|
Name |
Accession |
Description |
Interval |
E-value |
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-228 |
2.69e-93 |
|
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: 273.44 E-value: 2.69e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPD-TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladAQNRQQLH 80
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT------KKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:COG1122 75 RKVGLVFQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNStHQVDADLTRADL 228
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDD-GRIVADGTPREV 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-214 |
7.04e-90 |
|
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: 263.94 E-value: 7.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 3 KLVNICYDYPD--TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLAdaqnrqQLH 80
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLK------ELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:cd03225 75 RKVGLVFQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-214 |
9.62e-69 |
|
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: 212.70 E-value: 9.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDY-PDTC----GLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTylaDAQNR 76
Cdd:TIGR04521 1 IKLKNVSYIYqPGTPfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAK---KKKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 77 QQLHQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDC-ANLADRVPYQLSGGEKKRVALASVL 155
Cdd:TIGR04521 78 KDLRKKVGLVFQFPEHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 156 ALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQ-AAGKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMH 217
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-214 |
1.02e-62 |
|
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: 196.88 E-value: 1.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDT--CGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDqpITTtylADAQNRQQL 79
Cdd:TIGR04520 1 IEVENVSFSYPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDT---LDEENLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNP 159
Cdd:TIGR04520 76 RKKVGMVFQNPDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRLQA-AGKTIIMASHNYQQ-VQAvgERFIIFN 214
Cdd:TIGR04520 156 DIIILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDMEEaVLA--DRVIVMN 210
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-199 |
2.53e-61 |
|
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: 190.71 E-value: 2.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 11 YPD-TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtylaDAQNRQQLHQRIGMVFQN 89
Cdd:TIGR01166 1 YPGgPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDY----SRKGLLERRQRVGLVFQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 90 TDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLN 169
Cdd:TIGR01166 77 PDDQLFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|
gi 1729460384 170 GLTIAAQQQMLTLLQRLQAAGKTIIMASHN 199
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRAEGMTVVISTHD 186
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-198 |
8.41e-59 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 189.54 E-value: 8.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladaqnRQQLH 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT---------GLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QR-IGMVFQNTDvqLF-NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALN 158
Cdd:COG3842 76 KRnVGMVFQDYA--LFpHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1729460384 159 PEILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASH 198
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTH 194
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-198 |
2.38e-55 |
|
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: 177.54 E-value: 2.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladAQNRQQLH 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA------SLSRRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTDVQlFNTSVTEEVAFG--PRQ--LGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLA 156
Cdd:COG1120 75 RRIAYVPQEPPAP-FGLTVRELVALGryPHLglFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1729460384 157 LNPEILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASH 198
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLH 196
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-211 |
2.94e-55 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 176.40 E-value: 2.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYP-DTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPitttyLADAQNRQ-- 77
Cdd:COG2884 1 MIRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD-----LSRLKRREip 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 78 QLHQRIGMVFQntDVQL-FNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLA 156
Cdd:COG2884 76 YLRRRIGVVFQ--DFRLlPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1729460384 157 LNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFI 211
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVL 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-232 |
9.27e-55 |
|
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: 183.18 E-value: 9.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCG-----LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtylADAQN 75
Cdd:COG1123 260 LLEVRNLSKRYPVRGKggvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTK---LSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 76 RQQLHQRIGMVFQNTDVQLFNT-SVTEEVAFGPRQLG-LSAAMVAQRVADCLQLTD-CANLADRVPYQLSGGEKKRVALA 152
Cdd:COG1123 337 LRELRRRVQMVFQDPYSSLNPRmTVGDIIAEPLRLHGlLSRAERRERVAELLERVGlPPDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 153 SVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFIIFN--------STHQV---- 219
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYdgrivedgPTEEVfanp 496
|
250
....*....|...
gi 1729460384 220 DADLTRADLDQQP 232
Cdd:COG1123 497 QHPYTRALLAAVP 509
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-199 |
9.30e-55 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 176.81 E-value: 9.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPD-TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttYlaDAQNRQQL 79
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK--Y--DKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNP 159
Cdd:PRK13639 77 RKTVGIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHN 199
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD 196
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-214 |
2.01e-54 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 174.48 E-value: 2.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyladaqNRQQLHQ 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-------DPAEVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQNTDVQLfNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEI 161
Cdd:COG1131 74 RIGYVPQEPALYP-DLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1729460384 162 LLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIID 205
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-238 |
3.28e-54 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 175.31 E-value: 3.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPD-TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladAQNRQQLH 80
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN------AENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:PRK13647 79 SKVGLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNSTHQVDADLTRADLDQQPARQAQL 238
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQAGL 236
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-199 |
2.91e-53 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 172.58 E-value: 2.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCG----LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladaqnr 76
Cdd:COG1116 7 ALELRGVSKRFPTGGGgvtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 77 qQLHQRIGMVFQNTdvQLFN-TSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVL 155
Cdd:COG1116 77 -GPGPDRGVVFQEP--ALLPwLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1729460384 156 ALNPEILLLDEPLNGLTiaAQ--QQMLTLLQRL-QAAGKTIIMASHN 199
Cdd:COG1116 154 ANDPEVLLMDEPFGALD--ALtrERLQDELLRLwQETGKTVLFVTHD 198
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-215 |
1.08e-52 |
|
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: 170.11 E-value: 1.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTylaDAQNRQqlhq 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL---PPHKRP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 rIGMVFQNtdVQLF-NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:cd03300 74 -VNTVFQN--YALFpHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLQ-AAGKTIIMASHNYQQVQAVGERFIIFNS 215
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQkELGITFVFVTHDQEEALTMSDRIAVMNK 206
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-212 |
7.24e-52 |
|
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: 168.23 E-value: 7.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtylADAQNRQQLH 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITG---LSEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTdvQLFNT-SVTEEVAFGPRQLG-LSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALN 158
Cdd:COG1127 82 RRIGMLFQGG--ALFDSlTVFENVAFPLREHTdLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1729460384 159 PEILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFII 212
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAV 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-214 |
1.09e-51 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 166.93 E-value: 1.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaqnrqQLHQ 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV---------PPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 R-IGMVFQntDVQLF-NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNP 159
Cdd:cd03259 72 RnIGMVFQ--DYALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMN 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-214 |
5.82e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 163.34 E-value: 5.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPItttyladaqnrQQLH 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----------RRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTDVQL-FNTSVTEEVAFG-PRQLGL----SAAmVAQRVADCLQLTDCANLADRvPY-QLSGGEKKRVALAS 153
Cdd:COG1121 75 RRIGYVPQRAEVDWdFPITVRDVVLMGrYGRRGLfrrpSRA-DREAVDEALERVGLEDLADR-PIgELSGGQQQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1729460384 154 VLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLN 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-215 |
1.10e-49 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 161.87 E-value: 1.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCG----LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladaqnrq 77
Cdd:cd03293 1 LEVRNVSKTYGGGGGavtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 78 QLHQRIGMVFQNtDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLAL 157
Cdd:cd03293 70 GPGPDRGYVFQQ-DALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1729460384 158 NPEILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHNYQQVQAVGERFIIFNS 215
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-214 |
1.13e-49 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 164.07 E-value: 1.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDY----P-DTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLadaqNR 76
Cdd:PRK13637 3 IKIENLTHIYmegtPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKV----KL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 77 QQLHQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLT--DCANLADRVPYQLSGGEKKRVALASV 154
Cdd:PRK13637 79 SDIRKKVGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVglDYEDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1729460384 155 LALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGK-TIIMASHNYQQVQAVGERFIIFN 214
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMN 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-199 |
1.62e-49 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 161.75 E-value: 1.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPD----TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyLADAQnR 76
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISS--LSERE-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 77 QQL-HQRIGMVFQntDVQLFNT-SVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASV 154
Cdd:COG1136 81 ARLrRRHIGFVFQ--FFNLLPElTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1729460384 155 LALNPEILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHN 199
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHD 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-229 |
5.15e-49 |
|
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: 161.18 E-value: 5.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyladaqNRQQLH 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-------EPREAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTDVQLFNTsVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:COG4555 74 RQIGVLPDERGLYDRLT-VRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIF--------NSTHQVDADLTRADLD 229
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILhkgkvvaqGSLDELREEIGEENLE 229
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-211 |
2.49e-48 |
|
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: 159.20 E-value: 2.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyLADAQnRQQLHQ 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISG--LSEAE-LYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQntDVQLFNT-SVTEEVAFGPRQLG-LSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNP 159
Cdd:cd03261 78 RMGMLFQ--SGALFDSlTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFI 211
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIA 208
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-199 |
6.28e-48 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 161.47 E-value: 6.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTylADAQNRqqlhq 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN--LPPRER----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQNTDvqLF-NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:COG1118 76 RVGFVFQHYA--LFpHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHN 199
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHD 193
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-214 |
1.21e-47 |
|
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: 155.25 E-value: 1.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyladaqNRQQLHQ 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-------EPEEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQntDVQLFNT-SVTEevafgprqlglsaamvaqrvadclqltdcaNLadrvpyQLSGGEKKRVALASVLALNPE 160
Cdd:cd03230 74 RIGYLPE--EPSLYENlTVRE------------------------------NL------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILN 169
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-205 |
1.25e-47 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 160.62 E-value: 1.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTylaDAQNRqqlh 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL---PPKDR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 qRIGMVFQNTDvqLF-NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNP 159
Cdd:COG3839 76 -NIAMVFQSYA--LYpHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNyqQVQA 205
Cdd:COG3839 153 KVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHD--QVEA 197
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-215 |
3.14e-47 |
|
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: 154.27 E-value: 3.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtylaDAQNRQQLHQ 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTD----LEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQntDVQLFNT-SVTEEVAFGprqlglsaamvaqrvadclqltdcanladrvpyqLSGGEKKRVALASVLALNPE 160
Cdd:cd03229 77 RIGMVFQ--DFALFPHlTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLQA-AGKTIIMASHNYQQVQAVGERFIIFNS 215
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-216 |
6.74e-47 |
|
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: 154.61 E-value: 6.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 6 NICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladaqnrqQLHQRIGM 85
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----------KERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 86 VFQNTDV-QLFNTSVTEEVAFGPR-----QLGLSAAmVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNP 159
Cdd:cd03235 73 VPQRRSIdRDFPISVRDVVLMGLYghkglFRRLSKA-DKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNST 216
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-214 |
9.04e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 156.50 E-value: 9.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYP-DTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyladaQNRQQL 79
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK------ENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNP 159
Cdd:PRK13652 77 RKFVGLVFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMD 212
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-213 |
1.17e-46 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 154.77 E-value: 1.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttylADAQNRQQLH 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT----DSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNtdVQLF-NTSVTEEVAFGPRQ-LGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALN 158
Cdd:COG1126 77 RKVGMVFQQ--FNLFpHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1729460384 159 PEILLLDEPlnglTIAAQQQM----LTLLQRLQAAGKTIIMASHNYQQVQAVGERfIIF 213
Cdd:COG1126 155 PKVMLFDEP----TSALDPELvgevLDVMRDLAKEGMTMVVVTHEMGFAREVADR-VVF 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-215 |
1.27e-46 |
|
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: 153.57 E-value: 1.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 6 NICYDYPD-TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPItttyladaqNRQQLHQRIG 84
Cdd:cd03226 4 NISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---------KAKERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 85 MVFQNTDVQLFNTSVTEEVAFGPRQLGLSAamvaQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLL 164
Cdd:cd03226 75 YVMQDVDYQLFTDSVREELLLGLKELDAGN----EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1729460384 165 DEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNS 215
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-217 |
2.40e-46 |
|
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: 154.03 E-value: 2.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTylaDAQNRQqlhq 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV---PVQERN---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 rIGMVFQNtdVQLF-NTSVTEEVAFG----PRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLA 156
Cdd:cd03296 76 -VGFVFQH--YALFrHMTVFDNVAFGlrvkPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729460384 157 LNPEILLLDEPLNGLTIAAQQQMLTLLQRLQ-AAGKTIIMASHNYQQVQAVGERFIIFNSTH 217
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-203 |
4.29e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 155.01 E-value: 4.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPD-TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladAQNRQQL 79
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYS----RKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNP 159
Cdd:PRK13636 81 RESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQV 203
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIV 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-199 |
4.99e-46 |
|
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: 152.64 E-value: 4.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCG----LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyLADAQNRQ 77
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISK--LSEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 78 QLHQRIGMVFQNTdvQLFNT-SVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLA 156
Cdd:cd03255 79 FRRRHIGFVFQSF--NLLPDlTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1729460384 157 LNPEILLLDEPLNGLTIAAQQQMLTLLQRLQA-AGKTIIMASHN 199
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHD 200
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-211 |
5.25e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 152.28 E-value: 5.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaqNRQQLHQ 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM------PPPEWRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQntDVQLFNTSVTEEVAFGPR----------------QLGLSAAMVAQRVADclqltdcanladrvpyqLSGGE 145
Cdd:COG4619 75 QVAYVPQ--EPALWGGTVRDNLPFPFQlrerkfdreralelleRLGLPPDILDKPVER-----------------LSGGE 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729460384 146 KKRVALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHNYQQVQAVGERFI 211
Cdd:COG4619 136 RQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVL 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-241 |
7.53e-46 |
|
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: 159.68 E-value: 7.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPT---SGAYQFHDQPITttyladAQNRQQ 78
Cdd:COG1123 7 VRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLL------ELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 79 LHQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALN 158
Cdd:COG1123 81 RGRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 159 PEILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFIIFNSTHQVdADLTRADLDQQPARQAQ 237
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIV-EDGPPEEILAAPQALAA 239
|
....
gi 1729460384 238 LMTL 241
Cdd:COG1123 240 VPRL 243
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-214 |
2.13e-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: 148.93 E-value: 2.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 3 KLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaqNRQQLHQR 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKL------PLEELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 83 IGMVFQntdvqlfntsvteevafgprqlglsaamvaqrvadclqltdcanladrvpyqLSGGEKKRVALASVLALNPEIL 162
Cdd:cd00267 75 IGYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1729460384 163 LLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLK 154
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-209 |
3.62e-45 |
|
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: 150.81 E-value: 3.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCG----LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyLADAQNR 76
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTL--LSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 77 QQlHQRIGMVFQNtdVQLFNT-SVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVL 155
Cdd:cd03258 79 KA-RRRIGMIFQH--FNLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1729460384 156 ALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGER 209
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDR 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-214 |
4.98e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 152.55 E-value: 4.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGA--YQFHDQP----------------ITTTYLADAQNRQQ 78
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTieWIFKDEKnkkktkekekvleklvIQKTRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 79 LHQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDC-ANLADRVPYQLSGGEKKRVALASVLAL 157
Cdd:PRK13651 103 IRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1729460384 158 NPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-221 |
5.59e-45 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 153.70 E-value: 5.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYladAQNRQqlhq 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH---ARDRK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 rIGMVFQNtdVQLF-NTSVTEEVAFG----PRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLA 156
Cdd:PRK10851 76 -VGFVFQH--YALFrHMTVFDNIAFGltvlPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1729460384 157 LNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGK-TIIMASHNYQQVQAVGERFIIFNSTH--QVDA 221
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNieQAGT 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-198 |
5.89e-45 |
|
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: 148.74 E-value: 5.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 3 KLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaqNRQQLHQR 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL------SPKELARK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 83 IGMVFQntdvqlfntsvteevafgprqlglsaamvaqrvadCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEIL 162
Cdd:cd03214 75 IAYVPQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 1729460384 163 LLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASH 198
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLH 156
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-232 |
6.49e-45 |
|
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: 150.72 E-value: 6.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCG----LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYladaqnR 76
Cdd:COG1124 1 MLEVRNLSVSYGQGGRrvpvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRR------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 77 QQLHQRIGMVFQNTdvqlfntsvteEVAFGPRQ------------LGLSAamVAQRVADCLQLTD-CANLADRVPYQLSG 143
Cdd:COG1124 75 KAFRRRVQMVFQDP-----------YASLHPRHtvdrilaeplriHGLPD--REERIAELLEQVGlPPSFLDRYPHQLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 144 GEKKRVALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFIIFNSTHQVdAD 222
Cdd:COG1124 142 GQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV-EE 220
|
250
....*....|
gi 1729460384 223 LTRADLDQQP 232
Cdd:COG1124 221 LTVADLLAGP 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-203 |
6.82e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 151.91 E-value: 6.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDY-PDTC----GLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTylADAQNR 76
Cdd:PRK13641 3 IKFENVDYIYsPGTPmekkGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPE--TGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 77 QQLHQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQ---LTDcaNLADRVPYQLSGGEKKRVALAS 153
Cdd:PRK13641 81 KKLRKKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKkvgLSE--DLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1729460384 154 VLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQV 203
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDV 208
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-214 |
2.10e-44 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 150.17 E-value: 2.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTC--GLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADaqnrqqL 79
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD------V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNP 159
Cdd:PRK13635 80 RRQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHNYQQVqAVGERFIIFN 214
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEA-AQADRVIVMN 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-215 |
2.96e-44 |
|
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: 147.79 E-value: 2.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADaqnrqqlhQ 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQNtdVQLF-NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:cd03301 73 DIAMVFQN--YALYpHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFIIFNS 215
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMND 206
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-198 |
6.40e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 149.12 E-value: 6.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYP-----DTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttylADAQNR 76
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLIT----STSKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 77 --QQLHQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCA-NLADRVPYQLSGGEKKRVALAS 153
Cdd:PRK13649 79 diKQIRKKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1729460384 154 VLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-214 |
7.21e-44 |
|
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: 147.33 E-value: 7.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGL-----ASPTSGAYQFHDQPItttyLADAQNR 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDI----YDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 77 QQLHQRIGMVFQNTDvqLFNTSVTEEVAFGPRQLG-LSAAMVAQRVADCLQLtdcANLADRV-----PYQLSGGEKKRVA 150
Cdd:cd03260 77 LELRRRVGMVFQKPN--PFPGSIYDNVAYGLRLHGiKLKEELDERVEEALRK---AALWDEVkdrlhALGLSGGQQQRLC 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1729460384 151 LASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLqAAGKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAEL-KKEYTIVIVTHNMQQAARVADRTAFLL 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-212 |
1.64e-43 |
|
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: 147.79 E-value: 1.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 14 TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyLADAQNRQQLHQRIGMVFQNtdVQ 93
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAA--MSRKELRELRRKKISMVFQS--FA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 94 LF-NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLT 172
Cdd:cd03294 113 LLpHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1729460384 173 IAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFII 212
Cdd:cd03294 193 PLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAI 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-214 |
3.35e-43 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 145.91 E-value: 3.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPD-TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladAQNRQQLH 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR------EQDPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNtdVQLF-NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDC--ANLADRVPYQLSGGEKKRVALASVLAL 157
Cdd:cd03295 75 RKIGYVIQQ--IGLFpHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1729460384 158 NPEILLLDEP---LNGLTIAA-QQQMLTLLQRLqaaGKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:cd03295 153 DPPLLLMDEPfgaLDPITRDQlQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMK 210
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-212 |
3.51e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 147.47 E-value: 3.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 16 GLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTylADAQNRQQLHQRIGMVFQNTDVQLF 95
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAG--KKNKKLKPLRKKVGIVFQFPEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDC-ANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIA 174
Cdd:PRK13634 100 EETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1729460384 175 AQQQMLTLLQRL-QAAGKTIIMASHNYQQVQAVGERFII 212
Cdd:PRK13634 180 GRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVV 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-198 |
6.12e-43 |
|
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: 144.16 E-value: 6.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPItttyladAQNRQQLH 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-------RDAREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTDVQLFNTsVTEEVAFGPRQLGLSAAmvAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:COG4133 75 RRLAYLGHADGLKPELT-VRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-217 |
7.61e-43 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 148.94 E-value: 7.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTylaDAQNRQqlhq 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV---PAENRH---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 rIGMVFQNtdVQLF-NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:PRK09452 88 -VNTVFQS--YALFpHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFIIFNSTH 217
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-212 |
1.17e-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: 144.19 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtylADAQNRQQLHQRIGMVFQNTDVQLfN 96
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLK---LSRRLRKIRRKEIQMVFQDPMSSL-N 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVT--EEVAFGPRQLGLSAAMVAQRVADCL---QLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGL 171
Cdd:cd03257 97 PRMTigEQIAEPLRIHGKLSKKEARKEAVLLllvGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSAL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1729460384 172 TIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFII 212
