEHLAHR----------QIGE-LSGGQK 149
Cdd:PLN03130 1315 LGIIPQA-------PVLFSGTV---RFNLDPFNEHNDA----DLWESLERAHLKDVIRRnslgldaevsEAGEnFSVGQR 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 150 KRVFLARALAQQSPIILLDEPFTGVDVKTenaivDLLQQ--LREE--GHLILVSTHNLGSVPDfCDQVVminrtVIAAGK 225
Cdd:PLN03130 1381 QLLSLARALLRRSKILVLDEATAAVDVRT-----DALIQktIREEfkSCTMLIIAHRLNTIID-CDRIL-----VLDAGR 1449
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
10-216 |
6.92e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 65.68 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNG--HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQALKRNLVAYVPQS 87
Cdd:PRK13545 24 LKDLFFRSKDGeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 88 EEVDWQFpvsvydvVMMGrygymnflripkaIDKQKVQEAMQRV----NIEHLAHRQIGELSGGQKKRVFLARALAQQSP 163
Cdd:PRK13545 104 ENIELKG-------LMMG-------------LTKEKIKEIIPEIiefaDIGKFIYQPVKTYSSGMKSRLGFAISVHINPD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1169664 164 IILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMI 216
Cdd:PRK13545 164 ILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWL 216
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
27-183 |
2.88e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 64.10 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 27 MTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQ--QGEIKLCDLPISQALKRNLVAYVPQSeevDWQFP-VSVYDVVM 103
Cdd:PLN03140 899 VTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQETFARISGYCEQN---DIHSPqVTVRESLI 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 104 mgrygYMNFLRIPKAIDKQK----VQEAMQRVNIEHLAHRQIG-----ELSGGQKKRVFLARALAQQSPIILLDEPFTGV 174
Cdd:PLN03140 976 -----YSAFLRLPKEVSKEEkmmfVDEVMELVELDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
....*....
gi 1169664 175 DVKTEnAIV 183
Cdd:PLN03140 1051 DARAA-AIV 1058
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
100-228 |
4.32e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.83 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 100 DVVMMGRYgymnfLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTE 179
Cdd:NF000106 106 NLYMIGR*-----LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR 180
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1169664 180 NAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMINR-TVIAAGKTED 228
Cdd:NF000106 181 NEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRgRVIADGKVDE 230
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
10-193 |
4.95e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 60.25 E-value: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDlpisqalkRNLVAYVPQSee 89
Cdd:cd03223 3 LENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE--------GEDLLFLPQR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 90 vdwqfpvsvydvvmmgryGYMNF--LRipkaidkqkvqeamqrvniEHLAHRQIGELSGGQKKRVFLARALAQQSPIILL 167
Cdd:cd03223 73 ------------------PYLPLgtLR-------------------EQLIYPWDDVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180
....*....|....*....|....*.
gi 1169664 168 DEPFTGVDVKTENAivdLLQQLREEG 193
Cdd:cd03223 116 DEATSALDEESEDR---LYQLLKELG 138
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-203 |
6.62e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.88 E-value: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 33 SGTICALVGVNGSGKSTLFKSIMGLVKPQQGEI-----------------------KLCDLPISQALKRNLVAYVPQsee 89
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkrfrgtelqdyfkKLANGEIKVAHKPQYVDLIPK--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 90 vdwQFPVSVYDVVMmgrygymnflripKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDE 169
Cdd:COG1245 175 ---VFKGTVRELLE-------------KVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....
