|
Name |
Accession |
Description |
Interval |
E-value |
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
23-212 |
2.06e-94 |
|
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: 276.61 E-value: 2.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 23 YEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTRLRTTVQLVVQDPDDQ 102
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 103 LFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDP 182
Cdd:TIGR01166 81 LFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180 190
....*....|....*....|....*....|
gi 664496302 183 DGQERLLATLDRLRAAGTTVLMATHDVDLA 212
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-244 |
9.25e-94 |
|
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: 276.14 E-value: 9.25e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRydRGGLTRLRTTVQ 93
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT--KKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 94 LVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLIL 173
Cdd:COG1122 79 LVFQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664496302 174 DEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGVH-TGPAAATLARTELLRQ 244
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVaDGTPREVFSDYELLEE 230
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-222 |
3.48e-79 |
|
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: 238.52 E-value: 3.48e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEEG-PPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRggLTRLRTTVQL 94
Cdd:cd03225 2 LKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS--LKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 95 VVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILD 174
Cdd:cd03225 80 VFQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 664496302 175 EPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALL 222
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-251 |
6.18e-76 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 232.66 E-value: 6.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 17 RGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTRLRTTVQLVV 96
Cdd:PRK13639 5 RDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 97 QDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEP 176
Cdd:PRK13639 85 QNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 664496302 177 TAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAAATLARTELLRQAGLRLPW 251
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKiIKEGTPKEVFSDIETIRKANLRLPR 240
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-250 |
1.56e-73 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 226.54 E-value: 1.56e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 19 VSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVryDRGGLTRLRTTVQLVVQD 98
Cdd:PRK13647 10 LHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV--NAENEKWVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 99 PDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTA 178
Cdd:PRK13647 88 PDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664496302 179 GLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGVHTGPAAATLARTELLRQAGLRLP 250
Cdd:PRK13647 168 YLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQAGLRLP 239
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
13-250 |
7.29e-70 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 217.41 E-value: 7.29e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 13 LVALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTRLRTTV 92
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 QLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLI 172
Cdd:PRK13636 85 GMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 173 LDEPTAGLDPDGQERLLATL-DRLRAAGTTVLMATHDVDLALRWADEVALLTPGGV-HTGPAAATLARTELLRQAGLRLP 250
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLvEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRViLQGNPKEVFAEKEMLRKVNLRLP 244
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-280 |
8.77e-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: 214.24 E-value: 8.77e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEEGPP----VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGG-LTRLRT 90
Cdd:TIGR04521 3 LKNVSYIYQPGTPfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKkLKDLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 91 TVQLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALD-IAALADRPTHLLSYGQRKRAAIAGAVAMRPR 169
Cdd:TIGR04521 83 KVGLVFQFPEHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGlDEEYLERSPFELSGGQMRRVAIAGVLAMEPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 170 VLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGGVH-TGPAAATLARTELLRQAGL 247
Cdd:TIGR04521 163 VLILDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVlDGTPREVFSDVDELEKIGL 242
|
250 260 270
....*....|....*....|....*....|...
gi 664496302 248 RLPWGVAAASVLRARGLLAESAagPRTAEELAA 280
Cdd:TIGR04521 243 DVPEITELARKLKEKGLPVPKD--PLTVEEAAD 273
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-253 |
1.07e-59 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 190.99 E-value: 1.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 13 LVALRGVSFAYEEgPPVLTGL--DFAVHEgrALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTRLRT 90
Cdd:PRK13638 1 MLATSDLWFRYQD-EPVLKGLnlDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 91 TVQLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRV 170
Cdd:PRK13638 78 QVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 171 LILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGVHT-GPAAATLARTELLRQAGLRL 249
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILThGAPGEVFACTEAMEQAGLTQ 237
|
....
gi 664496302 250 PWGV 253
Cdd:PRK13638 238 PWLV 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-248 |
3.93e-54 |
|
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: 3.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 4 PDRSTESTALVALRGVSFAYEEGPP----VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV- 78
Cdd:COG1123 251 APAAAAAEPLLEVRNLSKRYPVRGKggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLt 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 79 RYDRGGLTRLRTTVQLVVQDPDDQLFAA-SVAQDVSFGPLNLG-LSDAEVRSRVGEALAALD-IAALADRPTHLLSYGQR 155
Cdd:COG1123 331 KLSRRSLRELRRRVQMVFQDPYSSLNPRmTVGDIIAEPLRLHGlLSRAERRERVAELLERVGlPPDLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 156 KRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAA 233
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRiVEDGPTE 490
|
250
....*....|....*.
gi 664496302 234 ATLAR-TELLRQAGLR 248
Cdd:COG1123 491 EVFANpQHPYTRALLA 506
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-276 |
7.80e-54 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 176.15 E-value: 7.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 13 LVALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVryDRGGLTRLRTTV 92
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI--TKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 QLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLI 172
Cdd:PRK13652 81 GLVFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 173 LDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAAATLARTELLRQAGLRLP 250
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRiVAYGTVEEIFLQPDLLARVHLDLP 240
|
250 260
....*....|....*....|....*.
gi 664496302 251 WGVAAASVLRARGLLAESAAGPRTAE 276
Cdd:PRK13652 241 SLPKLIRSLQAQGIAIDMAYTYQEAE 266
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-279 |
6.11e-52 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 171.35 E-value: 6.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 13 LVALRGVSFAYEEGP-PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVryDRGGLTRLRTT 91
Cdd:PRK13635 5 IIRVEHISFRYPDAAtYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL--SEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 VQLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVL 171
Cdd:PRK13635 83 VGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 172 ILDEPTAGLDPDGQERLLATLDRLRAAGT-TVLMATHDVDLALRwADEVALLTPGGVHT-GPAAATLARTELLRQAGLRL 249
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEeGTPEEIFKSGHMLQEIGLDV 241
|
250 260 270
....*....|....*....|....*....|
gi 664496302 250 PWGVAAASVLRARGLLAESAAgpRTAEELA 279
Cdd:PRK13635 242 PFSVKLKELLKRNGILLPNTY--LTMESLV 269
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-264 |
1.60e-51 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 176.25 E-value: 1.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 11 TALVALRGVSFAYEEGP-PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHA---GRLTLGGEPVRydRGGLT 86
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLL--ELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 87 RLRTTVQLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAM 166
Cdd:COG1123 80 LRGRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 167 RPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPG-GVHTGPAAATLARTELLR- 243
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGrIVEDGPPEEILAAPQALAa 239
|
250 260
....*....|....*....|....*..
gi 664496302 244 ------QAGLRLPWGVAAASVLRARGL 264
Cdd:COG1123 240 vprlgaARGRAAPAAAAAEPLLEVRNL 266
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-251 |
4.28e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 165.26 E-value: 4.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 10 STALVALRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGgltrlr 89
Cdd:COG1121 3 MMPAIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARR------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 90 tTVQLVVQDPD-DQLFAASVAQDVSFG-----PLNLGLSDAEvRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGA 163
Cdd:COG1121 76 -RIGYVPQRAEvDWDFPITVRDVVLMGrygrrGLFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 164 VAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGVHTGPAAATLARTELLR 243
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENLSR 233
|
....*...
gi 664496302 244 QAGLRLPW 251
Cdd:COG1121 234 AYGGPVAL 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-280 |
3.06e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 159.42 E-value: 3.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 19 VSFAYEEGPP----VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV--RYDRGGLTRLRTTV 92
Cdd:PRK13634 8 VEHRYQYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItaGKKNKKLKPLRKKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 QLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAAL-DIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVL 171
Cdd:PRK13634 88 GIVFQFPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVgLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 172 ILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGGV-HTGPAAATLARTELLRQAGLRL 249
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVfLQGTPREIFADPDELEAIGLDL 247
|
250 260 270
....*....|....*....|....*....|..
gi 664496302 250 PWGVAAASVLRAR-GLLAESAagPRTAEELAA 280
Cdd:PRK13634 248 PETVKFKRALEEKfGISFPKP--CLTLEELAH 277
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-263 |
5.10e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 158.67 E-value: 5.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 18 GVSFAYEEGPP----VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTRLRTTVQ 93
Cdd:PRK13637 7 NLTHIYMEGTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 94 LVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAA--LDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVL 171
Cdd:PRK13637 87 LVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 172 ILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVDLALRWADEVALLTPGGVH-TGPAAATLARTELLRQAGLRL 249
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCElQGTPREVFKEVETLESIGLAV 246
|
250
....*....|....
gi 664496302 250 PWGVAAASVLRARG 263
Cdd:PRK13637 247 PQVTYLVRKLRKKG 260
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-228 |
3.04e-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: 154.34 E-value: 3.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 18 GVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYdrgglTRLRTTVQLVVQ 97
Cdd:cd03226 4 NISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-----KERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 98 DPDDQLFAASVAQDVSFGPLNLGLSDAEVRsrvgEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPT 177
Cdd:cd03226 79 DVDYQLFTDSVREELLLGLKELDAGNEQAE----TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 664496302 178 AGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGVH 228
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-264 |
3.12e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 156.40 E-value: 3.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 19 VSFAYEEG-----PPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRyDRGGLTRLRTTVQ 93
Cdd:PRK13633 10 VSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS-DEENLWDIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 94 LVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLIL 173
Cdd:PRK13633 89 MVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 174 DEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRwADEVALLTPGGV-HTGPAAATLARTELLRQAGLRLPW 251
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVvMEGTPKEIFKEVEMMKKIGLDVPQ 247
|
250
....*....|...
gi 664496302 252 GVAAASVLRARGL 264
Cdd:PRK13633 248 VTELAYELKKEGV 260
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-245 |
9.55e-46 |
|
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: 154.43 E-value: 9.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 13 LVALRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRLRTt 91
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaSLSRRELARRIA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 vqLVVQDPDDQlFAASVAQDVSFGPL----NLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMR 167
Cdd:COG1120 79 --YVPQEPPAP-FGLTVRELVALGRYphlgLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 168 PRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGGVH-TGPAAATLaRTELLRQA 245
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVaQGPPEEVL-TPELLEEV 234
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
11-264 |
1.92e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 154.50 E-value: 1.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 11 TALVALRGVSFAYEEGP--PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRggLTRL 88
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN--VWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 89 RTTVQLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRP 168
Cdd:PRK13650 80 RHKIGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 169 RVLILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVD-LALrwADEVALLTPGGVHTGPAAATL-ARTELLRQA 245
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDeVAL--SDRVLVMKNGQVESTSTPRELfSRGNDLLQL 237
|
250
....*....|....*....
gi 664496302 246 GLRLPWGVAAASVLRARGL 264
Cdd:PRK13650 238 GLDIPFTTSLVQSLRQNGY 256
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-279 |
1.97e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 154.52 E-value: 1.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPP----VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGG--LTR 87
Cdd:PRK13649 3 INLQNVSYTYQAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 88 LRTTVQLVVQDPDDQLFAASVAQDVSFGPLNLGLS--DAEVRSRVGEALAALDIAALADRPTHLlSYGQRKRAAIAGAVA 165
Cdd:PRK13649 83 IRKKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSqeEAEALAREKLALVGISESLFEKNPFEL-SGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 166 MRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAAATLARTELLRQ 244
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKlVLSGKPKDIFQDVDFLEE 241
|
250 260 270
....*....|....*....|....*....|....*
gi 664496302 245 AGLRLPWGVAAASVLRARGLLAESAagPRTAEELA 279
Cdd:PRK13649 242 KQLGVPKITKFAQRLADRGISFSSL--PITIEEFR 274
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-279 |
8.05e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 153.06 E-value: 8.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 19 VSFAYEEGPPV----LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRG--GLTRLRTTV 92
Cdd:PRK13641 8 VDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnkNLKKLRKKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 QLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRS-------RVGealaalDIAALADRPTHLLSYGQRKRAAIAGAVA 165
Cdd:PRK13641 88 SLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEkalkwlkKVG------LSEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 166 MRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGV--HTGPaAATLARTELLR 243
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLikHASP-KEIFSDKEWLK 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 664496302 244 QAGLRLPWGVAAASVLRARGLlaESAAGPRTAEELA 279
Cdd:PRK13641 241 KHYLDEPATSRFASKLEKGGF--KFSEMPLTIDELV 274
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
16-227 |
2.37e-44 |
|
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: 150.34 E-value: 2.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEEGPpVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRLRTTVQL 94
Cdd:cd03261 3 LRGLTKSFGGRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsGLSEAELYRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 95 VVQDPddQLFAA-SVAQDVSFgPL--NLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVL 171
Cdd:cd03261 82 LFQSG--ALFDSlTVFENVAF-PLreHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 664496302 172 ILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVDLALRWADEVALLTPGGV 227
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-245 |
2.52e-44 |
|
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: 2.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 13 LVALRGVSFAYEEGP---PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGltRLR 89
Cdd:COG1124 1 MLEVRNLSVSYGQGGrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK--AFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 90 TTVQLVVQDPddqlFAA-----SVAQDVSFGPLNLGLSDAEVR-----SRVGealaaLDIAALADRPtHLLSYGQRKRAA 159
Cdd:COG1124 79 RRVQMVFQDP----YASlhprhTVDRILAEPLRIHGLPDREERiaellEQVG-----LPPSFLDRYP-HQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 160 IAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVDLALRWADEVALLtpggvHTGPAAATLAR 238
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVM-----QNGRIVEELTV 223
|
....*..
gi 664496302 239 TELLRQA 245
Cdd:COG1124 224 ADLLAGP 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-211 |
7.48e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 145.97 E-value: 7.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRLRTTV 92
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsRLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 QLVVQDPddQLFAA-SVAQDVSFgPLN-LGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRV 170
Cdd:COG2884 82 GVVFQDF--RLLPDrTVYENVAL-PLRvTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 664496302 171 LILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDL 211
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLEL 199
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-222 |
7.98e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 146.36 E-value: 7.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPpVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRgglTRLRTTVQ 93
Cdd:COG1131 1 IEVRGLTKRYGDKT-ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP---AEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 94 LVVQDP--DDQLfaaSVAQDVSF-GPLNlGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRV 170
Cdd:COG1131 77 YVPQEPalYPDL---TVRENLRFfARLY-GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 664496302 171 LILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALL 222
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAII 204
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
13-281 |
1.65e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 146.67 E-value: 1.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 13 LVALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGepvrYDRGGLTRL---R 89
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG----IDTGDFSKLqgiR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 90 TTVQLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPR 169
Cdd:PRK13644 77 KLVGIVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 170 VLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDlALRWADEVALLTPGGVHTGPAAATLARTELLRQAGLRL 249
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTP 235
|
250 260 270
....*....|....*....|....*....|....*
gi 664496302 250 PWGVAAASVLRARGLLA--ESAAGPRT-AEELAAL 281
Cdd:PRK13644 236 PSLIELAENLKMHGVVIpwENTSSPSSfAEEICRL 270
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-222 |
1.99e-42 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 145.51 E-value: 1.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 10 STALVALRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRL 88
Cdd:COG1127 2 SEPMIEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 89 RTTVQLVVQdpddqlFAA-----SVAQDVSFgPL--NLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIA 161
Cdd:COG1127 81 RRRIGMLFQ------GGAlfdslTVFENVAF-PLreHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664496302 162 GAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVDLALRWADEVALL 222
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVL 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
16-225 |
1.26e-41 |
|
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: 142.66 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEEGPpVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVrydrGGLTRLRTTVQLV 95
Cdd:cd03259 3 LKGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV----TGVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 96 VQDPddQLFA-ASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILD 174
Cdd:cd03259 78 FQDY--ALFPhLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 664496302 175 EPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:cd03259 156 EPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
18-222 |
1.90e-41 |
|
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: 141.90 E-value: 1.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 18 GVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGltrlrttVQLVVQ 97
Cdd:cd03235 4 DLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-------IGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 98 DPD-DQLFAASVAQDVSFGPLN----LGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLI 172
Cdd:cd03235 76 RRSiDRDFPISVRDVVLMGLYGhkglFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 664496302 173 LDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALL 222
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
10-250 |
3.18e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 143.21 E-value: 3.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 10 STALVALRGVSFAY-EEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRggLTRL 88
Cdd:PRK13632 4 KSVMIKVENVSFSYpNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN--LKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 89 RTTVQLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRP 168
Cdd:PRK13632 82 RKKIGIIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 169 RVLILDEPTAGLDPDGQERLLATLDRLRAAGT-TVLMATHDVDLALRwADEVALLTPGG-VHTGPAAATLARTELLRQAG 246
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAIL-ADKVIVFSEGKlIAQGKPKEILNNKEILEKAK 240
|
....
gi 664496302 247 LRLP 250
Cdd:PRK13632 241 IDSP 244
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-222 |
3.70e-41 |
|
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: 139.84 E-value: 3.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPpVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRyDRGGLTRLRTtvq 93
Cdd:cd03230 1 IEVRNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK-KEPEEVKRRI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 94 lvvqdpddqlfaASVAQDVSFgPLNLglsdaevrsRVGEalaaldiaaladrptHL-LSYGQRKRAAIAGAVAMRPRVLI 172
Cdd:cd03230 76 ------------GYLPEEPSL-YENL---------TVRE---------------NLkLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 664496302 173 LDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALL 222
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAIL 168
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
16-225 |
5.92e-41 |
|
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: 138.92 E-value: 5.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEEGPpVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRydRGGLTRLRTTVQLV 95
Cdd:cd00267 2 IENLSFRYGGRT-ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA--KLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 96 VQdpddqlfaasvaqdvsfgplnlglsdaevrsrvgealaaldiaaladrpthlLSYGQRKRAAIAGAVAMRPRVLILDE 175
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 664496302 176 PTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-228 |
3.27e-40 |
|
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: 137.95 E-value: 3.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 15 ALRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVrydrggltrlrttvql 94
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 95 vvqdpdDQLFAASVAQDVSFGPLNLGLSDAEvrsrvgealaaldiaALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILD 174
Cdd:cd03214 64 ------ASLSPKELARKIAYVPQALELLGLA---------------HLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 175 EPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGGVH 228
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-250 |
4.16e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 138.01 E-value: 4.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGP-PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHA---GRLTLGGepVRYDRGGLTRLR 89
Cdd:PRK13640 6 VEFKHVSFTYPDSKkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDG--ITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 90 TTVQLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPR 169
Cdd:PRK13640 84 EKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 170 VLILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVDLALRwADEVALLTPGGV-HTGPAAATLARTELLRQAGL 247
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANM-ADQVLVLDDGKLlAQGSPVEIFSKVEMLKEIGL 242
|
...
gi 664496302 248 RLP 250
Cdd:PRK13640 243 DIP 245
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
16-222 |
6.55e-39 |
|
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: 136.53 E-value: 6.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRgglTRLRTTVQLV 95
Cdd:COG4555 4 VENLSKKYG-KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP---REARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 96 VQDPDdqLFAASVAQDV--SFGPLNlGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLIL 173
Cdd:COG4555 80 PDERG--LYDRLTVRENirYFAELY-GLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 664496302 174 DEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALL 222
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVIL 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-222 |
9.10e-39 |
|
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: 133.66 E-value: 9.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGP-PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR-YDrggLTRLRTT 91
Cdd:cd03228 1 IEFKNVSFSYPGRPkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRdLD---LESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 VQLVVQDPddQLFAASVAQdvsfgplNlglsdaevrsrvgealaaldiaaladrpthLLSYGQRKRAAIAGAVAMRPRVL 171
Cdd:cd03228 78 IAYVPQDP--FLFSGTIRE-------N------------------------------ILSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 664496302 172 ILDEPTAGLDPDGQERLLATLDRLRaAGTTVLMATHDVDLALRwADEVALL 222
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRD-ADRIIVL 167
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-224 |
8.64e-38 |
|
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: 132.60 E-value: 8.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGP---PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR---YDRGgltr 87
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTgpgPDRG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 88 lrttvqLVVQDpdDQLFA-ASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAM 166
Cdd:cd03293 77 ------YVFQQ--DALLPwLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664496302 167 RPRVLILDEPTAGLDP----DGQERLLATLDRlraAGTTVLMATHDVDLALRWADEVALLTP 224
Cdd:cd03293 149 DPDVLLLDEPFSALDAltreQLQEELLDIWRE---TGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-280 |
8.84e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 134.75 E-value: 8.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPP----VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLT--- 86
Cdd:PRK13645 7 IILDNVSYTYAKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 87 RLRTTVQLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAAL-ADRPTHLLSYGQRKRAAIAGAVA 165
Cdd:PRK13645 87 RLRKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 166 MRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGGV-HTGPAAATLARTELLR 243
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKViSIGSPFEIFSNQELLT 246
|
250 260 270
....*....|....*....|....*....|....*....
gi 664496302 244 QAGLRLPWGVAAASVLRARG--LLAESAagpRTAEELAA 280
Cdd:PRK13645 247 KIEIDPPKLYQLMYKLKNKGidLLNKNI---RTIEEFAK 282
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-264 |
9.38e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 134.86 E-value: 9.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 13 LVALRGVSFAYEEGPP----VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRY--DRGGLT 86
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStsKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 87 RLRTTVQLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHL-LSYGQRKRAAIAGAVA 165
Cdd:PRK13643 81 PVRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFeLSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 166 MRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAAATLARTELLRQ 244
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHiISCGTPSDVFQEVDFLKA 240
|
250 260
....*....|....*....|
gi 664496302 245 AGLRLPWGVAAASVLRARGL 264
Cdd:PRK13643 241 HELGVPKATHFADQLQKTGA 260
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-219 |
1.44e-37 |
|
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: 132.23 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGP---PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRLR 89
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 90 -TTVQLVVQD----PDdqlfaASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAV 164
Cdd:cd03255 81 rRHIGFVFQSfnllPD-----LTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 664496302 165 AMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLAlRWADEV 219
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELA-EYADRI 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
16-225 |
1.46e-37 |
|
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: 130.77 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEEgPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTRLRTTVQLV 95
Cdd:cd03229 3 LKNVSKRYGQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 96 VQDPddQLFA-ASVAQDVSFGplnlglsdaevrsrvgealaaldiaaladrpthlLSYGQRKRAAIAGAVAMRPRVLILD 174
Cdd:cd03229 82 FQDF--ALFPhLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 664496302 175 EPTAGLDPDGQERLLATLDRLRA-AGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-238 |
4.66e-37 |
|
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: 139.20 E-value: 4.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAY-EEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR-YDrggLTRLRTT 91
Cdd:COG2274 474 IELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqID---PASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 VQLVVQDpdDQLFAASVAQDVSFGplNLGLSDAEVR--------------------SRVGEALAAldiaaladrpthlLS 151
Cdd:COG2274 551 IGVVLQD--VFLFSGTIRENITLG--DPDATDEEIIeaarlaglhdfiealpmgydTVVGEGGSN-------------LS 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 152 YGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLrAAGTTVLMATHDVDLaLRWADEVALLTPGG-VHTG 230
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLST-IRLADRIIVLDKGRiVEDG 691
|
....*...
