|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-226 |
6.16e-74 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 224.56 E-value: 6.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKP---SIETKKIVSYLPE 90
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVardPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 91 RTYLNDWMKVSDLLKFFYDFY---SDFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIG 165
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYglpRKEARERIDELLELFGLTdaADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489525288 166 GVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIREE 226
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
15-235 |
1.08e-63 |
|
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: 198.54 E-value: 1.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 15 EFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGI---KPSIETKKIVSYLPER 91
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdvrKEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 92 TYLNDWMKVSDLLKFFYDFYSDFD---VRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGG 166
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDeelKKRIEELIELLGLEefLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 167 VDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIREEKGK-SIDALF 235
Cdd:COG4555 163 LDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEeNLEDAF 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-214 |
2.42e-56 |
|
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: 177.20 E-value: 2.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGI---KPSIETKKIVSYLPE 90
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKdikKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 91 RTYLNDWMKVSDLLKFfydfysdfdvrranemiksldidvneklktmSKGTKEKVQLILVMSRNASIYILDEPIGGVDPA 170
Cdd:cd03230 81 EPSLYENLTVRENLKL-------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489525288 171 ARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEI 214
Cdd:cd03230 130 SRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-229 |
1.03e-52 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 172.22 E-value: 1.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKIVSYLPERT 92
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYLPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 93 YLNDWMKVSDLLKFFYDF--YSDFDVR-RANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGV 167
Cdd:COG4152 81 GLYPKMKVGEQLVYLARLkgLSKAEAKrRADEWLERLGLGdrANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525288 168 DPAARSyILKTILKNY-SEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIREEKGK 229
Cdd:COG4152 161 DPVNVE-LLKDVIRELaAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGR 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-218 |
1.07e-51 |
|
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: 166.69 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKIVSYLPERTY 93
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 94 LNDWMKVSDLLKFFYDF--YSDFDVRR-ANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVD 168
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLkgLKKEEARRrIDEWLERLELSeyANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489525288 169 PAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:cd03269 161 PVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-218 |
2.38e-42 |
|
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: 143.06 E-value: 2.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 15 EFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGiKPSIETKKIVSYLPERTYL 94
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-KPLEKERKRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 95 nDW---MKVSDLL-------KFFYDFYSDFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDE 162
Cdd:cd03235 80 -DRdfpISVRDVVlmglyghKGLFRRLSKADKAKVDEALERVGLSelADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 163 PIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKgEIVLQG 218
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNR-TVVASG 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-218 |
4.55e-42 |
|
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: 142.64 E-value: 4.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYG--TKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIkpSIET-----KKIVS 86
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY--SIRTdrkaaRQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 87 YLPERTYLNDWMKVSDLLKFFYDF--YSDFDVRR-ANEMIKSLDI--DVNEKLKTMSKGTKEKVQLILVMSRNASIYILD 161
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLkgLPKSEIKEeVELLLRVLGLtdKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489525288 162 EPIGGVDPAARSYILKTILKnYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-223 |
2.62e-40 |
|
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: 138.23 E-value: 2.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSY-GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIET-----KKI--- 84
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNlrelrRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 ----------------VSYLPERTYLN-DWMKvsdllkffydfysdfdvRRANEMIKSLDIdvnEKLK-----TMSKGTK 142
Cdd:COG1122 81 fqnpddqlfaptveedVAFGPENLGLPrEEIR-----------------ERVEEALELVGL---EHLAdrpphELSGGQK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 143 EKVQL--ILVMsrNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDV 220
Cdd:COG1122 141 QRVAIagVLAM--EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
...