gi 1169664 170 PFTGVDVKTENAIVDLLQQLREEGHLILVSTHNL 203
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-237 |
1.44e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.73 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 20 GHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGlVKPQ---QGEI----KLCDLP-ISQALKRNLV------AYVP 85
Cdd:NF040905 13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEIlfdgEVCRFKdIRDSEALGIViihqelALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 86 QseevdwqfpVSVYDVVMMG----RYGYMNFLRIpkaidKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQ 161
Cdd:NF040905 92 Y---------LSIAENIFLGneraKRGVIDWNET-----NRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169664 162 SPIILLDEPFTGVDVKTENAIVDLLQQLREEG-HLILVStHNLGSVPDFCDQVvminrTVIAAGKTEDTFNQHNLEI 237
Cdd:NF040905 158 VKLLILDEPTAALNEEDSAALLDLLLELKAQGiTSIIIS-HKLNEIRRVADSI-----TVLRDGRTIETLDCRADEV 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-201 |
1.56e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.68 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 22 TAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPI---SQALKRNlVAYVPQSeevdwqFpvSV 98
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdagDIATRRR-VGYMSQA------F--SL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 99 Y-------DVVMMGRygymnFLRIPKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPF 171
Cdd:NF033858 351 YgeltvrqNLELHAR-----LFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190
....*....|....*....|....*....|.
gi 1169664 172 TGVDVKTENAIVDLLQQL-REEGHLILVSTH 201
Cdd:NF033858 426 SGVDPVARDMFWRLLIELsREDGVTIFISTH 456
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-203 |
1.59e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 58.87 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 21 HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSImglvkpqqgeiklcdlpISQALKRNLVAYVPqseevdwqfpvsvyd 100
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG-----------------LYASGKARLISFLP--------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 101 vvmmgRYGYMNFLRIpkaiDKQKvqeAMQRVNIEHLA-HRQIGELSGGQKKRVFLARALAQQSP--IILLDEPFTGVDVK 177
Cdd:cd03238 56 -----KFSRNKLIFI----DQLQ---FLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180
....*....|....*....|....*.
gi 1169664 178 TENAIVDLLQQLREEGHLILVSTHNL 203
Cdd:cd03238 124 DINQLLEVIKGLIDLGNTVILIEHNL 149
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-205 |
2.25e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 22 TAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQ--QGEIKLCD-LPISQALKRnlVAYVPQSeevDWQFP-VS 97
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNrKPTKQILKR--TGFVTQD---DILYPhLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 98 VYDVVMmgrygYMNFLRIPKAIDKQKVQEAMQRVNIEH---------LAHRQIGELSGGQKKRVFLARALAQQSPIILLD 168
Cdd:PLN03211 157 VRETLV-----FCSLLRLPKSLTKQEKILVAESVISELgltkcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190
....*....|....*....|....*....|....*..
gi 1169664 169 EPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGS 205
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
23-235 |
2.67e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.20 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 23 AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQ---------GEIKLcdLPISQALKRNLVAY-------VPQ 86
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWrvtadrmrfDDIDL--LRLSPRERRKLVGHnvsmifqEPQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 87 S-----EEVDWQFPVSVYDVVMMGRYGYMNFLRIPKAIdkqkvqEAMQRVNIEhlAHRQIG-----ELSGGQKKRVFLAR 156
Cdd:PRK15093 100 ScldpsERVGRQLMQNIPGWTYKGRWWQRFGWRKRRAI------ELLHRVGIK--DHKDAMrsfpyELTEGECQKVMIAI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 157 ALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHL-ILVSTHNLGSVPDFCDQVvminrTVIAAGKTEDTFNQHNL 235
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTtILLISHDLQMLSQWADKI-----NVLYCGQTVETAPSKEL 246
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
15-207 |
3.52e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 58.34 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 15 VRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISQaLKRNLVAYVpqSEEVDWQF 94
Cdd:PRK13541 7 LQFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN-IAKPYCTYI--GHNLGLKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 95 PVSVYDVVMMGRYGYMNFLRIPKAIDKQKVQEamqrvniehLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGV 174
Cdd:PRK13541 84 EMTVFENLKFWSEIYNSAETLYAAIHYFKLHD---------LLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL 154
|
170 180 190
....*....|....*....|....*....|...