gi 664496302 231 PAAATLAR 238
Cdd:COG2274 692 THEELLAR 699
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-222 |
5.12e-37 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 131.09 E-value: 5.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 13 LVALRGVSFAYEEG---PPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRL 88
Cdd:cd03257 1 LLEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 89 RTTVQLVVQDPddqlFAA-----SVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPT---HLLSYGQRKRAAI 160
Cdd:cd03257 81 RKEIQMVFQDP----MSSlnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNrypHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664496302 161 AGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVDLALRWADEVALL 222
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVM 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
11-219 |
6.38e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 130.55 E-value: 6.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 11 TALVALRGVSFAYEEGP---PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLT 86
Cdd:COG1136 2 SPLLELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 87 RLR-TTVQLVVQDPddQLFAA-SVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAV 164
Cdd:COG1136 82 RLRrRHIGFVFQFF--NLLPElTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 664496302 165 AMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLAlRWADEV 219
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELA-ARADRV 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
10-222 |
6.66e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.07 E-value: 6.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 10 STALVALRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR----YDRGgl 85
Cdd:COG3842 2 AMPALELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglppEKRN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 86 trlrttVQLVVQDPDdqLFA-ASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAV 164
Cdd:COG3842 79 ------VGMVFQDYA--LFPhLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 664496302 165 AMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALL 222
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVM 209
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
16-264 |
6.94e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 132.90 E-value: 6.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEEGPP----VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRL------------TLGGEPVR 79
Cdd:PRK13651 5 VKNIVKIFNKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkkTKEKEKVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 80 YDRG-GLTR---------LRTTVQLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAAL-ADRPTH 148
Cdd:PRK13651 85 EKLViQKTRfkkikkikeIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESyLQRSPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 149 LLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGG-V 227
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKiI 244
|
250 260 270
....*....|....*....|....*....|....*..
gi 664496302 228 HTGPAAATLARTELLRQAGLRLPWGVAAASVLRARGL 264
Cdd:PRK13651 245 KDGDTYDILSDNKFLIENNMEPPKLLNFVNKLEKKGI 281
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-221 |
2.60e-36 |
|
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: 128.37 E-value: 2.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 12 ALVALRGVSFAYEEgPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTRlrtt 91
Cdd:COG4133 1 MMLEAENLSCRRGE-RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 vQLVVQDPDDQLFAA-SVAQDVSFGPLNLGLSDAevRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRV 170
Cdd:COG4133 76 -RLAYLGHADGLKPElTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 664496302 171 LILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDvDLALRWADEVAL 221
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ-PLELAAARVLDL 202
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-225 |
1.08e-35 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 127.74 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRydrgGLTRLRTTVQ 93
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT----NLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 94 LVVQDPddQLFA-ASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLI 172
Cdd:cd03300 76 TVFQNY--ALFPhLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 664496302 173 LDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKG 207
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-264 |
1.88e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 128.29 E-value: 1.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 13 LVALRGVSFAYEEGPPV--LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEpvRYDRGGLTRLRT 90
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE--LLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 91 TVQLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRV 170
Cdd:PRK13642 82 KIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 171 LILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVDLALRwADEVALLTPGGVHTGPAAATL-ARTELLRQAGLR 248
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELfATSEDMVEIGLD 240
|
250
....*....|....*.
gi 664496302 249 LPWGVAAASVLRARGL 264
Cdd:PRK13642 241 VPFSSNLMKDLRKNGF 256
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
10-259 |
4.81e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 127.17 E-value: 4.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 10 STALVALRGVSFAYE-EGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVryDRGGLTRL 88
Cdd:PRK13648 4 KNSIIVFKNVSFQYQsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI--TDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 89 RTTVQLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRP 168
Cdd:PRK13648 82 RKHIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 169 RVLILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVDLALRwADEVALLTPGGVH-TGPAAATLARTELLRQAG 246
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYkEGTPTEIFDHAEELTRIG 240
|
250
....*....|...
gi 664496302 247 LRLPWGVAAASVL 259
Cdd:PRK13648 241 LDLPFPIKINQML 253
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
13-279 |
4.82e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 128.43 E-value: 4.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 13 LVALRGVSFAYEEGPP----VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLG----GEPVRYDRGG 84
Cdd:PRK13631 21 ILRVKNLYCVFDEKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 85 LT----------RLRTTVQLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAAL-ADRPTHLLSYG 153
Cdd:PRK13631 101 TNpyskkiknfkELRRRVSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 154 QRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPA 232
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKiLKTGTP 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 664496302 233 AATLARTELLRQAGLRLPWGVAAASVLRARGLLAESAAG--PRTAEELA 279
Cdd:PRK13631 261 YEIFTDQHIINSTSIQVPRVIQVINDLIKKDPKYKKLYQkqPRTIEQLA 309
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-240 |
1.37e-34 |
|
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: 131.03 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRydRGGLTRLRTTVQ 93
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS--DLDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 94 LVVQDPddQLFAASVAQDVSFGplNLGLSDAEVR--------------------SRVGEALAAldiaaladrpthlLSYG 153
Cdd:COG4988 415 WVPQNP--YLFAGTIRENLRLG--RPDASDEELEaaleaagldefvaalpdgldTPLGEGGRG-------------LSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 154 QRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLrAAGTTVLMATHDVDLaLRWADEVALLTPGGVHTGPAA 233
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLAL-LAQADRILVLDDGRIVEQGTH 555
|
....*..
gi 664496302 234 ATLARTE 240
Cdd:COG4988 556 EELLAKN 562
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-225 |
1.48e-34 |
|
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: 125.11 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR-YDrggLTRLRTTV 92
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReQD---PVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 QLVVQDPDdqLFA-ASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAAL--ADRPTHLLSYGQRKRAAIAGAVAMRPR 169
Cdd:cd03295 78 GYVIQQIG--LFPhMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 664496302 170 VLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNG 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-225 |
1.83e-34 |
|
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: 124.22 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPpVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSG-----GLRPHAGRLTLGGEPVRYDRGGLTRL 88
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 89 RTTVQLVVQDPDdqLFAASVAQDVSFGP-LNLGLSDAEVRSRVGEALAALDIAALADRPTHL--LSYGQRKRAAIAGAVA 165
Cdd:cd03260 80 RRRVGMVFQKPN--PFPGSIYDNVAYGLrLHGIKLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 166 MRPRVLILDEPTAGLDPDGQERLLATLDRLRAAgTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNG 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-207 |
2.57e-34 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 130.67 E-value: 2.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR-YDrggLTRLRTTV 92
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRdLT---LESLRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 QLVVQDPddQLFAASVAQDVSFGplNLGLSDAEVR--------------------SRVGEALAAldiaaladrpthlLSY 152
Cdd:COG1132 417 GVVPQDT--FLFSGTIRENIRYG--RPDATDEEVEeaakaaqahefiealpdgydTVVGERGVN-------------LSG 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 153 GQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRaAGTTVLMATH 207
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAH 533
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
29-222 |
5.13e-34 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 123.32 E-value: 5.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGE------PVRYDRGGLTRlrtTVQLVvqdpddQ 102
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglpPHEIARLGIGR---TFQIP------R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 103 LF-----------AASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVL 171
Cdd:cd03219 86 LFpeltvlenvmvAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 664496302 172 ILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALL 222
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVL 216
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
13-214 |
7.76e-34 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 122.36 E-value: 7.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 13 LVALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRLRTT 91
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVnRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 VQLVVQDpDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVL 171
Cdd:TIGR02673 81 IGVVFQD-FRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 664496302 172 ILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALR 214
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDR 202
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-227 |
1.12e-33 |
|
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: 120.78 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEEG-PPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRydRGGLTRLRTTVQL 94
Cdd:cd03246 3 VENVSFRYPGAePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS--QWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 95 VVQdpDDQLFAASVAQDVsfgplnlglsdaevrsrvgealaaldiaaladrpthlLSYGQRKRAAIAGAVAMRPRVLILD 174
Cdd:cd03246 81 LPQ--DDELFSGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 664496302 175 EPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLaLRWADEVALLTPGGV 227
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPET-LASADRILVLEDGRV 173
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
12-219 |
1.43e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 122.47 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 12 ALVALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRLRT 90
Cdd:COG3638 1 PMLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtALRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 91 TVQLVVQDPD--DQLfaaSVAQDVSFGPLN--------LGLSDAEVR-------SRVGealaaldIAALADRPTHLLSYG 153
Cdd:COG3638 81 RIGMIFQQFNlvPRL---SVLTNVLAGRLGrtstwrslLGLFPPEDReralealERVG-------LADKAYQRADQLSGG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 664496302 154 QRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEV 219
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRI 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
11-236 |
3.39e-33 |
|
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: 121.73 E-value: 3.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 11 TALVALRGVSFAYEEGPpVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRP-HAGRLTLGGEpvryDRGG--LTR 87
Cdd:COG1119 1 DPLLELRNVTVRRGGKT-ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGE----RRGGedVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 88 LRTTVQLVVQDPDDQLFAASVAQDV----SFGplNLGLS---DAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAI 160
Cdd:COG1119 76 LRKRIGLVSPALQLRFPRDETVLDVvlsgFFD--SIGLYrepTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 664496302 161 AGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAG-TTVLMATHDVDLALRWADEVALLTPGGV-HTGPAAATL 236
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVvAAGPKEEVL 231
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-222 |
9.39e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 121.75 E-value: 9.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYD-----------RGGLTRLrtTVQlvvq 97
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEdrrrigylpeeRGLYPKM--KVG---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 98 dpdDQLfaasvaqdVSFGPLNlGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPT 177
Cdd:COG4152 90 ---EQL--------VYLARLK-GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 664496302 178 AGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALL 222
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVII 202
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-222 |
1.43e-32 |
|
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: 117.53 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDrggltrlrttvq 93
Cdd:cd03216 1 LELRGITKRFG-GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 94 lvvqDPDDQLFA--ASVAQdvsfgplnlglsdaevrsrvgealaaldiaaladrpthlLSYGQRKRAAIAGAVAMRPRVL 171
Cdd:cd03216 68 ----SPRDARRAgiAMVYQ---------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 664496302 172 ILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALL 222
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVL 155
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-250 |
2.23e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 120.65 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 19 VSFAYEEGPP----VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRY---DRGgLTRLRTT 91
Cdd:PRK13646 8 VSYTYQKGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkDKY-IRPVRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 VQLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHL-LSYGQRKRAAIAGAVAMRPRV 170
Cdd:PRK13646 87 IGMVFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFqMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 171 LILDEPTAGLDPDGQERLLATLDRLRA-AGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAAATLARTELLRQAGLR 248
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQTdENKTIILVSHDMNEVARYADEVIVMKEGSiVSQTSPKELFKDKKKLADWHIG 246
|
..
gi 664496302 249 LP 250
Cdd:PRK13646 247 LP 248
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
29-225 |
3.66e-32 |
|
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: 117.77 E-value: 3.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRG----------GLTRlRTTVQlvvqd 98
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARnrigylpeerGLYP-KMKVI----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 99 pdDQLfaasvaqdVSFGPLNlGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTA 178
Cdd:cd03269 89 --DQL--------VYLAQLK-GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 664496302 179 GLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
30-178 |
4.73e-32 |
|
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: 115.82 E-value: 4.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 30 LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRggLTRLRTTVQLVVQDPddQLF-AASV 108
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE--RKSLRKEIGYVFQDP--QLFpRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664496302 109 AQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRP----THLLSYGQRKRAAIAGAVAMRPRVLILDEPTA 178
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-222 |
8.02e-32 |
|
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: 118.22 E-value: 8.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 10 STALVALRGVS--FAyeeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV------RYD 81
Cdd:COG0411 1 SDPLLEVRGLTkrFG---GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglpphRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 82 RGGLTRlrtTVQLVvqdpddQLF-----------AASVAQDVSFGPLNLGL-----SDAEVRSRVGEALAALDIAALADR 145
Cdd:COG0411 78 RLGIAR---TFQNP------RLFpeltvlenvlvAAHARLGRGLLAALLRLprarrEEREARERAEELLERVGLADRADE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 664496302 146 PTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVDLALRWADEVALL 222
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVL 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
29-225 |
3.54e-31 |
|
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: 115.32 E-value: 3.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTRLRTTVQLVVQDPDdqLFA-AS 107
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGMVFQQFN--LFPhLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 108 VAQDVSFGPLN-LGLSDAEVRS-------RVGealaalDIAALADRPTHLlSYGQRKRAAIAGAVAMRPRVLILDEPTAG 179
Cdd:cd03262 93 VLENITLAPIKvKGMSKAEAEEralelleKVG------LADKADAYPAQL-SGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 664496302 180 LDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:cd03262 166 LDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
16-227 |
3.95e-31 |
|
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: 115.29 E-value: 3.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEEGP-PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRgglTRLRTTVQL 94
Cdd:cd03263 3 IRNLTKTYKKGTkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR---KAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 95 VVQDpdDQLFAA-SVAQDVSF-GPLNlGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLI 172
Cdd:cd03263 80 CPQF--DALFDElTVREHLRFyARLK-GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 173 LDEPTAGLDPDGQERLLATLDRLRaAGTTVLMATHDVDLALRWADEVALLTPGGV 227
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
16-237 |
6.05e-31 |
|
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: 114.84 E-value: 6.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSfAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRydrgGLT---RLRTTV 92
Cdd:cd03224 3 VENLN-AGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT----GLPpheRARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 QLVVQDpdDQLFAA-SVAQdvsfgplNLglsdaevrsRVGEALAALDIAALA---------------DRPTHLLSYGQRK 156
Cdd:cd03224 78 GYVPEG--RRIFPElTVEE-------NL---------LLGAYARRRAKRKARlervyelfprlkerrKQLAGTLSGGEQQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 157 RAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAAAT 235
Cdd:cd03224 140 MLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRvVLEGTAAEL 219
|
..
gi 664496302 236 LA 237
Cdd:cd03224 220 LA 221
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
10-245 |
6.98e-31 |
|
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: 120.64 E-value: 6.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 10 STALVALRGVSFAY-EEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR-YDRgglTR 87
Cdd:COG4987 330 GGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdLDE---DD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 88 LRTTVQLVVQDPDdqLFAASVAQDVSFGplNLGLSDAEVR--------------------SRVGEALAAldiaaladrpt 147
Cdd:COG4987 407 LRRRIAVVPQRPH--LFDTTLRENLRLA--RPDATDEELWaalervglgdwlaalpdgldTWLGEGGRR----------- 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 148 hlLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLrAAGTTVLMATHDvDLALRWADEVALLTPGG- 226
Cdd:COG4987 472 --LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHR-LAGLERMDRILVLEDGRi 547
|
250
....*....|....*....
gi 664496302 227 VHTGPAAATLARTELLRQA 245
Cdd:COG4987 548 VEQGTHEELLAQNGRYRQL 566
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
28-245 |
2.82e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.10 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 28 PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRLR------TTVQlvvqdpd 100
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLaDWSPAELARRRavlpqhSSLS------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 101 dqlFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIA------GAVAMRPRVLILD 174
Cdd:PRK13548 89 ---FPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArvlaqlWEPDGPPRWLLLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664496302 175 EPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGGVH-TGPAAATLaRTELLRQA 245
Cdd:PRK13548 166 EPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVaDGTPAEVL-TPETLRRV 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-235 |
3.85e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.20 E-value: 3.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 10 STALVALRGVS--FAyeeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRY------- 80
Cdd:COG1129 1 AEPLLEMRGISksFG---GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFrsprdaq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 81 DRGgltrlrttVQLVVQDPD--DQLfaaSVAQDVSFG--PLNLGLSD-AEVRSRVGEALAALDIAALADRPTHLLSYGQR 155
Cdd:COG1129 78 AAG--------IAIIHQELNlvPNL---SVAENIFLGrePRRGGLIDwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 156 KRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAAA 234
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRlVGTGPVAE 226
|
.
gi 664496302 235 T 235
Cdd:COG1129 227 L 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
28-222 |
4.92e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 113.17 E-value: 4.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 28 PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTRLRTTVQLVVQDPddQLFA-A 106
Cdd:COG1126 15 EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVGMVFQQF--NLFPhL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 107 SVAQDVSFGPLN-LGLSDAEVRS-------RVGealaalDIAALADRPTHLlSYGQRKRAAIAGAVAMRPRVLILDEPTA 178
Cdd:COG1126 93 TVLENVTLAPIKvKKMSKAEAEEramelleRVG------LADKADAYPAQL-SGGQQQRVAIARALAMEPKVMLFDEPTS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 664496302 179 GLDPdgqER---LLATLDRLRAAGTTVLMATHDVDLALRWADEVALL 222
Cdd:COG1126 166 ALDP---ELvgeVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFM 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
16-219 |
1.24e-29 |
|
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: 111.89 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGG-LTRLRTTVQL 94
Cdd:cd03256 3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKaLRQLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 95 VVQDPD--DQLfaaSVAQDVSFGPLN--------LGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAV 164
Cdd:cd03256 83 IFQQFNliERL---SVLENVLSGRLGrrstwrslFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 664496302 165 AMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEV 219
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRI 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
28-222 |
3.60e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 113.32 E-value: 3.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 28 PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGE------PVRyDRGgltrlrttVQLVVQDPDd 101
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftnlPPR-ERR--------VGFVFQHYA- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 102 qLFA-ASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGL 180
Cdd:COG1118 86 -LFPhMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 664496302 181 DP---DGQERLLATLdrLRAAGTTVLMATHDVDLALRWADEVALL 222
Cdd:COG1118 165 DAkvrKELRRWLRRL--HDELGGTTVFVTHDQEEALELADRVVVM 207
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
11-244 |
4.34e-29 |
|
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: 110.46 E-value: 4.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 11 TALVALRGVSFAYEEGPpVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPvrydrggLTRLRT 90
Cdd:COG0410 1 MPMLEVENLHAGYGGIH-VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED-------ITGLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 91 --TVQL-VVQDP-DDQLFAA-SVAQdvsfgplNLglsdaevrsRVGEALAALDIAALAD----------------RPTHL 149
Cdd:COG0410 73 hrIARLgIGYVPeGRRIFPSlTVEE-------NL---------LLGAYARRDRAEVRADlervyelfprlkerrrQRAGT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 150 LSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGG-VH 228
Cdd:COG0410 137 LSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRiVL 216
|
250
....*....|....*.