Cdd:cd03257 177 DVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAV 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-214 |
3.58e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 144.36 E-value: 3.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPD--TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPItttylaDAQNRQQ 78
Cdd:PRK13632 7 MIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI------SKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 79 LHQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALN 158
Cdd:PRK13632 81 IRKKIGIIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1729460384 159 PEILLLDEPLNGLTIAAQQQMLTLLQRLQAAG-KTIIMASHNYQQVqAVGERFIIFN 214
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEA-ILADKVIVFS 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
17-215 |
5.20e-42 |
|
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: 142.96 E-value: 5.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaqnrqQLHQR----IGMVFQNTdv 92
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL---------PPHEIarlgIGRTFQIP-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 93 QLF-NTSVTEEVAFG-PRQLGLSAAM---------VAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEI 161
Cdd:cd03219 85 RLFpELTVLENVMVAaQARTGSGLLLararreereARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1729460384 162 LLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNS 215
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQ 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-215 |
6.06e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 144.07 E-value: 6.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPD------TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDqpITTTylaDAQ 74
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTS---DEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 75 NRQQLHQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASV 154
Cdd:PRK13633 79 NLWDIRNKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729460384 155 LALNPEILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHnYQQVQAVGERFIIFNS 215
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITH-YMEEAVEADRIIVMDS 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-220 |
1.50e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 143.00 E-value: 1.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDqpITTTYLADAQNRQQLHQRIGMVFQNTDVQLFN 96
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDD--ITITHKTKDKYIRPVRKRIGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVAFGPRQLGLSAAMVAQRVADCL-QLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAA 175
Cdd:PRK13646 101 DTVEREIIFGPKNFKMNLDEVKNYAHRLLmDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQS 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1729460384 176 QQQMLTLLQRLQA-AGKTIIMASHNYQQVQAVGERFIIFNSTHQVD 220
Cdd:PRK13646 181 KRQVMRLLKSLQTdENKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-211 |
1.57e-41 |
|
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: 141.01 E-value: 1.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYP-DTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPitttyLADAQNRQ--Q 78
Cdd:cd03292 1 IEFINVTKTYPnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQD-----VSDLRGRAipY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 79 LHQRIGMVFQNTDVqLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALN 158
Cdd:cd03292 76 LRRKIGVVFQDFRL-LPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1729460384 159 PEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFI 211
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVI 207
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
17-213 |
1.77e-41 |
|
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: 140.74 E-value: 1.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttylADAQNRQQLHQRIGMVFQNTDvqLF- 95
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT----DDKKNINELRQKVGMVFQQFN--LFp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 NTSVTEEVAFGPRQ-LGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIA 174
Cdd:cd03262 90 HLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 1729460384 175 AQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERfIIF 213
Cdd:cd03262 170 LVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADR-VIF 207
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-231 |
3.37e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 142.18 E-value: 3.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDY-PDTC----GLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTylADAQN 75
Cdd:PRK13643 1 MIKFEKVNYTYqPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSST--SKQKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 76 RQQLHQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCAN-LADRVPYQLSGGEKKRVALASV 154
Cdd:PRK13643 79 IKPVRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729460384 155 LALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNSTHQVDADlTRADLDQQ 231
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG-TPSDVFQE 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-169 |
3.78e-41 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 137.78 E-value: 3.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladAQNRQQLHQRIGMVFQntDVQLFN 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT------DDERKSLRKEIGYVFQ--DPQLFP 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1729460384 97 -TSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRV----PYQLSGGEKKRVALASVLALNPEILLLDEPLN 169
Cdd:pfam00005 73 rLTVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-198 |
3.11e-40 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 138.71 E-value: 3.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPItttylaDAQNRQQLH 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL------AAWSPWELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTDVQlFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRvPYQ-LSGGEKKRVALASVLA--- 156
Cdd:COG4559 75 RRRAVLPQHSSLA-FPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGR-SYQtLSGGEQQRVQLARVLAqlw 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1729460384 157 ----LNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:COG4559 153 epvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLH 198
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-198 |
3.21e-40 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 140.98 E-value: 3.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCG----LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyLADAQNR 76
Cdd:COG1135 1 MIELENLSKTFPTKGGpvtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTA--LSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 77 QqLHQRIGMVFQNtdvqlFN-----TsVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVAL 151
Cdd:COG1135 79 A-ARRKIGMIFQH-----FNllssrT-VAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1729460384 152 ASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASH 198
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITH 199
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-211 |
3.27e-40 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 137.96 E-value: 3.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTcgLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLAdaqnrqqlh 80
Cdd:COG3840 1 MLRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QR-IGMVFQNTDvqLFN-TSVTEEVAFG--PRqLGLSAAmVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLA 156
Cdd:COG3840 70 ERpVSMLFQENN--LFPhLTVAQNIGLGlrPG-LKLTAE-QRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1729460384 157 LNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFI 211
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVL 201
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-204 |
8.30e-40 |
|
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: 135.20 E-value: 8.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCG--LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaqNRQQL 79
Cdd:cd03228 1 IEFKNVSFSYPGRPKpvLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL------DLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQntDVQLFNTSVTEevafgprqlglsaamvaqrvadclqltdcaNLadrvpyqLSGGEKKRVALASVLALNP 159
Cdd:cd03228 75 RKNIAYVPQ--DPFLFSGTIRE------------------------------NI-------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRLqAAGKTIIMASHNYQQVQ 204
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIR 159
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-214 |
8.90e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 138.20 E-value: 8.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPD-TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQfhdqpITTTYLADAQNRQQL 79
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVL-----VSGIDTGDFSKLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNP 159
Cdd:PRK13644 76 RKLVGIVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAvGERFIIFN 214
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMD 209
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-220 |
9.28e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 135.91 E-value: 9.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTC-----GLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyLADAQNR 76
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAN-LKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 77 QQLHQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCA-NLADRVPYQLSGGEKKRVALASVL 155
Cdd:PRK13645 86 KRLRKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729460384 156 ALNPEILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHNYQQVQAVGERFIIFNSTHQVD 220
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-213 |
3.13e-38 |
|
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: 130.63 E-value: 3.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADAQNRqqlhq 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVfqntdvqlfntsvteevafgprqlglsaamvaqrvadclqltdcanladrvpYQLSGGEKKRVALASVLALNPEI 161
Cdd:cd03216 76 GIAMV----------------------------------------------------YQLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1729460384 162 LLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIF 213
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVL 155
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-199 |
3.77e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 133.72 E-value: 3.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladAQNRQQLHQRIGMVFQNTDVQLFN 96
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT------DDNFEKLRKHIGIVFQNPDNQFVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQ 176
Cdd:PRK13648 99 SIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180
....*....|....*....|....
gi 1729460384 177 QQMLTLLQRLQAAGK-TIIMASHN 199
Cdd:PRK13648 179 QNLLDLVRKVKSEHNiTIISITHD 202
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-186 |
1.17e-37 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 132.20 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaqNRQQLH 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADW------SPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTDVQlFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRvPY-QLSGGEKKRVALASVLA--- 156
Cdd:PRK13548 76 RRRAVLPQHSSLS-FPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGR-DYpQLSGGEQQRVQLARVLAqlw 153
|
170 180 190
....*....|....*....|....*....|...
gi 1729460384 157 ---LNPEILLLDEPLNGLTIAAQQQMLTLLQRL 186
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDLAHQHHVLRLARQL 186
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-212 |
1.30e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 133.82 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADAQ----------NRQQLHQRIGMV 86
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELitnpyskkikNFKELRRRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 87 FQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQ---LTDcaNLADRVPYQLSGGEKKRVALASVLALNPEILL 163
Cdd:PRK13631 122 FQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNkmgLDD--SYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1729460384 164 LDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFII 212
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIV 248
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-198 |
1.65e-37 |
|
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: 131.75 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSG--AYQFhDQPITTTYLADaqnrqq 78
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndVRLF-GERRGGEDVWE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 79 LHQRIGMVfqNTDVQLF---NTSVtEEV----AFGprQLGL----SAAMVaQRVADCLQLTDCANLADRVPYQLSGGEKK 147
Cdd:COG1119 76 LRKRIGLV--SPALQLRfprDETV-LDVvlsgFFD--SIGLyrepTDEQR-ERARELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1729460384 148 RVALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASH 198
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTH 201
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-213 |
2.28e-37 |
|
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: 130.11 E-value: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 19 DLSLTVNsGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPitttyLADAQNRQQL--HQR-IGMVFQNtdVQLF 95
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV-----LFDSRKKINLppQQRkIGLVFQQ--YALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 -NTSVTEEVAFGPRqlGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIA 174
Cdd:cd03297 88 pHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1729460384 175 AQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFIIF 213
Cdd:cd03297 166 LRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-199 |
4.98e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 130.90 E-value: 4.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladAQNRQQLH 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYS----KRGLLALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRvPYQ-LSGGEKKRVALASVLALNP 159
Cdd:PRK13638 77 QQVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQ-PIQcLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHN 199
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHD 195
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-198 |
6.71e-37 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 130.37 E-value: 6.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttylADAQNRqqlhqriGMVFQNtDVQLFN 96
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT----GPGADR-------GVVFQK-DALLPW 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQ 176
Cdd:COG4525 91 LNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTR 170
|
170 180
....*....|....*....|...
gi 1729460384 177 QQMLTLLQRL-QAAGKTIIMASH 198
Cdd:COG4525 171 EQMQELLLDVwQRTGKGVFLITH 193
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
17-199 |
2.29e-36 |
|
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: 128.62 E-value: 2.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladaqnRQQLHQRI--GMV--FQNTdv 92
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT---------GLPPHRIArlGIArtFQNP-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 93 QLFNT-SVTEEV---AFGPRQLGLSAAM------------VAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLA 156
Cdd:COG0411 89 RLFPElTVLENVlvaAHARLGRGLLAALlrlprarreereARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1729460384 157 LNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHN 199
Cdd:COG0411 169 TEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHD 212
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-198 |
2.55e-36 |
|
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: 135.35 E-value: 2.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPD--TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaqNRQQL 79
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI------DPASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQntDVQLFNTSVTEEVAFGPRQLGLsaamvaQRVADCLQLTDCANLADRVP--YQ---------LSGGEKKR 148
Cdd:COG2274 548 RRQIGVVLQ--DVFLFSGTIRENITLGDPDATD------EEIIEAARLAGLHDFIEALPmgYDtvvgeggsnLSGGQRQR 619
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1729460384 149 VALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLqAAGKTIIMASH 198
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAH 668
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-214 |
4.45e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 128.70 E-value: 4.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDY---PDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGayqfhdQPITTTYLADAQNRQ 77
Cdd:PRK13650 4 IIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESG------QIIIDGDLLTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 78 QLHQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLAL 157
Cdd:PRK13650 78 DIRHKIGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1729460384 158 NPEILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHNYQQVqAVGERFIIFN 214
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIrDDYQMTVISITHDLDEV-ALSDRVLVMK 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
19-214 |
4.51e-36 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 131.11 E-value: 4.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 19 DLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYqfhdqpitttyLADAQNRQQL--HQR-IGMVFQNtdVQLF 95
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-----------MLDGVDLSHVppYQRpINMMFQS--YALF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 -NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIA 174
Cdd:PRK11607 104 pHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1729460384 175 AQQQM-LTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:PRK11607 184 LRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMN 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-211 |
7.01e-36 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 127.13 E-value: 7.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPItttyLADAQNRQQLH 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV----NDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNtdVQLF-NTSVTEEVAFGPRQL-GLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALN 158
Cdd:PRK09493 77 QEAGMVFQQ--FYLFpHLTALENVMFGPLRVrGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1729460384 159 PEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFI 211
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLI 207
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-217 |
7.62e-36 |
|
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: 126.15 E-value: 7.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGdFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladaQNRQQLHQ 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-------KQPQKLRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQntDVQLF-NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:cd03264 73 RIGYLPQ--EFGVYpNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLqAAGKTIIMASHNYQQVQAVGERFIIFNSTH 217
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGK 206
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-205 |
1.43e-35 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 129.38 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADaqnrqqlhQ 81
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--------R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQNtdVQLF-NTSVTEEVAFGPRQLGLSAAMVAQRV---ADCLQLtdcANLADRVPYQLSGGEKKRVALASVLAL 157
Cdd:PRK11000 76 GVGMVFQS--YALYpHLSVAENMSFGLKLAGAKKEEINQRVnqvAEVLQL---AHLLDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1729460384 158 NPEILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNyqQVQA 205
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHD--QVEA 197
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
17-212 |
2.50e-35 |
|
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: 125.17 E-value: 2.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAyqfhdqpITTTYLADAQNRQQLHQRIGMVFQNTDV--QL 94
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGF-------ATVDGFDVVKEPAEARRRLGFVSDSTGLydRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 95 fntSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIA 174
Cdd:cd03266 94 ---TARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 1729460384 175 AQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFII 212
Cdd:cd03266 171 ATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVV 208
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-233 |
2.52e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 128.30 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 4 LVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLadaQNRQqlhqrI 83
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI---QQRD-----I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 84 GMVFQNtdVQLF-NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEIL 162
Cdd:PRK11432 81 CMVFQS--YALFpHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729460384 163 LLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFIIFNSTHQVDADlTRADLDQQPA 233
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIG-SPQELYRQPA 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-219 |
1.27e-34 |
|
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: 123.16 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttylADAQNRqqlhq 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNR----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 rIGmvFQNTDVQLF-NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:cd03269 72 -IG--YLPEERGLYpKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNSTHQV 219
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-231 |
1.31e-34 |
|
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: 123.83 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPD-TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyLADAQNRQQLH 80
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINK--LKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QrIGMVFQNtdvqlFN----TSVTEEVAFG--PRQ------LGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKR 148
Cdd:cd03256 79 Q-IGMIFQQ-----FNlierLSVLENVLSGrlGRRstwrslFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 149 VALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHNYQQVQAVGERFIIFNSTHQVdADLTRAD 227
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIV-FDGPPAE 231
|
....
gi 1729460384 228 LDQQ 231
Cdd:cd03256 232 LTDE 235
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-241 |
1.72e-34 |
|
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: 129.50 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCG--LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladAQNRQQL 79
Cdd:COG4987 334 LELEDVSFRYPGAGRpvLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR------DLDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQntDVQLFNTSVTEEVAFGPRQLGLSAAM-VAQRVadclQLTDcanLADRVPY-----------QLSGGEKK 147
Cdd:COG4987 408 RRRIAVVPQ--RPHLFDTTLRENLRLARPDATDEELWaALERV----GLGD---WLAALPDgldtwlgeggrRLSGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 148 RVALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLqAAGKTIIMASHNYQQVQAVGErfIIFNSTHQVDADLTRAD 227
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERMDR--ILVLEDGRIVEQGTHEE 555
|
250
....*....|....
gi 1729460384 228 LDQQPARQAQLMTL 241
Cdd:COG4987 556 LLAQNGRYRQLYQR 569
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-217 |
2.95e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 122.21 E-value: 2.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASP---TSGAYQFHDQPITTtyladaqnRQ 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTA--------LP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 78 QLHQRIGMVFQntDVQLF-NTSVTEEVAFG-PRQLGLSAAmvAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVL 155
Cdd:COG4136 73 AEQRRIGILFQ--DDLLFpHLSVGENLAFAlPPTIGRAQR--RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1729460384 156 ALNPEILLLDEPLNGLTIAAQQQMLTL-LQRLQAAGKTIIMASHNYQQVQAVGERFIIFNSTH 217
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGNWQH 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-199 |
3.51e-34 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 123.27 E-value: 3.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttylADAQNRqqlh 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE----GPGAER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 qriGMVFQNtDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:PRK11248 73 ---GVVFQN-EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHN 199
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHD 188
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
17-209 |
5.28e-34 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 121.46 E-value: 5.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyladaqNRQQLHQRIGMVFQNtDVQLFN 96
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-------DRKAARQSLGYCPQF-DALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVAFGPRQLGLS---AAMVAQRVADCLQLTDCANLADRvpyQLSGGEKKRVALASVLALNPEILLLDEPLNGLTI 173
Cdd:cd03263 90 LTVREHLRFYARLKGLPkseIKEEVELLLRVLGLTDKANKRAR---TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1729460384 174 AAQQQMLTLLQRLQaAGKTIIMASHNYQQVQAVGER 209
Cdd:cd03263 167 ASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDR 201
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-214 |
1.25e-33 |
|
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: 121.29 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTcGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTylaDAQNRqqlhq 81
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL---PPEKR----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQNTdvQLF-NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:cd03299 72 DISYVPQNY--ALFpHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLQ-AAGKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRkEFGVTVLHVTHDFEEAWALADKVAIML 204
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-198 |
4.79e-33 |
|
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: 125.26 E-value: 4.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPD-TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladAQNRQQLH 80
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS------DLDPASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTdvQLFNTSVTEEVAFGPRQLGlsaamvAQRVADCLQLTDCANLADRVP-----------YQLSGGEKKRV 149
Cdd:COG4988 411 RQIAWVPQNP--YLFAGTIRENLRLGRPDAS------DEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1729460384 150 ALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLqAAGKTIIMASH 198
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITH 530
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-214 |
5.75e-33 |
|
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: 119.36 E-value: 5.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 10 DYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDqpitttyLADAQNRQQLHQRIGMVF-Q 88
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-------LVPWKRRKKFLRRIGVVFgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 89 NTdvQL-FNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEP 167
Cdd:cd03267 103 KT--QLwWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1729460384 168 LNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-199 |
1.49e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 119.52 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDT--CGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAyqfhDQPITTTYLA-DAQNRQQ 78
Cdd:PRK13640 6 VEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNP----NSKITVDGITlTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 79 LHQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALN 158
Cdd:PRK13640 82 IREKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1729460384 159 PEILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHN 199
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHD 203
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-198 |
1.79e-32 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 118.65 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaqNRQQLH 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATT------PSRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTDVQLFNTsVTEEVAFG--PRQLG-LSA---AMVAQRVaDCLQLTDcanLADRVPYQLSGGEKKRVALASV 154
Cdd:COG4604 75 KRLAILRQENHINSRLT-VRELVAFGrfPYSKGrLTAedrEIIDEAI-AYLDLED---LADRYLDELSGGQRQRAFIAMV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1729460384 155 LALNPEILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASH 198
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLH 194
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-215 |
2.42e-32 |
|
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: 117.31 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCG--LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADaqnrqqL 79
Cdd:cd03245 3 IEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD------L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQntDVQLFNTSVTEEVAFGpRQLGLSAAMVaqRVADCLQLTDcanLADRVP-----------YQLSGGEKKR 148
Cdd:cd03245 77 RRNIGYVPQ--DVTLFYGTLRDNITLG-APLADDERIL--RAAELAGVTD---FVNKHPngldlqigergRGLSGGQRQA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729460384 149 VALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLqAAGKTIIMASHNYQQVQAVgERFIIFNS 215
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPSLLDLV-DRIIVMDS 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-198 |
2.68e-32 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 117.81 E-value: 2.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADAQNRQQLHQ 81
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQNtdvqlFN----TSVTEEVAFGP-RQLGLS---AAMVAQRVADCLQLTDcanLADRVPYQLSGGEKKRVALAS 153
Cdd:COG4161 83 KVGMVFQQ-----YNlwphLTVMENLIEAPcKVLGLSkeqAREKAMKLLARLRLTD---KADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1729460384 154 VLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTH 199
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-212 |
3.26e-32 |
|
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: 117.15 E-value: 3.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladaqnRQQLHQR----IGMVFQNTdv 92
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT---------GLPPHERaragIGYVPEGR-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 93 QLF-NTSVTEEVAFGPRQLGLSAamVAQRVADCLQL-TDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNG 170
Cdd:cd03224 85 RIFpELTVEENLLLGAYARRRAK--RKARLERVYELfPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1729460384 171 LTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFII 212
Cdd:cd03224 163 LAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYV 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-198 |
4.83e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 118.75 E-value: 4.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPItttyladAQNRQQLHQ 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-------PSRARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMV--FQNTDVQLfntSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNP 159
Cdd:PRK13537 81 RVGVVpqFDNLDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-198 |
5.59e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 119.52 E-value: 5.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYP----DTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyLADAQNR 76
Cdd:PRK11153 1 MIELKNISKVFPqggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTA--LSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 77 QqLHQRIGMVFQNtdvqlFN----TSVTEEVAFgPRQL-GLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVAL 151
Cdd:PRK11153 79 K-ARRQIGMIFQH-----FNllssRTVFDNVAL-PLELaGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1729460384 152 ASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASH 198
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITH 199
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-198 |
8.25e-32 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 116.65 E-value: 8.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADAQNRQQLHQ 81
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQNTDVQLFNTsVTEEVAFGP-RQLGLS---AAMVAQRVADCLQLTDcanLADRVPYQLSGGEKKRVALASVLAL 157
Cdd:PRK11124 83 NVGMVFQQYNLWPHLT-VQQNLIEAPcRVLGLSkdqALARAEKLLERLRLKP---YADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1729460384 158 NPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTH 199
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
19-204 |
1.39e-31 |
|
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: 118.66 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 19 DLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPitttyLADAQNRQQL--HQR-IGMVFQntDVQLF 95
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV-----LQDSARGIFLppHRRrIGYVFQ--EARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 NT-SVTEEVAFGPRQLGLSAAMVA-QRVADCLQLTDcanLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTI 173
Cdd:COG4148 90 PHlSVRGNLLYGRKRAPRAERRISfDEVVELLGIGH---LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190
....*....|....*....|....*....|..