gi 1169664 175 DVKTENAIVDLLQQLREEGHLILVSTHNLGSVP 207
Cdd:PRK13541 155 SKENRDLLNNLIVMKANSGGIVLLSSHLESSIK 187
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-237 |
6.24e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 6.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 23 AIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPI--SQALK--RNLVAYVpqSEE--------- 89
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnHNANEaiNHGFALV--TEErrstgiyay 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 90 VDWQFPVSVYDV-VMMGRYGYMNFLRIPKaiDKQKVQEAMqrvNIEHLAHR-QIGELSGGQKKRVFLARALAQQSPIILL 167
Cdd:PRK10982 341 LDIGFNSLISNIrNYKNKVGLLDNSRMKS--DTQWVIDSM---RVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 168 DEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQV-VMINRTVIAAGKTEDTFNQHNLEI 237
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRIlVMSNGLVAGIVDTKTTTQNEILRL 486
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-231 |
1.93e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.41 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 20 GHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISqalKRNLVAYVPQSE---------EV 90
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLG---GRSIFNYRDVLEfrrrvgmlfQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 91 DWQFPVSVYDVVMMGRYGYMnflRIPKAIDKQKVQEAMQRVNIEHLAHRQIGE----LSGGQKKRVFLARALAQQSPIIL 166
Cdd:PRK14271 110 PNPFPMSIMDNVLAGVRAHK---LVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 167 LDEPFTGVDVKTENAIVDLLQQLREEGHLILVsTHNLGSVPDFCDQVVM-INRTVIAAGKTEDTFN 231
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADRLTVIIV-THNLAQAARISDRAALfFDGRLVEEGPTEQLFS 251
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-189 |
2.02e-09 |
|
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: 56.50 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 19 NGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQ---QGEIKLCDLPISQALK--RNLVAYVPQSeevDWQ 93
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEkyPGEIIYVSEE---DVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 94 FPVSVydvvmmgrygymnflripkaidkqkVQEAMQRVnIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTG 173
Cdd:cd03233 95 FPTLT-------------------------VRETLDFA-LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170
....*....|....*.
gi 1169664 174 VDVKTENAIVDLLQQL 189
Cdd:cd03233 149 LDSSTALEILKCIRTM 164
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-216 |
2.04e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.13 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 18 NNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIK----LCDLPISQALKRNLVAYvpqsEEVDwq 93
Cdd:PRK13546 34 NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDrngeVSVIAISAGLSGQLTGI----ENIE-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 94 fpvsvYDVVMMGrygymnFLRipKAIdKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTG 173
Cdd:PRK13546 108 -----FKMLCMG------FKR--KEI-KAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1169664 174 VDVKTENAIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMI 216
Cdd:PRK13546 174 GDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWI 216
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
10-216 |
3.70e-09 |
|
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: 56.40 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRY-NNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKpQQGEIKL-----CDLPISQ--------- 74
Cdd:cd03289 5 VKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIdgvswNSVPLQKwrkafgvip 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 75 --------ALKRNLVAYVPQSEEVDWQFPVSVYDVVMMGRY-GYMNFLripkAIDKQKVqeamqrvniehlahrqigeLS 145
Cdd:cd03289 84 qkvfifsgTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFpGQLDFV----LVDGGCV-------------------LS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169664 146 GGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILvSTHNLGSVPDfCDQVVMI 216
Cdd:cd03289 141 HGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVIL-SEHRIEAMLE-CQRFLVI 209
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
10-199 |
5.28e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGhTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDlpisqalkRNLVAYVPQSEE 89
Cdd:PRK15064 322 VENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSE--------NANIGYYAQDHA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 90 VDWQFPVSVYDvvmmgrygYMNFLRIPKAiDKQKVQEAMQRVniehL-----AHRQIGELSGGQKKRVFLARALAQQSPI 164
Cdd:PRK15064 393 YDFENDLTLFD--------WMSQWRQEGD-DEQAVRGTLGRL----LfsqddIKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190
....*....|....*....|....*....|....*
gi 1169664 165 ILLDEPFTGVDVKTENAIVDLLQQLreEGHLILVS 199
Cdd:PRK15064 460 LVMDEPTNHMDMESIESLNMALEKY--EGTLIFVS 492
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-190 |
7.86e-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: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 19 NGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGL--------VKPQQGEIklcdlpisqalkrnlvAYVPQS--- 87
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKL----------------FYVPQRpym 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 88 ------EEVdwQFPVSVYDVVMMGrygymnflripkaIDKQKVQEAMQRVNIEHLAHRQIG---------ELSGGQKKRV 152
Cdd:TIGR00954 527 tlgtlrDQI--IYPDSSEDMKRRG-------------LSDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRI 591
|
170 180 190
....*....|....*....|....*....|....*...