gi 664496302 229 TGPAAATLARTELLRQ 244
Cdd:COG0410 217 EGTAAELLADPEVREA 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
28-234 |
1.09e-28 |
|
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: 109.74 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 28 PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEpvryDRGGLTRLRTTVQLVVQDPddQLFA-A 106
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE----DATDVPVQERNVGFVFQHY--ALFRhM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 107 SVAQDVSFG----PLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDP 182
Cdd:cd03296 90 TVFDNVAFGlrvkPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664496302 183 DGQERLLATLDRLR-AAGTTVLMATHDVDLALRWADEVALL---------TPGGVHTGPAAA 234
Cdd:cd03296 170 KVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMnkgrieqvgTPDEVYDHPASP 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
11-225 |
8.38e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 110.31 E-value: 8.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 11 TALVALRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEpvryDRGGLTRLRT 90
Cdd:PRK11607 17 TPLLEIRNLTKSFD-GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV----DLSHVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 91 TVQLVVQDPddQLFA-ASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPR 169
Cdd:PRK11607 92 PINMMFQSY--ALFPhMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 664496302 170 VLILDEPTAGLDPDGQERL-LATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-228 |
8.90e-28 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 106.51 E-value: 8.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPpVLTGLDFAVHEGrALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRgglTRLRTTVQ 93
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP---QKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 94 LVVQDPD--------DQLFAASVAQdvsfgplnlGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVA 165
Cdd:cd03264 76 YLPQEFGvypnftvrEFLDYIAWLK---------GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664496302 166 MRPRVLILDEPTAGLDPDGQERLLATLDRLrAAGTTVLMATHDVDLALRWADEVALLTPGGVH 228
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
28-225 |
2.90e-27 |
|
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: 105.88 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 28 PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEpVRYDRGglTRLRTTVQLVVQDPDDQLFAAS 107
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRR--KKFLRRIGVVFGQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 108 VAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQER 187
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 664496302 188 LLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:cd03267 192 IRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
25-222 |
4.56e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 103.85 E-value: 4.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 25 EGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTlggepvrydRGGLTRLRTTVQlvvQDPDDQLF 104
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR---------RAGGARVAYVPQ---RSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 105 AASVAQDVSFG----PLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGL 180
Cdd:NF040873 71 PLTVRDLVAMGrwarRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 664496302 181 DPDGQERLLATLDRLRAAGTTVLMATHDVDLALRwADEVALL 222
Cdd:NF040873 151 DAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-207 |
6.59e-27 |
|
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: 104.21 E-value: 6.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGP-PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR-YDRgglTRLRTT 91
Cdd:cd03245 3 IEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqLDP---ADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 VQLVVQDPddQLFAASVAQDVSFGplNLGLSDAEVRsRVGEALAALDIAALADRPTHL--------LSYGQRKRAAIAGA 163
Cdd:cd03245 80 IGYVPQDV--TLFYGTLRDNITLG--APLADDERIL-RAAELAGVTDFVNKHPNGLDLqigergrgLSGGQRQAVALARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 664496302 164 VAMRPRVLILDEPTAGLDPDGQERLLATLDRLrAAGTTVLMATH 207
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITH 197
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
32-225 |
7.02e-27 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 104.37 E-value: 7.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 32 GLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLtrlRTTVQLVVQDP--DDQLFAASva 109
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREV---RRRIGIVFQDLsvDDELTGWE-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 110 QDVSFGPLnLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLL 189
Cdd:cd03265 93 NLYIHARL-YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVW 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 664496302 190 ATLDRLRAA-GTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:cd03265 172 EYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHG 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-211 |
8.94e-27 |
|
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: 104.03 E-value: 8.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRLRTTV 92
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 QLVVQDpDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLI 172
Cdd:cd03292 81 GVVFQD-FRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 664496302 173 LDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDL 211
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKEL 198
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
19-245 |
9.97e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 107.62 E-value: 9.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 19 VSFAyeeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYdrgglTRLRTTVQLVVQD 98
Cdd:PRK09536 11 VEFG---DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEA-----LSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 99 PDDQL--FAASVAQDVSFGPL----NLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLI 172
Cdd:PRK09536 83 PQDTSlsFEFDVRQVVEMGRTphrsRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664496302 173 LDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGVHTGPAAATLARTELLRQA 245
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAA 235
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
28-225 |
1.36e-26 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 105.55 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 28 PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGepvrYDrggLTR----LRTTVQLVVQD--PDD 101
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAG----YD---VVReprkVRRSIGIVPQYasVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 102 QLFAASvaQDVSFGPLnLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLD 181
Cdd:TIGR01188 80 DLTGRE--NLEMMGRL-YGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 664496302 182 PDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:TIGR01188 157 PRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHG 200
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-213 |
1.97e-26 |
|
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: 103.46 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 17 RGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRydrgGLTR--LRTTVQL 94
Cdd:cd03254 6 ENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR----DISRksLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 95 VVQDPddQLFAASVAQDVSFGplNLGLSDAEVR--------------------SRVGEALaaldiaaladrptHLLSYGQ 154
Cdd:cd03254 82 VLQDT--FLFSGTIMENIRLG--RPNATDEEVIeaakeagahdfimklpngydTVLGENG-------------GNLSQGE 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 155 RKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRaAGTTVLMATH------DVDLAL 213
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHrlstikNADKIL 208
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
14-207 |
3.68e-26 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 107.64 E-value: 3.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAY-EEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR-YDRgglTRLRTT 91
Cdd:TIGR03375 464 IEFRNVSFAYpGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRqIDP---ADLRRN 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 VQLVVQDPddQLFAASVAQDVSFGplNLGLSDAEVRS---RVGEALAALDIAALADRPTH----LLSYGQRKRAAIAGAV 164
Cdd:TIGR03375 541 IGYVPQDP--RLFYGTLRDNIALG--APYADDEEILRaaeLAGVTEFVRRHPDGLDMQIGergrSLSGGQRQAVALARAL 616
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 664496302 165 AMRPRVLILDEPTAGLDPDGQERLLATLDRLrAAGTTVLMATH 207
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTH 658
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-220 |
3.99e-26 |
|
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: 104.36 E-value: 3.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 19 VSFAYEEGP-PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHA---GRLTLGGEPV-RYDRGGLTRLR-TTV 92
Cdd:COG0444 9 VYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLlKLSEKELRKIRgREI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 QLVVQDP----------DDQLfaASVAQdvsfgpLNLGLSDAEVRSRVGEALAALDIAALADR----PtHLLSYGQRKRA 158
Cdd:COG0444 89 QMIFQDPmtslnpvmtvGDQI--AEPLR------IHGGLSKAEARERAIELLERVGLPDPERRldryP-HELSGGMRQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664496302 159 AIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVDLALRWADEVA 220
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVA 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
12-222 |
8.22e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 104.38 E-value: 8.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 12 ALVALRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRY----DRGgltr 87
Cdd:COG3839 2 ASLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDlppkDRN---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 88 lrttVQLVVQDPDdqLF-AASVAQDVSFGPLNLGLSDAEVRSRVGEALAALdiaaladRPTHL-------LSYGQRKRAA 159
Cdd:COG3839 77 ----IAMVFQSYA--LYpHMTVYENIAFPLKLRKVPKAEIDRRVREAAELL-------GLEDLldrkpkqLSGGQRQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664496302 160 IAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALL 222
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVM 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
29-237 |
8.71e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 102.46 E-value: 8.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRLRTTVQLVVQDPDDQLFAAS 107
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaKLNRAQRKAFRRDIQMVFQDSISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 108 VAQDVSFGPLN--LGLSDAEVRSRVGEalaalDIAALADRPTHL------LSYGQRKRAAIAGAVAMRPRVLILDEPTAG 179
Cdd:PRK10419 107 TVREIIREPLRhlLSLDKAERLARASE-----MLRAVDLDDSVLdkrppqLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 180 LDPDGQERLLATLDRLRA-AGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAAATLA 237
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERFCQRVMVMDNGQiVETQPVGDKLT 241
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
11-238 |
9.94e-26 |
|
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: 105.99 E-value: 9.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 11 TALVALRGVSFAYEEGP-PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR-YDRGGLTRL 88
Cdd:COG4618 328 KGRLSVENLTVVPPGSKrPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 89 rttVQLVVQDPddQLFAASVAQDVS-FGPLNlglsDAEV--------------------RSRVGEALaaldiaaladrpt 147
Cdd:COG4618 408 ---IGYLPQDV--ELFDGTIAENIArFGDAD----PEKVvaaaklagvhemilrlpdgyDTRIGEGG------------- 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 148 HLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLaLRWADEVALLTPGGV 227
Cdd:COG4618 466 ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSL-LAAVDKLLVLRDGRV 544
|
250
....*....|..
gi 664496302 228 -HTGPAAATLAR 238
Cdd:COG4618 545 qAFGPRDEVLAR 556
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
29-228 |
1.11e-25 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 100.91 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGG-----EPVRYDRG-----GLTRL--RTTVQLVV 96
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAEARRRlgfvsDSTGLydRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 97 QdpddqlfaasvaqdvSFGPLNlGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEP 176
Cdd:cd03266 100 E---------------YFAGLY-GLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 664496302 177 TAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGVH 228
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-225 |
1.22e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.96 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 10 STALVALRGVSFAYEEgPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRyDRGGLTRLR 89
Cdd:PRK13537 4 SVAPIDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP-SRARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 90 TTV--QLVVQDPDdqlfaASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMR 167
Cdd:PRK13537 82 VGVvpQFDNLDPD-----FTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 664496302 168 PRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
28-207 |
1.44e-25 |
|
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: 100.37 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 28 PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTRLRTtvqlVVQDPddQLFAAS 107
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGA----LIEAP--GFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 108 VAQDvsfgplNLGLSDAEVR---SRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDG 184
Cdd:cd03268 88 TARE------NLRLLARLLGirkKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180
....*....|....*....|...
gi 664496302 185 QERLLATLDRLRAAGTTVLMATH 207
Cdd:cd03268 162 IKELRELILSLRDQGITVLISSH 184
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-227 |
2.74e-25 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 100.31 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGP--PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLsggLR---PHAGRLTLGGEPVRydRGGLTRL 88
Cdd:cd03249 1 IEFKNVSFRYPSRPdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL---ERfydPTSGEILLDGVDIR--DLNLRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 89 RTTVQLVVQDPddQLFAASVAQDVSFGPLNLGLSDAEVRSR------------------VGEALAaldiaaladrpthLL 150
Cdd:cd03249 76 RSQIGLVSQEP--VLFDGTIAENIRYGKPDATDEEVEEAAKkanihdfimslpdgydtlVGERGS-------------QL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 664496302 151 SYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRaAGTTVLMATHDVdLALRWADEVALLTPGGV 227
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRL-STIRNADLIAVLQNGQV 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
29-225 |
5.21e-25 |
|
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: 99.72 E-value: 5.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEpvryDRGGLTRLRTTVQLVVQDpdDQLFA-AS 107
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK----DITNLPPEKRDISYVPQN--YALFPhMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 108 VAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQER 187
Cdd:cd03299 88 VYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 664496302 188 LLATLDRLR-AAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:cd03299 168 LREELKKIRkEFGVTVLHVTHDFEEAWALADKVAIMLNG 206
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
34-239 |
5.72e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 99.44 E-value: 5.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 34 DFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR----YDRGgltrlrttVQLVVQDpdDQLFAA-SV 108
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTalppAERP--------VSMLFQE--NNLFPHlTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 109 AQDVSFG--PlNLGLSDAEvRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQE 186
Cdd:COG3840 89 AQNIGLGlrP-GLKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 187 RLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGGVH-TGPAAATLART 239
Cdd:COG3840 167 EMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAaDGPTAALLDGE 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-227 |
6.41e-25 |
|
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: 99.23 E-value: 6.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYE-EGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDrgGLTRLRTTV 92
Cdd:cd03251 1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY--TLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 QLVVQDPddQLFAASVAQDVSFGplNLGLSDAEVR--------------------SRVGEALAAldiaaladrpthlLSY 152
Cdd:cd03251 79 GLVSQDV--FLFNDTVAENIAYG--RPGATREEVEeaaraanahefimelpegydTVIGERGVK-------------LSG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 153 GQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLrAAGTTVLMATHDVDlALRWADEVALLTPGGV 227
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLS-TIENADRIVVLEDGKI 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-225 |
9.10e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.95 E-value: 9.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 8 TESTALVALRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVrydrgglTR 87
Cdd:PRK09452 9 SSLSPLVELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-------TH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 88 L---RTTVQLVVQDPddQLFA-ASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGA 163
Cdd:PRK09452 81 VpaeNRHVNTVFQSY--ALFPhMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664496302 164 VAMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-222 |
1.06e-24 |
|
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: 103.14 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVryDRGGLTRLRTTVQ 93
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL--ADADADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 94 LVVQDPddQLFAASVAQDVSFGplNLGLSDAEVR---SRVGEALAALDIAALADRPT----HLLSYGQRKRAAIAGAVAM 166
Cdd:TIGR02857 400 WVPQHP--FLFAGTIAENIRLA--RPDASDAEIRealERAGLDEFVAALPQGLDTPIgeggAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 664496302 167 RPRVLILDEPTAGLDPDGQERLLATLDRLrAAGTTVLMATHDVDLAlRWADEVALL 222
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-227 |
1.06e-24 |
|
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: 98.84 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLsggLR---PHAGRLTLGGEPVR-YDrggLTRLR 89
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL---FRfydVSSGSILIDGQDIReVT---LDSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 90 TTVQLVVQdpDDQLFAASVAQDVSFGplNLGLSDAEVR--------------------SRVGEalaaldiaaladRPTHl 149
Cdd:cd03253 75 RAIGVVPQ--DTVLFNDTIGYNIRYG--RPDATDEEVIeaakaaqihdkimrfpdgydTIVGE------------RGLK- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 664496302 150 LSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLrAAGTTVLMATHDVDLALRwADEVALLTPGGV 227
Cdd:cd03253 138 LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
26-237 |
2.52e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 98.28 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 26 GPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLG------GEPVRYDRGGLTRLRTTVQLVVQDP 99
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtARSLSQQKGLIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 100 DdqLFA-ASVAQDVSFGPLNL-GLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPT 177
Cdd:PRK11264 95 N--LFPhRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 664496302 178 AGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAAATLA 237
Cdd:PRK11264 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRiVEQGPAKALFA 233
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
29-244 |
3.36e-24 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 97.95 E-value: 3.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRY--DRGG---------LTRLRTTVQLVVQ 97
Cdd:COG4598 23 VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLkpDRDGelvpadrrqLQRIRTRLGMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 98 DPDdqLFA-ASVAQDVSFGPLN-LGLSDAEVRSR-------VGealaalDIAALADRPTHLlSYGQRKRAAIAGAVAMRP 168
Cdd:COG4598 103 SFN--LWShMTVLENVIEAPVHvLGRPKAEAIERaeallakVG------LADKRDAYPAHL-SGGQQQRAAIARALAMEP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664496302 169 RVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGV-HTGPAAATLA--RTELLRQ 244
Cdd:COG4598 174 EVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIeEQGPPAEVFGnpKSERLRQ 252
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
32-208 |
3.54e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 99.42 E-value: 3.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 32 GLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRLRTTVQLVVQDPddqlFAA---- 106
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItGLSGRELRPLRRRMQMVFQDP----YASlnpr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 107 -SVAQDVSFGPLNLGL-SDAEVRSRVGEALAALDIaaladRPTHL------LSYGQRKRAAIAGAVAMRPRVLILDEPTA 178
Cdd:COG4608 112 mTVGDIIAEPLRIHGLaSKAERRERVAELLELVGL-----RPEHAdrypheFSGGQRQRIGIARALALNPKLIVCDEPVS 186
|
170 180 190
....*....|....*....|....*....|.
gi 664496302 179 GLDPDGQERLLATLDRLRAA-GTTVLMATHD 208
Cdd:COG4608 187 ALDVSIQAQVLNLLEDLQDElGLTYLFISHD 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
13-227 |
3.92e-24 |
|
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: 97.27 E-value: 3.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 13 LVALRGVSFAYEEGP---PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGG-EPVRYDRGGLTRL 88
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 89 RTTVQLVVQDpdDQLFAA-SVAQDVSFgPLNL-GLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAM 166
Cdd:cd03258 81 RRRIGMIFQH--FNLLSSrTVFENVAL-PLEIaGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664496302 167 RPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGGV 227
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
28-244 |
4.68e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.78 E-value: 4.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 28 PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVrydrGGLT--RLRTTVQLVVQD---PDDq 102
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI----SMLSsrQLARRLALLPQHhltPEG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 103 lfaASVAQDVSFG--P-LNL-GLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTA 178
Cdd:PRK11231 91 ---ITVRELVAYGrsPwLSLwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 664496302 179 GLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGVHTGPAAATLARTELLRQ 244
Cdd:PRK11231 168 YLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRT 233
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-230 |
4.84e-24 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 96.87 E-value: 4.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 19 VSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRLRTTVQLVVQ 97
Cdd:PRK10908 7 VSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItRLKNREVPFLRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 98 DpDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPT 177
Cdd:PRK10908 87 D-HHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 664496302 178 AGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGVHTG 230
Cdd:PRK10908 166 GNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-222 |
6.11e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.49 E-value: 6.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 9 ESTALVALRGVSFAYeegPPV--LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRydrgglt 86
Cdd:COG3845 1 MMPPALELRGITKRF---GGVvaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 87 rlrttvqlvVQDPDD-------------QLFAA-SVAQDVSFG--PLNLGLSD-AEVRSRVGEALAALDIAALADRPTHL 149
Cdd:COG3845 71 ---------IRSPRDaialgigmvhqhfMLVPNlTVAENIVLGlePTKGGRLDrKAARARIRELSERYGLDVDPDAKVED 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664496302 150 LSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALL 222
Cdd:COG3845 142 LSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVL 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
28-227 |
6.70e-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: 95.70 E-value: 6.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 28 PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHA--GRLTLGGEPVRydrggLTRLRTTVQLVVQdpDDQLFA 105
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLD-----KRSFRKIIGYVPQ--DDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 106 ASVAQDvsfgplNLGLSdAEVRSrvgealaaldiaaladrpthlLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQ 185
Cdd:cd03213 96 TLTVRE------TLMFA-AKLRG---------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 664496302 186 ERLLATLDRLRAAGTTVLMATHDV-DLALRWADEVALLTPGGV 227
Cdd:cd03213 148 LQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
32-250 |
6.84e-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: 100.53 E-value: 6.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 32 GLDFAVHEGRALALLGRNGSGKTTLMR-LLsgGLRPHAGRLTLGGEPV-RYDRGGLTRLRTTVQLVVQDPddqlFAA--- 106
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLaLL--RLIPSEGEIRFDGQDLdGLSRRALRPLRRRMQVVFQDP----FGSlsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 107 --SVAQDVSFG--PLNLGLSDAEVRSRVGEALAALD-IAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLD 181
Cdd:COG4172 378 rmTVGQIIAEGlrVHGPGLSAAERRARVAEALEEVGlDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 664496302 182 PDGQERLLATLDRLRAA-GTTVLMATHDVDL--ALrwADEVALLTPGG-VHTGPAAATLAR-----TELLRQAGLRLP 250
Cdd:COG4172 458 VSVQAQILDLLRDLQREhGLAYLFISHDLAVvrAL--AHRVMVMKDGKvVEQGPTEQVFDApqhpyTRALLAAAPLLE 533
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
34-262 |
9.23e-24 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 98.63 E-value: 9.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 34 DFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVrYDRGGLTRLRT---TVQLVVQDPddQLFA-ASVA 109
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL-QDSARGIFLPPhrrRIGYVFQEA--RLFPhLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 110 QDVSFGplnlglsdaevRSRVGEALAALDIAALA---------DRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGL 180
Cdd:COG4148 96 GNLLYG-----------RKRAPRAERRISFDEVVellgighllDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 181 DPDGQERLLATLDRLRA-AGTTVLMATHDVDLALRWADEVALLTPGGV-HTGPAAATLARTELLRQAGLRlpwgvAAASV 258
Cdd:COG4148 165 DLARKAEILPYLERLRDeLDIPILYVSHSLDEVARLADHVVLLEQGRVvASGPLAEVLSRPDLLPLAGGE-----EAGSV 239
|
....
gi 664496302 259 LRAR 262
Cdd:COG4148 240 LEAT 243
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-208 |
9.25e-24 |
|
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: 100.13 E-value: 9.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLtrLRTTVQLV 95
Cdd:TIGR02868 337 LRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE--VRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 96 VQDPddQLFAASVAQDVSFGplNLGLSDAEVR---SRVGEALAALDIAALADRPTH----LLSYGQRKRAAIAGAVAMRP 168
Cdd:TIGR02868 415 AQDA--HLFDTTVRENLRLA--RPDATDEELWaalERVGLADWLRALPDGLDTVLGeggaRLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 664496302 169 RVLILDEPTAGLDPDGQERLLATLdRLRAAGTTVLMATHD 208
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDL-LAALSGRTVVLITHH 529
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
26-225 |
1.05e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 96.69 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 26 GPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR---YDRGgltrlrttvqlVVQDPDDQ 102
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgAERG-----------VVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 103 LFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDP 182
Cdd:PRK11248 82 LPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 664496302 183 DGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:PRK11248 162 FTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-225 |
1.05e-23 |
|
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: 94.69 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAY-EEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGgltRLRTTV 92
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK---ALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 QLVVQDPddQLFAASVAQdvsfgplNLGLSdaevrsrvgealaaldiaaladrpthlLSYGQRKRAAIAGAVAMRPRVLI 172
Cdd:cd03247 78 SVLNQRP--YLFDTTLRN-------NLGRR---------------------------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 664496302 173 LDEPTAGLDPDGQERLLATL-DRLRaaGTTVLMATHDVdLALRWADEVALLTPG 225
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIfEVLK--DKTLIWITHHL-TGIEHMDKILFLENG 172
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
7-214 |
1.46e-23 |
|
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: 95.58 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 7 STESTALVALRGVSFAYEEGP---PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDR 82
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAgelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 83 GGLTRLR-TTVQLVVQDpdDQLFAASVAQDVSFGPLNL-GLSDAEVRS-----RVGealaaldiaaLADRPTHL---LSY 152
Cdd:COG4181 82 DARARLRaRHVGFVFQS--FQLLPTLTALENVMLPLELaGRRDARARAralleRVG----------LGHRLDHYpaqLSG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664496302 153 GQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALR 214
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAAR 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
29-222 |
1.89e-23 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 95.29 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVrydrgGLTRLRTTVqlvvqDPDdqlfaASV 108
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-----SLLGLGGGF-----NPE-----LTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 109 AQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERL 188
Cdd:cd03220 102 RENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190
....*....|....*....|....*....|....