gi 1729460384 174 AAQQQMLTLLQRLQAAGKT-IIMASHNYQQVQ 204
Cdd:COG4148 167 ARKAEILPYLERLRDELDIpILYVSHSLDEVA 198
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
17-214 |
1.65e-31 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 115.01 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQpitttylaDAQNRQQLHQRIGMVFqntDVQLF- 95
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--------SYQKNIEALRRIGALI---EAPGFy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 -NTSVTEEVAFGPRQLGLSAamvaQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIA 174
Cdd:cd03268 85 pNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1729460384 175 AQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:cd03268 161 GIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIIN 200
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-215 |
2.49e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 116.35 E-value: 2.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDY---PDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladAQNRQ 77
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT------AENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 78 QLHQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLAL 157
Cdd:PRK13642 78 NLRRKIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1729460384 158 NPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGK-TIIMASHNYQQVqAVGERFIIFNS 215
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEA-ASSDRILVMKA 215
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-202 |
2.58e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 115.50 E-value: 2.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyLADaqnrQQLH 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM--LSS----RQLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQntdvQLF---NTSVTEEVAFGpRQLGLS-----AAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALA 152
Cdd:PRK11231 76 RRLALLPQ----HHLtpeGITVRELVAYG-RSPWLSlwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1729460384 153 SVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQ 202
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQ 200
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-198 |
2.67e-31 |
|
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: 114.84 E-value: 2.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCG----LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyL---ADA 73
Cdd:COG4181 8 IIELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA--LdedARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 74 QNRQqlhQRIGMVFQNtdVQLFNT-SVTEEVAFgPRQL-GLSAAmvAQRVADCLQLTDCANLADRVPYQLSGGEKKRVAL 151
Cdd:COG4181 86 RLRA---RHVGFVFQS--FQLLPTlTALENVML-PLELaGRRDA--RARARALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1729460384 152 ASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQA-AGKTIIMASH 198
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTH 205
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-213 |
5.50e-31 |
|
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: 113.78 E-value: 5.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPittTYLADaqnrqqlhqrIGMVFQNtdvqlfN 96
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV---SSLLG----------LGGGFNP------E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRvPY-QLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAA 175
Cdd:cd03220 99 LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDL-PVkTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 1729460384 176 QQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIF 213
Cdd:cd03220 178 QEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVL 215
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
17-218 |
8.11e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 114.30 E-value: 8.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTY-------LADAQNRQQLHQRIGMVFQN 89
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRdkdgqlkVADKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 90 TDVQLFNTsVTEEVAFGPRQ-LGLSAAMVAQRVADCLQLTDCANLA-DRVPYQLSGGEKKRVALASVLALNPEILLLDEP 167
Cdd:PRK10619 101 FNLWSHMT-VLENVMEAPIQvLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1729460384 168 LNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFnstHQ 218
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFL---HQ 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-212 |
1.13e-30 |
|
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: 113.33 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttylADAQNRQqlhqrigMVFQNTDVQLFN 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT----EPGPDRM-------VVFQNYSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TsVTEEVAFGPRQLGLSAAMVAQR--VADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEP---LNGL 171
Cdd:TIGR01184 70 T-VRENIALAVDRVLPDLSKSERRaiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPfgaLDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1729460384 172 TIAAQQQmlTLLQRLQAAGKTIIMASHNYQQVQAVGERFII 212
Cdd:TIGR01184 149 TRGNLQE--ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVM 187
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-212 |
1.17e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 114.40 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyLADAQNRQqLHQRIGMVFQNTdVQLFN 96
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK--LNRAQRKA-FRRDIQMVFQDS-ISAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 --TSVTEEVAFGPRQL-GLSAAMVAQRVADCLQLTDCA-NLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLT 172
Cdd:PRK10419 104 prKTVREIIREPLRHLlSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1729460384 173 IAAQQQMLTLLQRLQAAGKT-IIMASHNYQQVQAVGERFII 212
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMV 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-199 |
3.22e-30 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 112.63 E-value: 3.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLaSPTSGAYQFHDQPitttyLADAQNRQQLHQRiGMVFQNTdVQLFN 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRP-----LSDWSAAELARHR-AYLSQQQ-SPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVAFGpRQLGLSAAMVAQRVAdclQLTDCANLADRVP---YQLSGGEKKRVALASVL-----ALNPE--ILLLDE 166
Cdd:COG4138 84 MPVFQYLALH-QPAGASSEAVEQLLA---QLAEALGLEDKLSrplTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDE 159
|
170 180 190
....*....|....*....|....*....|...
gi 1729460384 167 PLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHN 199
Cdd:COG4138 160 PMNSLDVAQQAALDRLLRELCQQGITVVMSSHD 192
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
19-211 |
3.59e-30 |
|
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: 111.43 E-value: 3.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 19 DLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADaqnrqqlhQRIGMVFQNTDvqLF-NT 97
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--------RPVSMLFQENN--LFaHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 98 SVTEEVAFG--PRqLGLSAAMvAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAA 175
Cdd:cd03298 86 TVEQNVGLGlsPG-LKLTAED-RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1729460384 176 QQQMLTLLQRLQA-AGKTIIMASHNYQQVQAVGERFI 211
Cdd:cd03298 164 RAEMLDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVV 200
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-217 |
6.56e-30 |
|
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: 108.69 E-value: 6.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQfHDQPITTTYLAdaqnrqqlhq 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-WGSTVKIGYFE---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 rigmvfqntdvqlfntsvteevafgprqlglsaamvaqrvadclqltdcanladrvpyQLSGGEKKRVALASVLALNPEI 161
Cdd:cd03221 70 ----------------------------------------------------------QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1729460384 162 LLLDEPLNGLTIAAQQQMLTLLQRLQaagKTIIMASHNYQQVQAVGERFIIFNSTH 217
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYP---GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
14-215 |
6.83e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 115.13 E-value: 6.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 14 TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGayQFHDQPITTTYLADAQNRQQLHQRIGMVFQNTDVq 93
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG--QVLIDGVDIAKISDAELREVRRKKIAMVFQSFAL- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 94 LFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTI 173
Cdd:PRK10070 118 MPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1729460384 174 AAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFIIFNS 215
Cdd:PRK10070 198 LIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQN 240
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-198 |
1.16e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.03 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYP-DTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaqNRQQLH 80
Cdd:COG1132 340 IEFENVSFSYPgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL------TLESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQntDVQLFNTSVTEEVAFGPrqlgLSAAMvaQRVADCLQLTDCANLADRVP--YQ---------LSGGEKKRV 149
Cdd:COG1132 414 RQIGVVPQ--DTFLFSGTIRENIRYGR----PDATD--EEVEEAAKAAQAHEFIEALPdgYDtvvgergvnLSGGQRQRI 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1729460384 150 ALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLqAAGKTIIMASH 198
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAH 533
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
17-212 |
1.42e-29 |
|
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: 111.44 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTylaDAQNRQQLHQRIGMVFQNTDVQLFN 96
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQL---DRKQRRAFRRDVQLVFQDSPSAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVAFGPRQ--LGLSAAMVAQRVADCLQLTDC-ANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTI 173
Cdd:TIGR02769 104 RMTVRQIIGEPLRhlTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1729460384 174 AAQQQMLTLLQRLQAAGKT-IIMASHNYQQVQAVGERFII 212
Cdd:TIGR02769 184 VLQAVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAV 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-199 |
2.51e-29 |
|
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: 111.68 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 19 DLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASP---TSGAYQFHDQPITTtyLADAQNRQQLHQRIGMVFQNtdvqlf 95
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLK--LSEKELRKIRGREIQMIFQD------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 ntSVTeevAFGPR-----QL--------GLSAAMVAQRVADCLQ---LTDCANLADRVPYQLSGGEKKRVALASVLALNP 159
Cdd:COG0444 95 --PMT---SLNPVmtvgdQIaeplrihgGLSKAEARERAIELLErvgLPDPERRLDRYPHELSGGMRQRVMIARALALEP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1729460384 160 EILLLDEPLNGL--TIaaQQQMLTLLQRLQAA-GKTIIMASHN 199
Cdd:COG0444 170 KLLIADEPTTALdvTI--QAQILNLLKDLQRElGLAILFITHD 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-199 |
3.43e-29 |
|
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: 107.69 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCG--LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLAdaqnrqQL 79
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN------EL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQntDVQLFNTSVTEEVafgprqlglsaamvaqrvadclqltdcanladrvpyqLSGGEKKRVALASVLALNP 159
Cdd:cd03246 75 GDHVGYLPQ--DDELFSGSIAENI-------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHN 199
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR 155
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-214 |
3.99e-29 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 109.00 E-value: 3.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSG-AYQF-HDqpitttYLADAQNrqqL 79
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGrATVAgHD------VVREPRE---V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQNTDVQLFNTSvTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNP 159
Cdd:cd03265 72 RRRIGIVFQDLSVDDELTG-WENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIID 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-240 |
5.70e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.57 E-value: 5.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADAQnrqqlH 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQ-----A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQntDVQLFNT-SVTEEVAFG--PRQLGL--SAAMVAqRVADCLQLTDCA-NLADRVpYQLSGGEKKRVALASV 154
Cdd:COG1129 79 AGIAIIHQ--ELNLVPNlSVAENIFLGrePRRGGLidWRAMRR-RARELLARLGLDiDPDTPV-GDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 155 LALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFN-----STHQVdADLTRADLd 229
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRdgrlvGTGPV-AELTEDEL- 232
|
250
....*....|.
gi 1729460384 230 qqparqAQLMT 240
Cdd:COG1129 233 ------VRLMV 237
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-199 |
7.07e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 112.24 E-value: 7.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPItttylaDAQNRQQLH 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV------EALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTDVQlFNTSVTEEVAFG--PRQLGLSAAMVAQR--VADCLQLTDCANLADRVPYQLSGGEKKRVALASVLA 156
Cdd:PRK09536 77 RRVASVPQDTSLS-FEFDVRQVVEMGrtPHRSRFDTWTETDRaaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1729460384 157 LNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHN 199
Cdd:PRK09536 156 QATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHD 198
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-209 |
1.47e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.43 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADAqnrqqLH 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDA-----IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNtdVQLFNT-SVTEEVAFG---PRQLGLSAAMVAQRVADclqLTDCANLA---DRVPYQLSGGEKKRVALAS 153
Cdd:COG3845 80 LGIGMVHQH--FMLVPNlTVAENIVLGlepTKGGRLDRKAARARIRE---LSERYGLDvdpDAKVEDLSVGEQQRVEILK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1729460384 154 VLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGER 209
Cdd:COG3845 155 ALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADR 210
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-198 |
1.56e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 106.55 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 11 YPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYqfhdqpitttyladaqnRQQLHQRIGMVFQNT 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------------RRAGGARVAYVPQRS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 91 DV-QLFNTSVTEEVAFGP-RQLGLSAAMVAQ---RVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLD 165
Cdd:NF040873 65 EVpDSLPLTVRDLVAMGRwARRGLWRRLTRDdraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190
....*....|....*....|....*....|...
gi 1729460384 166 EPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARGATVVVVTH 177
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-231 |
1.74e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 109.92 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladAQNRQQlHQ 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP------ARARLA-RA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMV--FQNTDVQLfntSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNP 159
Cdd:PRK13536 115 RIGVVpqFDNLDLEF---TVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNSTHQVDADLTRADLDQQ 231
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-213 |
2.31e-28 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 107.24 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladaqnRQQLHQ 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT---------KLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 R--IGMVFQNTDVQLF-NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALN 158
Cdd:cd03218 72 RarLGIGYLPQEASIFrKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1729460384 159 PEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGER-FIIF 213
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRaYIIY 207
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-235 |
2.32e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 107.91 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADAQNRQ--Q 78
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLirQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 79 LHQRIGMVFQNTDvqLF-NTSVTEEVAFGPRQL-GLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLA 156
Cdd:PRK11264 83 LRQHVGFVFQNFN--LFpHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 157 LNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNS---THQVDADLTRADLDQQPA 233
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQgriVEQGPAKALFADPQQPRT 240
|
..
gi 1729460384 234 RQ 235
Cdd:PRK11264 241 RQ 242
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-212 |
3.74e-28 |
|
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: 109.43 E-value: 3.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 19 DLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDqpittTYLADAQNRQQL--HQR-IGMVFQntDVQLF 95
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG-----RTLFDSRKGIFLppEKRrIGYVFQ--EARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 -NTSVTEEVAFGprqlgLSAAMVAQRVADCLQLTDCAN---LADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGL 171
Cdd:TIGR02142 88 pHLSVRGNLRYG-----MKRARPSERRISFERVIELLGighLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1729460384 172 TIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFII 212
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVV 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-212 |
3.97e-28 |
|
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: 106.60 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladaqnRQQLH 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT---------GLPPH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QR----IGMVFQNTDV--QLfntSVTE--EVAFGPRQlglSAAMVAQRVADCLQL-TDCANLADRVPYQLSGGEKKRVAL 151
Cdd:COG0410 74 RIarlgIGYVPEGRRIfpSL---TVEEnlLLGAYARR---DRAEVRADLERVYELfPRLKERRRQRAGTLSGGEQQMLAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1729460384 152 ASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFII 212
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYV 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-202 |
6.53e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 106.66 E-value: 6.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDypDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLR-------LLSGLAspTSGAYQFHDQPItttyLADAQ 74
Cdd:COG1117 14 VRNLNVYYG--DKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEDI----YDPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 75 NRQQLHQRIGMVFQ--NtdvqLFNTSVTEEVAFGPRQLGL-SAAMVAQRVADCLQLtdcANLADRV-------PYQLSGG 144
Cdd:COG1117 86 DVVELRRRVGMVFQkpN----PFPKSIYDNVAYGLRLHGIkSKSELDEIVEESLRK---AALWDEVkdrlkksALGLSGG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1729460384 145 EKKRVALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLqaagK---TIIMASHNYQQ 202
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL----KkdyTIVIVTHNMQQ 215
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-199 |
8.48e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 107.90 E-value: 8.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 19 DLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtylADAQNRQQLHQRIGMVFQNTDVQLfNT- 97
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITG---LSGRELRPLRRRMQMVFQDPYASL-NPr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 98 -SVTEEVAFGPRQLGL-SAAMVAQRVADCLQLTDC-ANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIA 174
Cdd:COG4608 112 mTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVS 191
|
170 180
....*....|....*....|....*.
gi 1729460384 175 AQQQMLTLLQRLQAA-GKTIIMASHN 199
Cdd:COG4608 192 IQAQVLNLLEDLQDElGLTYLFISHD 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-213 |
1.01e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.15 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQpITTTYLadAQNRQQLH 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET-VKIGYF--DQHQEELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 --QRigmVFQNtdVQLFNTSVTEEVAfgpRQL----GLSAAMVAQRVADclqltdcanladrvpyqLSGGEKKRVALASV 154
Cdd:COG0488 392 pdKT---VLDE--LRDGAPGGTEQEV---RGYlgrfLFSGDDAFKPVGV-----------------LSGGEKARLALAKL 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1729460384 155 LALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQaaGkTIIMASHNYQQVQAVGERFIIF 213
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEALDDFP--G-TVLLVSHDRYFLDRVATRILEF 502
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-199 |
4.16e-27 |
|
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: 104.23 E-value: 4.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDY-PDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLadaqnrQQLH 80
Cdd:cd03253 1 IEFENVTFAYdPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTL------DSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQntDVQLFNTSVTEEVAFGprqlGLSAAMVAQRVAdCLQltdcANLADRV---P--YQ---------LSGGEK 146
Cdd:cd03253 75 RAIGVVPQ--DTVLFNDTIGYNIRYG----RPDATDEEVIEA-AKA----AQIHDKImrfPdgYDtivgerglkLSGGEK 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1729460384 147 KRVALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLqAAGKTIIMASHN 199
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHR 195
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-198 |
6.14e-27 |
|
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: 6.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLA---SPTSGAYQFHDQPItttyladaqNRQQLHQRIGMVFQNtDVQ 93
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPR---------KPDQFQKCVAYVRQD-DIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 94 LFNTSVTEEVAFGPRQLG--LSAAMVAQRVADCLQLTDCAN--LADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLN 169
Cdd:cd03234 93 LPGLTVRETLTYTAILRLprKSSDAIRKKRVEDVLLRDLALtrIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180
....*....|....*....|....*....
gi 1729460384 170 GLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-198 |
7.19e-27 |
|
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: 107.76 E-value: 7.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDT-CGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPitttyLADAqNRQQLH 80
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP-----LADA-DADSWR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTdvQLFNTSVTEEVAFGprQLGLSAAMVAQRVADClQLTDCAN--------LADRVPYQLSGGEKKRVALA 152
Cdd:TIGR02857 396 DQIAWVPQHP--FLFAGTIAENIRLA--RPDASDAEIREALERA-GLDEFVAalpqgldtPIGEGGAGLSGGQAQRLALA 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1729460384 153 SVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLqAAGKTIIMASH 198
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTH 515
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-211 |
1.32e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 102.85 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAyqfhdqpITTtyladaqnrqqlHQRIGMVFqntDVQL-F 95
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR-------VEV------------NGRVSALL---ELGAgF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 NTSVT--EEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRvPYQ-LSGGEKKRVALASVLALNPEILLLDEplnglT 172
Cdd:COG1134 100 HPELTgrENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQ-PVKtYSSGMRARLAFAVATAVDPDILLVDE-----V 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1729460384 173 IAA-----QQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFI 211
Cdd:COG1134 174 LAVgdaafQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAI 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-198 |
1.77e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.69 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 6 NICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSG----------AY--Q----FHDQPITTTY 69
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGevsipkglriGYlpQepplDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 70 LADAQNRQQLHQRIgmvfqntdvQLFNTSVTEEVAFGPRQLGLSAAMV----------AQRVADCLQLTDcaNLADRVPY 139
Cdd:COG0488 83 LDGDAELRALEAEL---------EELEAKLAEPDEDLERLAELQEEFEalggweaearAEEILSGLGFPE--EDLDRPVS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 140 QLSGGEKKRVALASVLALNPEILLLDEPLNGLTIaaqqQMLTLLQR-LQAAGKTIIMASH 198
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL----ESIEWLEEfLKNYPGTVLVVSH 207
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-212 |
2.10e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.97 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPdtcGLK-DLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLAdaqnrqql 79
Cdd:PRK10771 1 MLKLTDITWLYH---HLPmRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 hQR-IGMVFQNTDvqLFN-TSVTEEVAFG--PrQLGLSAAMVAQrVADCLQLTDCANLADRVPYQLSGGEKKRVALASVL 155
Cdd:PRK10771 70 -RRpVSMLFQENN--LFShLTVAQNIGLGlnP-GLKLNAAQREK-LHAIARQMGIEDLLARLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1729460384 156 ALNPEILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHNYQQVQAVGERFII 212
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLV 202
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-205 |
3.07e-26 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 104.15 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYP-DTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADaqnrqql 79
Cdd:PRK11650 3 GLKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 hqR-IGMVFQNtdVQLF-NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLAL 157
Cdd:PRK11650 76 --RdIAMVFQN--YALYpHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1729460384 158 NPEILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNyqQVQA 205
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHD--QVEA 198
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
17-212 |
3.52e-26 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 102.06 E-value: 3.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPitttyLADAQNRqqlhqrIGMVFQntDVQLFN 96
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP-----LAEARED------TRLMFQ--DARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 -TSVTEEVAfgprqLGLSAAMVAQrvadCLQLTDCANLADRV---PYQLSGGEKKRVALASVLALNPEILLLDEPLNGLT 172
Cdd:PRK11247 95 wKKVIDNVG-----LGLKGQWRDA----ALQALAAVGLADRAnewPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1729460384 173 IAAQQQMLTLLQRL-QAAGKTIIMASHNYQQVQAVGERFII 212
Cdd:PRK11247 166 ALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLL 206
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
12-241 |
4.13e-26 |
|
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: 101.46 E-value: 4.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 12 PDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyladaQNRQQLHQRIGMVFQntD 91
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRD------LNLRWLRSQIGLVSQ--E 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 92 VQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTdcANLADRvpY---------QLSGGEKKRVALASVLALNPEIL 162
Cdd:cd03249 86 PVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFI--MSLPDG--YdtlvgergsQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729460384 163 LLDEPLNGLTIAAQQQMLTLLQRLqAAGKTIIMASHNYQQVQAVgERFIIFNSTHQVDADlTRADLDQQPARQAQLMTL 241
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLSTIRNA-DLIAVLQNGQVVEQG-THDELMAQKGVYAKLVKA 237
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-196 |
5.47e-26 |
|
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: 101.15 E-value: 5.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCG--LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADaqnrqqL 79
Cdd:cd03251 1 VEFKNVTFRYPGDGPpvLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS------L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQntDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDC------ANLADRvPYQLSGGEKKRVALAS 153
Cdd:cd03251 75 RRQIGLVSQ--DVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMElpegydTVIGER-GVKLSGGQRQRIAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1729460384 154 VLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMA 196
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIA 194
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-199 |
9.72e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 104.91 E-value: 9.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPD--TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladAQNRQQL 79
Cdd:PRK11160 339 LTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA------DYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQNtdVQLFNTSVTEEVAFGprqlglSAAMVAQRVADCLQLTDCANLADRVP----------YQLSGGEKKRV 149
Cdd:PRK11160 413 RQAISVVSQR--VHLFSATLRDNLLLA------APNASDEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRL 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1729460384 150 ALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLqAAGKTIIMASHN 199
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHR 533
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-199 |
3.00e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 98.41 E-value: 3.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPIT-------TTYLA--DAQNRqqlhqrigmvf 87
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdpdvaeaCHYLGhrNAMKP----------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 88 qntdvqlfNTSVTEEVAF-----GPRQLGLSAAmvaqrvADCLQLTDCANLadrvPYQ-LSGGEKKRVALASVLALNPEI 161
Cdd:PRK13539 87 --------ALTVAENLEFwaaflGGEELDIAAA------LEAVGLAPLAHL----PFGyLSAGQKRRVALARLLVSNRPI 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 1729460384 162 LLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHN 199
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-198 |
5.60e-25 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 98.85 E-value: 5.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 20 LSLTVNSGDFICLMGPNGSGKSTLLRLLSGLaSPTSGAYQFHDQPITTTYLAD-AQNRQQLHQRIGMVFqNTDV----QL 94
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAElARHRAYLSQQQTPPF-AMPVfqylTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 95 FNTSVTEEVAfgprqlglsAAMVAQRVADCLQLTDcanLADRVPYQLSGGEKKRVALASVL-----ALNPE--ILLLDEP 167
Cdd:PRK03695 93 HQPDKTRTEA---------VASALNEVAEALGLDD---KLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEP 160
|
170 180 190
....*....|....*....|....*....|.