gi 1169664 153 FLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLR 190
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFG 629
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
97-203 |
8.87e-09 |
|
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: 55.31 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 97 SVYDVVMMGRY-GYMNFLRIPKAidKQKVQeAMQRVNIEHLahrQIG----ELSGGQKKRVFLARALAQQSP---IILLD 168
Cdd:cd03271 124 SIADVLDMTVEeALEFFENIPKI--ARKLQ-TLCDVGLGYI---KLGqpatTLSGGEAQRIKLAKELSKRSTgktLYILD 197
|
90 100 110
....*....|....*....|....*....|....*
gi 1169664 169 EPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNL 203
Cdd:cd03271 198 EPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL 232
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-208 |
1.21e-08 |
|
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: 53.15 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 33 SGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDLPISqalkrnlvayvpqseevdwqfpvsvydvvmmgrygymnf 112
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDI--------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 113 lripkaidkqkvQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDL-----LQ 187
Cdd:smart00382 42 ------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLL 109
|
170 180
....*....|....*....|.
gi 1169664 188 QLREEGHLILVSTHNLGSVPD 208
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLG 130
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-216 |
1.94e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 55.69 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 10 VNDVTVRYNNGHTAI-HNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKpQQGEIKLCDLP----------------- 71
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSwnsvtlqtwrkafgvip 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 72 -----ISQALKRNLVAYVPQSEEVDWQFPVSVYDVVMMGRYgymnflriPKAIDKQKVQEAMQrvniehlahrqigeLSG 146
Cdd:TIGR01271 1299 qkvfiFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQF--------PDKLDFVLVDGGYV--------------LSN 1356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 147 GQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILvSTHNLGSVPDfCDQVVMI 216
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVIL-SEHRVEALLE-CQQFLVI 1424
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
34-201 |
1.98e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 34 GTICALVGVNGSGKSTLFKSI-----MGLVkpQQGEIKLCDLPISQALKRNlVAYVPQSeevDWQFP-VSVYDVVMmgry 107
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDSSFQRS-IGYVQQQ---DLHLPtSTVRESLR---- 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 108 gYMNFLRIPKAI-DKQK---VQEAMQRVNIEHLAHRQIGE----LSGGQKKRVFLARAL-AQQSPIILLDEPFTGVDVKT 178
Cdd:TIGR00956 859 -FSAYLRQPKSVsKSEKmeyVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELvAKPKLLLFLDEPTSGLDSQT 937
|
170 180
....*....|....*....|...