gi 664496302 189 LATLDRLRAAGTTVLMATHDVDLALRWADEVALL 222
Cdd:cd03220 182 QRRLRELLKQGKTVILVSHDPSSIKRLCDRALVL 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-225 |
1.97e-23 |
|
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: 95.05 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 33 LDFAVHEGRaLALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGG--LTRLRTTVQLVVQDpdDQLFA-ASVA 109
Cdd:cd03297 17 IDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinLPPQQRKIGLVFQQ--YALFPhLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 110 QDVSFGPLnlGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLL 189
Cdd:cd03297 94 ENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 664496302 190 ATLDRLRAA-GTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:cd03297 172 PELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-210 |
3.11e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 96.69 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 30 LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLT-LGGEPVRyDRGGLTRLRTTV-----QLV----VQDp 99
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvLGYVPFK-RRKEFARRIGVVfgqrsQLWwdlpAID- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 100 ddqlfaasvaqdvSFgplNL-----GLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILD 174
Cdd:COG4586 116 -------------SF---RLlkaiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 664496302 175 EPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVD 210
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMD 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-221 |
4.32e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.79 E-value: 4.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 26 GPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLtrlrttvQLVVQDPDDQLFA 105
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE-------ACHYLGHRNAMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 106 A-SVAQDVSF-----GPLNLGLSDAevRSRVGealaaldIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAG 179
Cdd:PRK13539 87 AlTVAENLEFwaaflGGEELDIAAA--LEAVG-------LAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 664496302 180 LDPDGQERLLATLDRLRAAGTTVLMATHdVDLALRWADEVAL 221
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIVIAATH-IPLGLPGARELDL 198
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
30-238 |
4.51e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 96.19 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 30 LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRLRTTVQLVVQDPDDQLFAASV 108
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlKADPEAQKLLRQKIQIVFQNPYGSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 109 AQDVSFGPL--NLGLSDAEVRSRVGEALAALDIAAL-ADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQ 185
Cdd:PRK11308 111 VGQILEEPLliNTSLSAAERREKALAMMAKVGLRPEhYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 186 ERLLATL-DRLRAAGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAAATLAR 238
Cdd:PRK11308 191 AQVLNLMmDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRcVEKGTKEQIFNN 245
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
11-227 |
5.28e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 98.26 E-value: 5.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 11 TALVALRGVSFAYEEGP--PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR-YDRgglTR 87
Cdd:TIGR00958 476 EGLIEFQDVSFSYPNRPdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqYDH---HY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 88 LRTTVQLVVQDPddQLFAASVAQDVSFGPLNlgLSDAEVRSRVGE-------ALAALDIAALADRPTHLLSYGQRKRAAI 160
Cdd:TIGR00958 553 LHRQVALVGQEP--VLFSGSVRENIAYGLTD--TPDEEIMAAAKAanahdfiMEFPNGYDTEVGEKGSQLSGGQKQRIAI 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 664496302 161 AGAVAMRPRVLILDEPTAGLDPDGQerllATLDRLR-AAGTTVLMATHDVDLALRwADEVALLTPGGV 227
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALDAECE----QLLQESRsRASRTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
29-237 |
5.59e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 94.65 E-value: 5.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR-----------YDRGGLTRLRTTVQLVVQ 97
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvADKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 98 DPDDQLFAaSVAQDVSFGPLN-LGLSDAEVRSRVGE--ALAALDIAALADRPTHLlSYGQRKRAAIAGAVAMRPRVLILD 174
Cdd:PRK10619 100 HFNLWSHM-TVLENVMEAPIQvLGLSKQEARERAVKylAKVGIDERAQGKYPVHL-SGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664496302 175 EPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGV-HTGPAAATLA 237
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIeEEGAPEQLFG 241
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
29-228 |
7.52e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 93.99 E-value: 7.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGepvrydrggltrlRTTVQLVVQ---DPDdqlfa 105
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------------RVSALLELGagfHPE----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 106 ASVAQDVSFGPLNLGLSDAEVRSRV---------GEalaaldiaaLADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEP 176
Cdd:COG1134 103 LTGRENIYLNGRLLGLSRKEIDEKFdeivefaelGD---------FIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 664496302 177 TAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGVH 228
Cdd:COG1134 174 LAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
16-226 |
9.34e-23 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 90.97 E-value: 9.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGepvrydrggltrlRTTVQLV 95
Cdd:cd03221 3 LENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-------------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 96 VQdpddqlfaasvaqdvsfgplnlglsdaevrsrvgealaaldiaaladrpthlLSYGQRKRAAIAGAVAMRPRVLILDE 175
Cdd:cd03221 69 EQ----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 664496302 176 PTAGLDPDGQERLLATLDRLRAagtTVLMATHDVDLALRWADEVALLTPGG 226
Cdd:cd03221 97 PTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-264 |
1.38e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 97.06 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 10 STALVALRG--VSFAYEEGP-PVLTGLDFAVHEGRALALLGRNGSGKT----TLMRLLSGGLRPHAGRLTLGGEP-VRYD 81
Cdd:COG4172 3 SMPLLSVEDlsVAFGQGGGTvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDlLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 82 RGGLTRLR-TTVQLVVQDP----------DDQLfAASVAqdvsfgpLNLGLSDAEVRSRVGEALAALDIAALADRPT--- 147
Cdd:COG4172 83 ERELRRIRgNRIAMIFQEPmtslnplhtiGKQI-AEVLR-------LHRGLSGAAARARALELLERVGIPDPERRLDayp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 148 HLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVDLALRWADEVALLTPGG 226
Cdd:COG4172 155 HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGE 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 664496302 227 -VHTGPAAATLAR-----TELLRQA---GLRLPWGVAAASVLRARGL 264
Cdd:COG4172 235 iVEQGPTAELFAApqhpyTRKLLAAeprGDPRPVPPDAPPLLEARDL 281
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
18-234 |
2.55e-22 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 92.75 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 18 GVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRG-GLTRLRTTVQLVV 96
Cdd:TIGR02315 6 NLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGkKLRKLRRRIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 97 QDpdDQLFA-ASVAQDVSFGPLN--------LGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMR 167
Cdd:TIGR02315 86 QH--YNLIErLTVLENVLHGRLGykptwrslLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQ 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664496302 168 PRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAAA 234
Cdd:TIGR02315 164 PDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLKAGEiVFDGAPSE 232
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
35-222 |
3.27e-22 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 91.84 E-value: 3.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 35 FAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTRLrttvqlvvqdPDDQLFAASVAQDVSF 114
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYV----------PQRHEFAWDFPISVAH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 115 GPLN--LGLSDAEVRSR------VGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQE 186
Cdd:TIGR03771 71 TVMSgrTGHIGWLRRPCvadfaaVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 664496302 187 RLLATLDRLRAAGTTVLMATHDVDLALRWADEVALL 222
Cdd:TIGR03771 151 LLTELFIELAGAGTAILMTTHDLAQAMATCDRVVLL 186
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-225 |
5.42e-22 |
|
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: 91.16 E-value: 5.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEgPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR----YDRGgltrlr 89
Cdd:cd03301 1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTdlppKDRD------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 90 ttVQLVVQDpddqlFA----ASVAQDVSFgPLNL-GLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAV 164
Cdd:cd03301 74 --IAMVFQN-----YAlyphMTVYDNIAF-GLKLrKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664496302 165 AMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-205 |
6.35e-22 |
|
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: 95.17 E-value: 6.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 3 EPDRST----ESTALVALRGVSFAY-EEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEP 77
Cdd:TIGR02203 316 EKDTGTraieRARGDVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 78 VRYDRggLTRLRTTVQLVVQDPddQLFAASVAQDVSFGPLNlGLSDAEVRsRVGEALAALDIAALADRPTH--------L 149
Cdd:TIGR02203 396 LADYT--LASLRRQVALVSQDV--VLFNDTIANNIAYGRTE-QADRAEIE-RALAAAYAQDFVDKLPLGLDtpigengvL 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 664496302 150 LSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMA 205
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIA 525
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
16-227 |
8.10e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 91.23 E-value: 8.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGE----PVRYDRGGLTRLRTT 91
Cdd:COG4161 5 LKNINCFYG-SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfSQKPSEKAIRLLRQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 VQLVVQD----PDdqlfaASVAQDVSFGPLN-LGLSDAEVRSRVGEALAALDIAALADR-PTHLlSYGQRKRAAIAGAVA 165
Cdd:COG4161 84 VGMVFQQynlwPH-----LTVMENLIEAPCKvLGLSKEQAREKAMKLLARLRLTDKADRfPLHL-SGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664496302 166 MRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGV 227
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-222 |
9.85e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 92.83 E-value: 9.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGP---PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRLR 89
Cdd:COG1135 2 IELENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 90 TTVQLVVQDpdDQLFAA-SVAQDVSFgPLNL-GLSDAEVRSRVGEalaaldiaaladrpthLL----------SY----- 152
Cdd:COG1135 82 RKIGMIFQH--FNLLSSrTVAENVAL-PLEIaGVPKAEIRKRVAE----------------LLelvglsdkadAYpsqls 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664496302 153 -GQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVDLALRWADEVALL 222
Cdd:COG1135 143 gGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVL 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-228 |
1.59e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 13 LVALRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGgEPVR--Y---DRGGLtR 87
Cdd:COG0488 315 VLELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG-ETVKigYfdqHQEEL-D 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 88 LRTTVQLVVQD--PD-DQLFAASVAQDvsfgplnLGLSDAEVRSRVGEalaaldiaaladrpthlLSYGQRKRAAIAGAV 164
Cdd:COG0488 392 PDKTVLDELRDgaPGgTEQEVRGYLGR-------FLFSGDDAFKPVGV-----------------LSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664496302 165 AMRPRVLILDEPTAGLDPDGQERLLATLDRLraAGtTVLMATHDVDLALRWADEVALLTPGGVH 228
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-227 |
1.85e-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: 89.84 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 13 LVALRGVSFAYEEGP--PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRgglTRLR 89
Cdd:cd03248 11 IVKFQNVTFAYPTRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsQYEH---KYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 90 TTVQLVVQDPddQLFAASVAQDVSFgplnlGLSDAEVrSRVGEALAALDIAALADRPTH-----------LLSYGQRKRA 158
Cdd:cd03248 88 SKVSLVGQEP--VLFARSLQDNIAY-----GLQSCSF-ECVKEAAQKAHAHSFISELASgydtevgekgsQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664496302 159 AIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLdRLRAAGTTVLMATHDVDLALRwADEVALLTPGGV 227
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQAL-YDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-225 |
3.54e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.43 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 1 MNEPDRSTESTAlVALRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRy 80
Cdd:PRK13536 30 KASIPGSMSTVA-IDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 81 DRGGLTRLRTTVqlVVQ-DPDDQLFaaSVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAA 159
Cdd:PRK13536 107 ARARLARARIGV--VPQfDNLDLEF--TVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 664496302 160 IAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
14-227 |
4.31e-21 |
|
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: 88.70 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPpvlTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEpvryDRGGLTRLRTTVQ 93
Cdd:cd03298 1 VRLDKIRFSYGEQP---MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV----DVTAAPPADRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 94 LVVQDpdDQLFA-ASVAQDVSFGpLNLGLS-DAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVL 171
Cdd:cd03298 74 MLFQE--NNLFAhLTVEQNVGLG-LSPGLKlTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 664496302 172 ILDEPTAGLDPDGQERLLATLDRLRA-AGTTVLMATHDVDLALRWADEVALLTPGGV 227
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-244 |
4.76e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.85 E-value: 4.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 1 MNEPDRSTESTalVALRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-R 79
Cdd:PRK10575 1 MQEYTNHSDTT--FALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 80 YDRGGLTRlrtTVQLVVQdpddQLFAA---SVAQDVSFG--PLN--LGLSDAEVRSRVGEALAALDIAALADRPTHLLSY 152
Cdd:PRK10575 78 WSSKAFAR---KVAYLPQ----QLPAAegmTVRELVAIGryPWHgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 153 GQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGGVHTGP 231
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
|
250
....*....|...
gi 664496302 232 AAATLARTELLRQ 244
Cdd:PRK10575 231 TPAELMRGETLEQ 243
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
29-225 |
1.30e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 88.15 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEpvRYDRGGLT------RLRTTVQLVVQD---- 98
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN--HFDFSKTPsdkairELRRNVGMVFQQynlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 99 PDdqlfaASVAQDVSFGPLN-LGLSDAEVRSRVGEALAALDIAALADR-PTHLlSYGQRKRAAIAGAVAMRPRVLILDEP 176
Cdd:PRK11124 95 PH-----LTVQQNLIEAPCRvLGLSKDQALARAEKLLERLRLKPYADRfPLHL-SGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 664496302 177 TAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENG 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-244 |
1.34e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.13 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 10 STALVALRGVSFAYeegPPV--LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDR----- 82
Cdd:PRK11288 1 SSPYLSFDGIGKTF---PGVkaLDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASttaal 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 83 -GGLTRLRTTVQLVvqdPDdqlfaASVAQDVSFG--PLNLGLSD-AEVRSRVGEALAALDIAALADRPTHLLSYGQRKRA 158
Cdd:PRK11288 78 aAGVAIIYQELHLV---PE-----MTVAENLYLGqlPHKGGIVNrRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 159 AIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAAATLA 237
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRyVATFDDMAQVD 229
|
....*..
gi 664496302 238 RTELLRQ 244
Cdd:PRK11288 230 RDQLVQA 236
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
29-225 |
1.70e-20 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 87.45 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEP-VRYDrggltrLRTTVQLVVQDPddqLFAAS 107
Cdd:TIGR03740 15 AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPwTRKD------LHKIGSLIESPP---LYENL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 108 VAQD-VSFGPLNLGLSDaevrSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQE 186
Cdd:TIGR03740 86 TAREnLKVHTTLLGLPD----SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQ 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 664496302 187 RLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:TIGR03740 162 ELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEG 200
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
34-227 |
2.59e-20 |
|
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: 87.70 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 34 DFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRLR-TTVQLVVQDpddqlFA----AS 107
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaAMSRKELRELRrKKISMVFQS-----FAllphRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 108 VAQDVSFGpLNL-GLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDP---- 182
Cdd:cd03294 119 VLENVAFG-LEVqGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPlirr 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 664496302 183 DGQERLLATLDRLRaagTTVLMATHDVDLALRWADEVALLTPGGV 227
Cdd:cd03294 198 EMQDELLRLQAELQ---KTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
26-207 |
2.65e-20 |
|
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: 86.26 E-value: 2.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 26 GPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTRlrttVQLVVQDPDDQLFA 105
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE----NILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 106 ASVAQDVSF-----GPLNLGLSDAevRSRVGealaaldIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGL 180
Cdd:TIGR01189 88 LSALENLHFwaaihGGAQRTIEDA--LAAVG-------LTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180
....*....|....*....|....*..
gi 664496302 181 DPDGQERLLATLDRLRAAGTTVLMATH 207
Cdd:TIGR01189 159 DKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
29-207 |
3.10e-20 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 86.01 E-value: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTRlrttVQLVVQDPDDQLFAASV 108
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR----GLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 109 AQDVSFgplnlgLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERL 188
Cdd:cd03231 91 LENLRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170
....*....|....*....
gi 664496302 189 LATLDRLRAAGTTVLMATH 207
Cdd:cd03231 165 AEAMAGHCARGGMVVLTTH 183
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-231 |
6.31e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.51 E-value: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSG--GLRPHA---GRLTLGGEPVRydRGGLTRLRTTVQLVVQDPDdQL 103
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDGQDIF--KMDVIELRRRVQMVFQIPN-PI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 104 FAASVAQDVSFGP-LN-LGLSDAEVRSRVGEALAALD----IAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPT 177
Cdd:PRK14247 95 PNLSIFENVALGLkLNrLVKSKKELQERVRWALEKAQlwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 178 AGLDPDGQERLLATLDRLRAAgTTVLMATHDVDLALRWADEVALLTPGG-VHTGP 231
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQiVEWGP 228
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
28-228 |
1.84e-19 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 87.79 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 28 PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR-YDRGGLTRlrtTVQLVVQDPddQLFAA 106
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqWDRETFGK---HIGYLPQDV--ELFPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 107 SVAQDVS-FGplnlglSDAEVRSRVGEALAALDIAALADRP----THL------LSYGQRKRAAIAGAVAMRPRVLILDE 175
Cdd:TIGR01842 407 TVAENIArFG------ENADPEKIIEAAKLAGVHELILRLPdgydTVIgpggatLSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 664496302 176 PTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLaLRWADEVALLTPGGVH 228
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKALKARGITVVVITHRPSL-LGCVDKILVLQDGRIA 532
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
28-238 |
2.06e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 84.76 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 28 PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTRLRTTVQLVVQDPDdqLFAAS 107
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVFQQFY--LFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 108 VA-QDVSFGPLNL-GLSDAEVRSRVGEALAALDIAAladRPTHL---LSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDP 182
Cdd:PRK09493 93 TAlENVMFGPLRVrGASKEEAEKQARELLAKVGLAE---RAHHYpseLSGGQQQRVAIARALAVKPKLMLFDEPTSALDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 664496302 183 DGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGV-HTGPAAATLAR 238
Cdd:PRK09493 170 ELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIaEDGDPQVLIKN 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
32-211 |
2.44e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 84.66 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 32 GLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV------RYDRGGLTRlrtTVQLVvqdpddQLFA 105
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghQIARMGVVR---TFQHV------RLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 106 AS-------VAQDVSfgpLNLGL------------SDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAM 166
Cdd:PRK11300 94 EMtvienllVAQHQQ---LKTGLfsgllktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 664496302 167 RPRVLILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVDL 211
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKL 216
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-225 |
3.31e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 84.32 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 1 MNEPDRSTESTalVALRGVSFAYEEGPpVLTGLDFAVHEGRALALLGRNGSGKTTLMRL------LSGGLRpHAGRLTLG 74
Cdd:COG1117 1 MTAPASTLEPK--IEVRNLNVYYGDKQ-ALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndLIPGAR-VEGEILLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 75 GEPVrYDRGG-LTRLRTTVQLVVQDPddQLFAASVAQDVSFGPLNLG--------------LSDA----EVRSRVGEala 135
Cdd:COG1117 77 GEDI-YDPDVdVVELRRRVGMVFQKP--NPFPKSIYDNVAYGLRLHGikskseldeiveesLRKAalwdEVKDRLKK--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 136 aldiaaladrPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAgTTVLMATHDVDLALRW 215
Cdd:COG1117 151 ----------SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARV 219
|
250
....*....|
gi 664496302 216 ADEVALLTPG 225
Cdd:COG1117 220 SDYTAFFYLG 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
16-225 |
4.19e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 85.62 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEEGPPVLTGLD---FAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRLRTT 91
Cdd:PRK11153 4 LKNISKVFPQGGRTIHALNnvsLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtALSEKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 VQLVVQDpddqlF----AASVAQDVSFgPLNL-GLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAM 166
Cdd:PRK11153 84 IGMIFQH-----FnllsSRTVFDNVAL-PLELaGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 167 RPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-227 |
4.33e-19 |
|
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: 83.69 E-value: 4.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYE-EGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGepvrYDRG--GLTRLRT 90
Cdd:cd03252 1 ITFEHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG----HDLAlaDPAWLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 91 TVQLVVQDpdDQLFAASVAQDVSFGPLNLGLSDAEVRSR------------------VGEALAAldiaaladrpthlLSY 152
Cdd:cd03252 77 QVGVVLQE--NVLFNRSIRDNIALADPGMSMERVIEAAKlagahdfiselpegydtiVGEQGAG-------------LSG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 153 GQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLrAAGTTVLMATHDVDlALRWADEVALLTPGGV 227
Cdd:cd03252 142 GQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLS-TVKNADRIIVMEKGRI 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-211 |
5.11e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.27 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGG---------EPVRYD----- 81
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpqEPPLDDdltvl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 82 ---RGGLTRLRTTVQ------LVVQDPDDQLFAASVAQDVsFGPLNLGLSDAEVR---SRVGealaalDIAALADRPTHL 149
Cdd:COG0488 80 dtvLDGDAELRALEAeleeleAKLAEPDEDLERLAELQEE-FEALGGWEAEARAEeilSGLG------FPEEDLDRPVSE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664496302 150 LSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAagtTVLMATHDVDL 211
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG---TVLVVSHDRYF 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
29-239 |
8.28e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.77 E-value: 8.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRyDRGGLTRlrtTVQLVVQDPddQLFA-AS 107
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT-HRSIQQR---DICMVFQSY--ALFPhMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 108 VAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQER 187
Cdd:PRK11432 95 LGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 664496302 188 LLATLDRLRAA-GTTVLMATHDVDLALRWADEVALLTPGGVHTGPAAATLART 239
Cdd:PRK11432 175 MREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-220 |
1.12e-18 |
|
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: 81.32 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 12 ALVALRGVSfayeeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGlTRLRTT 91
Cdd:cd03215 3 PVLEVRGLS-----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPR-DAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 VQLVVQDPDDQLFA--ASVAQdvsfgplNLGLSdaevrsrvgealaaldiaaladrptHLLSYGQRKRAAIAGAVAMRPR 169
Cdd:cd03215 77 IAYVPEDRKREGLVldLSVAE-------NIALS-------------------------SLLSGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 664496302 170 VLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVA 220
Cdd:cd03215 125 VLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRIL 175
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
28-244 |
1.46e-18 |
|
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: 82.21 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 28 PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV------RYDRGGLTRLRttvqlvvQDPdd 101
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItklpmhKRARLGIGYLP-------QEA-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 102 QLFAA-SVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGL 180
Cdd:cd03218 85 SIFRKlTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664496302 181 DPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGVHTGPAAATLARTELLRQ 244
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRK 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-222 |
1.53e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.78 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEgPPVLTGLDFAVHEGRALALLGRNGSGKTTL------MRLLSGGLRPHaGRLTLGGEPVRYDRGGLTR 87
Cdd:PRK14258 8 IKVNNLSFYYDT-QKILEGVSMEIYQSKVTAIIGPSGCGKSTFlkclnrMNELESEVRVE-GRVEFFNQNIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 88 LRTTVQLVVQDPDdqLFAASVAQDVSFGPLNLGLS-----DAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAG 162
Cdd:PRK14258 86 LRRQVSMVHPKPN--LFPMSVYDNVAYGVKIVGWRpkleiDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664496302 163 AVAMRPRVLILDEPTAGLDPDGQ---ERLLATLdRLRAAgTTVLMATHDVDLALRWADEVALL 222
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASmkvESLIQSL-RLRSE-LTMVIVSHNLHQVSRLSDFTAFF 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-210 |
2.59e-18 |
|
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: 81.39 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAY-EEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLM----RLLSgglrPHAGRLTLGGEPVRydRGGLTRL 88
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLlalfRLVE----LSSGSILIDGVDIS--KIGLHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 89 RTTVQLVVQDPddQLFAASVAQDVsfGPLNLgLSDAEVRS---RVG-----EALAALDIAALADRPTHLlSYGQRKRAAI 160
Cdd:cd03244 77 RSRISIIPQDP--VLFSGTIRSNL--DPFGE-YSDEELWQaleRVGlkefvESLPGGLDTVVEEGGENL-SVGQRQLLCL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 664496302 161 AGAVAMRPRVLILDEPTAGLDPDGQERLLATLdRLRAAGTTVLMATHDVD 210
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTI-REAFKDCTVLTIAHRLD 199
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-205 |
5.41e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.47 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 13 LVALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRydrgGLTR--LRT 90
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR----TVTRasLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 91 TVQLVVQDPddQLFAASVAQDVSFGplNLGLSDAEVR--------------------SRVGEALAAldiaaladrpthlL 150
Cdd:PRK13657 410 NIAVVFQDA--GLFNRSIEDNIRVG--RPDATDEEMRaaaeraqahdfierkpdgydTVVGERGRQ-------------L 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 151 SYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMA 205
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIA 527
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
28-225 |
6.68e-18 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 80.17 E-value: 6.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 28 PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRltlggepVRYDRGG------------LTRLR-TTVQL 94
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGS-------ILVRHDGgwvdlaqaspreILALRrRTIGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 95 VVQdpddqlFAASV----AQDVSFGPL-NLGLSDAEVRSRVGEALAALDIaaladrPTHL-------LSYGQRKRAAIAG 162
Cdd:COG4778 98 VSQ------FLRVIprvsALDVVAEPLlERGVDREEARARARELLARLNL------PERLwdlppatFSGGEQQRVNIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664496302 163 AVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:COG4778 166 GFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-242 |
7.94e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.79 E-value: 7.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 4 PDRSTESTALVALRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPvrydrg 83
Cdd:PRK15439 2 QTSDTTAPPLLCARSISKQYS-GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 84 gLTRLRTT------VQLVVQDPddQLFAA-SVAQDVSFGPLNlglsDAEVRSRVGEALAALDIAALADRPTHLLSYGQRK 156
Cdd:PRK15439 75 -CARLTPAkahqlgIYLVPQEP--LLFPNlSVKENILFGLPK----RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 157 RAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGVHTGPAAATL 236
Cdd:PRK15439 148 IVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
....*.