gi 1729460384 168 LNGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGIAVVMSSH 191
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-214 |
6.31e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 99.80 E-value: 6.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladaqnrQQLH 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----------PEDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIG-M-----VFQNTDV--QLfntsvteeVAFGprQL-GLSAAMVAQRVADCL---QLTDCANlaDRVPyQLSGGEKKR 148
Cdd:COG4152 71 RRIGyLpeergLYPKMKVgeQL--------VYLA--RLkGLSKAEAKRRADEWLerlGLGDRAN--KKVE-ELSKGNQQK 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729460384 149 VALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIIN 203
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-213 |
1.27e-24 |
|
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: 96.23 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYP--DTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPItttylADAQNrqQL 79
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-----SDLEK--AL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQNtdVQLFNTSVTEevafgprqlglsaamvaqrvadclqltdcaNLADRvpyqLSGGEKKRVALASVLALNP 159
Cdd:cd03247 74 SSLISVLNQR--PYLFDTTLRN------------------------------NLGRR----FSGGERQRLALARILLQDA 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRlQAAGKTIIMASHNYQQVQAVGErfIIF 213
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFE-VLKDKTLIWITHHLTGIEHMDK--ILF 168
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-188 |
1.30e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 101.30 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTL----LRLLsglasPTSGAYQFHDQPITTtylADAQNRQQLHQRIGMVFQNTdv 92
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDG---LSRRALRPLRRRMQVVFQDP-- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 93 qlFNT-----SVTEEVAFGPR--QLGLSAAMVAQRVADCLQ---LTdcANLADRVPYQLSGGEKKRVALASVLALNPEIL 162
Cdd:COG4172 372 --FGSlsprmTVGQIIAEGLRvhGPGLSAAERRARVAEALEevgLD--PAARHRYPHEFSGGQRQRIAIARALILEPKLL 447
|
170 180
....*....|....*....|....*.
gi 1729460384 163 LLDEPLNGLTIAAQQQMLTLLQRLQA 188
Cdd:COG4172 448 VLDEPTSALDVSVQAQILDLLRDLQR 473
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
17-198 |
1.44e-24 |
|
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: 101.36 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPItttylaDAQNRQQLHQRIGMVFQntDVQLFN 96
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL------SQWDREELGRHIGYLPQ--DVELFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVA-FGprqlGLSAAMV--AQRVADC----LQL-----TDcanLADRvPYQLSGGEKKRVALASVLALNPEILLL 164
Cdd:COG4618 420 GTIAENIArFG----DADPEKVvaAAKLAGVhemiLRLpdgydTR---IGEG-GARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190
....*....|....*....|....*....|....
gi 1729460384 165 DEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRALKARGATVVVITH 525
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-198 |
1.80e-24 |
|
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: 96.08 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASP--TSGAYQFHDQPITttyladaqnRQQLHQRIGMVFQNtDVQL 94
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLD---------KRSFRKIIGYVPQD-DILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 95 FNTSVTEEVAFgprqlglSAAMvaqrvadclqltdcanladrvpYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIA 174
Cdd:cd03213 95 PTLTVRETLMF-------AAKL----------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180
....*....|....*....|....
gi 1729460384 175 AQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:cd03213 146 SALQVMSLLRRLADTGRTIICSIH 169
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-199 |
5.87e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 99.76 E-value: 5.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKS----TLLRLLSGLASPTSGAYQFHDQPITTtyLADAQNRQQLHQRIGMVFQntdv 92
Cdd:COG4172 26 VKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG--LSERELRRIRGNRIAMIFQ---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 93 qlfntsvteE--VAFGP-----RQL--------GLSAAMVAQRVADCLQLT---DCANLADRVPYQLSGGEKKRVALASV 154
Cdd:COG4172 100 ---------EpmTSLNPlhtigKQIaevlrlhrGLSGAAARARALELLERVgipDPERRLDAYPHQLSGGQRQRVMIAMA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1729460384 155 LALNPEILLLDEPLNGL--TIaaQQQMLTLLQRLQAA-GKTIIMASHN 199
Cdd:COG4172 171 LANEPDLLIADEPTTALdvTV--QAQILDLLKDLQRElGMALLLITHD 216
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
16-214 |
6.15e-24 |
|
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: 95.58 E-value: 6.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 16 GLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGA--YQFHDQPITttyLADAQNRQQLHQR---IGMVFQnt 90
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGGWVD---LAQASPREILALRrrtIGYVSQ-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 91 dvqlFNTSV----TEEVAFGP-RQLGLSAAMVAQRVADCL-QLtdcaNLADRV----PYQLSGGEKKRVALASVLALNPE 160
Cdd:COG4778 101 ----FLRVIprvsALDVVAEPlLERGVDREEARARARELLaRL----NLPERLwdlpPATFSGGEQQRVNIARGFIADPP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:COG4778 173 LLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-212 |
7.38e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.80 E-value: 7.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYP---DTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaqNRQQ 78
Cdd:TIGR00958 479 IEFQDVSFSYPnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY------DHHY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 79 LHQRIGMVFQntDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQL---------TDCANLADrvpyQLSGGEKKRV 149
Cdd:TIGR00958 553 LHRQVALVGQ--EPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFimefpngydTEVGEKGS----QLSGGQKQRI 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1729460384 150 ALASVLALNPEILLLDEPLNGLTIAAQQqmlTLLQRLQAAGKTIIMASHNYQQVQAVGERFII 212
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDAECEQ---LLQESRSRASRTVLLIAHRLSTVERADQILVL 686
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-198 |
7.46e-24 |
|
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: 95.37 E-value: 7.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDY-PDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaqNRQQLH 80
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI------SRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQntDVQLFNTSVTEEVAFGprqlGLSAAMvaQRVADCLQLTDCANLADRVP--YQ---------LSGGEKKRV 149
Cdd:cd03254 77 SMIGVVLQ--DTFLFSGTIMENIRLG----RPNATD--EEVIEAAKEAGAHDFIMKLPngYDtvlgenggnLSQGERQLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1729460384 150 ALASVLALNPEILLLDEPLNGLTI----AAQQQMLTLLQrlqaaGKTIIMASH 198
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTetekLIQEALEKLMK-----GRTSIIIAH 196
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-199 |
7.81e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.01 E-value: 7.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 4 LVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITT----------TYLAda 73
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsskafarkvAYLP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 74 qnrQQLHQRIGMvfqntdvqlfntSVTEEVAFG--PRQ--LGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRV 149
Cdd:PRK10575 92 ---QQLPAAEGM------------TVRELVAIGryPWHgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1729460384 150 ALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHN 199
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHD 207
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-214 |
9.61e-24 |
|
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: 9.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAyqfhdqpITTTYLADAQNRQQLHQRIGMVF-QNTdvQLF 95
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGE-------VRVLGYVPFKRRKEFARRIGVVFgQRS--QLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 -NTSVTEevAFgprQL-----GLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLN 169
Cdd:COG4586 109 wDLPAID--SF---RLlkaiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1729460384 170 GLTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:COG4586 184 GLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVID 229
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-217 |
1.15e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 94.56 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaQNRQQ--LHQRIGMVFQNTDVqL 94
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRL-----KNREVpfLRRQIGMIFQDHHL-L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 95 FNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIA 174
Cdd:PRK10908 92 MDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1729460384 175 AQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNSTH 217
Cdd:PRK10908 172 LSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
17-201 |
2.72e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 94.36 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLAS--PTSGAYQFHDQPITttyladaqnrqQL--HQR----IGMVFQ 88
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDIL-----------ELspDERaragIFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 89 N-------TDVQLFNTSVTEEvafgpRQLGLSAAMVAQRVADCLQLTDCAN-LADR-VPYQLSGGEKKRVALASVLALNP 159
Cdd:COG0396 85 YpveipgvSVSNFLRTALNAR-----RGEELSAREFLKLLKEKMKELGLDEdFLDRyVNEGFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHnYQ 201
Cdd:COG0396 160 KLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH-YQ 200
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-198 |
3.19e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 92.94 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 19 DLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPItttyladAQNRQQLHQrigmvfqntdvQLF--- 95
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-------RRQRDEYHQ-----------DLLylg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 -----NTSVT--EEVAFgprqlgLSAAMVAQRVADCLQLTDCANLADR--VP-YQLSGGEKKRVALASvLALNPEIL-LL 164
Cdd:PRK13538 81 hqpgiKTELTalENLRF------YQRLHGPGDDEALWEALAQVGLAGFedVPvRQLSAGQQRRVALAR-LWLTRAPLwIL 153
|
170 180 190
....*....|....*....|....*....|....
gi 1729460384 165 DEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
9-198 |
3.84e-23 |
|
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: 97.58 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 9 YDyPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADaqnrqqLHQRIGMVFQ 88
Cdd:COG5265 367 YD-PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS------LRAAIGIVPQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 89 ntDVQLFNTSVTEEVAFGprQLGLSAAMVAQrVADCLQLTDcanLADRVP--YQ---------LSGGEKKRVALASVLAL 157
Cdd:COG5265 440 --DTVLFNDTIAYNIAYG--RPDASEEEVEA-AARAAQIHD---FIESLPdgYDtrvgerglkLSGGEKQRVAIARTLLK 511
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1729460384 158 NPEILLLDEPLNGLTIAAQQQMLTLLQRLqAAGKTIIMASH 198
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREV-ARGRTTLVIAH 551
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
17-213 |
4.66e-23 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 93.49 E-value: 4.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyladaqnrQQLHQR--IGMVFQNTDVQL 94
Cdd:TIGR04406 17 VNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITH---------LPMHERarLGIGYLPQEASI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 95 FNT-SVTEEV-AFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLT 172
Cdd:TIGR04406 88 FRKlTVEENImAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1729460384 173 IAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGER-FIIF 213
Cdd:TIGR04406 168 PIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRaYIIS 209
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
19-235 |
6.18e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 93.68 E-value: 6.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 19 DLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladAQNRQQLHQ---RIGMVFQN----TD 91
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIP------AMSRSRLYTvrkRMSMLFQSgalfTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 92 VQLFntsvtEEVAFGPRQ-LGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNG 170
Cdd:PRK11831 99 MNVF-----DNVAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729460384 171 LTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFIIFnSTHQVDADLTRADLDQQPARQ 235
Cdd:PRK11831 174 QDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIV-ADKKIVAHGSAQALQANPDPR 238
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-219 |
8.21e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.30 E-value: 8.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 11 YPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLS--GLASP---TSGA--YQFHD--QPITTTYladaqnrqQLHQ 81
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSivYNGHNiySPRTDTV--------DLRK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQNTDVqlFNTSVTEEVAFGPRQLG--------------LSAAMVAQRVADclQLTDCAnladrvpYQLSGGEKK 147
Cdd:PRK14239 87 EIGMVFQQPNP--FPMSIYENVVYGLRLKGikdkqvldeaveksLKGASIWDEVKD--RLHDSA-------LGLSGGQQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 148 RVALASVLALNPEILLLDEPLNGLT-IAAQQQMLTLLQRLQAAgkTIIMASHNYQQVQAVGER--------FIIFNSTHQ 218
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDpISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRtgffldgdLIEYNDTKQ 233
|
.
gi 1729460384 219 V 219
Cdd:PRK14239 234 M 234
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-198 |
1.01e-22 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 96.19 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTC-GLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladAQNRQQLH 80
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT------AEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFqnTDVQLFntsvteEVAFGPRQLGLSAAMVAQRVADcLQLTDCANLAD-RVP-YQLSGGEKKRVALASVLALN 158
Cdd:PRK10522 397 KLFSAVF--TDFHLF------DQLLGPEGKPANPALVEKWLER-LKMAHKLELEDgRISnLKLSKGQKKRLALLLALAEE 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1729460384 159 PEILLLDEplngltIAAQQQ-------MLTLLQRLQAAGKTIIMASH 198
Cdd:PRK10522 468 RDILLLDE------WAADQDphfrrefYQVLLPLLQEMGKTIFAISH 508
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-198 |
1.06e-22 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 91.65 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 20 LSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADAQNRQQLHQRIGMvfqNTDVqlfntSV 99
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGL---KPEL-----SA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 100 TEEVAFGPRQLGlsaamVAQR-VADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQQQ 178
Cdd:TIGR01189 91 LENLHFWAAIHG-----GAQRtIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|
gi 1729460384 179 MLTLLQRLQAAGKTIIMASH 198
Cdd:TIGR01189 166 LAGLLRAHLARGGIVLLTTH 185
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-198 |
1.28e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.88 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASP---TSGAYQFHDQPItttyladaqNRQQLHQRIGMVFQntdVQ 93
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI---------DAKEMRAISAYVQQ---DD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 94 LFNTSVT--EEVAFG-----PRQLGLSAAMvaQRVADCLQ---LTDCANLADRVPYQ---LSGGEKKRVALASVLALNPE 160
Cdd:TIGR00955 109 LFIPTLTvrEHLMFQahlrmPRRVTKKEKR--ERVDEVLQalgLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPP 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-199 |
1.99e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.63 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladaqnRQQLH 80
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT---------HLPMH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QR----IGMVFQNTDVqlF-NTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVL 155
Cdd:COG1137 74 KRarlgIGYLPQEASI--FrKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1729460384 156 ALNPEILLLDEPLNG---LTIAAQQQMltlLQRLQAAGKTIIMASHN 199
Cdd:COG1137 152 ATNPKFILLDEPFAGvdpIAVADIQKI---IRHLKERGIGVLITDHN 195
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
17-214 |
2.12e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 93.79 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVN-----SGdfIC-LMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQpitttYLADAQNRQQL--HQR-IGMVF 87
Cdd:PRK11144 10 LGDLCLTVNltlpaQG--ITaIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR-----VLFDAEKGICLppEKRrIGYVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 88 QntDVQLF-NTSVTeevafGPRQLGLSAAMVAQrVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDE 166
Cdd:PRK11144 83 Q--DARLFpHYKVR-----GNLRYGMAKSMVAQ-FDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1729460384 167 PLNGLTIAAQQQMLTLLQRLQAAGKT-IIMASHNYQQVQAVGERFIIFN 214
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLE 203
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
11-216 |
2.15e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.15 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 11 YPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGL-----ASPTSGAYQFHDQPITTTYLADAQNRQqlhqRIGM 85
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipGFRVEGKVTFHGKNLYAPDVDPVEVRR----RIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 86 VFQNTDVqlFNTSVTEEVAFGPRQLGLSAAMvAQRVADCLQLtdcANLADRVP-------YQLSGGEKKRVALASVLALN 158
Cdd:PRK14243 96 VFQKPNP--FPKSIYDNIAYGARINGYKGDM-DELVERSLRQ---AALWDEVKdklkqsgLSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729460384 159 PEILLLDEPLNGL----TIAAQQQMLTLLQRLqaagkTIIMASHNYQQVQAVGERFIIFNST 216
Cdd:PRK14243 170 PEVILMDEPCSALdpisTLRIEELMHELKEQY-----TIIIVTHNMQQAARVSDMTAFFNVE 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-233 |
2.70e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.18 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYP----DTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyLADAQNR 76
Cdd:PRK10535 4 LLELKDIRRSYPsgeeQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAT--LDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 77 QQLHQRIGMVFQNTDVqLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTdcaNLADRVPY---QLSGGEKKRVALAS 153
Cdd:PRK10535 82 QLRREHFGFIFQRYHL-LSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRL---GLEDRVEYqpsQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 154 VLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNyQQVQAVGERFI-------IFNSTHQVDADLTRA 226
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIeirdgeiVRNPPAQEKVNVAGG 236
|
....*..
gi 1729460384 227 DLDQQPA 233
Cdd:PRK10535 237 TEPVVNT 243
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
17-203 |
2.81e-22 |
|
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: 90.28 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLAS--PTSGAYQFHDQPITTtylADAQNRQQLHqrIGMVFQNtdvql 94
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITD---LPPEERARLG--IFLAFQY----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 95 fntsvteevafgprqlglSAAMVAQRVADCLQltdcanladRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIA 174
Cdd:cd03217 86 ------------------PPEIPGVKNADFLR---------YVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180
....*....|....*....|....*....
gi 1729460384 175 AQQQMLTLLQRLQAAGKTIIMASHnYQQV 203
Cdd:cd03217 139 ALRLVAEVINKLREEGKSVLIITH-YQRL 166
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-198 |
2.92e-22 |
|
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: 94.86 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCG-----LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladAQNR 76
Cdd:COG4615 328 LELRGVTYRYPGEDGdegftLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT------ADNR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 77 QQLHQRIGMVFqnTDVQLFNtsvteevafgpRQLGLSAAMVAQRVADCLQLTDcanLADRVPYQ--------LSGGEKKR 148
Cdd:COG4615 402 EAYRQLFSAVF--SDFHLFD-----------RLLGLDGEADPARARELLERLE---LDHKVSVEdgrfsttdLSQGQRKR 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1729460384 149 VALASVLALNPEILLLDEplngltIAAQQQML-------TLLQRLQAAGKTIIMASH 198
Cdd:COG4615 466 LALLVALLEDRPILVFDE------WAADQDPEfrrvfytELLPELKARGKTVIAISH 516
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-199 |
4.16e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 92.72 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtylADAQNRQQLHQRIGMVFQNTDVQLfn 96
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK---ADPEAQKLLRQKIQIVFQNPYGSL-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 tsvteevafGPRQ-----LG--------LSAAmvaQRVADCLQLTDCANL----ADRVPYQLSGGEKKRVALASVLALNP 159
Cdd:PRK11308 106 ---------NPRKkvgqiLEepllintsLSAA---ERREKALAMMAKVGLrpehYDRYPHMFSGGQRQRIAIARALMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHN 199
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHD 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-212 |
6.35e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.62 E-value: 6.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKST----LLRLLsglasPTSGAYQFHDQPITTTyladaqNRQQL---HQRIGMVFQN 89
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNL------NRRQLlpvRHRIQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 90 TDVQLF-NTSVTEEVAFGPR--QLGLSAAMVAQRVADCLQLTDC-ANLADRVPYQLSGGEKKRVALASVLALNPEILLLD 165
Cdd:PRK15134 371 PNSSLNpRLNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1729460384 166 EPLNGLTIAAQQQMLTLLQRLQAAGK-TIIMASHNYQQVQAVGERFII 212
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIV 498
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-197 |
6.65e-22 |
|
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: 89.03 E-value: 6.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADAQnrqqlhqRIGMVFqntdvqlfn 96
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAI-------RAGIAY--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 tsVTEEvafgPRQLGLsaaMVAQRVADclqltdcaNLAdrVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQ 176
Cdd:cd03215 80 --VPED----RKREGL---VLDLSVAE--------NIA--LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180
....*....|....*....|.