gi 489525288 221 EAI 223
Cdd:COG1122 219 REV 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-213 |
2.64e-40 |
|
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: 135.84 E-value: 2.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 15 EFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGI----KPSIETKKIVSYLPE 90
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKdiakLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 91 rtylndwmkvsdllkffydfysdfdvrranemiksldidvneklktMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPA 170
Cdd:cd00267 81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489525288 171 ARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGE 213
Cdd:cd00267 115 SRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-218 |
3.68e-40 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 137.32 E-value: 3.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGkIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKI---VSYLPE 90
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 91 RTYLNDWMKVSDLLKFFYDFY--SDFDVR-RANEMIKSLDI-DV-NEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIG 165
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKgiPSKEVKaRVDEVLELVNLgDRaKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489525288 166 GVDPAARsYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:cd03264 160 GLDPEER-IRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-213 |
7.34e-40 |
|
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: 136.44 E-value: 7.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 15 EFKGVNKSYGTKN--VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGI----KPSIETKKIVSYL 88
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltkLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 ---PERTYLNDwmKVSDLLKF---FYDFYSDFDVRRANEMIKSLDIDV--NEKLKTMSKGTKEKVQLILVMSRNASIYIL 160
Cdd:cd03225 81 fqnPDDQFFGP--TVEEEVAFgleNLGLPEEEIEERVEEALELVGLEGlrDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489525288 161 DEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGE 213
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-223 |
7.68e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.53 E-value: 7.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGiKPSIETKKIVSYLPERT 92
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-KPPRRARRRIGYVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 93 YLnDW---MKVSDL--------LKFFyDFYSDFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYI 159
Cdd:COG1121 85 EV-DWdfpITVRDVvlmgrygrRGLF-RRPSRADREAVDEALERVGLEdlADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489525288 160 LDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGeIVLQGDVEAI 223
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEV 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-218 |
7.97e-40 |
|
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: 136.19 E-value: 7.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPS--IETKKIVSYLPER 91
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQknIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 92 TYLNDWMKVSDLLKFFYDFY--SDFDVRRANEMIkSLDIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDP 169
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLgiRKKRIDEVLDVV-GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489525288 170 AARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:cd03268 160 DGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-223 |
4.24e-38 |
|
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: 133.25 E-value: 4.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGiKP--SIETK---KIVSY 87
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG-RDlaSLSRRelaRRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 88 LPERTYLNDWMKVSDL--------LKFFyDFYSDFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASI 157
Cdd:COG1120 80 VPQEPPAPFGLTVRELvalgryphLGLF-GRPSAEDREAVEEALERTGLEhlADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 158 YILDEPIGGVDPAARSYILKtILKNYSEDS--TLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLE-LLRRLARERgrTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
14-221 |
3.78e-37 |
|
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: 129.80 E-value: 3.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING---IKPSIETKKIVSYLPE 90
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 91 RTYLNDWMKVSDLLKFF---YDFYSDFDVRRANEMIKSLDI-DVNEKL-KTMSKGTKEKVQLILVMSRNASIYILDEPIG 165
Cdd:cd03265 81 DLSVDDELTGWENLYIHarlYGVPGAERRERIDELLDFVGLlEAADRLvKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489525288 166 GVDPAARSYILKTILK-NYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVE 221
Cdd:cd03265 161 GLDPQTRAHVWEYIEKlKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
13-218 |
4.23e-36 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 127.10 E-value: 4.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSY----GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGI---KPSIETKKIV 85
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFdvvKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 86 SYLPERTYLNDWMKVSDLLKFFYDFYS---DFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYIL 160
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGlkgDELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 161 DEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-218 |
3.43e-35 |
|
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: 123.31 E-value: 3.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 15 EFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK----PSIETKKIVSYLPE 90
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaslSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 91 rtylndWMKVSDLLKFfydfysdfdvrrANEMIKSLdidvneklktmSKGTKEKVQLILVMSRNASIYILDEPIGGVDPA 170
Cdd:cd03214 81 ------ALELLGLAHL------------ADRPFNEL-----------SGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489525288 171 ARSYILKtILKNYSEDS--TLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:cd03214 132 HQIELLE-LLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-224 |
4.03e-34 |
|
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: 122.23 E-value: 4.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPS-------IETKKIVS 86
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseaelYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 87 YLPERTYLNDWMKVSDLLKFFYDFYSDFDvrraNEMIKSLdidVNEKLKT-------------MSKGTKEKVQLILVMSR 153
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLS----EEEIREI---VLEKLEAvglrgaedlypaeLSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489525288 154 NASIYILDEPIGGVDPAARSYILKTILK-NYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIR 224
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-225 |
5.92e-34 |
|
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: 122.01 E-value: 5.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 9 SQDGIVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietkKIVSYL 88
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDG--------QDITGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 PERTY---------------LNDWMKVSDLLKFFYDFYSDFDVRRANEMiksldidVNEKLKTM-------------SKG 140
Cdd:COG1127 73 SEKELyelrrrigmlfqggaLFDSLTVFENVAFPLREHTDLSEAEIREL-------VLEKLELVglpgaadkmpselSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 141 TKEKVQLI--LVMsrNASIYILDEPIGGVDPAARSYILKTILK-NYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQ 217
Cdd:COG1127 146 MRKRVALAraLAL--DPEILLYDEPTAGLDPITSAVIDELIRElRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
....*...