gi 1169664 179 ENAIVDLLQQLREEGHLILVSTH 201
Cdd:TIGR00956 938 AWSICKLMRKLADHGQAILCTIH 960
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-227 |
2.15e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 19 NGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQ--QGEIK-----LCDLPISQALKRNLVayvpqseeVD 91
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILfkgesILDLEPEERAHLGIF--------LA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 92 WQFPVSVYDVvmmgryGYMNFLRIpkAID-KQKVQ---------------EAMQRVNI-EHLAHRQIGE-LSGGQKKR-V 152
Cdd:CHL00131 90 FQYPIEIPGV------SNADFLRL--AYNsKRKFQglpeldplefleiinEKLKLVGMdPSFLSRNVNEgFSGGEKKRnE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169664 153 FLARALAqQSPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTH--NLGS--VPDFCDqvVMINRTVIAAGKTE 227
Cdd:CHL00131 162 ILQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqRLLDyiKPDYVH--VMQNGKIIKTGDAE 237
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-206 |
3.54e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 26 NMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLCDlpiSQALK-------RNLVAYVPQ-----SEEVDWQ 93
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND---SHNLKdinlkwwRSKIGVVSQdpllfSNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 94 FPVSVY---DVVMMGRY-----------------------GYMN----------FLRIPK---AIDKQKVQEAMQRVNI- 133
Cdd:PTZ00265 480 IKYSLYslkDLEALSNYynedgndsqenknkrnscrakcaGDLNdmsnttdsneLIEMRKnyqTIKDSEVVDVSKKVLIh 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 134 ----------EHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLR-EEGHLILVSTHN 202
Cdd:PTZ00265 560 dfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHR 639
|
....
gi 1169664 203 LGSV 206
Cdd:PTZ00265 640 LSTI 643
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
8-199 |
4.18e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRYNNGHTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIklcdlpISQALKRnlVAYVPQs 87
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVR--MAVFSQ- 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 88 EEVDwQFPVSVYDVVMMGRYgymnFLRIPkaidKQKVQEAMQRVNIE-HLAHRQIGELSGGQKKRVFLARALAQQSPIIL 166
Cdd:PLN03073 580 HHVD-GLDLSSNPLLYMMRC----FPGVP----EQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILL 650
|
170 180 190
....*....|....*....|....*....|....
gi 1169664 167 LDEPFTGVDVkteNAIVDLLQQLRE-EGHLILVS 199
Cdd:PLN03073 651 LDEPSNHLDL---DAVEALIQGLVLfQGGVLMVS 681
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
22-208 |
5.15e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.02 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 22 TAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLcdlpiSQALKrnlVAYVPQ-------SEEVDWQF 94
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-----AKGIK---LGYFAQhqleflrADESPLQH 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 95 PVSVYDVVM-------MGRYGYMNflripkaidkQKVQEAMQRvniehlahrqigeLSGGQKKRVFLARALAQQSPIILL 167
Cdd:PRK10636 398 LARLAPQELeqklrdyLGGFGFQG----------DKVTEETRR-------------FSGGEKARLVLALIVWQRPNLLLL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1169664 168 DEPFTGVDVKTENAIVDLLQQLreEGHLILVS--THNLGSVPD 208
Cdd:PRK10636 455 DEPTNHLDLDMRQALTEALIDF--EGALVVVShdRHLLRSTTD 495
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-217 |
6.12e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 8 IWVNDVTVRY-NNGHTAIH-NMTFSLNSGTICALVGVNGSGKSTLFKSIMGLV---------------------KPQQGE 64
Cdd:PTZ00265 1166 IEIMDVNFRYiSRPNVPIYkDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtneQDYQGD 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 65 --------------------------------------IKLCDLPISQAlkRNLVAYVPQSEEVdwqFPVSVYDVVMMGR 106
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstvfknsgkilldgVDICDYNLKDL--RNLFSIVSQEPML---FNMSIYENIKFGK 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 107 ygymnflripkaidKQKVQEAMQRVN--------IEHLAHR---QIG----ELSGGQKKRVFLARALAQQSPIILLDEPF 171
Cdd:PTZ00265 1321 --------------EDATREDVKRACkfaaidefIESLPNKydtNVGpygkSLSGGQKQRIAIARALLREPKILLLDEAT 1386
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1169664 172 TGVDVKTENAIVDLLQQLREEG-HLILVSTHNLGSVPDfCDQVVMIN 217
Cdd:PTZ00265 1387 SSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKR-SDKIVVFN 1432
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
36-178 |
1.20e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 36 ICaLVGVNGSGKSTLFKSIMGLVKPQQGEIKlcdlpISQALKrnlVAYVPQSEEVDWQfpVSVYDVVMMG---------R 106
Cdd:PRK11147 32 VC-LVGRNGAGKSTLMKILNGEVLLDDGRII-----YEQDLI---VARLQQDPPRNVE--GTVYDFVAEGieeqaeylkR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 107 YGYMNFLRIPKAIDK-----QKVQEAMQRVNIEHL--------------AHRQIGELSGGQKKRVFLARALAQQSPIILL 167
Cdd:PRK11147 101 YHDISHLVETDPSEKnlnelAKLQEQLDHHNLWQLenrinevlaqlgldPDAALSSLSGGWLRKAALGRALVSNPDVLLL 180
|
170
....*....|.