gi 1729460384 177 QQMLTLLQRLQAAGKTIIMAS 197
Cdd:cd03215 141 AEIYRLIRELADAGKAVLLIS 161
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-203 |
8.01e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 91.10 E-value: 8.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPItttyladaqnRQQLHQR-IGMVFQNTDVQLF 95
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT----------RQALQKNlVAYVPQSEEVDWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 NTSVTEEVAFGPRQ-----LGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNG 170
Cdd:PRK15056 93 FPVLVEDVVMMGRYghmgwLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190
....*....|....*....|....*....|...
gi 1729460384 171 LTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQV 203
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGKTMLVSTHNLGSV 205
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-204 |
1.79e-21 |
|
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: 89.07 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDY---PDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladAQNRQQ 78
Cdd:cd03248 12 VKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS------QYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 79 LHQRIGMVFQntDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADC------LQL---TDcanlADRVPYQLSGGEKKRV 149
Cdd:cd03248 86 LHSKVSLVGQ--EPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAhsfiseLASgydTE----VGEKGSQLSGGQKQRV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1729460384 150 ALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRlQAAGKTIIMASHNYQQVQ 204
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVE 213
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-201 |
1.90e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.10 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 6 NICYDYPD----TCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyLADAQNRQQLHQ 81
Cdd:PRK11629 10 NLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSK--LSSAAKAELRNQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQNTDVqLFNTSVTEEVAFgPRQLGLSAAMVAQRVA-DCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:PRK11629 88 KLGFIYQFHHL-LPDFTALENVAM-PLLIGKKKPAEINSRAlEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHNYQ 201
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-215 |
2.83e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 89.33 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTS-----GAYQFHDQPITTTYLadaqNR 76
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRV----NL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 77 QQLHQRIGMVFQNTDvqLFNTSVTEEVAFGPRQLGLSAAM-----VAQRVADCLQLTDCANLADRVPYQLSGGEKKRVAL 151
Cdd:PRK14258 84 NRLRRQVSMVHPKPN--LFPMSVYDNVAYGVKIVGWRPKLeiddiVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1729460384 152 ASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGK-TIIMASHNYQQVQAVGERFIIFNS 215
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
17-217 |
3.74e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.41 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaqnrqQLHQR----IGMVFQNTDV 92
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL---------PLHARarrgIGYLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 93 qLFNTSVTEEV-AFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGL 171
Cdd:PRK10895 90 -FRRLSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1729460384 172 TIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNSTH 217
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGH 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-213 |
8.15e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.23 E-value: 8.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 5 VNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADAQNRQQLHQRIG 84
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 85 MVFQNTDVqlFNTSVTEEVAFGPRQLGLSAAMVAQRVADClQLTDCA---NLADRV---PYQLSGGEKKRVALASVLALN 158
Cdd:PRK14271 105 MLFQRPNP--FPMSIMDNVLAGVRAHKLVPRKEFRGVAQA-RLTEVGlwdAVKDRLsdsPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1729460384 159 PEILLLDEPLNGLTIAAQQQMLTLLQRLqAAGKTIIMASHNYQQVQAVGERFIIF 213
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALF 235
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-211 |
9.35e-21 |
|
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: 86.39 E-value: 9.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 20 LSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPitttylaDAQNRQQLHQRIGMVFQNTDVQLFnTSV 99
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP-------LDFQRDSIARGLLYLGHAPGIKTT-LSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 100 TEEVAFGPRQLGLSAamvaqrVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQQQM 179
Cdd:cd03231 91 LENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180 190
....*....|....*....|....*....|..
gi 1729460384 180 LTLLQRLQAAGKTIIMASHNYQQVQAVGERFI 211
Cdd:cd03231 165 AEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-202 |
1.82e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 87.35 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 18 KDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGaYQFHDQPITTTYLAdaqnrQQLHQRIGMVFQNTDVQlFNT 97
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHG-HVWLDGEHIQHYAS-----KEVARRIGLLAQNATTP-GDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 98 SVTEEVAFG--PRQLGLSA--AMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTI 173
Cdd:PRK10253 97 TVQELVARGryPHQPLFTRwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190
....*....|....*....|....*....|
gi 1729460384 174 AAQQQMLTLLQRL-QAAGKTIIMASHNYQQ 202
Cdd:PRK10253 177 SHQIDLLELLSELnREKGYTLAAVLHDLNQ 206
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-195 |
2.18e-20 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 89.30 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLadaqnrQQLH 80
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSF------EQLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQ--NTDVqlfnTSVTEEvafgprQLGLSAAMVAQ----RVADCLQLTD---CANLADRVPYQLSGGEKKRVAL 151
Cdd:PRK10938 77 KLVSDEWQrnNTDM----LSPGED------DTGRTTAEIIQdevkDPARCEQLAQqfgITALLDRRFKYLSTGETRKTLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1729460384 152 ASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIM 195
Cdd:PRK10938 147 CQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVL 190
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-211 |
2.91e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 86.29 E-value: 2.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYD-YPDT----CGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladaqn 75
Cdd:COG1101 1 MLELKNLSKTfNPGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 76 RQQLHQR---IGMVFQNTdvqLFNT----SVTEEVA--------FGPRqLGLSAAMVAQ---RVADcLQLtdcaNLADRV 137
Cdd:COG1101 72 KLPEYKRakyIGRVFQDP---MMGTapsmTIEENLAlayrrgkrRGLR-RGLTKKRRELfreLLAT-LGL----GLENRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 138 PYQ---LSGGEkkRVALASVLAL--NPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGK-TIIMASHNYQQVQAVGERFI 211
Cdd:COG1101 143 DTKvglLSGGQ--RQALSLLMATltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRLI 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-166 |
6.05e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.77 E-value: 6.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyLADAQNRQQlh 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST--LKPEIYRQQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 qrIGMVFQNTdvQLFNTSVTEEVAFgPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:PRK10247 83 --VSYCAQTP--TLFGDTVYDNLIF-PWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
....*.
gi 1729460384 161 ILLLDE 166
Cdd:PRK10247 158 VLLLDE 163
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-212 |
6.51e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.92 E-value: 6.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQF--HDQPITTTYLAdAQNrqq 78
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITInnINYNKLDHKLA-AQL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 79 lhqRIGMVFQNTDVqLFNTSVTEEVAFGP--------------RQLGLSAAMVAQRVADCLQLtdcanlaDRVPYQLSGG 144
Cdd:PRK09700 81 ---GIGIIYQELSV-IDELTVLENLYIGRhltkkvcgvniidwREMRVRAAMMLLRVGLKVDL-------DEKVANLSIS 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1729460384 145 EKKRVALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFII 212
Cdd:PRK09700 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTV 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-231 |
6.74e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 87.66 E-value: 6.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 6 NICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADAqnrqqLHQRIGM 85
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAA-----LAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 86 VFQntDVQLF-NTSVTEEVAFG--PRQLGL--SAAMVAqRVADCLQltdcaNLADRV-PYQ----LSGGEKKRVALASVL 155
Cdd:PRK11288 84 IYQ--ELHLVpEMTVAENLYLGqlPHKGGIvnRRLLNY-EAREQLE-----HLGVDIdPDTplkyLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 156 ALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFN-----STHQVDADLTRADLDQ 230
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKdgryvATFDDMAQVDRDQLVQ 235
|
.
gi 1729460384 231 Q 231
Cdd:PRK11288 236 A 236
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-208 |
6.88e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 85.35 E-value: 6.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLAsptsgayQFHDQP-ITTTYLADAQN-----RQQLHQRIGMVFQNT 90
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLI-------ELYPEArVSGEVYLDGQDifkmdVIELRRRVQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 91 DvQLFNTSVTEEVAFGPR--QLGLSAAMVAQRVADCL---QLTD-CANLADRVPYQLSGGEKKRVALASVLALNPEILLL 164
Cdd:PRK14247 92 N-PIPNLSIFENVALGLKlnRLVKSKKELQERVRWALekaQLWDeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1729460384 165 DEPLNGLTIAAQQQMLTLLQRLQAAgKTIIMASHNYQQVQAVGE 208
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISD 213
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-198 |
7.16e-20 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 88.01 E-value: 7.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 27 GDFICLMGPNGSGKSTLLRLLSGlasptsgayQFHDQPITTTYLA-DAQNRQQLHQRIGMVFQNtDVQLFNTSVTEEVAF 105
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAG---------RIQGNNFTGTILAnNRKPTKQILKRTGFVTQD-DILYPHLTVRETLVF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 106 G-----PRQLGLSAAM-VAQRVADCLQLTDCAN--LADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQQ 177
Cdd:PLN03211 164 CsllrlPKSLTKQEKIlVAESVISELGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180
....*....|....*....|.
gi 1729460384 178 QMLTLLQRLQAAGKTIIMASH 198
Cdd:PLN03211 244 RLVLTLGSLAQKGKTIVTSMH 264
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-238 |
1.93e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.77 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttylaDAQNRQQLH 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT-----DWQTAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTDVqLFNTSVTEEVAFGprqlGLSA--AMVAQRVADCLQLTdcANLADRVPYQ---LSGGEKKRVALASVL 155
Cdd:PRK11614 80 EAVAIVPEGRRV-FSRMTVEENLAMG----GFFAerDQFQERIKWVYELF--PRLHERRIQRagtMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 156 ALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNSTHQVDADLTRADLDQQPARQ 235
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRS 232
|
...
gi 1729460384 236 AQL 238
Cdd:PRK11614 233 AYL 235
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-199 |
2.09e-19 |
|
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: 86.65 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADaqnrqqLHQRIGMVFQntDVQLFN 96
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE------VRRRVSVCAQ--DAHLFD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVAFG-PRQLGLSAAMVAQRVadclQLtdcANLADRVPY-----------QLSGGEKKRVALASVLALNPEILLL 164
Cdd:TIGR02868 423 TTVRENLRLArPDATDEELWAALERV----GL---ADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*.
gi 1729460384 165 DEPLNGLTIAAQQQMLTLLqrLQA-AGKTIIMASHN 199
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDL--LAAlSGRTVVLITHH 529
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-187 |
2.27e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.07 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyLADAQNRQqlhQRIGMVFQNTDVQLFN 96
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH---FGDYSYRS---QRIRMIFQDPSTSLNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVAFGPRQL--GLSAAMVAQRVADCLQ----LTDCANLadrVPYQLSGGEKKRVALASVLALNPEILLLDEPLNG 170
Cdd:PRK15112 103 RQRISQILDFPLRLntDLEPEQREKQIIETLRqvglLPDHASY---YPHMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170
....*....|....*..
gi 1729460384 171 LTIAAQQQMLTLLQRLQ 187
Cdd:PRK15112 180 LDMSMRSQLINLMLELQ 196
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-208 |
3.52e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.56 E-value: 3.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 13 DTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLAS------PTSGAYQFHDQPItttYLADAQnrqQLHQRIGMV 86
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDI---FQIDAI---KLRKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 87 FQNTDvQLFNTSVTEEVAFGPRQLGLSAAM-VAQRVADCLQLTDC-ANLADRV---PYQLSGGEKKRVALASVLALNPEI 161
Cdd:PRK14246 96 FQQPN-PFPHLSIYDNIAYPLKSHGIKEKReIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1729460384 162 LLLDEPLNGLTIAAQQQMLTLLQRLQAAgKTIIMASHNYQQVQAVGE 208
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVAD 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-226 |
4.90e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.53 E-value: 4.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 19 DLSLTVNSGDFICLMGPNGSGKS-TLLRLLSGLASP----TSGAYQFHDQPITTtylADAQNRQQLH-QRIGMVFQNTDV 92
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLH---ASEQTLRGVRgNKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 93 QLFNTSVTE----EVAFGPRQLGLSAAMVaqRVADCLQLTDCANLADRV---PYQLSGGEKKRVALASVLALNPEILLLD 165
Cdd:PRK15134 104 SLNPLHTLEkqlyEVLSLHRGMRREAARG--EILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIAD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729460384 166 EPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHNYQQVQAVGERFIIFNSTHQVDADLTRA 226
Cdd:PRK15134 182 EPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAAT 243
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-196 |
6.22e-19 |
|
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: 85.15 E-value: 6.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 6 NICYDYPDT--CGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADaqnrqqLHQRI 83
Cdd:TIGR02203 335 NVTFRYPGRdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS------LRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 84 GMVFQntDVQLFNTSVTEEVAFGPRqlglsAAMVAQRVADCLQLTDCANLADRVP-----------YQLSGGEKKRVALA 152
Cdd:TIGR02203 409 ALVSQ--DVVLFNDTIANNIAYGRT-----EQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1729460384 153 SVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMA 196
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIA 525
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-201 |
1.75e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.98 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTylaDAQNRQQLH-QRIGMVFQNtdVQLF 95
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQM---DEEARAKLRaKHVGFVFQS--FMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 NTSVTEEVAFGPRQL-GLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIA 174
Cdd:PRK10584 101 PTLNALENVELPALLrGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180
....*....|....*....|....*...
gi 1729460384 175 AQQQMLTLLQRL-QAAGKTIIMASHNYQ 201
Cdd:PRK10584 181 TGDKIADLLFSLnREHGTTLILVTHDLQ 208
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-211 |
2.82e-18 |
|
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: 83.31 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLAS--PTSGAYQFH----------DQP----- 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyvERPskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 65 -------ITTTYLADAQN-----RQQLHQRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCAN 132
Cdd:TIGR03269 81 pcpvcggTLEPEEVDFWNlsdklRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 133 LADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNglTIAAQQQML---TLLQRLQAAGKTIIMASHNYQQVQAVGER 209
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTG--TLDPQTAKLvhnALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
..
gi 1729460384 210 FI 211
Cdd:TIGR03269 239 AI 240
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
17-203 |
7.51e-18 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 79.61 E-value: 7.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLAS--PTSGAYQFHDQPITttylaDAQNRQQLHQRIGMVFQN----- 89
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyeVTSGTILFKGQDLL-----ELEPDERARAGLFLAFQYpeeip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 90 -TDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDC-ANLADR-VPYQLSGGEKKRVALASVLALNPEILLLDE 166
Cdd:TIGR01978 91 gVSNLEFLRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMdEEFLNRsVNEGFSGGEKKRNEILQMALLEPKLAILDE 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1729460384 167 PLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHnYQQV 203
Cdd:TIGR01978 171 IDSGLDIDALKIVAEGINRLREPDRSFLIITH-YQRL 206
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-166 |
1.32e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.16 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 6 NICYDYPDTC-GLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaqNRQQLHQRIG 84
Cdd:PRK13657 339 DVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV------TRASLRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 85 MVFQntDVQLFNTSVTEEVAFG-----PRQLgLSAAMVAQ------RVADCLQltdcANLADRvPYQLSGGEKKRVALAS 153
Cdd:PRK13657 413 VVFQ--DAGLFNRSIEDNIRVGrpdatDEEM-RAAAERAQahdfieRKPDGYD----TVVGER-GRQLSGGERQRLAIAR 484
|
170
....*....|...
gi 1729460384 154 VLALNPEILLLDE 166
Cdd:PRK13657 485 ALLKDPPILILDE 497
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-209 |
2.37e-17 |
|
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: 80.62 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 20 LSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFH--DQPITTTYLAdAQNRQQLHQRIGMVFQNTDVQLFNT 97
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgDEWVDMTKPG-PDGRGRAKRYIGILHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 98 ---SVTEEVAFG-PRQLGLSAAMVAQRVADcLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLT- 172
Cdd:TIGR03269 382 vldNLTEAIGLElPDELARMKAVITLKMVG-FDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDp 460
|
170 180 190
....*....|....*....|....*....|....*..
gi 1729460384 173 IAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGER 209
Cdd:TIGR03269 461 ITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDR 497
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-205 |
2.39e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.23 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQfHDQPITTTYLAdaqnrQQLH 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-RNGKLRIGYVP-----QKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 qrigmvfqntdvqlFNTSVTEEVAfgpRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:PRK09544 78 --------------LDTTLPLTVN---RFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHNYQQVQA 205
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLVMA 186
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-196 |
2.44e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.55 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPItttylADAQNRQQLHQ 81
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM-----ADARHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQNTDVQLFNT-SVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:NF033858 77 RIAYMPQGLGKNLYPTlSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLQA--AGKTIIMA 196
Cdd:NF033858 157 LLILDEPTTGVDPLSRRQFWELIDRIRAerPGMSVLVA 194
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-204 |
4.18e-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: 77.53 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLAdaqnrqQLHQRIGMVFQntDVQLFN 96
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPA------WLRRQVGVVLQ--ENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVAFGprqlglSAAMVAQRVADCLQLTDCANLADRVP--YQ---------LSGGEKKRVALASVLALNPEILLLD 165
Cdd:cd03252 90 RSIRDNIALA------DPGMSMERVIEAAKLAGAHDFISELPegYDtivgeqgagLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1729460384 166 EPLNGLTIAAQQQMLTLLQRLqAAGKTIIMASHNYQQVQ 204
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLSTVK 201
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
5-198 |
5.54e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 79.37 E-value: 5.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 5 VNI---CYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADaqnrqqLHQ 81
Cdd:PRK10789 316 VNIrqfTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS------WRS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQNTdvQLFNTSVTEEVAfgprqLGLSAAMVAQ--RVAdclQLtdcANLAD---RVP--YQ---------LSGGE 145
Cdd:PRK10789 390 RLAVVSQTP--FLFSDTVANNIA-----LGRPDATQQEieHVA---RL---ASVHDdilRLPqgYDtevgergvmLSGGQ 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1729460384 146 KKRVALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLqRLQAAGKTIIMASH 198
Cdd:PRK10789 457 KQRISIARALLLNAEILILDDALSAVDGRTEHQILHNL-RQWGEGRTVIISAH 508
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-231 |
6.37e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.29 E-value: 6.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 16 GLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADAqnrqqLHQRIGMV--------- 86
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDA-----IRAGIAYVpedrkgegl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 87 FQNTDVQlFNTSVTEEVAFGPRQLgLSAAMVAQRVADCLQLTD--CANLADRVpYQLSGGEKKRVALASVLALNPEILLL 164
Cdd:COG1129 342 VLDLSIR-ENITLASLDRLSRGGL-LDRRRERALAEEYIKRLRikTPSPEQPV-GNLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729460384 165 DEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNSTHQVdADLTRADLDQQ 231
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV-GELDREEATEE 484
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-198 |
8.19e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 76.14 E-value: 8.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladaQNRQQLH 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-------KDLCTYQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTDVQLfNTSVTEEVAFgprqlGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPE 160
Cdd:PRK13540 74 KQLCFVGHRSGINP-YLTLRENCLY-----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAK 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-230 |
9.44e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 78.71 E-value: 9.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGL--ASPTSGAYQFHDQPITTTYLADAqnrqq 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDT----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 79 lhQRIGMVFQNTDVQLF-NTSVTEEVAFG-----PRQLGLSAAMV--AQRVADCLQLTDCANlaDRVPYQLSGGEKKRVA 150
Cdd:TIGR02633 76 --ERAGIVIIHQELTLVpELSVAENIFLGneitlPGGRMAYNAMYlrAKNLLRELQLDADNV--TRPVGDYGGGQQQLVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 151 LASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERF-IIFNSTHQVDADLTRADLD 229
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTIcVIRDGQHVATKDMSTMSED 231
|
.