gi 489525288 218 GDVEAIRE 225
Cdd:COG1127 224 GTPEELLA 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-229 |
1.65e-33 |
|
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: 127.26 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 11 DGIVEFKGVNKSYG--TKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIkpSIET------K 82
Cdd:COG2274 471 KGDIELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI--DLRQidpaslR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 83 KIVSYLPERTYL-------NdwmkvsdlLKFFYDFYSDFDVRRA------NEMIKSL----DIDVNEKLKTMSKGTKEKV 145
Cdd:COG2274 549 RQIGVVLQDVFLfsgtireN--------ITLGDPDATDEEIIEAarlaglHDFIEALpmgyDTVVGEGGSNLSGGQRQRL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 146 QLILVMSRNASIYILDEPIGGVDPAARSYILKTiLKNYSEDSTLLIATHLISEIENiCDEVIFISKGEIVLQGDVEAIRE 225
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILEN-LRRLLKGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLA 698
|
....
gi 489525288 226 EKGK 229
Cdd:COG2274 699 RKGL 702
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-218 |
1.28e-32 |
|
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: 118.01 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietkKIVSYLPER-- 91
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG--------RDVTGVPPErr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 92 -------TY-LNDWMKVSDLLKF-FYDFYSDFDV--RRANEMIKSLDIDVNEKLK--TMSKGTKEKVQLILVMSRNASIY 158
Cdd:cd03259 73 nigmvfqDYaLFPHLTVAENIAFgLKLRGVPKAEirARVRELLELVGLEGLLNRYphELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525288 159 ILDEPIGGVDPAARSYI---LKTILKNysEDSTLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:cd03259 153 LLDEPLSALDAKLREELreeLKELQRE--LGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-218 |
8.50e-32 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 116.28 E-value: 8.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 19 VNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKIVSYLP----ERTYL 94
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGvvfgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 95 ndW--MKVSDLLKFFYDFYsDFDVRRANEMIKSLD--IDVNEKLKT----MSKGTKEKVQLILVMSRNASIYILDEPIGG 166
Cdd:cd03267 107 --WwdLPVIDSFYLLAAIY-DLPPARFKKRLDELSelLDLEELLDTpvrqLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489525288 167 VDPAARSYILKtILKNYSED--STLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:cd03267 184 LDVVAQENIRN-FLKEYNRErgTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-213 |
1.21e-31 |
|
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: 114.02 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKN--VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGI---KPSIET-KKIVSY 87
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrDLDLESlRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 88 LPERTYLndwmkvsdllkffydfysdFD--VRranEMIksldidvneklktMSKGTKEKVQLILVMSRNASIYILDEPIG 165
Cdd:cd03228 81 VPQDPFL-------------------FSgtIR---ENI-------------LSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489525288 166 GVDPAARSYILKTILKnYSEDSTLLIATHLISEIENiCDEVIFISKGE 213
Cdd:cd03228 126 ALDPETEALILEALRA-LAKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-213 |
1.48e-31 |
|
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: 114.21 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKIvsyLPERTy 93
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDEL---PPLRR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 94 lnDWMKVsdllkfFYDF--YSDFDVRRaNEMIksldidvneklkTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAA 171
Cdd:cd03229 77 --RIGMV------FQDFalFPHLTVLE-NIAL------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489525288 172 RSYILKTILKNYSEDS-TLLIATHLISEIENICDEVIFISKGE 213
Cdd:cd03229 136 RREVRALLKSLQAQLGiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-215 |
2.29e-31 |
|
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: 112.91 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKpsietkkivsylperty 93
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 94 lndwmkvsdllkffYDFYSDFDVRRAN-EMIKSLDIdvneklktmskGTKEKVQLILVMSRNASIYILDEPIGGVDPAAR 172
Cdd:cd03216 64 --------------VSFASPRDARRAGiAMVYQLSV-----------GERQMVEIARALARNARLLILDEPTAALTPAEV 118
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489525288 173 SYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIV 215
Cdd:cd03216 119 ERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
15-227 |
3.34e-31 |
|
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: 114.97 E-value: 3.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 15 EFKGVNKSYGT-KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK-PSIETKKIVSY----- 87
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDiNKLKGKALRQLrrqig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 88 -------LPERTY---------LNDWMKVSDLLKFFydfySDFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLIL 149
Cdd:cd03256 82 mifqqfnLIERLSvlenvlsgrLGRRSTWRSLFGLF----PKEEKQRALAALERVGLLdkAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489525288 150 VMSRNASIYILDEPIGGVDPAARSYILKTILK-NYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIREEK 227
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRiNREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
15-214 |
4.18e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 113.76 E-value: 4.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 15 EFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGI----KPSIETKKIVSYLPE 90
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsaMPPPEWRRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 91 RTYLndW-MKVSDLLKFFYDFYSD-FDVRRANEMIKSLDI--DVNEK-LKTMSKGTKEKVQLILVMSRNASIYILDEPIG 165
Cdd:COG4619 82 EPAL--WgGTVRDNLPFPFQLRERkFDRERALELLERLGLppDILDKpVERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489525288 166 GVDPAARSYILKTILKNYSEDS-TLLIATHLISEIENICDEVIFISKGEI 214
Cdd:COG4619 160 ALDPENTRRVEELLREYLAEEGrAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-240 |
1.04e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 115.57 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 23 YGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKIVS--------------YL 88
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARrigvvfgqrsqlwwDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 PertylndwmkVSDLLKFFYDFY----SDFDvRRANEMIKSLDIDvnEKLKT----MSKGTKEKVQLILVMSRNASIYIL 160
Cdd:COG4586 112 P----------AIDSFRLLKAIYripdAEYK-KRLDELVELLDLG--ELLDTpvrqLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 161 DEPIGGVDPAARSYILKTILK-NYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIRE--EKGKSIDALFRE 237
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEyNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKErfGPYKTIVLELAE 258
|
...