gi 1169664 168 DEPFTGVDVKT 178
Cdd:PRK11147 181 DEPTNHLDIET 191
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
83-214 |
1.45e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.91 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 83 YVPQSEEVDWQFPvSVYDVVMMGRYGYMNFLRIPKAIdKQKVQeAMQRVNIEHLA-HRQIGELSGGQKKRVFLARALAQQ 161
Cdd:PRK00635 751 FLPQVLEVRYKGK-NIADILEMTAYEAEKFFLDEPSI-HEKIH-ALCSLGLDYLPlGRPLSSLSGGEIQRLKLAYELLAP 827
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 162 SP---IILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVpDFCDQVV 214
Cdd:PRK00635 828 SKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVV-KVADYVL 882
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-203 |
2.44e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 34 GTICALVGVNGSGKSTLFKSIMGLVKPQQGEI-----------------------KLCDLPISQALKRNLVAYVPQseev 90
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkrfrgtelqnyfkKLYNGEIKVVHKPQYVDLIPK---- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 91 dwQFPVSVYDVVMmgrygymnflripKAIDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRVFLARALAQQSPIILLDEP 170
Cdd:PRK13409 175 --VFKGKVRELLK-------------KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|...
gi 1169664 171 FTGVDVKTENAIVDLLQQLrEEGHLILVSTHNL 203
Cdd:PRK13409 240 TSYLDIRQRLNVARLIREL-AEGKYVLVVEHDL 271
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-222 |
2.77e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.87 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 12 DVTVRYNNG-HTAIHNMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIK----------LCDL---------- 70
Cdd:TIGR00957 1289 NYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIidglniakigLHDLrfkitiipqd 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 71 PI--SQALKRNLVAYVPQSEEVDWqfpvsvYDVVMMGRYGYMNFLriPKAIDKQKVQEamqrvniehlahrqiGE-LSGG 147
Cdd:TIGR00957 1369 PVlfSGSLRMNLDPFSQYSDEEVW------WALELAHLKTFVSAL--PDKLDHECAEG---------------GEnLSVG 1425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169664 148 QKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQlREEGHLILVSTHNLGSVPDFCdQVVMINRTVIA 222
Cdd:TIGR00957 1426 QRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVA 1498
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
30-203 |
8.19e-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: 48.12 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 30 SLNSGTICALVGVNGSGKSTLFKSImGLVKPQQGeiklcdlpiSQALKRNLVAYVPQSEEVDWQFPVSVydvvmmgrygy 109
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDAI-GLALGGAQ---------SATRRRSGVKAGCIVAAVSAELIFTR----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 110 mnflripkaidkqkvqeaMQrvniehlahrqigeLSGGQKKRVFLARALA----QQSPIILLDEPFTGVDVKTENAIVDL 185
Cdd:cd03227 76 ------------------LQ--------------LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEA 123
|
170
....*....|....*...