gi 1729460384 230 Q 230
Cdd:TIGR02633 232 D 232
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-220 |
1.25e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.44 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 18 KDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyLADAQNRQqLHQRIGMVFQNTDVQLfNT 97
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG--MKDDEWRA-VRSDIQMIFQDPLASL-NP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 98 SVT--EEVA-----FGPRqlgLSAAMVAQRV-ADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLN 169
Cdd:PRK15079 114 RMTigEIIAeplrtYHPK---LSRQEVKDRVkAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1729460384 170 GLTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFIIFNSTHQVD 220
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 242
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
6-210 |
2.44e-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: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 6 NICYDYPDTCG----LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGlaSPTSGAyqfhdqpITTTYLADAQNRQQLHQ 81
Cdd:cd03232 8 NLNYTVPVKGGkrqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGV-------ITGEILINGRPLDKNFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 R-IGMVFQNtDVQLFNTSVTEEVAFgprqlglSAAMVAqrvadclqltdcanladrvpyqLSGGEKKRVALASVLALNPE 160
Cdd:cd03232 79 RsTGYVEQQ-DVHSPNLTVREALRF-------SALLRG----------------------LSVEQRKRLTIGVELAAKPS 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHnyQQVQAVGERF 210
Cdd:cd03232 129 ILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIH--QPSASIFEKF 176
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-208 |
4.02e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 75.26 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPI--TTTYLADAqNRQQL 79
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLfgRNIYSPDV-DPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQNTDvQLFNTSVTEEVAFGPRQLGL--SAAMVAQRVADCLQLtdcANLADRV-------PYQLSGGEKKRVA 150
Cdd:PRK14267 84 RREVGMVFQYPN-PFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKK---AALWDEVkdrlndyPSNLSGGQRQRLV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1729460384 151 LASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAgKTIIMASHNYQQVQAVGE 208
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSD 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-212 |
1.31e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 75.82 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 20 LSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyladaqNRQQLHQRIGMVFQNtDVQLFNTSV 99
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-------NLDAVRQSLGMCPQH-NILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 100 TEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQQQM 179
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190
....*....|....*....|....*....|...
gi 1729460384 180 LTLLQRLQaAGKTIIMASHNYQQVQAVGERFII 212
Cdd:TIGR01257 1101 WDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAI 1132
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-200 |
2.32e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLAS--PTSGAYQFHDQPITTtyladaqnrqqlhqrigmvfqntdvql 94
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGR--------------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 95 fNTSVTEevAFGPRQlglSAAMVAQRVADClQLTDcANLADRVPYQLSGGEKKRVALASVLALNPEILLLDE---PLNGL 171
Cdd:COG2401 99 -EASLID--AIGRKG---DFKDAVELLNAV-GLSD-AVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEfcsHLDRQ 170
|
170 180
....*....|....*....|....*....
gi 1729460384 172 TiaAQQQMLTLLQRLQAAGKTIIMASHNY 200
Cdd:COG2401 171 T--AKRVARNLQKLARRAGITLVVATHHY 197
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
9-213 |
2.54e-15 |
|
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: 72.83 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 9 YDYPD-TCGLKDLSLTVNSGDF-----ICLMGPNGSGKSTLLRLLSGLASPTSGayqfhDQPI---TTTYLAdaqnrqql 79
Cdd:cd03237 1 YTYPTmKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEG-----DIEIeldTVSYKP-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 hQRIGMVFQNTdVQLFNTSVTEEVafgprqlgLSAAMVAQRVADCLQLTDcanLADRVPYQLSGGEKKRVALASVLALNP 159
Cdd:cd03237 68 -QYIKADYEGT-VRDLLSSITKDF--------YTHPYFKTEIAKPLQIEQ---ILDREVPELSGGELQRVAIAACLSKDA 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1729460384 160 EILLLDEPlngltiaaqQQMLTLLQRLQAA----------GKTIIMASHNYQQVQAVGERFIIF 213
Cdd:cd03237 135 DIYLLDEP---------SAYLDVEQRLMASkvirrfaennEKTAFVVEHDIIMIDYLADRLIVF 189
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-171 |
2.61e-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: 74.59 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFhdQP-ITTTYL--------------------ADAQN 75
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--QPgIKVGYLpqepqldptktvrenveegvAEIKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 76 RQQLHQRIGMVFQNTDVQlFNTSVTEevafgprQLGLSAAMVAQRVADCLQLTDCANLADRVP------YQLSGGEKKRV 149
Cdd:TIGR03719 99 ALDRFNEISAKYAEPDAD-FDKLAAE-------QAELQEIIDAADAWDLDSQLEIAMDALRCPpwdadvTKLSGGERRRV 170
|
170 180
....*....|....*....|..
gi 1729460384 150 ALASVLALNPEILLLDEPLNGL 171
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHL 192
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-212 |
2.99e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.51 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 10 DYPDTCGLKDLSLTVNSGDFICLMGPNGSGKS----TLLRLLSGLASPTSGAYQF----HDQPITTTYLADAQNRQQLHQ 81
Cdd:PRK10261 25 EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLlrrrSRQVIELSEQSAAQMRHVRGA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQNTDVQLFNT-SVTEEVAFGPR---QLGLSAAMV-AQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLA 156
Cdd:PRK10261 105 DMAMIFQEPMTSLNPVfTVGEQIAESIRlhqGASREEAMVeAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1729460384 157 LNPEILLLDEPLNGLTIAAQQQMLTLLQRLQA-AGKTIIMASHNYQQVQAVGERFII 212
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKeMSMGVIFITHDMGVVAEIADRVLV 241
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-206 |
3.24e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLaSPtSGAYQ----FHDQPITTTYLADAQNR 76
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YP-HGTYEgeiiFEGEELQASNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 77 --QQLHQRIGMVFQntdvqlfnTSVTEEVAFG--PRQLGLS--AAMV--AQRVADCLQLTdcANLADRVpYQLSGGEKKR 148
Cdd:PRK13549 83 giAIIHQELALVKE--------LSVLENIFLGneITPGGIMdyDAMYlrAQKLLAQLKLD--INPATPV-GNLGLGQQQL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1729460384 149 VALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAV 206
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAI 209
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-198 |
4.25e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.07 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHD---------QPitttYLADAQNRQQLhqrigmVF 87
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAgarvlflpqRP----YLPLGTLREAL------LY 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 88 QNTDvqlfnTSVTEEVafgprqlgLSAAMvaqrvaDCLQLTDCANLADRV---PYQLSGGEKKRVALASVLALNPEILLL 164
Cdd:COG4178 449 PATA-----EAFSDAE--------LREAL------EAVGLGHLAERLDEEadwDQVLSLGEQQRLAFARLLLHKPDWLFL 509
|
170 180 190
....*....|....*....|....*....|....
gi 1729460384 165 DEPLNGLTIAAQQQMLTLLQRlQAAGKTIIMASH 198
Cdd:COG4178 510 DEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
17-201 |
4.75e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.98 E-value: 4.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLAS--PTSGAYQFHDQPITttylaDAQNRQQLHQRIGMVFQNTdVQL 94
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESIL-----DLEPEERAHLGIFLAFQYP-IEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 95 fnTSVTEE----VAFGPRQ--LGLSAamvaqrvADCLQ----LTDCANLADRVPYQL--------SGGEKKRVALASVLA 156
Cdd:CHL00131 97 --PGVSNAdflrLAYNSKRkfQGLPE-------LDPLEfleiINEKLKLVGMDPSFLsrnvnegfSGGEKKRNEILQMAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1729460384 157 LNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHnYQ 201
Cdd:CHL00131 168 LDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH-YQ 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-198 |
4.91e-15 |
|
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: 70.26 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQpitttyladaqnrqqlhqrigmvfqntdvqlfn 96
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG--------------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 tsvtEEVAFGPRQLGLSAAmvaqrvadclqltdcaNLADRVPY----QLSGGEKKRVALASVLALNPEILLLDEPLNGLT 172
Cdd:cd03223 64 ----EDLLFLPQRPYLPLG----------------TLREQLIYpwddVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180
....*....|....*....|....*.
gi 1729460384 173 IAAQQQMltlLQRLQAAGKTIIMASH 198
Cdd:cd03223 124 EESEDRL---YQLLKELGITVISVGH 146
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-209 |
8.52e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.16 E-value: 8.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADAqnrQQLH 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKA---HQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 qrIGMVFQntDVQLF-NTSVTEEVAFG-PRQLGLSaamvaQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALN 158
Cdd:PRK15439 88 --IYLVPQ--EPLLFpNLSVKENILFGlPKRQASM-----QKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1729460384 159 PEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGER 209
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADR 209
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-201 |
1.33e-14 |
|
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: 69.81 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDqpitttyladaqnrqqlhqRIGMVFQNTdvQLFN 96
Cdd:cd03250 21 LKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------------SIAYVSQEP--WIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVAFGPRqlgLSAAMVAQRVADCLQLTDCANLADRVPYQ-------LSGGEKKRVALASVLALNPEILLLDEPLN 169
Cdd:cd03250 80 GTIRENILFGKP---FDEERYEKVIKACALEPDLEILPDGDLTEigekginLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190
....*....|....*....|....*....|...
gi 1729460384 170 GLTIA-AQQQMLTLLQRLQAAGKTIIMASHNYQ 201
Cdd:cd03250 157 AVDAHvGRHIFENCILGLLLNNKTRILVTHQLQ 189
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-213 |
1.52e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 18 KDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADAqnrqqLHQRIGMVFQNTDVQLF-- 95
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDA-----VKKGMAYITESRRDNGFfp 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 NTSVTEEVAFGP--RQLGLSAAM----------VAQRVADCLQLTdCANLADRVPyQLSGGEKKRVALASVLALNPEILL 163
Cdd:PRK09700 355 NFSIAQNMAISRslKDGGYKGAMglfhevdeqrTAENQRELLALK-CHSVNQNIT-ELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1729460384 164 LDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIF 213
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVF 482
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
17-198 |
1.63e-14 |
|
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: 72.46 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPItttylaDAQNRQQLHQRIGMVFQntDVQLFN 96
Cdd:TIGR01193 490 LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL------KDIDRHTLRQFINYLPQ--EPYIFS 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVAFGPRQlGLSAAMVAQRVADCLQLTDCANLAdrVPYQ---------LSGGEKKRVALASVLALNPEILLLDEP 167
Cdd:TIGR01193 562 GSILENLLLGAKE-NVSQDEIWAACEIAEIKDDIENMP--LGYQtelseegssISGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190
....*....|....*....|....*....|.
gi 1729460384 168 LNGLTIAAQQQMLTLLQRLQAagKTIIMASH 198
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNLQD--KTIIFVAH 667
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-212 |
1.81e-14 |
|
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: 72.35 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTC--GLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyladaqNRQQ 78
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-------NISD 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 79 LHQRIGMVFQNTDVQLFNTSvTEEVAFGPRQLGLSAAMVaQRVAD-CLQLTDCANLADRVPYQLSGGEKKRVALASVLAL 157
Cdd:TIGR01257 2010 VHQNMGYCPQFDAIDDLLTG-REHLYLYARLRGVPAEEI-EKVANwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1729460384 158 NPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFII 212
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAI 2142
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-214 |
2.20e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.40 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 21 SLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttyladaqnRQQLHQ--RIGMV--FQNtdVQLFN 96
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE---------GLPGHQiaRMGVVrtFQH--VRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEE---VAfGPRQL--GLSAAMVA------------QRVADCLQ---LTDCANladRVPYQLSGGEKKRVALASVLA 156
Cdd:PRK11300 94 EMTVIEnllVA-QHQQLktGLFSGLLKtpafrraesealDRAATWLErvgLLEHAN---RQAGNLAYGQQRRLEIARCMV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1729460384 157 LNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVN 228
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-203 |
2.79e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.52 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 3 KLV----NICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGayQFHdqpiTTTYLADA---QN 75
Cdd:PRK11147 317 KIVfemeNVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSG--RIH----CGTKLEVAyfdQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 76 RQQLhqrigmvfqntDVQlfnTSVTEEVAFGPRQLglsaaMVAQRVADCLqltdcANLAD--------RVPYQ-LSGGEK 146
Cdd:PRK11147 391 RAEL-----------DPE---KTVMDNLAEGKQEV-----MVNGRPRHVL-----GYLQDflfhpkraMTPVKaLSGGER 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1729460384 147 KRVALASVLaLNPEILL-LDEPLNGLTIaaqqQMLTLLQRLQAAGK-TIIMASHNYQQV 203
Cdd:PRK11147 447 NRLLLARLF-LKPSNLLiLDEPTNDLDV----ETLELLEELLDSYQgTVLLVSHDRQFV 500
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-173 |
3.65e-14 |
|
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: 71.12 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDqpiTTtyladaqnrqqlhq 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE---TV-------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRvADCLQL----TDCANLADrvpyQLSGGEKKRVALASVLAL 157
Cdd:TIGR03719 386 KLAYVDQSRDALDPNKTVWEEISGGLDIIKLGKREIPSR-AYVGRFnfkgSDQQKKVG----QLSGGERNRVHLAKTLKS 460
|
170
....*....|....*.
gi 1729460384 158 NPEILLLDEPLNGLTI 173
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDV 476
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-204 |
7.17e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 69.07 E-value: 7.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLAdaqnrqqlhqriGMVFQNTDVqlfn 96
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISA------------GLSGQLTGI---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 tsvtEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQ 176
Cdd:PRK13546 104 ----ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA 179
|
170 180
....*....|....*....|....*...
gi 1729460384 177 QQMLTLLQRLQAAGKTIIMASHNYQQVQ 204
Cdd:PRK13546 180 QKCLDKIYEFKEQNKTIFFVSHNLGQVR 207
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
17-217 |
9.18e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.89 E-value: 9.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSgAYQFHDQPITTTYLAD---AQNRQQLHQRIGMVFQNTDVq 93
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK-SAGSHIELLGRTVQREgrlARDIRKSRANTGYIFQQFNL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 94 LFNTSVTEEVAFGPrqLGLS----------AAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILL 163
Cdd:PRK09984 98 VNRLSVLENVLIGA--LGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1729460384 164 LDEPLNGLTI-AAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNSTH 217
Cdd:PRK09984 176 ADEPIASLDPeSARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-186 |
1.74e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.93 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSG-LASP--TSGAYQFHDQPITTTYLAdAQNRQQLhQRIGMVFQNTDVQ 93
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgaPRGARVTGDVTLNGEPLA-AIDAPRL-ARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 94 LFNTSVTEEVAFGPRQLGLSAAMVAQR---VADC-LQLTDCANLADRVPYQLSGGEKKRVALASVLA---------LNPE 160
Cdd:PRK13547 95 AFAFSAREIVLLGRYPHARRAGALTHRdgeIAWQaLALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPR 174
|
170 180
....*....|....*....|....*.
gi 1729460384 161 ILLLDEPLNGLTIAAQQQMLTLLQRL 186
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRL 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
16-238 |
3.03e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 16 GLK-DLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADAQnrqqlhqRIGMVFQNTD--- 91
Cdd:PRK11288 267 GLRePISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAI-------RAGIMLCPEDrka 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 92 ---VQLfnTSVTEEVAFGPRQLGLSAAMVAQRVADclqltdcANLADRV----------PYQ----LSGGEKKRVALASV 154
Cdd:PRK11288 340 egiIPV--HSVADNINISARRHHLRAGCLINNRWE-------AENADRFirslniktpsREQlimnLSGGNQQKAILGRW 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 155 LALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERfIIFNSTHQVDADLTRADLDQQPAR 234
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADR-IVVMREGRIAGELAREQATERQAL 489
|
....
gi 1729460384 235 QAQL 238
Cdd:PRK11288 490 SLAL 493
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
16-235 |
3.95e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.87 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 16 GLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHD---QPITTTYLADAQNRQQLHQRIGMVFQNTDV 92
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgQLRDLYALSEAERRRLLRTEWGFVHQHPRD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 93 QLfNTSVTEEVAFGPRQLGLSA---AMVAQRVADCLQLTDCAnlADRV---PYQLSGGEKKRVALASVLALNPEILLLDE 166
Cdd:PRK11701 101 GL-RMQVSAGGNIGERLMAVGArhyGDIRATAGDWLERVEID--AARIddlPTTFSGGMQQRLQIARNLVTHPRLVFMDE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729460384 167 PLNGLTIAAQQQMLTLLQRLQA-AGKTIIMASHNYQQVQAVGERFIIFNSTHQVDADLTRADLD--QQPARQ 235
Cdd:PRK11701 178 PTGGLDVSVQARLLDLLRGLVReLGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDdpQHPYTQ 249
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-201 |
6.62e-13 |
|
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: 65.82 E-value: 6.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 12 PDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADAQNRQqlhqRIGMVFQNTD 91
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRN----RYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 92 VQLFNTSVTEEVAFGP-----RQLGLSAAMVAQRVADCLQLTDCANLADRvPYQLSGGEKKRVALASVLALNPEILLLDE 166
Cdd:cd03290 88 PWLLNATVEENITFGSpfnkqRYKAVTDACSLQPDIDLLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 1729460384 167 PLNGLTIAAQQQMLT--LLQRLQAAGKTIIMASHNYQ 201
Cdd:cd03290 167 PFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ 203
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
21-241 |
7.45e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.85 E-value: 7.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 21 SLTVNSGDFICLMGPNGSGKSTLLRLLSGLASP--TSGAYQFHDQPITTTYLADAQNRQQLHQRIGMVFQNTDVQLfNTS 98
Cdd:COG4170 27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwHVTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQEPSSCL-DPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 99 VT-----EEVAFGPRQLGlsaaMVAQRVADclQLTDCANLADRV------------PYQLSGGEKKRVALASVLALNPEI 161
Cdd:COG4170 106 AKigdqlIEAIPSWTFKG----KWWQRFKW--RKKRAIELLHRVgikdhkdimnsyPHELTEGECQKVMIAMAIANQPRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 162 LLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHNYQQV-------------QAV--GERFIIFNSTHQ--VDAdL 223
Cdd:COG4170 180 LIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESIsqwadtitvlycgQTVesGPTEQILKSPHHpyTKA-L 258
|
250 260
....*....|....*....|
gi 1729460384 224 TRA--DLDQQPARQAQLMTL 241
Cdd:COG4170 259 LRSmpDFRQPLPHKSRLNTL 278
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
18-199 |
9.82e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 67.19 E-value: 9.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 18 KDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGayqfhdqpittTYLADAQNRQQlhqrigmVFQNTDVQLFNT 97
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG-----------TVFRSAKVRMA-------VFSQHHVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 98 SVTEEVAF-----GPRQLGLSAAMVAQRVAdclqltdcANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLT 172
Cdd:PLN03073 588 SSNPLLYMmrcfpGVPEQKLRAHLGSFGVT--------GNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
170 180
....*....|....*....|....*..
gi 1729460384 173 IAAQQQMLTLLQRLQAAgktIIMASHN 199
Cdd:PLN03073 660 LDAVEALIQGLVLFQGG---VLMVSHD 683
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-199 |
9.93e-13 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 65.85 E-value: 9.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 23 TVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQfhDQPITTTYLADaqnrqqlhqrigmvFQNTDVQLFNTSVTEE 102
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD--DPPDWDEILDE--------------FRGSELQNYFTKLLEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 103 ---VAFGPRQLGLSAAMVAQRVADCLQLTD-------------CANLADRVPYQLSGGEKKRVALASVLALNPEILLLDE 166
Cdd:cd03236 86 dvkVIVKPQYVDLIPKAVKGKVGELLKKKDergkldelvdqleLRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190
....*....|....*....|....*....|...
gi 1729460384 167 PLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHN 199
Cdd:cd03236 166 PSSYLDIKQRLNAARLIRELAEDDNYVLVVEHD 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
17-171 |
1.37e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.68 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFhdQP-ITTTYL--------------------ADAQN 75
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP--APgIKVGYLpqepqldpektvrenveegvAEVKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 76 RQQLHQRIGMVFQNTDVQlFNTSVTEevafgprQLGLSAAMVAQ----------RVADCLQLTDcanlADRVPYQLSGGE 145
Cdd:PRK11819 101 ALDRFNEIYAAYAEPDAD-FDALAAE-------QGELQEIIDAAdawdldsqleIAMDALRCPP----WDAKVTKLSGGE 168
|
170 180
....*....|....*....|....*.
gi 1729460384 146 KKRVALASVLALNPEILLLDEPLNGL 171
Cdd:PRK11819 169 RRRVALCRLLLEKPDMLLLDEPTNHL 194
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
17-185 |
1.47e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 66.67 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaqNRQQLHQRIGMVFQntDVQLFN 96
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL------SHSVLRQGVAMVQQ--DPVVLA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVAFGpRQLGlsaamvAQRVADCLQLTDCANLADRVP-----------YQLSGGEKKRVALASVLALNPEILLLD 165
Cdd:PRK10790 429 DTFLANVTLG-RDIS------EEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILD 501
|
170 180
....*....|....*....|...