gi 664496302 237 ARTELL 242
Cdd:PRK15439 228 STDDII 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
14-207 |
1.07e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 82.56 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRydrgGLTR--LRTT 91
Cdd:COG5265 358 VRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR----DVTQasLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 VQLVVQDPddQLFAASVAQDVSFGplNLGLSDAEVR--------------------SRVGEALAAldiaaladrpthlLS 151
Cdd:COG5265 434 IGIVPQDT--VLFNDTIAYNIAYG--RPDASEEEVEaaaraaqihdfieslpdgydTRVGERGLK-------------LS 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 664496302 152 YGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLrAAGTTVLMATH 207
Cdd:COG5265 497 GGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV-ARGRTTLVIAH 551
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
29-225 |
1.15e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.59 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTG-LDFAVHEGRALALLGRNGSGKTTLMRLLSGGLrPHAGRLTLGGEPVRydRGGLTRLRTTVQLVVQDPddQLFAAS 107
Cdd:PRK11174 364 TLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELR--ELDPESWRKHLSWVGQNP--QLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 108 VAQDVSFGplNLGLSDAEVR--------------------SRVGEALAAldiaaladrpthlLSYGQRKRAAIAGAVAMR 167
Cdd:PRK11174 439 LRDNVLLG--NPDASDEQLQqalenawvseflpllpqgldTPIGDQAAG-------------LSVGQAQRLALARALLQP 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 664496302 168 PRVLILDEPTAGLDPDGQERLLATLDRLrAAGTTVLMATHDVDlALRWADEVALLTPG 225
Cdd:PRK11174 504 CQLLLLDEPTASLDAHSEQLVMQALNAA-SRRQTTLMVTHQLE-DLAQWDQIWVMQDG 559
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
34-237 |
1.21e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 79.63 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 34 DFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEpvryDRGGLTRLRTTVQLVVQdpDDQLFA-ASVAQDV 112
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ----DHTTTPPSRRPVSMLFQ--ENNLFShLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 113 SFGpLNLGLS-DAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLAT 191
Cdd:PRK10771 93 GLG-LNPGLKlNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 664496302 192 LDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGGV-HTGPAAATLA 237
Cdd:PRK10771 172 VSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIaWDGPTDELLS 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
29-227 |
1.28e-17 |
|
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: 79.62 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHA---GRLTLGGEPVRYDRggltrLRTTVQLVVQDpDDQLFA 105
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQ-----FQKCVAYVRQD-DILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 106 ASVAQDVSFGPLNLG--LSDAEVRSRVGEALAALDIAALADRPTHL--LSYGQRKRAAIAGAVAMRPRVLILDEPTAGLD 181
Cdd:cd03234 96 LTVRETLTYTAILRLprKSSDAIRKKRVEDVLLRDLALTRIGGNLVkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 664496302 182 PDGQERLLATLDRLRAAGTTVLMATHD--VDLaLRWADEVALLTPGGV 227
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIHQprSDL-FRLFDRILLLSSGEI 222
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
29-219 |
1.80e-17 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 78.81 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGE--PVRYDRGGLTRLRTTVQLVVQDpddqlFAA 106
Cdd:TIGR03608 13 ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetPPLNSKKASKFRREKLGYLFQN-----FAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 107 SVAQDVSFGpLNLGL-----SDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLD 181
Cdd:TIGR03608 88 IENETVEEN-LDLGLkykklSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLD 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 664496302 182 PDGQERLLATLDRLRAAGTTVLMATHDVDLALRwADEV 219
Cdd:TIGR03608 167 PKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQ-ADRV 203
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
29-244 |
2.20e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 79.87 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSG----GLRPHA----GRLTLGGEPV-RYDRGGLTRLRTtvqlVVQDP 99
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRGarvtGDVTLNGEPLaAIDAPRLARLRA----VLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 100 DDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGE----ALAALDIAALADRPTHLLSYGQRKRAAIAGAVAM--------- 166
Cdd:PRK13547 92 AQPAFAFSAREIVLLGRYPHARRAGALTHRDGEiawqALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664496302 167 RPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGGVHTGPAAATLARTELLRQ 244
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIAR 250
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
26-210 |
3.00e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 78.29 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 26 GPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHA---GRLTLGGEPVRydrgGLTRLRTTVQLVVQDpdDQ 102
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLT----ALPAEQRRIGILFQD--DL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 103 LFA-ASVAQDVSFGpLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLD 181
Cdd:COG4136 87 LFPhLSVGENLAFA-LPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190
....*....|....*....|....*....|
gi 664496302 182 PDGQERLLA-TLDRLRAAGTTVLMATHDVD 210
Cdd:COG4136 166 AALRAQFREfVFEQIRQRGIPALLVTHDEE 195
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
10-243 |
3.99e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.16 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 10 STALVALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYdrgglTRLR 89
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-----ALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 90 TTVQLVVQDPD-DQLFAASVAQDVSFGPLN----LGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAV 164
Cdd:PRK15056 78 NLVAYVPQSEEvDWSFPVLVEDVVMMGRYGhmgwLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664496302 165 AMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGVHTGPAAATLARTELLR 243
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLEL 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
11-212 |
8.98e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.15 E-value: 8.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 11 TALVALRGVSFAY---EEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLT 86
Cdd:PRK10535 2 TALLELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVaTLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 87 RLRTTVQLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAM 166
Cdd:PRK10535 82 QLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 664496302 167 RPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLA 212
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVA 207
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
14-227 |
8.99e-17 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 76.82 E-value: 8.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPpvlTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEpvryDRGGLTRLRTTVQ 93
Cdd:TIGR01277 1 LALDKVRYEYEHLP---MEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ----SHTGLAPYQRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 94 LVVQDpdDQLFA-ASVAQDVSFGpLNLGLS-DAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVL 171
Cdd:TIGR01277 74 MLFQE--NNLFAhLTVRQNIGLG-LHPGLKlNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 664496302 172 ILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGGV 227
Cdd:TIGR01277 151 LLDEPFSALDPLLREEMLALVKQLcSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-225 |
1.07e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 80.06 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 26 GPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDrggLTRLRTTVQLVVQdpDDQLF- 104
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN---LDAVRQSLGMCPQ--HNILFh 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 105 AASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDG 184
Cdd:TIGR01257 1017 HLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 664496302 185 QERLLATLDRLRaAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:TIGR01257 1097 RRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-207 |
1.56e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.10 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 12 ALVALRGVSFAYEEGP-PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR-YDRgglTRLR 89
Cdd:PRK11160 337 VSLTLNNVSFTYPDQPqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdYSE---AALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 90 TTVQLVVQDPDdqLFAASVAQDvsfgpLNLGLSDA------EVRSRVGEALAALDIAALAD------RPthlLSYGQRKR 157
Cdd:PRK11160 414 QAISVVSQRVH--LFSATLRDN-----LLLAAPNAsdealiEVLQQVGLEKLLEDDKGLNAwlgeggRQ---LSGGEQRR 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 664496302 158 AAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLdRLRAAGTTVLMATH 207
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELL-AEHAQNKTVLMITH 532
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-217 |
1.74e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.11 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 7 STESTALVALRGVSFAYEEgPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGL 85
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGN-RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpAMSRSRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 86 TRLRTTVQLVVQdpDDQLFA-ASVAQDVSFgPL--NLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAG 162
Cdd:PRK11831 80 YTVRKRMSMLFQ--SGALFTdMNVFDNVAY-PLreHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALAR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 664496302 163 AVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVDLALRWAD 217
Cdd:PRK11831 157 AIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIAD 212
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-214 |
4.32e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.89 E-value: 4.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVrydrgglTRLRT-----TVQLVVQDP---- 99
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-------TKLPEykrakYIGRVFQDPmmgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 100 -----------------------------DDQLFAASVAQdvsfgpLNLGLSDaEVRSRVGealaaldiaaladrpthLL 150
Cdd:COG1101 94 apsmtieenlalayrrgkrrglrrgltkkRRELFRELLAT------LGLGLEN-RLDTKVG-----------------LL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 151 SYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALR 214
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALD 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-207 |
6.60e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 74.10 E-value: 6.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 22 AYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSG--GLRPHAGRLTLGGEpvryDRGGLT---RLRTTVQLVV 96
Cdd:cd03217 8 VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGE----DITDLPpeeRARLGIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 97 QDPddqlfaasvaQDVSfgplnlGLSDAE-VRSrVGEAlaaldiaaladrpthlLSYGQRKRAAIAGAVAMRPRVLILDE 175
Cdd:cd03217 84 QYP----------PEIP------GVKNADfLRY-VNEG----------------FSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190
....*....|....*....|....*....|..
gi 664496302 176 PTAGLDPDGQERLLATLDRLRAAGTTVLMATH 207
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-227 |
7.76e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.10 E-value: 7.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 1 MNEPDRSTESTALvALRGVSFAYEEGPpVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPvry 80
Cdd:PRK11247 1 MMNTARLNQGTPL-LLNAVSKRYGERT-VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 81 drggLTRLRTTVQLVVQDPDdQLFAASVAQDVSfgplnLGLSdAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAI 160
Cdd:PRK11247 76 ----LAEAREDTRLMFQDAR-LLPWKKVIDNVG-----LGLK-GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 664496302 161 AGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGGV 227
Cdd:PRK11247 145 ARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-245 |
8.85e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.97 E-value: 8.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 30 LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGgLRPHAGRLTLGGEPVR-YDRGGLTRLRTtvQLVVQDPddQLFAASV 108
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEaWSAAELARHRA--YLSQQQT--PPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 109 aqdvsFGPLNLGLSD----AEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAV-----AMRP--RVLILDEPT 177
Cdd:PRK03695 87 -----FQYLTLHQPDktrtEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 664496302 178 AGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGVHTGPAAATLARTELLRQA 245
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQV 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
29-225 |
8.86e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 76.28 E-value: 8.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEpvryDRGGLTRLRTTVQLVVQDPddQLFA-AS 107
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT----DVSRLHARDRKVGFVFQHY--ALFRhMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 108 VAQDVSFG----PLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPD 183
Cdd:PRK10851 91 VFDNIAFGltvlPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 664496302 184 GQERLLATLDRLRAA-GTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:PRK10851 171 VRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
16-208 |
1.13e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 76.55 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVryDRGGLTRLRttvqlv 95
Cdd:PRK10522 325 LRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV--TAEQPEDYR------ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 96 vqdpddQLFAAsVAQDVSF-----GPLNLGLSDAEVRSRVGEALAALDIAALADRPTHL-LSYGQRKRAAIAGAVAMRPR 169
Cdd:PRK10522 397 ------KLFSA-VFTDFHLfdqllGPEGKPANPALVEKWLERLKMAHKLELEDGRISNLkLSKGQKKRLALLLALAEERD 469
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 664496302 170 VLILDEPTAGLDPD-GQERLLATLDRLRAAGTTVLMATHD 208
Cdd:PRK10522 470 ILLLDEWAADQDPHfRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
31-207 |
2.31e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.91 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 31 TGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDR-------------GGLTRLRTtvqlvvq 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRdeyhqdllylghqPGIKTELT------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 98 dPDDQL-FAASVAQDVsfgplnlglSDAEVRS---RVGEALAALDiaaladrPTHLLSYGQRKRAAIAGAVAMRPRVLIL 173
Cdd:PRK13538 91 -ALENLrFYQRLHGPG---------DDEALWEalaQVGLAGFEDV-------PVRQLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190
....*....|....*....|....*....|....
gi 664496302 174 DEPTAGLDPDGQERLLATLDRLRAAGTTVLMATH 207
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
29-214 |
2.79e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 73.27 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRLRT-TVQLVVQD----Pddq 102
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhQMDEEARAKLRAkHVGFVFQSfmliP--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 103 lfAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAAladRPTHL---LSYGQRKRAAIAGAVAMRPRVLILDEPTAG 179
Cdd:PRK10584 102 --TLNALENVELPALLRGESSRQSRNGAKALLEQLGLGK---RLDHLpaqLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 664496302 180 LDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALR 214
Cdd:PRK10584 177 LDRQTGDKIADLLFSLnREHGTTLILVTHDLQLAAR 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
30-227 |
3.50e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.51 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 30 LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSG---GLRPHAGRLTLGGEPVRYD---RGGLTRLRTTVQLVVQDPD--D 101
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitGDKSAGSHIELLGRTVQREgrlARDIRKSRANTGYIFQQFNlvN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 102 QLfaaSVAQDVSFGPLN--------LGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLIL 173
Cdd:PRK09984 100 RL---SVLENVLIGALGstpfwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 174 DEPTAGLDPDGQERLLATL-DRLRAAGTTVLMATHDVDLALRWADEVALLTPGGV 227
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLrDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-205 |
3.81e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.14 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVrydrGGLTR--LRTT 91
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL----SSLSHsvLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 VQLVVQDP---DDQLFAA-------------SVAQDVSFGPLNLGLSDAeVRSRVGEALAAldiaaladrpthlLSYGQR 155
Cdd:PRK10790 417 VAMVQQDPvvlADTFLANvtlgrdiseeqvwQALETVQLAELARSLPDG-LYTPLGEQGNN-------------LSVGQK 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 664496302 156 KRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMA 205
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA 532
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
44-225 |
4.76e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 72.89 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 44 ALLGRNGSGKTTLMRLLS--GGLRPH---AGRLTLGGEPVRYDRGGLTRLRTTVQLVVQDPDDqlFAASVAQDVSFGPLN 118
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIYSPRTDTVDLRKEIGMVFQQPNP--FPMSIYENVVYGLRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 119 LGLSDAEVRSRVGEALAALDIAALADRpTHL------LSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATL 192
Cdd:PRK14239 113 KGIKDKQVLDEAVEKSLKGASIWDEVK-DRLhdsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETL 191
|
170 180 190
....*....|....*....|....*....|...
gi 664496302 193 DRLRAAgTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:PRK14239 192 LGLKDD-YTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-217 |
6.65e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 71.52 E-value: 6.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 19 VSFAYEEgPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTRL------RTTV 92
Cdd:PRK13540 7 LDFDYHD-QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQlcfvghRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 QLVVQDPDDQLFaasvaqDVSFGPLNLGLSDAEVRSRVGEALAAldiaaladrPTHLLSYGQRKRAAIAGAVAMRPRVLI 172
Cdd:PRK13540 86 NPYLTLRENCLY------DIHFSPGAVGITELCRLFSLEHLIDY---------PCGLLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 664496302 173 LDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDvDLALRWAD 217
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ-DLPLNKAD 194
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-232 |
8.50e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 72.18 E-value: 8.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSG--GLRPHA---GRLTLGGEPVRYDRGGLTRLRTTVQLVVQDPDdQL 103
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEArveGEVRLFGRNIYSPDVDPIEVRREVGMVFQYPN-PF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 104 FAASVAQDVSFG-PLN-LGLSDAEVRSRVGEALAALD-----IAALADRPTHLlSYGQRKRAAIAGAVAMRPRVLILDEP 176
Cdd:PRK14267 98 PHLTIYDNVAIGvKLNgLVKSKKELDERVEWALKKAAlwdevKDRLNDYPSNL-SGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 664496302 177 TAGLDPDGQERLLATLDRLRAAGTTVLMaTHDVDLALRWADEVALLTPGG-VHTGPA 232
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKEYTIVLV-THSPAQAARVSDYVAFLYLGKlIEVGPT 232
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
14-246 |
8.60e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 73.90 E-value: 8.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGP-PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR-YDrggLTRLRTT 91
Cdd:PRK11176 342 IEFRNVTFTYPGKEvPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdYT---LASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 VQLVVQDPddQLFAASVAQDVSFGPlnlglSDAEVRSRVGEALAALDIAALADRPTH-----------LLSYGQRKRAAI 160
Cdd:PRK11176 419 VALVSQNV--HLFNDTIANNIAYAR-----TEQYSREQIEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAI 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 161 AGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRaAGTTVLMATHDVDlALRWADEVALLTPG-----GVHtgpaaat 235
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAHRLS-TIEKADEILVVEDGeiverGTH------- 562
|
250
....*....|.
gi 664496302 236 larTELLRQAG 246
Cdd:PRK11176 563 ---AELLAQNG 570
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-196 |
8.85e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.97 E-value: 8.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTT----LMRLLSGglrphAGRLTLGGEPV-RYDRGGLTRLRTTVQLVVQDPDDQL 103
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLhNLNRRQLLPVRHRIQVVFQDPNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 104 FAA-SVAQDVSFGpLNL---GLSDAEVRSRVGEALAALDIAALAD-RPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTA 178
Cdd:PRK15134 376 NPRlNVLQIIEEG-LRVhqpTLSAAQREQQVIAVMEEVGLDPETRhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170
....*....|....*...
gi 664496302 179 GLDPDGQERLLATLDRLR 196
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQ 472
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-211 |
9.97e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.53 E-value: 9.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 2 NEPDRSTESTALVALRGVSFAYEEGPpVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGL--RPHAGRLTLGGEPVR 79
Cdd:COG2401 19 SVLDLSERVAIVLEAFGVELRVVERY-VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 80 YDRGGLTRLrttvqLVVQDPDDQLFAASVAqdvsfgplnlGLSDAevrsrvgealaaldiaALADRPTHLLSYGQRKRAA 159
Cdd:COG2401 98 REASLIDAI-----GRKGDFKDAVELLNAV----------GLSDA----------------VLWLRRFKELSTGQKFRFR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 664496302 160 IAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDL 211
Cdd:COG2401 147 LALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATHHYDV 199
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
32-237 |
1.15e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 73.68 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 32 GLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLT--LGGEPVRY-DRGGLTRLRTTVQLVVQDPDDQLFAASV 108
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEWVDMtKPGPDGRGRAKRYIGILHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 109 AQDVSFGPLNLGLSDAEVRSR-------VGeaLAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLD 181
Cdd:TIGR03269 382 VLDNLTEAIGLELPDELARMKavitlkmVG--FDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 664496302 182 PDGQERLLATLDRLRAA-GTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAAATLA 237
Cdd:TIGR03269 460 PITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKiVKIGDPEEIVE 517
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-222 |
1.27e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 11 TALVALRGVSFAYEEgPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAG------RLTLGGEPVRydrgg 84
Cdd:PRK09544 2 TSLVSLENVSVSFGQ-RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGvikrngKLRIGYVPQK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 85 lTRLRTTVQLVVQdpddqlfaasvaqdvSFGPLNLGLSDAEVrsrvGEALAALDIAALADRPTHLLSYGQRKRAAIAGAV 164
Cdd:PRK09544 76 -LYLDTTLPLTVN---------------RFLRLRPGTKKEDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLARAL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 664496302 165 AMRPRVLILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVDLALRWADEVALL 222
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
16-244 |
1.63e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 71.27 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTR----LRt 90
Cdd:COG4604 4 IKNVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVaTTPSRELAKrlaiLR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 91 tvqlvvQDPDdqlFAA--SVAQDVSFG--PLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAM 166
Cdd:COG4604 82 ------QENH---INSrlTVRELVAFGrfPYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 167 RPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGGV-HTGPAAATLaRTELLRQ 244
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDINFASCYADHIVAMKDGRVvAQGTPEEII-TPEVLSD 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
12-227 |
2.26e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.37 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 12 ALVALRGVSFAYEEgPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRY----DRGgltr 87
Cdd:PRK11000 2 ASVTLRNVTKAYGD-VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvppaERG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 88 lrttVQLVVQDpddqlFA----ASVAQDVSFGpLNL-GLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAG 162
Cdd:PRK11000 77 ----VGMVFQS-----YAlyphLSVAENMSFG-LKLaGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 664496302 163 AVAMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGGV 227
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
27-207 |
2.37e-14 |
|
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: 70.13 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 27 PPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGepVRYDRGGLTRLRTTVQLVVQDPddQLFAA 106
Cdd:cd03369 21 PPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG--IDISTIPLEDLRSSLTIIPQDP--TLFSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 107 SVAQDVSfgPLNLgLSDAEVRS--RVGEALAAldiaaladrpthlLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDG 184
Cdd:cd03369 97 TIRSNLD--PFDE-YSDEEIYGalRVSEGGLN-------------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180
....*....|....*....|...
gi 664496302 185 QERLLATLdRLRAAGTTVLMATH 207
Cdd:cd03369 161 DALIQKTI-REEFTNSTILTIAH 182
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
11-225 |
6.05e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.35 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 11 TALVALRGVSFAYeegPPV--LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGepVRYDRggLTRL 88
Cdd:PRK09700 3 TPYISMAGIGKSF---GPVhaLKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN--INYNK--LDHK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 89 RTT---VQLVVQDPD--DQLfaaSVAQDVSFGPL------NLGLSD-AEVRSRVGEALAALDIAALADRPTHLLSYGQRK 156
Cdd:PRK09700 76 LAAqlgIGIIYQELSviDEL---TVLENLYIGRHltkkvcGVNIIDwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664496302 157 RAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
33-181 |
7.97e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.82 E-value: 7.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 33 LDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYdrgGLTRLRTT-VQLVVQDPDDQLFAAS-VAQ 110
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF---GDYSYRSQrIRMIFQDPSTSLNPRQrISQ 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664496302 111 DVSFgP--LNLGLSDAEVRSRVGEALAALDIAAL-ADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLD 181
Cdd:PRK15112 109 ILDF-PlrLNTDLEPEQREKQIIETLRQVGLLPDhASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
28-209 |
8.64e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 69.29 E-value: 8.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 28 PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV------RYDRGGLTRLrttvqlvvqdpdd 101
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhKRARLGIGYL------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 102 qlfaasvAQDVS-FGPL----NL-------GLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPR 169
Cdd:COG1137 84 -------PQEASiFRKLtvedNIlavlelrKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 664496302 170 VLILDEPTAGLDPdgqerlLATLD------RLRAAGTTVLMATHDV 209
Cdd:COG1137 157 FILLDEPFAGVDP------IAVADiqkiirHLKERGIGVLITDHNV 196
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-214 |
9.43e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.07 E-value: 9.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 23 YEEG---PPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPvrydrggLTRLRTTVQLVVQD- 98
Cdd:PRK11629 15 YQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP-------MSKLSSAAKAELRNq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 99 ------------PDdqlFAAsvAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAM 166
Cdd:PRK11629 88 klgfiyqfhhllPD---FTA--LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 664496302 167 RPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALR 214
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKR 211
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-227 |
2.18e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 69.89 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 1 MNEPDRSTE--------STALVALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGrlt 72
Cdd:PLN03073 488 VNDPDYKFEfptpddrpGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG--- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 73 lggepvrydrgglTRLRTT-VQLVV--QDPDDQLfaasvaqDVSFGPLNL------GLSDAEVRSRVGEALAALDIAAla 143
Cdd:PLN03073 565 -------------TVFRSAkVRMAVfsQHHVDGL-------DLSSNPLLYmmrcfpGVPEQKLRAHLGSFGVTGNLAL-- 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 144 dRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAgttVLMATHDVDLALRWADEVALLT 223
Cdd:PLN03073 623 -QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG---VLMVSHDEHLISGSVDELWVVS 698
|
....
gi 664496302 224 PGGV 227
Cdd:PLN03073 699 EGKV 702
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
8-226 |
2.35e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.82 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 8 TESTALVALRGVSFAyEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV------RYd 81
Cdd:PRK10247 2 QENSPLLQLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIstlkpeIY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 82 rggltrlRTTVQLVVQDPddQLFAASVAQDVSFgPLnlglsdaEVRSRVGEALAALDIAALADRPTHLL-------SYGQ 154
Cdd:PRK10247 80 -------RQQVSYCAQTP--TLFGDTVYDNLIF-PW-------QIRNQQPDPAIFLDDLERFALPDTILtkniaelSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664496302 155 RKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDlALRWADEVALLTPGG 226
Cdd:PRK10247 143 KQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKD-EINHADKVITLQPHA 214
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-248 |
5.14e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.32 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 8 TESTAlvALRGVSFAYEEGP-PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGL 85
Cdd:PRK10253 2 TESVA--RLRGEQLTLGYGKyTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 86 TRlrtTVQLVVQD---PDDQLFAASVAQD-VSFGPLnLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIA 161
Cdd:PRK10253 80 AR---RIGLLAQNattPGDITVQELVARGrYPHQPL-FTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 162 GAVAMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGGVHTGPAAATLARTE 240
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAE 235
|
....*....