gi 1169664 186 LQQLREEGHLILVSTHNL 203
Cdd:cd03227 124 ILEHLVKGAQVIVITHLP 141
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
144-203 |
1.41e-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: 49.63 E-value: 1.41e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169664 144 LSGGQKKRVFLARALAQQS---PIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNL 203
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
144-203 |
1.50e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 49.64 E-value: 1.50e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 144 LSGGQKKRVFLARALAQQSP---IILLDEPFTGV---DVKTenaIVDLLQQLREEGHLILVSTHNL 203
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhDIRK---LLEVLHRLVDKGNTVVVIEHNL 889
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-201 |
1.15e-05 |
|
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: 45.29 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 36 ICALVGVNGSGKSTLFKSIM----GLVKPQ----QGEIKLC---------DLPISQALKRNL-----------VAYVPQs 87
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKyaltGELPPNskggAHDPKLIregevraqvKLAFENANGKKYtitrslailenVIFCHQ- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 88 EEVDWQFPvsvydvvmmgrygymnflripkaidkqkvqeamqrvniehlahRQIGELSGGQKK------RVFLARALAQQ 161
Cdd:cd03240 103 GESNWPLL-------------------------------------------DMRGRCSGGEKVlasliiRLALAETFGSN 139
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1169664 162 SPIILLDEPFTGVDV-KTENAIVDLLQQLREEGH-LILVSTH 201
Cdd:cd03240 140 CGILALDEPTTNLDEeNIEESLAEIIEERKSQKNfQLIVITH 181
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
30-209 |
2.08e-05 |
|
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: 44.57 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 30 SLNSGTICALVGVNGSGKSTLFKSIM------GLVKPQQGEIklcdlpisqalkRNLVAYVPQSEEVDWQFPVS--VYDV 101
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTILDAITyalygkTPRYGRQENL------------RSVFAPGEDTAEVSFTFQLGgkKYRV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 102 VmmgRYGYMNFlripkaidKQKVQEAMQRVN-IEHLAHRQIGELSGGQKKRVFLARALA-----QQSP-----IILLDEP 170
Cdd:cd03279 92 E---RSRGLDY--------DQFTRIVLLPQGeFDRFLARPVSTLSGGETFLASLSLALAlsevlQNRGgarleALFIDEG 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1169664 171 FTGVDVKTENAIVDLLQQLREEGHLILVSTHnlgsVPDF 209
Cdd:cd03279 161 FGTLDPEALEAVATALELIRTENRMVGVISH----VEEL 195
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-216 |
2.21e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 139 RQIGELSGGQKKRVFLARAL-AQQSPII-LLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNLGSVpDFCDQVVMI 216
Cdd:PRK00635 472 RALATLSGGEQERTALAKHLgAELIGITyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIIDI 550
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-214 |
2.25e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 26 NMTFSLNSGTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLcdlPISQALkrnlvAYVPQSEEVdwqFPVSVYDVVMMG 105
Cdd:PRK10636 19 NATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF---PGNWQL-----AWVNQETPA---LPQPALEYVIDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 106 RYGYMNFlripkaidKQKVQEAMQRVNIEHLAH--------------------------------RQIGELSGGQKKRVF 153
Cdd:PRK10636 88 DREYRQL--------EAQLHDANERNDGHAIATihgkldaidawtirsraasllhglgfsneqleRPVSDFSGGWRMRLN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169664 154 LARALAQQSPIILLDEPFTGVDVkteNAIVDLLQQLRE-EGHLILVStHNlgsvPDFCDQVV 214
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKSyQGTLILIS-HD----RDFLDPIV 213
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
141-203 |
2.67e-05 |
|
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: 45.07 E-value: 2.67e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 141 IGELSGGQKKRVFLARALAQQ---SPIILLDEPFTGVDVKTENAIVDLLQQLREEGHLILVSTHNL 203
Cdd:pfam13304 234 AFELSDGTKRLLALLAALLSAlpkGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSP 299
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
144-203 |
1.12e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.52 E-value: 1.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169664 144 LSGGQKKRVFLARALAQQS---PIILLDEPFTGV---DVKtenAIVDLLQQLREEGHLILVSTHNL 203
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfeDIR---KLLEVLHRLVDKGNTVVVIEHNL 893
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
34-216 |
2.85e-04 |
|
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: 41.02 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 34 GTICALVGVNGSGKSTLFKSIMGLVKPQQGEIKLcdlpisqalKRNLVAYVPQseevdwqfpvsvydvvmmgrygYMnfl 113
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW---------DGITPVYKPQ----------------------YI--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 114 ripkaidkqkvqeamqrvniehlahrqigELSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQLREEG 193
Cdd:cd03222 71 -----------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
170 180
....*....|....*....|....