gi 1729460384 166 EP---LNGLTIAAQQQMLTLLQR 185
Cdd:PRK10790 502 EAtanIDSGTEQAIQQALAAVRE 524
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-206 |
1.57e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.41 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 20 LSLTVNSGDFICLMGPNGSGKSTLLRLLSGLAsPTSGAYQFHDQPITTtyLADAQNRQQLhqriGMVFQNTdvQLFNTSV 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRE--LDPESWRKHL----SWVGQNP--QLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 100 TEEVAFGprqlglSAAMVAQRVADCLQLTDCANLADRVP----YQ-------LSGGEKKRVALASVLALNPEILLLDEPL 168
Cdd:PRK11174 440 RDNVLLG------NPDASDEQLQQALENAWVSEFLPLLPqgldTPigdqaagLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190
....*....|....*....|....*....|....*...
gi 1729460384 169 NGLTIAAQQQMLTLLQRLqAAGKTIIMASHNYQQVQAV 206
Cdd:PRK11174 514 ASLDAHSEQLVMQALNAA-SRRQTTLMVTHQLEDLAQW 550
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-212 |
1.64e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 65.92 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 20 LSLTVNSGDFICLMGPNGSGKSTLLRLLSGL----ASPTSGAYQFHDQPITTtyLADAQNRQQLHQRIGMVFQNTDVQLf 95
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQR--ISEKERRNLVGAEVAMIFQDPMTSL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 NTSVTeeVAFgprQL--------GLSAAMVAQRVADCLQLT---DCANLADRVPYQLSGGEKKRVALASVLALNPEILLL 164
Cdd:PRK11022 103 NPCYT--VGF---QImeaikvhqGGNKKTRRQRAIDLLNQVgipDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1729460384 165 DEPLNGLTIAAQQQMLTLLQRLQ-AAGKTIIMASHNYQQVQAVGERFII 212
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIV 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
13-199 |
2.11e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.52 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 13 DTCGLKDLSLTVNSGDFICLMGPNGSGKS-TLLRLLSGLASP--TSGAYQFHDQPITTtyLADAQ-NRQQLHQrIGMVFQ 88
Cdd:PRK09473 28 DVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILN--LPEKElNKLRAEQ-ISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 89 NTDVQLfN--TSVTE---EVAFGPRQLGLSAAMVAQ-RVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEIL 162
Cdd:PRK09473 105 DPMTSL-NpyMRVGEqlmEVLMLHKGMSKAEAFEESvRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 1729460384 163 LLDEPLNGLTIAAQQQMLTLLQRLQAAGKT-IIMASHN 199
Cdd:PRK09473 184 IADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHD 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-226 |
2.25e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 27 GDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtyLADAQnRQQLHQRIGMVFQNTDVQLfntsvteevafG 106
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT--LSPGK-LQALRRDIQFIFQDPYASL-----------D 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 107 PRQLGLSAAMVAQRVADCLQLTDCAN----LADRV----------PYQLSGGEKKRVALASVLALNPEILLLDEPLNGLT 172
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLLPGKAAAArvawLLERVgllpehawryPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1729460384 173 IAAQQQMLTLLQRLQAA-GKTIIMASHNYQQVQAVGERFIIFNSTHQVDADLTRA 226
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRA 550
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-230 |
2.83e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 4 LVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaQNRQQLHQRI 83
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFK-----SSKEALENGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 84 GMVFQNTDvQLFNTSVTEEVAFG--PRQlGL---SAAMVAQRVADCLQLTDCANLADRVPyQLSGGEKKRVALASVLALN 158
Cdd:PRK10982 76 SMVHQELN-LVLQRSVMDNMWLGryPTK-GMfvdQDKMYRDTKAIFDELDIDIDPRAKVA-TLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1729460384 159 PEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNSTHQVDA-DLTRADLDQ 230
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATqPLAGLTMDK 225
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-209 |
1.09e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.28 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 20 LSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASP----TSGAYQFHDqpITTTYLADAQNRQQLHQRIGMVFQNTDVQLf 95
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDD--IDLLRLSPRERRKLVGHNVSMIFQEPQSCL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 ntSVTEEVAfgpRQLGLS--------------------AAMVAQRVAdclqLTDCANLADRVPYQLSGGEKKRVALASVL 155
Cdd:PRK15093 103 --DPSERVG---RQLMQNipgwtykgrwwqrfgwrkrrAIELLHRVG----IKDHKDAMRSFPYELTEGECQKVMIAIAL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1729460384 156 ALNPEILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHNYQQVQAVGER 209
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADK 228
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-203 |
2.77e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 61.35 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLA--SPTSGAYQFHDQPitttyLADAQNRQQ 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKD-----LLELSPEDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 79 LHQRIGMVFQ------NTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDC-ANLADR-VPYQLSGGEKKRVA 150
Cdd:PRK09580 76 AGEGIFMAFQypveipGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMpEDLLTRsVNVGFSGGEKKRND 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1729460384 151 LASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHnYQQV 203
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH-YQRI 207
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
16-231 |
3.74e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 16 GLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADA---------QNRQQLHQRIGMV 86
Cdd:PRK10762 267 GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlangivyisEDRKRDGLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 87 FQNtdvqlfNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTdcaNL----ADRVPYQLSGGEKKRVALASVLALNPEIL 162
Cdd:PRK10762 347 VKE------NMSLTALRYFSRAGGSLKHADEQQAVSDFIRLF---NIktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729460384 163 LLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNSTHqVDADLTRADLDQQ 231
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR-ISGEFTREQATQE 485
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
10-213 |
4.36e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 10 DYPD-TCGLKDLSLTVNSGDF-----ICLMGPNGSGKSTLLRLLSGLASPTSGAYqfhDQPITTTYLAdaqnrqqlhQRI 83
Cdd:PRK13409 342 EYPDlTKKLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELKISYKP---------QYI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 84 GMVFQNTdVQLFNTSVTEEvafgprqlgLSAAMVAQRVADCLQLTDcanLADRVPYQLSGGEKKRVALASVLALNPEILL 163
Cdd:PRK13409 410 KPDYDGT-VEDLLRSITDD---------LGSSYYKSEIIKPLQLER---LLDKNVKDLSGGELQRVAIAACLSRDADLYL 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 164 LDEPLNGLTIAaqqqmltllQRLQAA----------GKTIIMASHNYQQVQAVGERFIIF 213
Cdd:PRK13409 477 LDEPSAHLDVE---------QRLAVAkairriaeerEATALVVDHDIYMIDYISDRLMVF 527
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-189 |
5.07e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 20 LSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTT----YLADAQNRQQLHQrigmvfqntdvqlf 95
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGdrsrFMAYLGHLPGLKA-------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 NTSVTEEVAFgprQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASvLALNPEIL-LLDEPLNGLTIA 174
Cdd:PRK13543 96 DLSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDLE 171
|
170
....*....|....*
gi 1729460384 175 AqqqmLTLLQRLQAA 189
Cdd:PRK13543 172 G----ITLVNRMISA 182
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
10-213 |
9.45e-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: 60.95 E-value: 9.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 10 DYPD-TCGLKDLSLTVNSGDF-----ICLMGPNGSGKSTLLRLLSGLASPTSGAYqfhDQPITTTYLAdaqnrqqlhQRI 83
Cdd:COG1245 343 EYPDlTKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLKISYKP---------QYI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 84 GMVFQNTDVQLFNTSVTEEvafgprqlgLSAAMVAQRVADCLQLTdcaNLADRVPYQLSGGEKKRVALASVLALNPEILL 163
Cdd:COG1245 411 SPDYDGTVEEFLRSANTDD---------FGSSYYKTEIIKPLGLE---KLLDKNVKDLSGGELQRVAIAACLSRDADLYL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 164 LDEPLNGLTIAaqqqmltllQRLQAA----------GKTIIMASHNYQQVQAVGERFIIF 213
Cdd:COG1245 479 LDEPSAHLDVE---------QRLAVAkairrfaenrGKTAMVVDHDIYLIDYISDRLMVF 529
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-197 |
1.12e-10 |
|
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: 59.20 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPT---SGAYQFHDQPItttyladAQNRQQLHQRIGMVFQNtDVQ 93
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY-------KEFAEKYPGEIIYVSEE-DVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 94 LFNTSVTEEVAFgprqlglsaamvaqrVADCLqltdcanlADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTI 173
Cdd:cd03233 95 FPTLTVRETLDF---------------ALRCK--------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180
....*....|....*....|....
gi 1729460384 174 AAQQQMLTLLQRLQAAGKTIIMAS 197
Cdd:cd03233 152 STALEILKCIRTMADVLKTTTFVS 175
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
16-212 |
1.51e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.45 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 16 GLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITttylaDAQNRQQLHQriGMVFQNTDVQ-- 93
Cdd:PRK15439 278 GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEIN-----ALSTAQRLAR--GLVYLPEDRQss 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 94 -LF-------NTS--VTEEVAFGPRQLGLSAAMVAQRVADCLQLTDcanlADRVPYQLSGGEKKRVALASVLALNPEILL 163
Cdd:PRK15439 351 gLYldaplawNVCalTHNRRGFWIKPARENAVLERYRRALNIKFNH----AEQAARTLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1729460384 164 LDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFII 212
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLV 475
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
141-238 |
2.79e-10 |
|
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: 59.84 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 141 LSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNSThQVD 220
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG-KLK 482
|
90
....*....|....*...
gi 1729460384 221 ADLTRADLDQQPARQAQL 238
Cdd:TIGR02633 483 GDFVNHALTQEQVLAAAL 500
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-198 |
3.93e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 11 YPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQF----------HDQP--ITTT---YLAD--- 72
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeqdlivarlqQDPPrnVEGTvydFVAEgie 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 73 --AQNRQQLHQ------------------RIGMVFQNTDVQLFNTSVTEEVAfgprQLGLSAAMvaqrvadclQLTDcan 132
Cdd:PRK11147 93 eqAEYLKRYHDishlvetdpseknlnelaKLQEQLDHHNLWQLENRINEVLA----QLGLDPDA---------ALSS--- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729460384 133 ladrvpyqLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAgktIIMASH 198
Cdd:PRK11147 157 --------LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGS---IIFISH 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-171 |
7.96e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGlasptsGAYQFH-DQPITTTYLADAQNRQQLHQRIGMVF-QNTDVQL 94
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS------NTDGFHiGVEGVITYDGITPEEIKKHYRGDVVYnAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 95 FNTSVTEEVAF-------GPRQLGLSAAMVAQRVAD----CLQLTDCAN--LADRVPYQLSGGEKKRVALASVLALNPEI 161
Cdd:TIGR00956 151 PHLTVGETLDFaarcktpQNRPDGVSREEYAKHIADvymaTYGLSHTRNtkVGNDFVRGVSGGERKRVSIAEASLGGAKI 230
|
170
....*....|
gi 1729460384 162 LLLDEPLNGL 171
Cdd:TIGR00956 231 QCWDNATRGL 240
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-198 |
9.31e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.11 E-value: 9.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 5 VNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGayqfhdqpittTYLADAQNRQQ-----L 79
Cdd:PRK11176 347 VTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEG-----------EILLDGHDLRDytlasL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQNtdVQLFNTSVTEEVAFgPRQLGLSAAMV--AQRVADCLQLTD-CANLADRVPYQ----LSGGEKKRVALA 152
Cdd:PRK11176 416 RNQVALVSQN--VHLFNDTIANNIAY-ARTEQYSREQIeeAARMAYAMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIA 492
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1729460384 153 SVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQaAGKTIIMASH 198
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAH 537
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
17-198 |
9.64e-10 |
|
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: 56.73 E-value: 9.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTyladaqNRQQLHQRIGMVFQntDVQLFN 96
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI------GLHDLRSRISIIPQ--DPVLFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSV-----------TEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANladrvpyQLSGGEKKRVALASVLALNPEILLLD 165
Cdd:cd03244 92 GTIrsnldpfgeysDEELWQALERVGLKEFVESLPGGLDTVVEEGGE-------NLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190
....*....|....*....|....*....|...
gi 1729460384 166 EPLNGLTIAAQQQMLTLLqRLQAAGKTIIMASH 198
Cdd:cd03244 165 EATASVDPETDALIQKTI-REAFKDCTVLTIAH 196
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-203 |
1.11e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADAQnrqqlH 80
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQ-----E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QRIGMVFQNTDVqLFNTSVTEEVAFGpRQ----LG--LSAAMVAQrvADCLqltdCANL-----ADRVPYQLSGGEKKRV 149
Cdd:PRK10762 79 AGIGIIHQELNL-IPQLTIAENIFLG-REfvnrFGriDWKKMYAE--ADKL----LARLnlrfsSDKLVGELSIGEQQMV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1729460384 150 ALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQV 203
Cdd:PRK10762 151 EIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEI 204
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
17-198 |
1.89e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.65 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITT------TYLAdaqnrQQLHQRIGM-VFQN 89
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiakpycTYIG-----HNLGLKLEMtVFEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 90 TDV--QLFNTSVTeevafgprqlgLSAAMVAQRVADCLqltdcanlaDRVPYQLSGGEKKRVALASVLALNPEILLLDEP 167
Cdd:PRK13541 91 LKFwsEIYNSAET-----------LYAAIHYFKLHDLL---------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEV 150
|
170 180 190
....*....|....*....|....*....|.
gi 1729460384 168 LNGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:PRK13541 151 ETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-215 |
1.93e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICY-DYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPIT--TTYLADAQNRQQ 78
Cdd:PTZ00265 1168 IMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTndMTNEQDYQGDEE 1247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 79 lhQRIGM-------------------VFQNT---------------------------DVQLFNTSVTEEVAFGPRQLGL 112
Cdd:PTZ00265 1248 --QNVGMknvnefsltkeggsgedstVFKNSgkilldgvdicdynlkdlrnlfsivsqEPMLFNMSIYENIKFGKEDATR 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 113 SAAMVAQRVADCLQLTDcaNLADRV-----PY--QLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQQQM-LTLLQ 184
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFIE--SLPNKYdtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIeKTIVD 1403
|
250 260 270
....*....|....*....|....*....|.
gi 1729460384 185 RLQAAGKTIIMASHNYQQVQAvGERFIIFNS 215
Cdd:PTZ00265 1404 IKDKADKTIITIAHRIASIKR-SDKIVVFNN 1433
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-205 |
4.17e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.05 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYqfhDQPITTTYLAdaqnrqqlhqrIGMVFQNtdvQLfn 96
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV---DIKGSAALIA-----------ISSGLNG---QL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 tSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQ 176
Cdd:PRK13545 101 -TGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180
....*....|....*....|....*....
gi 1729460384 177 QQMLTLLQRLQAAGKTIIMASHNYQQVQA 205
Cdd:PRK13545 180 KKCLDKMNEFKEQGKTIFFISHSLSQVKS 208
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-198 |
4.58e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 6 NICYDYP----DTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGlaSPTSGAyqfhdqpITT-TYLADAQNRQQLH 80
Cdd:TIGR00956 764 NLTYEVKikkeKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGV-------ITGgDRLVNGRPLDSSF 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QR-IGMVFQNtDVQLFNTSVTEEVAFG-----PRQLGLSAAM-VAQRVADCLQLTDCANLADRVPYQ-LSGGEKKRVALA 152
Cdd:TIGR00956 835 QRsIGYVQQQ-DLHLPTSTVRESLRFSaylrqPKSVSKSEKMeYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIG 913
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1729460384 153 SVLALNPEILL-LDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:TIGR00956 914 VELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
139-199 |
5.19e-09 |
|
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: 56.17 E-value: 5.19e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1729460384 139 YQLSGGEKKRVALASVL---ALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHN 199
Cdd:TIGR00630 828 TTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHN 891
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
16-198 |
6.53e-09 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 55.39 E-value: 6.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 16 GLKDLSLTVNSgDFICLMGPNGSGKSTLLRLLSGLASPTSGA-YQFHD-----------QPITTTY------LADAQNRQ 77
Cdd:COG3593 13 SIKDLSIELSD-DLTVLVGENNSGKSSILEALRLLLGPSSSRkFDEEDfylgddpdlpeIEIELTFgsllsrLLRLLLKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 78 QLHQRIGMVFQNTDVQL------FNTSVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDcANLAD--RVPYQLSG-GEKKR 148
Cdd:COG3593 92 EDKEELEEALEELNEELkealkaLNELLSEYLKELLDGLDLELELSLDELEDLLKSLS-LRIEDgkELPLDRLGsGFQRL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1729460384 149 VALASVLAL-------NPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:COG3593 171 ILLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
141-199 |
6.93e-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: 54.54 E-value: 6.93e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729460384 141 LSGGEKKRVALASVL---ALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHN 199
Cdd:cd03271 170 LSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-198 |
6.97e-09 |
|
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: 55.56 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 32 LMGPNGSGKSTLLRLLSGLASPTSGAYqfhDQPITT-------------TYLADAQNRQ-------QLHQRIGMVFQNTd 91
Cdd:COG1245 104 ILGPNGIGKSTALKILSGELKPNLGDY---DEEPSWdevlkrfrgtelqDYFKKLANGEikvahkpQYVDLIPKVFKGT- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 92 vqlfntsvteevafgPRQLgLSAA---MVAQRVADCLQLTdcaNLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPL 168
Cdd:COG1245 180 ---------------VREL-LEKVderGKLDELAEKLGLE---NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|
gi 1729460384 169 NGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:COG1245 241 SYLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
17-198 |
7.34e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 7.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLA---SPTSGAYQFHDQPIT---TTYL-----ADAQNRQQLHQRIGM 85
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAidgIPKNCQILHVEQEVVgddTTALqcvlnTDIERTQLLEEEAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 86 VFQNTDVQLFNTSVTEEvafGPRQLGLSAAMVAQRVADC---LQLTDC-----------------ANLADRVPYQLSGGE 145
Cdd:PLN03073 273 VAQQRELEFETETGKGK---GANKDGVDKDAVSQRLEEIykrLELIDAytaearaasilaglsftPEMQVKATKTFSGGW 349
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1729460384 146 KKRVALASVLALNPEILLLDEPLNGLTIAAqqqMLTLLQRLQAAGKTIIMASH 198
Cdd:PLN03073 350 RMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVSH 399
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-235 |
8.96e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 8.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 18 KDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDqpitTTYLADAqNRQQLHQRIGMVFQntDVQLFNT 97
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND----SHNLKDI-NLKWWRSKIGVVSQ--DPLLFSN 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 98 SVTEEVAF------------------------GPRQLGLSAAMVAQRVADCLQLTDCANLAD-RVPYQ------------ 140
Cdd:PTZ00265 475 SIKNNIKYslyslkdlealsnyynedgndsqeNKNKRNSCRAKCAGDLNDMSNTTDSNELIEmRKNYQtikdsevvdvsk 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 141 -------------------------LSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTI-I 194
Cdd:PTZ00265 555 kvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItI 634
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1729460384 195 MASHNYQQVQAVGERFIIFN----STHQVDADLTRADLDQQPARQ 235
Cdd:PTZ00265 635 IIAHRLSTIRYANTIFVLSNrergSTVDVDIIGEDPTKDNKENNN 679
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
18-171 |
9.25e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 9.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 18 KDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDqpitTTYLA--DaQNRQQLHQrigmvfqntdvqlf 95
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE----TVKLAyvD-QSRDALDP-------------- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 96 NTSVTEEVAFGPRQLGL------SAAMVA----------QRVAdclqltdcanladrvpyQLSGGEKKRVALASVLALNP 159
Cdd:PRK11819 402 NKTVWEEISGGLDIIKVgnreipSRAYVGrfnfkggdqqKKVG-----------------VLSGGERNRLHLAKTLKQGG 464
|
170
....*....|..
gi 1729460384 160 EILLLDEPLNGL 171
Cdd:PRK11819 465 NVLLLDEPTNDL 476
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
34-170 |
9.38e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 9.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 34 GPNGSGKSTLLRLLSGLASPTSG-AYQFhDQPItttylaDAQNRqQLHQRIG-M-----------VFQNTDV--QLFnts 98
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGeAWLF-GQPV------DAGDI-ATRRRVGyMsqafslygeltVRQNLELhaRLF--- 367
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729460384 99 vteevafgprqlGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNG 170
Cdd:NF033858 368 ------------HLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSG 427
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
140-240 |
1.50e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.55 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 140 QLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFNSThQV 219
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG-KL 483
|
90 100
....*....|....*....|.