gi 664496302 241 LLRQA-GLR 248
Cdd:PRK10253 236 LIERIyGLR 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
35-227 |
5.82e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 68.14 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 35 FAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-RYDRGGLTRLRTTVQLVVQDPDDQLFAASVAQDVS 113
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIaKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 114 FGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLD 193
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190
....*....|....*....|....*....|....*
gi 664496302 194 RLRAAGT-TVLMATHDVDLALRWADEVALLTPGGV 227
Cdd:PRK10070 209 KLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-231 |
9.94e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.08 E-value: 9.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 2 NEPDRSTESTALVALRGVSFAYEEG-PPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRy 80
Cdd:PLN03232 1223 NRPVSGWPSRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA- 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 81 dRGGLTRLRTTVQLVVQDPddQLFAASVAQDVS-FGPLN-LGLSDAEVRSRVGEALAALD--IAALADRPTHLLSYGQRK 156
Cdd:PLN03232 1302 -KFGLTDLRRVLSIIPQSP--VLFSGTVRFNIDpFSEHNdADLWEALERAHIKDVIDRNPfgLDAEVSEGGENFSVGQRQ 1378
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 664496302 157 RAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLdRLRAAGTTVLMATHDVDLALRwADEVALLTPGGV--HTGP 231
Cdd:PLN03232 1379 LLSLARALLRRSKILVLDEATASVDVRTDSLIQRTI-REEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVleYDSP 1453
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-233 |
1.96e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 30 LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSgGLRPHA---GRLTLGGEPVRY------DRGGLTRLRTTVQLVVQdpd 100
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLS-GVYPHGtyeGEIIFEGEELQAsnirdtERAGIAIIHQELALVKE--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 101 dqlfaASVAQDVSFG--PLNLGLSD-AEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPT 177
Cdd:PRK13549 97 -----LSVLENIFLGneITPGGIMDyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 664496302 178 AGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAA 233
Cdd:PRK13549 172 ASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRhIGTRPAA 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-225 |
2.01e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.45 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 21 FAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRG----GLTRLRTTVQLVV 96
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDifqiDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 97 QDPDdQLFAASVAQDVSFGPLNLGLSDA-EVRSRVGEALAA----LDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVL 171
Cdd:PRK14246 97 QQPN-PFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKvglwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 664496302 172 ILDEPTAGLDPDGQERLLATLDRLRAAgTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
25-207 |
2.38e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 65.09 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 25 EGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSG--GLRPHAGRLTLGGE---------------------PVRYD 81
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEdilelspderaragiflafqyPVEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 82 rgGLTR---LRTTVQLVVQDP-DDQLFAASVAQDVSFgplnLGLSDAEVRSRVGEAlaaldiaaladrpthlLSYGQRKR 157
Cdd:COG0396 91 --GVSVsnfLRTALNARRGEElSAREFLKLLKEKMKE----LGLDEDFLDRYVNEG----------------FSGGEKKR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 664496302 158 AAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATH 207
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH 198
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
148-238 |
2.67e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.08 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 148 HLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQE---RLLATLDRLRaaGTTVLMATHDVDLALRWADEVALLTP 224
Cdd:COG4170 157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAqifRLLARLNQLQ--GTSILLISHDLESISQWADTITVLYC 234
|
90
....*....|....*
gi 664496302 225 G-GVHTGPAAATLAR 238
Cdd:COG4170 235 GqTVESGPTEQILKS 249
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
15-208 |
3.52e-12 |
|
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: 66.36 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 15 ALRGVSFAY--EEGPPVLT-G-LDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVryDRGGLTRLRt 90
Cdd:COG4615 329 ELRGVTYRYpgEDGDEGFTlGpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV--TADNREAYR- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 91 tvqlvvqdpddQLFAAsVAQDVSFGPLNLGLSDAEVRSRVGEalaaldiaaladrptHL--------------------L 150
Cdd:COG4615 406 -----------QLFSA-VFSDFHLFDRLLGLDGEADPARARE---------------LLerleldhkvsvedgrfsttdL 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664496302 151 SYGQRKRAAIAGAVAM-RPrVLILDEPTAGLDPDGQ----ERLLAtldRLRAAGTTVLMATHD 208
Cdd:COG4615 459 SQGQRKRLALLVALLEdRP-ILVFDEWAADQDPEFRrvfyTELLP---ELKARGKTVIAISHD 517
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
29-247 |
5.31e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.13 E-value: 5.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRyDRGGLTRLRTTVQLVVQDpdDQLFA-AS 107
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT-DWQTAKIMREAVAIVPEG--RRVFSrMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 108 VAQDVSFGPLNLGLSDAEVR-SRVGEALAALDIAALADRPThlLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQE 186
Cdd:PRK11614 97 VEENLAMGGFFAERDQFQERiKWVYELFPRLHERRIQRAGT--MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 664496302 187 RLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGVHTGPAAATLARTELLRQAGL 247
Cdd:PRK11614 175 QIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYL 235
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-226 |
6.04e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.60 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGgLRPHA-GRLTL--GGE----------Pvry 80
Cdd:COG4178 363 LALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYGsGRIARpaGARvlflpqrpylP--- 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 81 drggLTRLRTTV---QLVVQDPDDQLfaASVAQDVSFGPLNLGLSDAEVRSRVgealaaldiaaladrpthlLSYGQRKR 157
Cdd:COG4178 439 ----LGTLREALlypATAEAFSDAEL--REALEAVGLGHLAERLDEEADWDQV-------------------LSLGEQQR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664496302 158 AAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLdRLRAAGTTVLMATHDVDLAlRWADEVALLTPGG 226
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLL-REELPGTTVISVGHRSTLA-AFHDRVLELTGDG 560
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-207 |
6.87e-12 |
|
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: 62.17 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLsGGLRPHA-GRLTLggePVRydrggltrlrttv 92
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPWGsGRIGM---PEG------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 qlvvqdpDDQLFaasVAQDVSFGPLNLglsdaevRSRVgealaaldiaalaDRP-THLLSYGQRKRAAIAGAVAMRPRVL 171
Cdd:cd03223 64 -------EDLLF---LPQRPYLPLGTL-------REQL-------------IYPwDDVLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....*.
gi 664496302 172 ILDEPTAGLDPDGQERLLATldrLRAAGTTVLMATH 207
Cdd:cd03223 114 FLDEATSALDEESEDRLYQL---LKELGITVISVGH 146
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
12-208 |
9.21e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 64.48 E-value: 9.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 12 ALVALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVR----YDRGgltr 87
Cdd:PRK11650 2 AGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNelepADRD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 88 lrttVQLVVQDpddqlFA----ASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGA 163
Cdd:PRK11650 78 ----IAMVFQN-----YAlyphMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 664496302 164 VAMRPRVLILDEPTAGLDPD--GQERLlaTLDRL-RAAGTTVLMATHD 208
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKlrVQMRL--EIQRLhRRLKTTSLYVTHD 194
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
30-230 |
9.32e-12 |
|
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: 62.34 E-value: 9.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 30 LTGLDFAVHEGRALALLGRNGSGKTTLmrLLSGGLRphAGRLTLGGEPVRYDRGGLTRLrttvqlvvqdpdDQLfaaSVA 109
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYA--SGKARLISFLPKFSRNKLIFI------------DQL---QFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 110 QDVSFGPLNLGlsdaevrsrvgealaaldiaaladRPTHLLSYGQRKRAAIAGAVAMRPR--VLILDEPTAGLDPDGQER 187
Cdd:cd03238 72 IDVGLGYLTLG------------------------QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQ 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 664496302 188 LLATLDRLRAAGTTVLMATHDVDLaLRWADEVALLTPGGVHTG 230
Cdd:cd03238 128 LLEVIKGLIDLGNTVILIEHNLDV-LSSADWIIDFGPGSGKSG 169
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-238 |
1.13e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 63.18 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFayEEGPPVLTGLDFAVHEGRALALLGRNGSGKT----TLMRLLSGGLRPHAGRLTLGGEPVrydrgGLTRLR 89
Cdd:PRK10418 5 IELRNIAL--QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPV-----APCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 90 -TTVQLVVQDPDDqlfaasvaqdvSFGPLNlglsdaEVRSRVGEALAALDIAALADRPTHLL------------------ 150
Cdd:PRK10418 78 gRKIATIMQNPRS-----------AFNPLH------TMHTHARETCLALGKPADDATLTAALeavglenaarvlklypfe 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 151 -SYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGG-V 227
Cdd:PRK10418 141 mSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRiV 220
|
250
....*....|.
gi 664496302 228 HTGPAAATLAR 238
Cdd:PRK10418 221 EQGDVETLFNA 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
35-234 |
1.34e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.49 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 35 FAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEpvRYDR---GGLTRLRTTVQLVVQDPDDQLFAASVAQD 111
Cdd:PRK10261 345 FDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQ--RIDTlspGKLQALRRDIQFIFQDPYASLDPRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 112 VSFGPLNL-GLSDAE-VRSRVGEALAALDIAALAD-RPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERL 188
Cdd:PRK10261 423 SIMEPLRVhGLLPGKaAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 664496302 189 L-ATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAAA 234
Cdd:PRK10261 503 InLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQiVEIGPRRA 550
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-227 |
1.35e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.02 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 10 STALVALRGVSFAYeeGPPV-LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRltlggepVRYD-RGGLTR 87
Cdd:PRK11701 3 DQPLLSVRGLTKLY--GPRKgCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGE-------VHYRmRDGQLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 88 -------------LRTTVQLVVQDPDDQL-FAASVAQDVSFGPLNLG--------------LSDAEV-RSRVGEalaald 138
Cdd:PRK11701 74 dlyalseaerrrlLRTEWGFVHQHPRDGLrMQVSAGGNIGERLMAVGarhygdiratagdwLERVEIdAARIDD------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 139 iaaladRPThLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWAD 217
Cdd:PRK11701 148 ------LPT-TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAH 220
|
250
....*....|
gi 664496302 218 EVALLTPGGV 227
Cdd:PRK11701 221 RLLVMKQGRV 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-225 |
1.53e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.34 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 10 STALVALRGVSFAYEEGP---PVLTGLDFAVHEGRALALLGRNGSGKT----TLMRLL--------SGGLRPHAGRLTLG 74
Cdd:PRK15134 2 TQPLLAIENLSVAFRQQQtvrTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypSGDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 75 GEP-VRYDRGgltrlrTTVQLVVQDPDdqlfaasvaqdVSFGPL-NLGLSDAEVRS-------------------RVGea 133
Cdd:PRK15134 82 SEQtLRGVRG------NKIAMIFQEPM-----------VSLNPLhTLEKQLYEVLSlhrgmrreaargeilncldRVG-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 134 lAALDIAALADRPtHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAA-GTTVLMATHDVDLA 212
Cdd:PRK15134 143 -IRQAAKRLTDYP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIV 220
|
250
....*....|...
gi 664496302 213 LRWADEVALLTPG 225
Cdd:PRK15134 221 RKLADRVAVMQNG 233
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
32-208 |
1.58e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.57 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 32 GLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLT-LGGEPVRYDRGGLTRLRTTVQLVVQDPDDQLFAASVAQ 110
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 111 DVSFGPLNL---GLSDAEVRSRVGEALAALDIAALA-DRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQE 186
Cdd:PRK15079 119 EIIAEPLRTyhpKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180
....*....|....*....|...
gi 664496302 187 RLLATLDRL-RAAGTTVLMATHD 208
Cdd:PRK15079 199 QVVNLLQQLqREMGLSLIFIAHD 221
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-231 |
1.73e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.19 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 44 ALLGRNGSGKTTLMRLLS------GGLRpHAGRLTLGGEPVrYDRGGLTRLRTTVQLVVQDPDDqlFAASVAQDVSFGPL 117
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNrmndkvSGYR-YSGDVLLGGRSI-FNYRDVLEFRRRVGMLFQRPNP--FPMSIMDNVLAGVR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 118 NLGLSDAE-----VRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATL 192
Cdd:PRK14271 127 AHKLVPRKefrgvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI 206
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 664496302 193 DRLrAAGTTVLMATHDVDLALRWADEVALLTPGG-VHTGP 231
Cdd:PRK14271 207 RSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRlVEEGP 245
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-208 |
1.97e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.20 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 19 VSFAYEEGP-PVLTGLDFAVHEGRALALLGRNGSGKT----TLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTRLRT-TV 92
Cdd:PRK09473 20 VTFSTPDGDvTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIGGSATFNGREILNLPEKELNKLRAeQI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 QLVVQDP----------DDQL---------------FAASVAqdvsfgplnlgLSDA----EVRSRVGealaaldiaala 143
Cdd:PRK09473 100 SMIFQDPmtslnpymrvGEQLmevlmlhkgmskaeaFEESVR-----------MLDAvkmpEARKRMK------------ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 664496302 144 DRPtHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHD 208
Cdd:PRK09473 157 MYP-HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHD 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
39-207 |
2.01e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.91 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 39 EGRALALLGRNGSGKTTLMRLLSGGLRPH---AGRLTLGGEPVryDRGGLTRLRTTVQ--------LVVQDpdDQLFAA- 106
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI--DAKEMRAISAYVQqddlfiptLTVRE--HLMFQAh 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 107 -----SVAQD-----VSFGPLNLGLSDAEvRSRVGEALAALDiaaladrpthlLSYGQRKRAAIAGAVAMRPRVLILDEP 176
Cdd:TIGR00955 126 lrmprRVTKKekrerVDEVLQALGLRKCA-NTRIGVPGRVKG-----------LSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190
....*....|....*....|....*....|.
gi 664496302 177 TAGLDPDGQERLLATLDRLRAAGTTVLMATH 207
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-256 |
2.35e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.50 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 4 PDRSTESTALV-ALRGVSfayeeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRydr 82
Cdd:COG1129 246 PKRAAAPGEVVlEVEGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR--- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 83 ggltrLRTTVQ-------LVVQDPDDQ-LFAA-SVAQDVSFGPL----NLG-LSDAEVRSRVGEALAALD-IAALADRPT 147
Cdd:COG1129 318 -----IRSPRDairagiaYVPEDRKGEgLVLDlSIRENITLASLdrlsRGGlLDRRRERALAEEYIKRLRiKTPSPEQPV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 148 HLLSYG-QRKrAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGG 226
Cdd:COG1129 393 GNLSGGnQQK-VVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGR 471
|
250 260 270
....*....|....*....|....*....|
gi 664496302 227 VhtgpaAATLARTELLRQAGLRLPWGVAAA 256
Cdd:COG1129 472 I-----VGELDREEATEEAIMAAATGGAAA 496
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
34-207 |
2.55e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.99 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 34 DFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVryDRGGL-TRLRT-------------TVQ--LVVQ 97
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV--DAGDIaTRRRVgymsqafslygelTVRqnLELH 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 98 DpddQLFaasvaqdvsfgplnlGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPT 177
Cdd:NF033858 364 A---RLF---------------HLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190
....*....|....*....|....*....|...
gi 664496302 178 AGLDP---DGQERLLATLDRLRaaGTTVLMATH 207
Cdd:NF033858 426 SGVDPvarDMFWRLLIELSRED--GVTIFISTH 456
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-234 |
3.78e-11 |
|
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: 62.92 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 30 LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGgLRPHA---GRLTLGGEPVR------YDRGGLTRLRTTVQLVvqdPD 100
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLKasnirdTERAGIVIIHQELTLV---PE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 101 dqlfaASVAQDVSFG---PLNLGLSDAEVRSRVGEA--LAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDE 175
Cdd:TIGR02633 93 -----LSVAENIFLGneiTLPGGRMAYNAMYLRAKNllRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 176 PTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAAA 234
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQhVATKDMST 227
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-219 |
3.79e-11 |
|
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: 61.66 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 39 EGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLT-RLRTTVQLVVQDPDDQLFAASVAQDVSFGPL 117
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKaDYEGTVRDLLSSITKDFYTHPYFKTEIAKPL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 118 NL-GLSDAEVRSrvgealaaldiaaladrpthlLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLdpDGQERLLAT--LDR 194
Cdd:cd03237 104 QIeQILDREVPE---------------------LSGGELQRVAIAACLSKDADIYLLDEPSAYL--DVEQRLMASkvIRR 160
|
170 180
....*....|....*....|....*.
gi 664496302 195 L-RAAGTTVLMATHDVDLALRWADEV 219
Cdd:cd03237 161 FaENNEKTAFVVEHDIIMIDYLADRL 186
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
44-242 |
3.96e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 62.11 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 44 ALLGRNGSGKTTLMRL------LSGGLRPHaGRLTLGGEPVRYDRGGLTRLRTTVQLVVQDPDDqlFAASVAQDVSFGPL 117
Cdd:PRK14243 40 AFIGPSGCGKSTILRCfnrlndLIPGFRVE-GKVTFHGKNLYAPDVDPVEVRRRIGMVFQKPNP--FPKSIYDNIAYGAR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 118 NLGLS---DAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQ---ERLLAT 191
Cdd:PRK14243 117 INGYKgdmDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTlriEELMHE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 192 LDRlraaGTTVLMATHDVDLALRWADEVAL----LTPGGVHTGpAAATLARTELL 242
Cdd:PRK14243 197 LKE----QYTIIIVTHNMQQAARVSDMTAFfnveLTEGGGRYG-YLVEFDRTEKI 246
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
30-226 |
8.69e-11 |
|
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: 59.95 E-value: 8.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 30 LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGglRPHA----GRLTLGGEPVRYDrggltrLRTTVQLVVQdpddqlfa 105
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAgvitGEILINGRPLDKN------FQRSTGYVEQ-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 106 asvaQDVSFGPLN----LGLSdAEVRSrvgealaaldiaaladrpthlLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLD 181
Cdd:cd03232 87 ----QDVHSPNLTvreaLRFS-ALLRG---------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 664496302 182 PDGQERLLATLDRLRAAGTTVLMATHDVDLAL-RWADEVALLTPGG 226
Cdd:cd03232 141 SQAAYNIVRFLKKLADSGQAILCTIHQPSASIfEKFDRLLLLKRGG 186
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-207 |
1.07e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.86 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 1 MNEPDRSTesTALVALRGVSFAYEEgPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRy 80
Cdd:PRK13543 1 MIEPLHTA--PPLLAAHALAFSRNE-EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 81 dRGGLTRLRTTV-QLVVQDPDdqlfaASVAQDVSFgpLNlGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAA 159
Cdd:PRK13543 77 -RGDRSRFMAYLgHLPGLKAD-----LSTLENLHF--LC-GLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 664496302 160 IAGAVAMRPRVLILDEPTAGLDPDG---QERLLATldRLRAAGTTvLMATH 207
Cdd:PRK13543 148 LARLWLSPAPLWLLDEPYANLDLEGitlVNRMISA--HLRGGGAA-LVTTH 195
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-222 |
1.44e-10 |
|
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: 59.41 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYE----EGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGepvrydrggltrlr 89
Cdd:cd03250 1 ISVEDASFTWDsgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 90 tTVQLVVQDPddQLFAASVAQDVSFG-PLN------------LgLSDAEV-----RSRVGEALAAldiaaladrpthlLS 151
Cdd:cd03250 67 -SIAYVSQEP--WIQNGTIRENILFGkPFDeeryekvikacaL-EPDLEIlpdgdLTEIGEKGIN-------------LS 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 152 YGQRKRAAIAGAVAMRPRVLILDEPTAGLDPD-GQ---ERLLATLDRLraaGTTVLMATHDVDLALRwADEVALL 222
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAHvGRhifENCILGLLLN---NKTRILVTHQLQLLPH-ADQIVVL 200
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
34-270 |
1.49e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.18 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 34 DFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLG-GEPVRYDRGGLTRL------RTTVQLVVQDPDDQ-LFA 105
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfSHITRLSFEQLQKLvsdewqRNNTDMLSPGEDDTgRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 106 ASVAQDvsfgplnlGLSDAEvrsRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQ 185
Cdd:PRK10938 103 AEIIQD--------EVKDPA---RCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 186 ERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAA--------ATLARTELLrqAGLRLPwgvaAA 256
Cdd:PRK10938 172 QQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTlAETGEREeilqqalvAQLAHSEQL--EGVQLP----EP 245
|
250
....*....|....
gi 664496302 257 SVLRARGLLAESAA 270
Cdd:PRK10938 246 DEPSARHALPANEP 259
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
14-227 |
1.66e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.90 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPPVlTGLDFAVHEGRALALLGRNGSGKTtlmrllSGGLRPHAGRLTLGGEPVRYDRGGLTR--LRTT 91
Cdd:NF000106 14 VEVRGLVKHFGEVKAV-DGVDLDVREGTVLGVLGP*GAA**------RGALPAHV*GPDAGRRPWRF*TWCANRraLRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 VQLVVQDPDDQLFAASVAQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVL 171
Cdd:NF000106 87 IG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 664496302 172 ILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGV 227
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-207 |
1.73e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.05 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGglRPHAGRLTlgGEPVRYDRGGLTRLRTTVQLVVQDpdDQLFA-AS 107
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG--RIQGNNFT--GTILANNRKPTKQILKRTGFVTQD--DILYPhLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 108 VAQDVSFGPLnLGLSDA---EVRSRVGEALAALDIAALADRPT------HLLSYGQRKRAAIAGAVAMRPRVLILDEPTA 178
Cdd:PLN03211 157 VRETLVFCSL-LRLPKSltkQEKILVAESVISELGLTKCENTIignsfiRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180
....*....|....*....|....*....
gi 664496302 179 GLDPDGQERLLATLDRLRAAGTTVLMATH 207
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-209 |
4.03e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 58.75 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 25 EGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGE-----PVRydrgglTRLRTTVQLVVQDP 99
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLH------ARARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 100 ddQLFAASVAQDVSFGPLNL--GLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPT 177
Cdd:PRK10895 88 --SIFRRLSVYDNLMAVLQIrdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190
....*....|....*....|....*....|..
gi 664496302 178 AGLDPDGQERLLATLDRLRAAGTTVLMATHDV 209
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDSGLGVLITDHNV 197
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
11-207 |
5.86e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 11 TALVALRGVSFAYEeGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYD------RGG 84
Cdd:PRK10762 2 QALLQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpkssqEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 85 LTRLRTTVQLVvqdpdDQLfaaSVAQDV--------SFGPLN--------------LGLSDAEvRSRVGEalaaldiaal 142
Cdd:PRK10762 81 IGIIHQELNLI-----PQL---TIAENIflgrefvnRFGRIDwkkmyaeadkllarLNLRFSS-DKLVGE---------- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 143 adrpthlLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATH 207
Cdd:PRK10762 142 -------LSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISH 199
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
145-230 |
8.19e-10 |
|
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: 57.65 E-value: 8.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 145 RPTHLLSYGQRKRAAIAGAVAMR-PRVL-ILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLaLRWADEVALL 222
Cdd:cd03270 133 RSAPTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDT-IRAADHVIDI 211
|
....*....