gi 1169664 194 H-LILVSTHNLGSVPDFCDQVVMI 216
Cdd:cd03222 122 KkTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
39-178 |
4.38e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 39 LVGVNGSGKSTLFKSIMGLVKPQQGEIKLcDLPISQA-LKRNLVAYvpqsEEvdwqfpVSVYDVVMMGRYG--------- 108
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSL-DPNERLGkLRQDQFAF----EE------FTVLDTVIMGHTElwevkqerd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 109 --YMNflriPKAI--DKQKVQE------------AMQR-------VNIEHLAHRQ-IGELSGGQKKRVFLARALAQQSPI 164
Cdd:PRK15064 101 riYAL----PEMSeeDGMKVADlevkfaemdgytAEARagelllgVGIPEEQHYGlMSEVAPGWKLRVLLAQALFSNPDI 176
|
170
....*....|....
gi 1169664 165 ILLDEPFTGVDVKT 178
Cdd:PRK15064 177 LLLDEPTNNLDINT 190
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
138-188 |
4.68e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 38.37 E-value: 4.68e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169664 138 HRQIGELSGGQKKRVF---LARALAQQ---------SP-IILLDEPFTGVDVKTENAIVDLLQQ 188
Cdd:pfam13558 27 YRRSGGLSGGEKQLLAylpLAAALAAQygsaegrppAPrLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
142-217 |
2.82e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 2.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169664 142 GELSGGQKKRVFLARALAQQSPIILLDEPFTGVDV--KTEnaIVDLLQQLREEGHLILVSTHNLGSVPDFCDQVVMIN 217
Cdd:NF040905 403 GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgaKYE--IYTIINELAAEGKGVIVISSELPELLGMCDRIYVMN 478
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
25-62 |
2.93e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.65 E-value: 2.93e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1169664 25 HNMTFSLNSGTicALVGVNGSGKSTLFKSIMGLVKPQQ 62
Cdd:pfam13555 15 HTIPIDPRGNT--LLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
144-189 |
4.84e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 38.67 E-value: 4.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1169664 144 LSGGQKKRVFLARALAQQSPIILLDEPFTGVDVKTENAIVDLLQQL 189
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQI 382
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
134-218 |
6.64e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 37.97 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169664 134 EHLAHRQIGELSGGQKKRVF---LARALAQQ-------SP---IILLDEPFT-GVDVKTENAIvDLLQQLreeG-HLILV 198
Cdd:COG4913 968 EVETYSSSGGKSGGEKQKLAyfiLAAALAYQlglegrgRPsfrTVVLDEAFSkMDEEFARRAL-RLFKEL---GlQLLIA 1043
|
90 100
....*....|....*....|.
gi 1169664 199 S-THNLGSVPDFCDQVVMINR 218
Cdd:COG4913 1044 TpLDKIQAIEPYVGSVLVVHK 1064
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
23-54 |
7.02e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.60 E-value: 7.02e-03
10 20 30
....*....|....*....|....*....|..
gi 1169664 23 AIHNMTFSLnsGTICALVGVNGSGKSTLFKSI 54
Cdd:COG4637 12 SLRDLELPL--GPLTVLIGANGSGKSNLLDAL 41
|
|
| |