gi 489525288 238 EFK 240
Cdd:COG4586 259 PVP 261
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
17-223 |
1.77e-29 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 110.44 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 17 KGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGI----KPSIETKKI-VSYLPER 91
Cdd:TIGR04406 5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQdithLPMHERARLgIGYLPQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 92 TYLNDWMKVSD----LLKFFYDFYSDFDVRRANEMIKSLDIDVNEKLKTM--SKGTKEKVQLILVMSRNASIYILDEPIG 165
Cdd:TIGR04406 85 ASIFRKLTVEEnimaVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMslSGGERRRVEIARALATNPKFILLDEPFA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 166 GVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:TIGR04406 165 GVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-218 |
2.36e-29 |
|
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: 109.90 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKN----VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING---IKPSIETKKI- 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 ---VSYLPE--RTYLNDWMKVSDLLKFFYDFYSDFDVRRANEMIKSLD---IDVNEKLKT-----MSKGTKEKVQLILVM 151
Cdd:cd03257 81 rkeIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLlvgVGLPEEVLNrypheLSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 152 SRNASIYILDEPIGGVDPAARSYILKTILKNYSE-DSTLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
12-218 |
2.99e-29 |
|
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: 109.22 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 12 GIVEFKGVNKSY-GTKN-VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK----PSIETKKIV 85
Cdd:cd03245 1 GRIEFRNVSFSYpNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDirqlDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 86 SYLPERTYLNdWMKVSDLLKFFYDFYSDFDVRRANEMI----------KSLDIDVNEKLKTMSKGTKEKVQLILVMSRNA 155
Cdd:cd03245 81 GYVPQDVTLF-YGTLRDNITLGAPLADDERILRAAELAgvtdfvnkhpNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525288 156 SIYILDEPIGGVDPAARSYILKTiLKNYSEDSTLLIATHLISeIENICDEVIFISKGEIVLQG 218
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKER-LRQLLGDKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-228 |
5.13e-29 |
|
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: 108.85 E-value: 5.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 12 GIVEFKGVNKSYGTKN-VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK----PSIETKKIVS 86
Cdd:cd03254 1 GEIEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDirdiSRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 87 YLPERTYL-NDwmKVSDLLKFFYDFYSDFDVRRA------NEMIKSL----DIDVNEKLKTMSKGTKEKVQLILVMSRNA 155
Cdd:cd03254 81 VVLQDTFLfSG--TIMENIRLGRPNATDEEVIEAakeagaHDFIMKLpngyDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525288 156 SIYILDEPIGGVDPAARSyILKTILKNYSEDSTLLIATHLISEIENiCDEVIFISKGEIVLQGDVEAIREEKG 228
Cdd:cd03254 159 KILILDEATSNIDTETEK-LIQEALEKLMKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-225 |
7.12e-29 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 109.44 E-value: 7.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSY--GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIET------KKI- 84
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnlweirKKVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 ------------------VSYLPErtylNdwMKVSdllkffydfysdfdvrrANEMIKSldidVNEKLKTM--------- 137
Cdd:TIGR04520 81 mvfqnpdnqfvgatveddVAFGLE----N--LGVP-----------------REEMRKR----VDEALKLVgmedfrdre 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 138 ----SKGTKEKVQL--ILVMsrNASIYILDEPIGGVDPAARSYILKTILK-NYSEDSTLLIATHLISEIENiCDEVIFIS 210
Cdd:TIGR04520 134 phllSGGQKQRVAIagVLAM--RPDIIILDEATSMLDPKGRKEVLETIRKlNKEEGITVISITHDMEEAVL-ADRVIVMN 210
|
250 260
....*....|....*....|..