gi 664496302 223 TPG-GVHTG 230
Cdd:cd03270 212 GPGaGVHGG 220
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
44-227 |
8.27e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 58.73 E-value: 8.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 44 ALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEpVRYDRGGLTRL---RTTVQLVVQDPddQLFAA-SVAqdvsfGPLNL 119
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR-VLFDAEKGICLppeKRRIGYVFQDA--RLFPHyKVR-----GNLRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 120 GLSdAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLD-PDGQErLLATLDRL-RA 197
Cdd:PRK11144 100 GMA-KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRE-LLPYLERLaRE 177
|
170 180 190
....*....|....*....|....*....|
gi 664496302 198 AGTTVLMATHDVDLALRWADEVALLTPGGV 227
Cdd:PRK11144 178 INIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
35-244 |
1.21e-09 |
|
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: 58.68 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 35 FAVHEGRALALLGRNGSGKTTLMRLLSGGLR-PHAGRLTLGGEPVRYdRGGLTRLRTTVQLVVQDPDDQLFAA--SVAQD 111
Cdd:TIGR02633 281 FSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDI-RNPAQAIRAGIAMVPEDRKRHGIVPilGVGKN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 112 VSFGPLN----LGLSD--AEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQ 185
Cdd:TIGR02633 360 ITLSVLKsfcfKMRIDaaAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAK 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 664496302 186 ERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALltpggVHTGPAAATLARTELLRQ 244
Cdd:TIGR02633 440 YEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLV-----IGEGKLKGDFVNHALTQE 493
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-230 |
1.50e-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: 58.49 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 145 RPTHLLSYGQRKRAAIAGAVAMR-PRVL-ILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDlALRWADEVALL 222
Cdd:TIGR00630 484 RAAGTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED-TIRAADYVIDI 562
|
....*....
gi 664496302 223 TPG-GVHTG 230
Cdd:TIGR00630 563 GPGaGEHGG 571
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-249 |
1.55e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.00 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 25 EGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTrLRTTVQLVvqdPDDQLF 104
Cdd:PRK11288 264 KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDA-IRAGIMLC---PEDRKA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 105 -----AASVAQdvsfgplNLGLSDAEVRSRVGEALAALDIAALADR--------------PTHLLSYGQRKRAAIAGAVA 165
Cdd:PRK11288 340 egiipVHSVAD-------NINISARRHHLRAGCLINNRWEAENADRfirslniktpsreqLIMNLSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 166 MRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPGGVhtgpaAATLARTELLRQA 245
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI-----AGELAREQATERQ 487
|
....
gi 664496302 246 GLRL 249
Cdd:PRK11288 488 ALSL 491
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-181 |
1.75e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 2 NEPDRSTESTALVALRGVSFAYE-EGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRy 80
Cdd:PLN03130 1226 NRPPPGWPSSGSIKFEDVVLRYRpELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS- 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 81 dRGGLTRLRTTVQLVVQDPddQLFAASVAqdVSFGPLN------------------------LGLsDAEVrSRVGEAlaa 136
Cdd:PLN03130 1305 -KFGLMDLRKVLGIIPQAP--VLFSGTVR--FNLDPFNehndadlweslerahlkdvirrnsLGL-DAEV-SEAGEN--- 1374
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 664496302 137 ldiaaladrpthlLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLD 181
Cdd:PLN03130 1375 -------------FSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-220 |
1.92e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.73 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 13 LVALRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV-------RYDRGGL 85
Cdd:COG3845 257 VLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglspreRRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 86 T----RLRT------TVQ--LVVQDPDDQLFAasvaqdvSFGPLNLGLSDAEVRSRVGEALAALDIAALadrPTHLLSYG 153
Cdd:COG3845 337 YipedRLGRglvpdmSVAenLILGRYRRPPFS-------RGGFLDRKAIRAFAEELIEEFDVRTPGPDT---PARSLSGG 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 664496302 154 QRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVA 220
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIA 473
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-209 |
2.49e-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: 57.49 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 37 VHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTlGGEPVRY-------DRGGltrlrtTVQLVVQDPDDQLFAASVA 109
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKISYkpqyispDYDG------TVEEFLRSANTDDFGSSYY 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 110 QDVSFGPLNLG-LSDAEVRSrvgealaaldiaaladrpthlLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDgqERL 188
Cdd:COG1245 436 KTEIIKPLGLEkLLDKNVKD---------------------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE--QRL 492
|
170 180
....*....|....*....|....
gi 664496302 189 LAT--LDRL-RAAGTTVLMATHDV 209
Cdd:COG1245 493 AVAkaIRRFaENRGKTAMVVDHDI 516
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-181 |
2.60e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 26 GPPVlTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPV--RYDRGGLtrlRTTVQLVVQD--PDD 101
Cdd:PRK10762 265 GPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtRSPQDGL---ANGIVYISEDrkRDG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 102 QLFAASVAQDVSFGPLNLgLSDAEVRSRVGEALAALD--------IAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLIL 173
Cdd:PRK10762 341 LVLGMSVKENMSLTALRY-FSRAGGSLKHADEQQAVSdfirlfniKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
....*...
gi 664496302 174 DEPTAGLD 181
Cdd:PRK10762 420 DEPTRGVD 427
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-222 |
2.88e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.49 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 27 PPV--LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGgLRPHA---GRLTLGGEPVRY------DRGGLTRLRTTVQLV 95
Cdd:NF040905 12 PGVkaLDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHGsyeGEILFDGEVCRFkdirdsEALGIVIIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 96 vqdPddQLfaaSVAQDVSFG--PLNLGLSD--------AEVRSRVGealaaldiaaLADRPTHL---LSYGQRKRAAIAG 162
Cdd:NF040905 91 ---P--YL---SIAENIFLGneRAKRGVIDwnetnrraRELLAKVG----------LDESPDTLvtdIGVGKQQLVEIAK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 163 AVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALL 222
Cdd:NF040905 153 ALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVL 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-247 |
3.26e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.65 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPP-VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGepVRYDRGGLTRLRTTV 92
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--LNIAKIGLHDLRFKI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 QLVVQDPddQLFAASVAQDVS-FGPLnlglSDAEVRSRVGEALAALDIAALADRPTHL-------LSYGQRKRAAIAGAV 164
Cdd:TIGR00957 1363 TIIPQDP--VLFSGSLRMNLDpFSQY----SDEEVWWALELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARAL 1436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 165 AMRPRVLILDEPTAGLDPDGQERLLATLdRLRAAGTTVLMATHDVDLALRWAdEVALLTPGGVHTGPAAAtlartELLRQ 244
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETDNLIQSTI-RTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPS-----NLLQQ 1509
|
...
gi 664496302 245 AGL 247
Cdd:TIGR00957 1510 RGI 1512
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-181 |
3.48e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 55.35 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 11 TALVALRGVSFAYEEGP---PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHA---GRLTLGGEPV-----R 79
Cdd:cd03233 1 ASTLSWRNISFTTGKGRskiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYkefaeK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 80 YDRggltrlrttvQLVVQDPDDQLFAA-SVAQDVSFGPLNLGlsDAEVRSrvgealaaldiaaladrpthlLSYGQRKRA 158
Cdd:cd03233 81 YPG----------EIIYVSEEDVHFPTlTVRETLDFALRCKG--NEFVRG---------------------ISGGERKRV 127
|
170 180
....*....|....*....|...
gi 664496302 159 AIAGAVAMRPRVLILDEPTAGLD 181
Cdd:cd03233 128 SIAEALVSRASVLCWDNSTRGLD 150
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
150-225 |
4.21e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 56.35 E-value: 4.21e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 664496302 150 LSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCG 235
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-213 |
4.83e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.23 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 24 EEGPPVLTGLDFAVHEGRALALLGRNGSGKTTL----MRLLSGglrphAGRLTLGGepVRYDRGGLTRLRTTVQLVVQ-- 97
Cdd:TIGR01271 1229 EAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLlsalLRLLST-----EGEIQIDG--VSWNSVTLQTWRKAFGVIPQkv 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 98 -----------DP-----DDQLFaaSVAQDVSF--------GPLNLGLSDAevrsrvgealaaldiaaladrpTHLLSYG 153
Cdd:TIGR01271 1302 fifsgtfrknlDPyeqwsDEEIW--KVAEEVGLksvieqfpDKLDFVLVDG----------------------GYVLSNG 1357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 154 QRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRlRAAGTTVLMATHDVDLAL 213
Cdd:TIGR01271 1358 HKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHRVEALL 1416
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-211 |
1.05e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 12 ALVALRGVSFAYEEGPpVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLT---------LGGEPVRYDR 82
Cdd:PRK11147 2 SLISIHGAWLSFSDAP-LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIyeqdlivarLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 83 GG---------------LTRLRTTVQLVVQDPDDQLFAA-SVAQDVsFGPLNLGLSDaevrSRVGEALAALDIAALAdrP 146
Cdd:PRK11147 81 GTvydfvaegieeqaeyLKRYHDISHLVETDPSEKNLNElAKLQEQ-LDHHNLWQLE----NRINEVLAQLGLDPDA--A 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 147 THLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRaaGTTVL----------MATHDVDL 211
Cdd:PRK11147 154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ--GSIIFishdrsfirnMATRIVDL 226
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
145-226 |
1.30e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 54.54 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 145 RPTHLLSYGQRKRAAIAGAVAMRPR---VLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLaLRWADEVAL 221
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDV-IKCADWIID 243
|
....*
gi 664496302 222 LTPGG 226
Cdd:cd03271 244 LGPEG 248
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-230 |
1.37e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.25 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 8 TESTALVALRGVSFAY-EEGPPV--LTGLDFAVHEGRALALLGRNGSGKT----TLMRLL-SGGLRPHAGRLTLGG---- 75
Cdd:PRK10261 7 LDARDVLAVENLNIAFmQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeQAGGLVQCDKMLLRRrsrq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 76 --EPVRYDRGGLTRLR-TTVQLVVQDPDDQL-----FAASVAQDVSfgpLNLGLSDAEVRS---RVGEALAALDIAALAD 144
Cdd:PRK10261 87 viELSEQSAAQMRHVRgADMAMIFQEPMTSLnpvftVGEQIAESIR---LHQGASREEAMVeakRMLDQVRIPEAQTILS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 145 RPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTT-VLMATHDVDLALRWADEVALLT 223
Cdd:PRK10261 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMY 243
|
....*...
gi 664496302 224 PG-GVHTG 230
Cdd:PRK10261 244 QGeAVETG 251
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
9-204 |
1.96e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 9 ESTALVALRGVSFAYEEgPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGlRP--HAGRLTLGGEpvryDRG-GL 85
Cdd:PRK10938 256 ANEPRIVLNNGVVSYND-RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPqgYSNDLTLFGR----RRGsGE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 86 T-------------------RLRTTVQLVV------------QDPDDQLFAASVAQDVsfgplnLGLSDAEVRSrvgeal 134
Cdd:PRK10938 330 TiwdikkhigyvssslhldyRVSTSVRNVIlsgffdsigiyqAVSDRQQKLAQQWLDI------LGIDKRTADA------ 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 135 aaldiaaladrPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLM 204
Cdd:PRK10938 398 -----------PFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLL 456
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-220 |
2.56e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.56 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 32 GLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGgepvrydrggltrlrTTVQL--VVQDPDDQLFAASVA 109
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG---------------ETVKLayVDQSRDALDPNKTVW 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 110 QDVSFGPLNLGLSDAEVRSR----------------VGEalaaldiaaladrpthlLSYGQRKRAAIAGAVAMRPRVLIL 173
Cdd:TIGR03719 405 EEISGGLDIIKLGKREIPSRayvgrfnfkgsdqqkkVGQ-----------------LSGGERNRVHLAKTLKSGGNVLLL 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 664496302 174 DEPTAGLDpdgQERLLATLDRLRAAGTTVLMATHDvdlalRW-ADEVA 220
Cdd:TIGR03719 468 DEPTNDLD---VETLRALEEALLNFAGCAVVISHD-----RWfLDRIA 507
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-209 |
4.44e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 37 VHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTlggepvrydrgglTRLRTTV--QLVVQDPDD--QLFAASVAQDV 112
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-------------PELKISYkpQYIKPDYDGtvEDLLRSITDDL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 113 S--------FGPLNLG-LSDAEVRSrvgealaaldiaaladrpthlLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPd 183
Cdd:PRK13409 429 GssyykseiIKPLQLErLLDKNVKD---------------------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV- 486
|
170 180
....*....|....*....|....*....
gi 664496302 184 gQERLLAT--LDRL-RAAGTTVLMATHDV 209
Cdd:PRK13409 487 -EQRLAVAkaIRRIaEEREATALVVDHDI 514
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
39-231 |
5.28e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 39 EGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTlgGEP-----VRYDRGglTRLRTTVQLVVqdpDDQLFAASVAQDVS 113
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYE--EEPswdevLKRFRG--TELQNYFKKLY---NGEIKVVHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 114 FGPLNL-G-----LSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDgqER 187
Cdd:PRK13409 171 LIPKVFkGkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR--QR 248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 664496302 188 L-LATLDRLRAAGTTVLMATHdvDLA-LRW-ADEVALL--TPG--GVHTGP 231
Cdd:PRK13409 249 LnVARLIRELAEGKYVLVVEH--DLAvLDYlADNVHIAygEPGayGVVSKP 297
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-227 |
5.86e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 6 RSTES--TALVALRGVSFAYEEgPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGG-------- 75
Cdd:PRK10636 303 RAPESlpNPLLKMEKVSAGYGD-RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiklgyfa 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 76 ----EPVRYDRGGLTRLrttVQLVVQDPDDQLfaasvaQDVSFGplnLGLSDAEVrsrvgealaaldiaalaDRPTHLLS 151
Cdd:PRK10636 382 qhqlEFLRADESPLQHL---ARLAPQELEQKL------RDYLGG---FGFQGDKV-----------------TEETRRFS 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 664496302 152 YGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAgttVLMATHDVDLALRWADEVALLTPGGV 227
Cdd:PRK10636 433 GGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGA---LVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-69 |
7.43e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 7.43e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 664496302 14 VALRGVSFAYEEGPpVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAG 69
Cdd:PRK15064 320 LEVENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
27-216 |
8.22e-08 |
|
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: 50.82 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 27 PPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSgglrphagrLTLGGEPVRYDRGGLTRLRTTVqlvvqdpddqlfaa 106
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG---------LALGGAQSATRRRSGVKAGCIV-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 107 svaqdvsfgplnlGLSDAEVRSRVgealaaldiaaladrptHLLSYGQRKRAAIAGAVAMR---PRVL-ILDEPTAGLDP 182
Cdd:cd03227 65 -------------AAVSAELIFTR-----------------LQLSGGEKELSALALILALAslkPRPLyILDEIDRGLDP 114
|
170 180 190
....*....|....*....|....*....|....
gi 664496302 183 DGQERLLATLDRLRAAGTTVLMATHDVDLALRWA 216
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIVITHLPELAELAD 148
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
24-213 |
8.76e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 52.16 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 24 EEGPPVLTGLDFAVHEGRALALLGRNGSGKTTL----MRLLSGglrphAGRLTLGGepVRYDRGGLTRLRTTVQLVVQ-- 97
Cdd:cd03289 14 EGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLNT-----EGDIQIDG--VSWNSVPLQKWRKAFGVIPQkv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 98 -----------DP-----DDQLFaaSVAQDVSF--------GPLNLGLSDAevrsrvgealaaldiaaladrpTHLLSYG 153
Cdd:cd03289 87 fifsgtfrknlDPygkwsDEEIW--KVAEEVGLksvieqfpGQLDFVLVDG----------------------GCVLSHG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 154 QRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLdRLRAAGTTVLMATHDVDLAL 213
Cdd:cd03289 143 HKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTL-KQAFADCTVILSEHRIEAML 201
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-227 |
1.01e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.79 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 20 SFAY-EEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLL-------SGGLRPHAGRLTlggepvrydRGGLTRLRTT 91
Cdd:PRK10789 320 QFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIqrhfdvsEGDIRFHDIPLT---------KLQLDSWRSR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 VQLVVQDPddQLFAASVAQDVSFGPLNLGLSDAEVRSR------------------VGEALAaldiaaladrpthLLSYG 153
Cdd:PRK10789 391 LAVVSQTP--FLFSDTVANNIALGRPDATQQEIEHVARlasvhddilrlpqgydteVGERGV-------------MLSGG 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664496302 154 QRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRaAGTTVLMATHDVDlALRWADEVALLTPGGV 227
Cdd:PRK10789 456 QKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLS-ALTEASEILVMQHGHI 527
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
146-211 |
1.10e-07 |
|
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: 52.01 E-value: 1.10e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664496302 146 PTHLLSYGQRKRAAIAGAV---AMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDL 211
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLL 301
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-225 |
1.19e-07 |
|
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: 52.71 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 28 PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVrydrggLTRLRTTVQLVVQDPDdqlFAAs 107
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI------LTNISDVHQNMGYCPQ---FDA- 2022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 108 vAQDVSFGPLNL-------GLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGL 180
Cdd:TIGR01257 2023 -IDDLLTGREHLylyarlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 664496302 181 DPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:TIGR01257 2102 DPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
30-209 |
1.22e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.74 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 30 LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGE-PVRYDRGGLTRLRTTVqlvvqdpddqlfaasv 108
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISAGLSGQLTGI---------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 109 aQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERL 188
Cdd:PRK13546 104 -ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180
....*....|....*....|.
gi 664496302 189 LATLDRLRAAGTTVLMATHDV 209
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNL 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-231 |
1.71e-07 |
|
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: 52.09 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 39 EGRALALLGRNGSGKTTLMRLLSGGLRPHAGRltLGGEP-----VRYDRGglTRLRTTVQLVVqdpDDQLFAASVAQDVS 113
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGD--YDEEPswdevLKRFRG--TELQDYFKKLA---NGEIKVAHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 114 FGPLNLG------LSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAgAVAMRPR-VLILDEPTAGLDPDgqE 186
Cdd:COG1245 171 LIPKVFKgtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIA-AALLRDAdFYFFDEPSSYLDIY--Q 247
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 664496302 187 RLLA--TLDRLRAAGTTVLMATHdvDLA-LRW-ADEVALL--TPG--GVHTGP 231
Cdd:COG1245 248 RLNVarLIRELAEEGKYVLVVEH--DLAiLDYlADYVHILygEPGvyGVVSKP 298
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-238 |
1.89e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.26 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEG-PPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEpVRYdrggltrlrTTV 92
Cdd:TIGR00957 637 ITVHNATFTWARDlPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAY---------VPQ 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 QLVVQDpddqlfaASVAQDVSFG-PLNLG-----------LSDAEV-----RSRVGEALAAldiaaladrpthlLSYGQR 155
Cdd:TIGR00957 707 QAWIQN-------DSLRENILFGkALNEKyyqqvleacalLPDLEIlpsgdRTEIGEKGVN-------------LSGGQK 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 156 KRAAIAGAVAMRPRVLILDEPTAGLDPD----------GQERLLatldrlraAGTTVLMATHDVDLaLRWADEVALLTPG 225
Cdd:TIGR00957 767 QRVSLARAVYSNADIYLFDDPLSAVDAHvgkhifehviGPEGVL--------KNKTRILVTHGISY-LPQVDVIIVMSGG 837
|
250
....*....|....
gi 664496302 226 GV-HTGPAAATLAR 238
Cdd:TIGR00957 838 KIsEMGSYQELLQR 851
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
25-227 |
2.40e-07 |
|
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: 51.34 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 25 EGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSG--GLRPHAGRL----------------TLGGEPVRYDRGGLT 86
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpSKVGEPCPVCGGTLE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 87 ---------------RLRTTVQLVVQdpddQLFAASVAQDVSFGPLNlGLSDAEVRSR--VGEALAALDIAALADRPTHL 149
Cdd:TIGR03269 91 peevdfwnlsdklrrRIRKRIAIMLQ----RTFALYGDDTVLDNVLE-ALEEIGYEGKeaVGRAVDLIEMVQLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 150 ---LSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:TIGR03269 166 ardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLSDKAIWLENG 245
|
..
gi 664496302 226 GV 227
Cdd:TIGR03269 246 EI 247
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
44-225 |
2.41e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 44 ALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYD------RGGLTRLRTTVQLVVQD-----------PDDQLFA- 105
Cdd:PRK10982 28 ALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKsskealENGISMVHQELNLVLQRsvmdnmwlgryPTKGMFVd 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 106 -ASVAQDVS--FGPLNLglsDAEVRSRVGEalaaldiaaladrpthlLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDP 182
Cdd:PRK10982 108 qDKMYRDTKaiFDELDI---DIDPRAKVAT-----------------LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 664496302 183 DGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:PRK10982 168 KEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-205 |
2.59e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.70 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPP-VLTGLDFAVHEGRALALLGRNGSGKTTL----MRLLSgglrphagrlTLGGEPVRYDRG----G 84
Cdd:PTZ00243 1309 LVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLlltfMRMVE----------VCGGEIRVNGREigayG 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 85 LTRLRTTVQLVVQDPddQLFAASVAQDVSfgPLnLGLSDAEV---------RSRVGEALAALDIAALADRPTHllSYGQR 155
Cdd:PTZ00243 1379 LRELRRQFSMIPQDP--VLFDGTVRQNVD--PF-LEASSAEVwaalelvglRERVASESEGIDSRVLEGGSNY--SVGQR 1451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 664496302 156 KRAAIAGAVAMRPRVLIL-DEPTAGLDPDGQERLLATLDRLRAAGTTVLMA 205
Cdd:PTZ00243 1452 QLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIA 1502
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
35-233 |
3.27e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.90 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 35 FAVHEGRALALLGRNGSGKTtLMRLLSGGLRPHAGRLTlgGEPVRYDRGGLTRLR---------TTVQLVVQDPDDQLFA 105
Cdd:PRK11022 28 YSVKQGEVVGIVGESGSGKS-VSSLAIMGLIDYPGRVM--AEKLEFNGQDLQRISekerrnlvgAEVAMIFQDPMTSLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 106 ASVA--QDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPT---HLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGL 180
Cdd:PRK11022 105 CYTVgfQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDvypHQLSGGMSQRVMIAMAIACRPKLLIADEPTTAL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 181 DPDGQERLLATLDRL-RAAGTTVLMATHDVDLALRWADEVALLTPGG-VHTGPAA 233
Cdd:PRK11022 185 DVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQvVETGKAH 239
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-209 |
5.12e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGP--PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLL------------------------------- 60
Cdd:PTZ00265 1166 IEIMDVNFRYISRPnvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 61 -----------------------SGGLRPHAGRLTLGGEPV-RYDrggLTRLRTTVQLVVQDPddQLFAASVAQDVSFGP 116
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgeDSTVFKNSGKILLDGVDIcDYN---LKDLRNLFSIVSQEP--MLFNMSIYENIKFGK 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 117 LNLGLSDAEVRSRVGeALAALDIAALADRPTHL------LSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLA 190
Cdd:PTZ00265 1321 EDATREDVKRACKFA-AIDEFIESLPNKYDTNVgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
250 260
....*....|....*....|
gi 664496302 191 TL-DRLRAAGTTVLMATHDV 209
Cdd:PTZ00265 1400 TIvDIKDKADKTIITIAHRI 1419
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-231 |
5.54e-07 |
|
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: 49.67 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 35 FAVH------EGRALALLGRNGSGKTTLMRLLSGGLRPHAGRltLGGEP-----VRYDRGG-----LTRLRttvqlvvqd 98
Cdd:cd03236 15 FKLHrlpvprEGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeiLDEFRGSelqnyFTKLL--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 99 pDDQLFAASVAQDVSF------GPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLI 172
Cdd:cd03236 84 -EGDVKVIVKPQYVDLipkavkGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664496302 173 LDEPTAGLDPdgQERLLA--TLDRLRAAGTTVLMATHDVDLALRWADEVALL--TPG--GVHTGP 231
Cdd:cd03236 163 FDEPSSYLDI--KQRLNAarLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLygEPGayGVVTLP 225
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
170-230 |
6.09e-07 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 50.46 E-value: 6.09e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664496302 170 VL-ILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDlALRWADEVALLTPG-GVHTG 230
Cdd:PRK00349 511 VLyVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDED-TIRAADYIVDIGPGaGVHGG 572
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
170-230 |
7.13e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.41 E-value: 7.13e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664496302 170 VL-ILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDlALRWADEVALLTPG-GVHTG 230
Cdd:COG0178 507 VLyVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDED-TIRAADYIIDIGPGaGEHGG 568
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
40-209 |
8.37e-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: 47.75 E-value: 8.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 40 GRALALLGRNGSGKTTLMRLLsgglrphAGRLTLGGEPVRYDRGGLTRLRTTVQLVVQDPDDQLFAASVAQDVsfgplnl 119
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARAL-------ARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRL------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 120 glsdaevrsrvgealaaldiaaladrpthllsygqrkRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLD------ 193
Cdd:smart00382 68 -------------------------------------RLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllll 110
|
170
....*....|....*.