gi 1729460384 220 DADLTRADLDQQparqaQLMT 240
Cdd:PRK13549 484 KGDLINHNLTQE-----QVME 499
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-198 |
1.90e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 54.37 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGL-KDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGL--------------------ASPTSGAYQ 59
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrltkpakgklfyvpQRPYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 60 FHDQPITTTYLADAQNRQQLHQRIGMVFQNtdVQLFNTsVTEEVafgprqlGLSAamvaqrVADCLQLtdcanladrvpy 139
Cdd:TIGR00954 531 LRDQIIYPDSSEDMKRRGLSDKDLEQILDN--VQLTHI-LEREG-------GWSA------VQDWMDV------------ 582
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1729460384 140 qLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRlqaAGKTIIMASH 198
Cdd:TIGR00954 583 -LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE---FGITLFSVSH 637
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-198 |
1.98e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 23 TVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQfhDQP------------ITTTYLADAQNRQ-------QLHQRI 83
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYE--EEPswdevlkrfrgtELQNYFKKLYNGEikvvhkpQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 84 GMVFQNTDVQLFN----TSVTEEVAfgpRQLGLSaamvaqrvadclqltdcaNLADRVPYQLSGGEKKRVALASVLALNP 159
Cdd:PRK13409 173 PKVFKGKVRELLKkvdeRGKLDEVV---ERLGLE------------------NILDRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190
....*....|....*....|....*....|....*....
gi 1729460384 160 EILLLDEPLNGLTIAAQQQMLTLLQRLqAAGKTIIMASH 198
Cdd:PRK13409 232 DFYFFDEPTSYLDIRQRLNVARLIREL-AEGKYVLVVEH 269
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-197 |
2.29e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTtylADAQNRQQLH--------QRIGMV-- 86
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITG---LSPRERRRLGvayipedrLGRGLVpd 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 87 FqntdvqlfntSVTEEVAFG-PRQLGLSAAMVAQR---VADCLQLTD-----CANLADRVPyQLSGGEKKRVALASVLAL 157
Cdd:COG3845 351 M----------SVAENLILGrYRRPPFSRGGFLDRkaiRAFAEELIEefdvrTPGPDTPAR-SLSGGNQQKVILARELSR 419
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1729460384 158 NPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMAS 197
Cdd:COG3845 420 DPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLIS 459
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-198 |
2.78e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.08 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGlasPTSGAYQFHDQPITttylaDAQNRQQLHQRIGMVFQNTDVQLFN 96
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRIS-----GFPKKQETFARISGYCEQNDIHSPQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVAFG-----PRQLGLSAAMVAqrVADCLQLTDCANLADRV---P--YQLSGGEKKRVALASVLALNPEILLLDE 166
Cdd:PLN03140 968 VTVRESLIYSaflrlPKEVSKEEKMMF--VDEVMELVELDNLKDAIvglPgvTGLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
170 180 190
....*....|....*....|....*....|..
gi 1729460384 167 PLNGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:PLN03140 1046 PTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
141-199 |
4.05e-08 |
|
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: 51.55 E-value: 4.05e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1729460384 141 LSGGEKKRVALASVLALNPE--ILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHN 199
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
141-197 |
4.59e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.87 E-value: 4.59e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1729460384 141 LSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMAS 197
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVIS 461
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-211 |
5.46e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 6 NICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQpITTTYLAdaqnrqQLHQRigm 85
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN-ANIGYYA------QDHAY--- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 86 VFQNtDVQLFntsvteEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVpyqLSGGEKKRVALASVLALNPEILLLD 165
Cdd:PRK15064 394 DFEN-DLTLF------DWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKV---LSGGEKGRMLFGKLMMQKPNVLVMD 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1729460384 166 EPLNGLTIAAQQQMLTLLQRLQAagkTIIMASHNYQQVQAVGERFI 211
Cdd:PRK15064 464 EPTNHMDMESIESLNMALEKYEG---TLIFVSHDREFVSSLATRII 506
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-199 |
1.00e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.09 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 1 MIKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFhDQPITTTYLADaqnrqqlH 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKLGYFAQ-------H 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 81 QrigMVFQNTDvqlfNTSVTEEVAFGPRQLglsaamvAQRVADCL--------QLTDCANladrvpyQLSGGEKKRVALA 152
Cdd:PRK10636 384 Q---LEFLRAD----ESPLQHLARLAPQEL-------EQKLRDYLggfgfqgdKVTEETR-------RFSGGEKARLVLA 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1729460384 153 SVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAgktIIMASHN 199
Cdd:PRK10636 443 LIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGA---LVVVSHD 486
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-223 |
1.19e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 49.68 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 26 SGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDqpitttylADAQNRQQLHQRIGMVFqntdvqlfntsvteevaf 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID--------GEDILEEVLDQLLLIIV------------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 106 gprqlglsaamvaqrvadclqltdcanlaDRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQQQML----- 180
Cdd:smart00382 55 -----------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleel 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1729460384 181 -TLLQRLQAAGKTIIMASHNyqqVQAVGERFIIFNSTHQVDADL 223
Cdd:smart00382 106 rLLLLLKSEKNLTVILTTND---EKDLGPALLRRRFDRRIVLLL 146
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-198 |
2.15e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGayqfhdqpitttyladaqnRQQLHQRIGMVFQNTdvQLFN 96
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG-------------------RVWAERSIAYVPQQA--WIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVAFGPRQlglsaamVAQRVAD---CLQL-TDCANLADRVPYQ-------LSGGEKKRVALASVLALNPEILLLD 165
Cdd:PTZ00243 735 ATVRGNILFFDEE-------DAARLADavrVSQLeADLAQLGGGLETEigekgvnLSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190
....*....|....*....|....*....|....*
gi 1729460384 166 EPLNGLTIAAQQQML--TLLQRLqaAGKTIIMASH 198
Cdd:PTZ00243 808 DPLSALDAHVGERVVeeCFLGAL--AGKTRVLATH 840
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-241 |
2.90e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.06 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASpTSGAYQFHDQPITTTYLadaqnrQQLHQRIGMVFQN------- 89
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTL------QTWRKAFGVIPQKvfifsgt 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 90 -----------TDVQLFNtsVTEEVafgprqlGLSAamVAQRVADCL--QLTDCAnladrvpYQLSGGEKKRVALASVLA 156
Cdd:TIGR01271 1308 frknldpyeqwSDEEIWK--VAEEV-------GLKS--VIEQFPDKLdfVLVDGG-------YVLSNGHKQLMCLARSIL 1369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 157 LNPEILLLDEPLNGLT-IAAQQQMLTLLQRLqaAGKTIIMASHnyqQVQAVGE--RFIIF--NSTHQVDAD---LTRADL 228
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDpVTLQIIRKTLKQSF--SNCTVILSEH---RVEALLEcqQFLVIegSSVKQYDSIqklLNETSL 1444
|
250
....*....|....*.
gi 1729460384 229 DQQ---PARQAQLMTL 241
Cdd:TIGR01271 1445 FKQamsAADRLKLFPL 1460
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
141-212 |
3.64e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 3.64e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729460384 141 LSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFII 212
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILV 463
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-199 |
2.08e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.39 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 18 KDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASP----TSGAYQFHDQPItttylADAQNRQQLhqrIGMVFQNTdvq 93
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPV-----APCALRGRK---IATIMQNP--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 94 lfntsvteEVAFGP------------RQLGLSAAmvAQRVADCLQ---LTDCANLADRVPYQLSGGEKKRVALASVLALN 158
Cdd:PRK10418 89 --------RSAFNPlhtmhtharetcLALGKPAD--DATLTAALEavgLENAARVLKLYPFEMSGGMLQRMMIALALLCE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1729460384 159 PEILLLDEPLNGLTIAAQQQMLTLLQRL-QAAGKTIIMASHN 199
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHD 200
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
141-205 |
2.51e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.87 E-value: 2.51e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729460384 141 LSGGEKKRVALASVL--ALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQA 205
Cdd:cd03270 138 LSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA 204
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-213 |
2.91e-06 |
|
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: 46.03 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 24 VNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGayqfhdqpitttyladaqnrqqlhqrigmvfqNTDVQLFNtsvteeV 103
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD--------------------------------NDEWDGIT------P 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 104 AFGPRQLglsaamvaqrvadclqltdcanladrvpyQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQQQMLTLL 183
Cdd:cd03222 64 VYKPQYI-----------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
170 180 190
....*....|....*....|....*....|.
gi 1729460384 184 QRL-QAAGKTIIMASHNYQQVQAVGERFIIF 213
Cdd:cd03222 115 RRLsEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-198 |
3.35e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAyqfhdqpitttyladaqnrqQLHQRIGMVFQNTDVQLFN 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS--------------------SVVIRGSVAYVPQVSWIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVAFG----PRQLGLSAAMVA-QRVADCLQLTDCANLADRvPYQLSGGEKKRVALASVLALNPEILLLDEPLNGL 171
Cdd:PLN03232 693 ATVRENILFGsdfeSERYWRAIDVTAlQHDLDLLPGRDLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180
....*....|....*....|....*..
gi 1729460384 172 TIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:PLN03232 772 DAHVAHQVFDSCMKDELKGKTRVLVTN 798
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-199 |
4.36e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFH---------------DQPITTTYLADAQNRQQLHQ 81
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPgnwqlawvnqetpalPQPALEYVIDGDREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 82 RIGMVFQNTDVQLFNT-----------SVTEEVAFGPRQLGLSAAMVAQRVADclqltdcanladrvpyqLSGGEKKRVA 150
Cdd:PRK10636 97 QLHDANERNDGHAIATihgkldaidawTIRSRAASLLHGLGFSNEQLERPVSD-----------------FSGGWRMRLN 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1729460384 151 LASVLALNPEILLLDEPLNGLTIAAqqqMLTLLQRLQAAGKTIIMASHN 199
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQGTLILISHD 205
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-171 |
5.31e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 47.25 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 10 DYPDTcgLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGayqfhdqpitttyladaqnRQQLHQRIGMVFQN 89
Cdd:TIGR00957 649 DLPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG-------------------HVHMKGSVAYVPQQ 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 90 TDVQlfNTSVTEEVAFGPRqlgLSAAMVAQRVADCLQLTDCANL--ADRVP-----YQLSGGEKKRVALASVLALNPEIL 162
Cdd:TIGR00957 708 AWIQ--NDSLRENILFGKA---LNEKYYQQVLEACALLPDLEILpsGDRTEigekgVNLSGGQKQRVSLARAVYSNADIY 782
|
....*....
gi 1729460384 163 LLDEPLNGL 171
Cdd:TIGR00957 783 LFDDPLSAV 791
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
16-212 |
6.00e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 46.14 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 16 GLKDLSLTVNSGD-FICLMGPNGSGKSTLLRLLS-GLASPTSGAYQFHDQPITTTYLADA----------------QNRQ 77
Cdd:COG3950 13 GFEDLEIDFDNPPrLTVLVGENGSGKTTLLEAIAlALSGLLSRLDDVKFRKLLIRNGEFGdsaklilyygtsrlllDGPL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 78 QLHQRIgMVFQNTDVQLFNTSVTEEVAFGP--RQLGLSAAMVAQRVADCLQ-------------LTDCANL--------- 133
Cdd:COG3950 93 KKLERL-KEEYFSRLDGYDSLLDEDSNLREflEWLREYLEDLENKLSDELDekleavrealnklLPDFKDIridrdpgrl 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 134 ------ADRVPY-QLSGGEKKRVALASVLA-----LNPE---------ILLLDEPLNGLTIAAQQQmltLLQRLQAAGKT 192
Cdd:COG3950 172 vildknGEELPLnQLSDGERSLLALVGDLArrlaeLNPAlenplegegIVLIDEIDLHLHPKWQRR---ILPDLRKIFPN 248
|
250 260
....*....|....*....|..
gi 1729460384 193 I--IMASHNYQQVQAVGERFII 212
Cdd:COG3950 249 IqfIVTTHSPLILSSLEDEEVI 270
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-198 |
6.44e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDYPDTCGLKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGlasptsgayqfhDQPitTTYLADAQ--NRQ-- 77
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG------------DHP--QGYSNDLTlfGRRrg 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 78 ------QLHQRIGMVfqNTDVQL---FNTSVteevafgpRQLGLSAAM----VAQRVADCLQLT-----DCANLADRV-- 137
Cdd:PRK10938 327 sgetiwDIKKHIGYV--SSSLHLdyrVSTSV--------RNVILSGFFdsigIYQAVSDRQQKLaqqwlDILGIDKRTad 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1729460384 138 -PYQ-LSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKT-IIMASH 198
Cdd:PRK10938 397 aPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSH 460
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
141-199 |
1.12e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.79 E-value: 1.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729460384 141 LSGGEKKRVALASVLA---LNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHN 199
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHN 888
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
144-198 |
1.17e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 1.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1729460384 144 GEKKRVALASVLALNPEILLLDEPLNGL---TIAAQQQMLTllQRlqaaGKTIIMASH 198
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLdinTIRWLEDVLN--ER----NSTMIIISH 210
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
20-238 |
1.18e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 20 LSLTVNSGDFICLMGPNGSGKSTLlRLLSGLASPTSG--AYQFHdqpittTYLAdaqNRQQLHQRIGMVFQNTDVQLFNT 97
Cdd:NF000106 32 VDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGrrPWRF*------TWCA---NRRALRRTIG*HRPVR*GRRESF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 98 SVTEEVAFGPRQLGLSAAMVAQRVADCLQLTDCANLADRVPYQLSGGEKKRVALASVLALNPEILLLDEPLNGLTIAAQQ 177
Cdd:NF000106 102 SGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729460384 178 QMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFN-----STHQVDADLTRA---DLDQQPARQAQL 238
Cdd:NF000106 182 EVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDrgrviADGKVDELKTKVggrTLQIRPAHAAEL 250
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
141-199 |
1.28e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.83 E-value: 1.28e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729460384 141 LSGGEKKRVALASVLALNPE---ILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHN 199
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHN 892
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-214 |
3.16e-05 |
|
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: 44.08 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQfHDQPITttyladaqnrqqlhqrigmvFQNTDVQLFN 96
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-HSGRIS--------------------FSSQFSWIMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 TSVTEEVAFGprqLGLSAAMVAQRVADCLQLTDCANLA--DRVPY-----QLSGGEKKRVALASVLALNPEILLLDEPLN 169
Cdd:cd03291 112 GTIKENIIFG---VSYDEYRYKSVVKACQLEEDITKFPekDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1729460384 170 GLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQAVGERFIIFN 214
Cdd:cd03291 189 YLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHE 233
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-203 |
3.41e-05 |
|
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: 43.56 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 2 IKLVNICYDY-PDTCG-LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYLADaqnrqqL 79
Cdd:cd03369 7 IEVENLSVRYaPDLPPvLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED------L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 80 HQRIGMVFQntDVQLFNTSVTEEV----AFGPRQLglsaaMVAQRVADClqltdcanladrvPYQLSGGEKKRVALASVL 155
Cdd:cd03369 81 RSSLTIIPQ--DPTLFSGTIRSNLdpfdEYSDEEI-----YGALRVSEG-------------GLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1729460384 156 ALNPEILLLDEPlnglTIAAQQQMLTLLQ---RLQAAGKTIIMASHNYQQV 203
Cdd:cd03369 141 LKRPRVLVLDEA----TASIDYATDALIQktiREEFTNSTILTIAHRLRTI 187
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-204 |
5.34e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 5.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729460384 139 YQLSGGEKKRVALASVL---ALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVQ 204
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK 876
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
138-199 |
5.90e-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: 43.15 E-value: 5.90e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1729460384 138 PYQLSGGEKKRVALASVLAL---NPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHN 199
Cdd:pfam13304 234 AFELSDGTKRLLALLAALLSalpKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHS 298
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-49 |
1.07e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 1.07e-04
10 20 30
....*....|....*....|....*....|...
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLSG 49
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-211 |
1.19e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729460384 135 DRVPYQLSGGEKKRVALASVLA--LNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQQVqAVGERFI 211
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGaeLIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRII 548
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
17-199 |
1.21e-04 |
|
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: 41.19 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 17 LKDLSLTVNSGDFICLMGPNGSGKSTLLRLLsGLAsptsgayqfhdqpitttyLADAQNRQqlhqrigmvfqntdvqlfn 96
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAI-GLA------------------LGGAQSAT------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 97 tsvteevafGPRQLGLSAAMVAQRVADCLQLTDcanladrvpyQLSGGEKKRVALASVLAL---NPEIL-LLDEPLNGLT 172
Cdd:cd03227 53 ---------RRRSGVKAGCIVAAVSAELIFTRL----------QLSGGEKELSALALILALaslKPRPLyILDEIDRGLD 113
|
170 180
....*....|....*....|....*..
gi 1729460384 173 IAAQQQMLTLLQRLQAAGKTIIMASHN 199
Cdd:cd03227 114 PRDGQALAEAILEHLVKGAQVIVITHL 140
|
|
| DUF2813 |
pfam11398 |
Protein of unknown function (DUF2813); This entry contains YjbD from Escherichia coli, which ... |
16-143 |
1.65e-04 |
|
Protein of unknown function (DUF2813); This entry contains YjbD from Escherichia coli, which is annotated as a nucleotide triphosphate hydrolase.
Pssm-ID: 431868 [Multi-domain] Cd Length: 372 Bit Score: 41.96 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 16 GLKDLSLTVNSgdFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPITTTYlaDAQNRQQLHQRIGMVFQNTDVQlf 95
Cdd:pfam11398 13 GINRLSLHFDQ--LTVLIGENAWGKSSLLDALSLLLNPTKELYQFTLDDFHQPY--AIENEPTRHLQIIFTFKESAPG-- 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1729460384 96 ntsvtEEVAfgPRQLGLSAAMVaqrvadclqltDCANLADRVPYQLSG 143
Cdd:pfam11398 87 -----EHKA--RRYRSLSALWV-----------PHKDGYQRIYYRVEG 116
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
21-52 |
3.16e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.07 E-value: 3.16e-04
10 20 30
....*....|....*....|....*....|....*
gi 1729460384 21 SLTVNSGDFICLMGPNGSGKSTL---LRLLSGLAS 52
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLldaLRFLSDAAR 49
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
16-198 |
7.84e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 39.95 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 16 GLKDLSLTVnsGDFICLMGPNGSGKSTLLRLLSGLAS-------------PTSGAYQFHDQ-------PITTTYLADAQN 75
Cdd:COG4938 11 PFKEAELEL--KPLTLLIGPNGSGKSTLIQALLLLLQsnfiylpaersgpARLYPSLVRELsdlgsrgEYTADFLAELEN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 76 RQQLH--------------QRIGMVFQNTDVQLFNTSVTEEVAFGPRQLGLSAAMVAQRVAdclqltdcanladrVPyql 141
Cdd:COG4938 89 LEILDdkskelleqveewlEKIFPGKVEVDASSDLVRLVFRPSGNGKRIPLSNVGSGVSEL--------------LP--- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1729460384 142 sggekkrVALASVLALNP-EILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASH 198
Cdd:COG4938 152 -------ILLALLSAAKPgSLLIIEEPEAHLHPKAQSALAELLAELANSGVQVIIETH 202
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
29-62 |
2.21e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.52 E-value: 2.21e-03
10 20 30
....*....|....*....|....*....|....
gi 1729460384 29 FICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHD 62
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTD 34
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-201 |
2.25e-03 |
|
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: 38.84 E-value: 2.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1729460384 141 LSGGEKKRVALASVL--ALNPEILLLDEPLNGLTIAAQQQMLTLLQRLQAAGKTIIMASHNYQ 201
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED 551
|
|
| DTMP_kinase |
TIGR00041 |
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ... |
26-220 |
4.41e-03 |
|
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage pathways of DTTP synthesis. Catalytic activity: ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 161676 Cd Length: 195 Bit Score: 36.96 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 26 SGDFICLMGPNGSGKSTLLRLLSGLASPTSGAYQFHDQPiTTTYLADAQNRQQLHQRIGMVFQNTDVQLFNTSVTEEVaf 105
Cdd:TIGR00041 2 RGMFIVIEGIDGAGKTTQANLLKKLLQENGYDVLFTREP-GGTPIGEKIRELLLNENDEPLTDKAEALLFAADRHEHL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729460384 106 gprQLGLSAAMvaqrvadclqLTDCANLADR-----VPYQlsgGEKKRVALASVLALNPEIlLLDEPlnGLTIAAQQQML 180
Cdd:TIGR00041 79 ---EDKIKPAL----------AEGKLVISDRyvfssIAYQ---GGARGIDEDLVLELNEDA-LGDMP--DLTIYLDIDPE 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1729460384 181 TLLQRLQAAG----------KTIIMASHNYQQVQAVGERFIIFNSTHQVD 220
Cdd:TIGR00041 140 VALERLRKRGeldreefeklDFFEKVRQRYLELADKEKSIHVIDATNSVE 189
|
|
| PrkA |
COG2766 |
Predicted Ser/Thr protein kinase [Signal transduction mechanisms]; |
32-47 |
6.82e-03 |
|
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
Pssm-ID: 442049 [Multi-domain] Cd Length: 675 Bit Score: 37.51 E-value: 6.82e-03
|
| |