gi 664496302 194 RLRAAGTTVLMATHDV 209
Cdd:smart00382 111 LKSEKNLTVILTTNDE 126
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-225 |
1.31e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.44 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 145 RPTHLLSYGQRKRAAIA---GAVAMRPrVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDvDLALRWADEVAL 221
Cdd:PRK00635 472 RALATLSGGEQERTALAkhlGAELIGI-TYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRIID 549
|
....
gi 664496302 222 LTPG 225
Cdd:PRK00635 550 IGPG 553
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-231 |
1.60e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 29 VLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGglRPHAGRLTLGGEPVrydrgGLTRLRTTVQLV---VQDPDDQLFA 105
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLV-----NGRPLDSSFQRSigyVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 106 ASVAQDVSFGP---LNLGLSDAEVRSRVGE----ALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLI-LDEPT 177
Cdd:TIGR00956 851 STVRESLRFSAylrQPKSVSKSEKMEYVEEviklLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPT 930
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 664496302 178 AGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWA-DEVALLTPGG--VHTGP 231
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEfDRLLLLQKGGqtVYFGD 987
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
30-225 |
2.54e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.51 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 30 LTG-----LDFAVHEGRALALLGRNGSGKTTLMRLLSGgLRP-HAGRLTLGGEPVRyDRGGLTRLRttvQLVVQDPDDQ- 102
Cdd:PRK15439 274 LTGegfrnISLEVRAGEILGLAGVVGAGRTELAETLYG-LRPaRGGRIMLNGKEIN-ALSTAQRLA---RGLVYLPEDRq 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 103 ---LFA-ASVAQDVS---FGPLNLGLSDAEVRSRV-GEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILD 174
Cdd:PRK15439 349 ssgLYLdAPLAWNVCaltHNRRGFWIKPARENAVLeRYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 664496302 175 EPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-207 |
3.08e-06 |
|
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: 46.94 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 21 FAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGGLTRLRT--TVQLVVQD 98
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrySVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 99 PddQLFAASVAQDVSFG-PLNLGLSDAEV----------------RSRVGEALAAldiaaladrpthlLSYGQRKRAAIA 161
Cdd:cd03290 88 P--WLLNATVEENITFGsPFNKQRYKAVTdacslqpdidllpfgdQTEIGERGIN-------------LSGGQRQRICVA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 664496302 162 GAVAMRPRVLILDEPTAGLDPDGQERLL--ATLDRLRAAGTTVLMATH 207
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTH 200
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
35-225 |
6.29e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.09 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 35 FAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRyDRGGLTRLRTTVQLVVQDPDDQLFAA--SVAQDV 112
Cdd:PRK09700 284 FSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS-PRSPLDAVKKGMAYITESRRDNGFFPnfSIAQNM 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 113 SFGPL--------NLGLSDAEVRSRVGEALAALDIAALADRPTHL--LSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDP 182
Cdd:PRK09700 363 AISRSlkdggykgAMGLFHEVDEQRTAENQRELLALKCHSVNQNIteLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 664496302 183 DGQERLLATLDRLRAAGTTVLMATHDVDLALRWADEVALLTPG 225
Cdd:PRK09700 443 GAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
26-225 |
8.34e-06 |
|
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: 46.39 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 26 GPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRP------HAGRLTLGGE---------------PVRYDRgg 84
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPsegkikHSGRISFSSQfswimpgtikeniifGVSYDE-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 85 lTRLRTTVQlvvqdpddqlfAASVAQDVSFGPlnlglsdAEVRSRVGEALAAldiaaladrpthlLSYGQRKRAAIAGAV 164
Cdd:cd03291 127 -YRYKSVVK-----------ACQLEEDITKFP-------EKDNTVLGEGGIT-------------LSGGQRARISLARAV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664496302 165 AMRPRVLILDEPTAGLDPDGQERLLAT-LDRLRAAGTTVLMaTHDVDlALRWADEVALLTPG 225
Cdd:cd03291 175 YKDADLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILV-TSKME-HLKKADKILILHEG 234
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-239 |
8.37e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.04 E-value: 8.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYeeGPPV-LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRyDRGGLTRLRTTV 92
Cdd:NF033858 2 ARLEGVSHRY--GKTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA-DARHRRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 93 QLVVQDPDDQLFAA-SVAQDVSF-GPLnLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRV 170
Cdd:NF033858 79 AYMPQGLGKNLYPTlSVFENLDFfGRL-FGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664496302 171 LILDEPTAGLDPDGQERLLATLDRLRA--AGTTVLMATHDVDLALRWaDEVALLTPGGV-HTGPAAATLART 239
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFWELIDRIRAerPGMSVLVATAYMEEAERF-DWLVAMDAGRVlATGTPAELLART 228
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-230 |
1.55e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 145 RPTHLLSYGQRKRAAIAGAVAMR---PRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLaLRWADEVAL 221
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDV-IKTADYIID 903
|
90
....*....|
gi 664496302 222 LTP-GGVHTG 230
Cdd:TIGR00630 904 LGPeGGDGGG 913
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
35-208 |
1.58e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 35 FAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGG--EPVRYD--RGGLTRLRTTVQLVVQDPDDQLF------ 104
Cdd:PRK11147 340 AQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTklEVAYFDqhRAELDPEKTVMDNLAEGKQEVMVngrprh 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 105 AASVAQDVSFGPLnlglsdaevRSRVgealaaldiaaladrPTHLLSYGQRKRAAIAgAVAMRP-RVLILDEPTAGLDPD 183
Cdd:PRK11147 420 VLGYLQDFLFHPK---------RAMT---------------PVKALSGGERNRLLLA-RLFLKPsNLLILDEPTNDLDVE 474
|
170 180
....*....|....*....|....*
gi 664496302 184 GQERLLATLDRLRAagtTVLMATHD 208
Cdd:PRK11147 475 TLELLEELLDSYQG---TVLLVSHD 496
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
150-241 |
2.11e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.93 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 150 LSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRwADEVALLTPGGVHT 229
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEF 861
|
90
....*....|..
gi 664496302 230 GPAAATLARTEL 241
Cdd:PTZ00243 862 SGSSADFMRTSL 873
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
30-209 |
2.19e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.65 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 30 LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEpvrydrggltrlrTTVQLVVQDPDDQLfaaSVA 109
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-------------AALIAISSGLNGQL---TGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 110 QDVSFGPLNLGLSDAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLL 189
Cdd:PRK13545 104 ENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183
|
170 180
....*....|....*....|
gi 664496302 190 ATLDRLRAAGTTVLMATHDV 209
Cdd:PRK13545 184 DKMNEFKEQGKTIFFISHSL 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
47-219 |
2.41e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.14 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 47 GRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRyDRGGLTRLRTTVQLVVQDPDDQLFAAS-----------VAQDVSFG 115
Cdd:cd03240 29 GQNGAGKTTIIEALKYALTGELPPNSKGGAHDP-KLIREGEVRAQVKLAFENANGKKYTITrslailenvifCHQGESNW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 116 PLnlglsdAEVRSRvgealaaldiaaladrpthlLSYGQRKRAAIAGAVAM------RPRVLILDEPTAGLDPDGQERLL 189
Cdd:cd03240 108 PL------LDMRGR--------------------CSGGEKVLASLIIRLALaetfgsNCGILALDEPTTNLDEENIEESL 161
|
170 180 190
....*....|....*....|....*....|..
gi 664496302 190 ATL--DRLRAAGTTVLMATHDVDLaLRWADEV 219
Cdd:cd03240 162 AEIieERKSQKNFQLIVITHDEEL-VDAADHI 192
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
150-231 |
2.62e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.61 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 150 LSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALRWA-DEVALLTPGG-- 226
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAfDELLLMKRGGqv 1099
|
....*
gi 664496302 227 VHTGP 231
Cdd:PLN03140 1100 IYSGP 1104
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
44-207 |
3.11e-05 |
|
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: 44.61 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 44 ALLGRNGSGKTTLMRLLsgglrphagRLTLGGEPVR-------YDRGGLTRLRTTVQLVVQDPDDQLFAASVAQDV---- 112
Cdd:COG3593 27 VLVGENNSGKSSILEAL---------RLLLGPSSSRkfdeedfYLGDDPDLPEIEIELTFGSLLSRLLRLLLKEEDkeel 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 113 -----------------------SFGPLNLGLSDAEVRSRVGEALAALDI-----AALADRPTHLLSYGQRKRAAIAGAV 164
Cdd:COG3593 98 eealeelneelkealkalnellsEYLKELLDGLDLELELSLDELEDLLKSlslriEDGKELPLDRLGSGFQRLILLALLS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 664496302 165 AM-------RPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATH 207
Cdd:COG3593 178 ALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
25-207 |
3.15e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.40 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 25 EGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSG--------GLRPHAGRLTLGGEPvrYDRGGlTRLRTTVQLVV 96
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGredyevtgGTVEFKGKDLLELSP--EDRAG-EGIFMAFQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 97 QDP--DDQLFAASVAQDVSfgplnlGLSDAEVRSRVGEALAALDIAALADRPTHLL--------SYGQRKRAAIAGAVAM 166
Cdd:PRK09580 89 EIPgvSNQFFLQTALNAVR------SYRGQEPLDRFDFQDLMEEKIALLKMPEDLLtrsvnvgfSGGEKKRNDILQMAVL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 664496302 167 RPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATH 207
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-223 |
3.96e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 14 VALRGVSFAYEEGPPV--LTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGEPVRYDRGgLTRLRTT 91
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDIN-LKWWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 92 VQLVVQDPddQLFAASVAQDVSF-------------------------------------GPLNL--------------- 119
Cdd:PTZ00265 462 IGVVSQDP--LLFSNSIKNNIKYslyslkdlealsnyynedgndsqenknkrnscrakcaGDLNDmsnttdsneliemrk 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 120 ---GLSDAEVRSRVGEALAALDIAALADRPTHL-------LSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGQERLL 189
Cdd:PTZ00265 540 nyqTIKDSEVVDVSKKVLIHDFVSALPDKYETLvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260 270
....*....|....*....|....*....|....*.
gi 664496302 190 ATLDRLRAAGT--TVLMAtHDVDlALRWADEVALLT 223
Cdd:PTZ00265 620 KTINNLKGNENriTIIIA-HRLS-TIRYANTIFVLS 653
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-181 |
1.40e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.18 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 32 GLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGgepvrydrggltrlrTTVQL--VVQ-----DPDdqlf 104
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG---------------ETVKLayVDQsrdalDPN---- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 105 aASVAQDVSFGPLNLGLSDAEVRSR----------------VGEalaaldiaaladrpthlLSYGQRKRAAIAGAVAMRP 168
Cdd:PRK11819 403 -KTVWEEISGGLDIIKVGNREIPSRayvgrfnfkggdqqkkVGV-----------------LSGGERNRLHLAKTLKQGG 464
|
170
....*....|...
gi 664496302 169 RVLILDEPTAGLD 181
Cdd:PRK11819 465 NVLLLDEPTNDLD 477
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
28-207 |
1.57e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 42.32 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 28 PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGglrpHAGRLTLGGEPVRYDRGGLT-----RLRTTVQLVVQDP--- 99
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG----HPAYKILEGDILFKGESILDlepeeRAHLGIFLAFQYPiei 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 100 -----DDQLFAASVAQDVSFG-----PLN-----------LGLSDAEVRSRVGEAlaaldiaaladrpthlLSYGQRKRA 158
Cdd:CHL00131 97 pgvsnADFLRLAYNSKRKFQGlpeldPLEfleiineklklVGMDPSFLSRNVNEG----------------FSGGEKKRN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 664496302 159 AIAGAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATH 207
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
45-207 |
1.64e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 42.26 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 45 LLGRNGSGKTTLMRLLSG--GLRPH---AGRL---TLGGEPVRYDRGGLTRLRTTVQL--------VVQDPDDQLFAASV 108
Cdd:COG4938 25 LIGPNGSGKSTLIQALLLllQSNFIylpAERSgpaRLYPSLVRELSDLGSRGEYTADFlaelenleILDDKSKELLEQVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 109 A--QDVSFGPLNLglsdaEVRSRVGEALAALDIAALADRPTHLlSYGQRKRAAI--AGAVAMRPR-VLILDEPTAGLDPD 183
Cdd:COG4938 105 EwlEKIFPGKVEV-----DASSDLVRLVFRPSGNGKRIPLSNV-GSGVSELLPIllALLSAAKPGsLLIIEEPEAHLHPK 178
|
170 180
....*....|....*....|....
gi 664496302 184 GQERLLATLDRLRAAGTTVLMATH 207
Cdd:COG4938 179 AQSALAELLAELANSGVQVIIETH 202
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
166-207 |
1.66e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 42.06 E-value: 1.66e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 664496302 166 MRPRVL-ILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATH 207
Cdd:COG3910 150 FRGNGLyLLDEPEAALSPSRQLALLALIHDLVREGSQFIIATH 192
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
172-210 |
2.04e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 2.04e-04
10 20 30
....*....|....*....|....*....|....*....
gi 664496302 172 ILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVD 210
Cdd:COG0178 852 ILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLD 890
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-72 |
2.34e-04 |
|
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: 42.59 E-value: 2.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 664496302 26 GPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRP------HAGRLT 72
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPsegkikHSGRIS 490
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
35-181 |
2.69e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.22 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 35 FAVHEGRALALLGRNGSGKTTLMRLLSGGLR-PHAGRLTLGGEPVRYdRGGLTRLRTTVQLVVQD-------PD----DQ 102
Cdd:PRK13549 283 FSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKI-RNPQQAIAQGIAMVPEDrkrdgivPVmgvgKN 361
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664496302 103 LFAASVAQDVSFGPLNLGlsdAEVRSRVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLD 181
Cdd:PRK13549 362 ITLAALDRFTGGSRIDDA---AELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
7-225 |
3.04e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 41.43 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 7 STESTALVALRG------VSFAYEEG-PPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGGepVR 79
Cdd:cd03288 7 GSSNSGLVGLGGeikihdLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--ID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 80 YDRGGLTRLRTTVQLVVQDPddQLFAASV----------AQDVSFGPLNLGLSDAEVRSRVGEALAALDIAALAdrpthl 149
Cdd:cd03288 85 ISKLPLHTLRSRLSIILQDP--ILFSGSIrfnldpeckcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGEN------ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 664496302 150 LSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPdGQERLLATLDRLRAAGTTVLMATHDVDLALRwADEVALLTPG 225
Cdd:cd03288 157 FSVGQRQLFCLARAFVRKSSILIMDEATASIDM-ATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRG 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-244 |
4.75e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.50 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 28 PVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLSGGLrPHAgrltlggEPVRYDrggltrLRTTVQLVVQDPddQLFAAS 107
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL-SHA-------ETSSVV------IRGSVAYVPQVS--WIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 108 VAQDVSFGP-----------------LNLGLSDAEVRSRVGEALAAldiaaladrpthlLSYGQRKRAAIAGAVAMRPRV 170
Cdd:PLN03232 695 VRENILFGSdfeserywraidvtalqHDLDLLPGRDLTEIGERGVN-------------ISGGQKQRVSMARAVYSNSDI 761
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664496302 171 LILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLaLRWADEVALLTPGGVHTGPAAATLARTELLRQ 244
Cdd:PLN03232 762 YIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHF-LPLMDRIILVSEGMIKEEGTFAELSKSGSLFK 834
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
25-207 |
7.27e-04 |
|
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: 40.89 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 25 EGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLLsGGLRP-HAGRLTLGGE------PVR-YdrGGLTRLRTtvQLVV 96
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPvYGGRLTKPAKgklfyvPQRpY--MTLGTLRD--QIIY 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 97 QDPDDQLFAAsvaqdvsfgplnlGLSDAEVRS-----RVGEALAALDIAALADRPTHLLSYGQRKRAAIAGAVAMRPRVL 171
Cdd:TIGR00954 538 PDSSEDMKRR-------------GLSDKDLEQildnvQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190
....*....|....*....|....*....|....*.
gi 664496302 172 ILDEPTAGLDPDGQERLlatLDRLRAAGTTVLMATH 207
Cdd:TIGR00954 605 ILDECTSAVSVDVEGYM---YRLCREFGITLFSVSH 637
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
172-210 |
8.17e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.83 E-value: 8.17e-04
10 20 30
....*....|....*....|....*....|....*....
gi 664496302 172 ILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVD 210
Cdd:PRK00349 856 ILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLD 894
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
33-214 |
1.16e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 39.17 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 33 LDFAVHEGRALALL-GRNGSGKTTLMRLLSgglrphagrLTLGGEPVRYDRGGLTRlrttvqlVVQDPDDQlfAASVAQD 111
Cdd:cd03279 20 IDFTGLDNNGLFLIcGPTGAGKSTILDAIT---------YALYGKTPRYGRQENLR-------SVFAPGED--TAEVSFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 112 VSFGPLN------LGLsDAEVRSRV-----GEALAALDiaaladRPTHLLSYGQRKRAAIAGAVAM----------RPRV 170
Cdd:cd03279 82 FQLGGKKyrversRGL-DYDQFTRIvllpqGEFDRFLA------RPVSTLSGGETFLASLSLALALsevlqnrggaRLEA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 664496302 171 LILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLALR 214
Cdd:cd03279 155 LFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKER 198
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
37-210 |
1.47e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.77 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 37 VHEGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTLGG---------EPVRYDRGGLTRL----RTTVQLvvqdpDDQL 103
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqETPALPQPALEYVidgdREYRQL-----EAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 104 FAASVAQDVSFGPLNLGLSDA----EVRSRVGEALAALD-IAALADRPTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTA 178
Cdd:PRK10636 99 HDANERNDGHAIATIHGKLDAidawTIRSRAASLLHGLGfSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTN 178
|
170 180 190
....*....|....*....|....*....|...
gi 664496302 179 GLDPDGqerlLATLDR-LRAAGTTVLMATHDVD 210
Cdd:PRK10636 179 HLDLDA----VIWLEKwLKSYQGTLILISHDRD 207
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
40-181 |
1.64e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.84 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 40 GRALALLGRNGSGKTTLMRLLS----GGLRPHAGRLTLGGEPVRYDRGGL----------TRLRTTVQLVVQDPDDQLFA 105
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMAmhaiDGIPKNCQILHVEQEVVGDDTTALqcvlntdierTQLLEEEAQLVAQQRELEFE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 106 ASVAQDVsfGPLNLGLSDAEVRSRVGE--------------------ALAALDIAALADRPTHLLSYGQRKRAAIAGAVA 165
Cdd:PLN03073 283 TETGKGK--GANKDGVDKDAVSQRLEEiykrlelidaytaearaasiLAGLSFTPEMQVKATKTFSGGWRMRIALARALF 360
|
170
....*....|....*.
gi 664496302 166 MRPRVLILDEPTAGLD 181
Cdd:PLN03073 361 IEPDLLLLDEPTNHLD 376
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
39-73 |
1.92e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 1.92e-03
10 20 30
....*....|....*....|....*....|....*
gi 664496302 39 EGRALALLGRNGSGKTTLMRLLSGGLRPHAGRLTL 73
Cdd:PRK15064 26 GGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL 60
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-230 |
3.35e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 145 RPTHLLSYGQRKRAAIA---GAVAMRPRVLILDEPTAGLDPDGQERLLATLDRLRAAGTTVLMATHDVDLaLRWADEVAL 221
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHV-VKVADYVLE 883
|
....*....
gi 664496302 222 LTPGGVHTG 230
Cdd:PRK00635 884 LGPEGGNLG 892
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-208 |
4.82e-03 |
|
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: 38.38 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 16 LRGVSFAYEEGPPVLTGLDFAVHEGRALALLGRNGSGKTTLMRLL-------SGGLRPHAGrLTLG---GEP-------- 77
Cdd:TIGR03719 7 MNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdkdfNGEARPQPG-IKVGylpQEPqldptktv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664496302 78 -------VRYDRGGLTRLrTTVQLVVQDPD---DQLFAASVA-QDVsfgplnLGLSDA-EVRSRVgEALAALDIAALADR 145
Cdd:TIGR03719 86 renveegVAEIKDALDRF-NEISAKYAEPDadfDKLAAEQAElQEI------IDAADAwDLDSQL-EIAMDALRCPPWDA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664496302 146 PTHLLSYGQRKRAAIAGAVAMRPRVLILDEPTAGLDPDGqerlLATLDR-LRAAGTTVLMATHD 208
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERhLQEYPGTVVAVTHD 217
|
|
| |