gi 489525288 211 KGEIVLQG-------DVEAIRE 225
Cdd:TIGR04520 211 KGKIVAEGtpreifsQVELLKE 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-218 |
8.79e-29 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 107.01 E-value: 8.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKN--VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSI---ETKKIVSYL 88
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDlekALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 PERTYLndwmkvsdllkffydfysdFDVrranemikSLDIDVNEKLktmSKGTKEKVQLILVMSRNASIYILDEPIGGVD 168
Cdd:cd03247 81 NQRPYL-------------------FDT--------TLRNNLGRRF---SGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489525288 169 PAARSYILKTILKnYSEDSTLLIATHLISEIENIcDEVIFISKGEIVLQG 218
Cdd:cd03247 131 PITERQLLSLIFE-VLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
13-223 |
1.05e-28 |
|
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: 108.63 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQP-DNGEIMING----------IKPSIet 81
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGerrggedvweLRKRI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 82 kKIVS-----YLPERTylndwmKVSDLLK--FF-----YDFYSDFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQL 147
Cdd:COG1119 81 -GLVSpalqlRFPRDE------TVLDVVLsgFFdsiglYREPTDEQRERARELLELLGLAhlADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 148 ILVMSRNASIYILDEPIGGVDPAARSYILKTILK-NYSEDSTLLIATHLISEI-ENIcDEVIFISKGEIVLQGDVEAI 223
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVLVTHHVEEIpPGI-THVLLLKDGRVVAAGPKEEV 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-223 |
1.05e-28 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 108.01 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 18 GVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIkpSIETKKI-------VSYLPE 90
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ--DITKLPMhkrarlgIGYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 91 RTYLNDWMKVSD----LLKFFYDFYsDFDVRRANEMIKSLDIDVNEKLK--TMSKGTKEKVQLILVMSRNASIYILDEPI 164
Cdd:cd03218 83 EASIFRKLTVEEnilaVLEIRGLSK-KEREEKLEELLEEFHITHLRKSKasSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489525288 165 GGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-223 |
1.27e-28 |
|
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: 112.69 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKN-----VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETK----- 82
Cdd:COG1123 260 LLEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 83 --KIVSYLPERTY--LNDWMKVSDLLKFFYDFYSDFD----VRRANEMIKS--LDIDVNEKL-KTMSKGTKEKVQL--IL 149
Cdd:COG1123 340 lrRRVQMVFQDPYssLNPRMTVGDIIAEPLRLHGLLSraerRERVAELLERvgLPPDLADRYpHELSGGQRQRVAIarAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 150 VMsrNASIYILDEPIGGVDPAARSYILKtILKNYSEDS--TLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:COG1123 420 AL--EPKLLILDEPTSALDVSVQAQILN-LLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
29-163 |
1.93e-28 |
|
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: 105.04 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 29 LKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGI----KPSIETKKIVSYLPERTYLNDWMKVSDLL 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 105 KF---FYDFYSDFDVRRANEMIKSLDID------VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEP 163
Cdd:pfam00005 81 RLgllLKGLSKREKDARAEEALEKLGLGdladrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-228 |
3.43e-28 |
|
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: 111.78 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 9 SQDGIVEFKGVNKSY--GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSI----ETK 82
Cdd:COG4987 329 PGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDldedDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 83 KIVSYLPERTYLNDwMKVSDLLKFFYDFYSDFDVRRA----------NEMIKSLDIDVNEKLKTMSKGTKEKVQL--ILV 150
Cdd:COG4987 409 RRIAVVPQRPHLFD-TTLRENLRLARPDATDEELWAAlervglgdwlAALPDGLDTWLGEGGRRLSGGERRRLALarALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 151 msRNASIYILDEPIGGVDPAARSYILKTILKnYSEDSTLLIATHLISEIENiCDEVIFISKGEIVLQGDVEAIREEKG 228
Cdd:COG4987 488 --RDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
14-201 |
4.30e-28 |
|
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: 106.02 E-value: 4.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGI---KPSIETKKIVSYLPE 90
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 91 RTYLNDWMKVSDLLKFFYDFY-SDFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGV 167
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYgLRADREAIDEALEAVGLAglADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190
....*....|....*....|....*....|....
gi 489525288 168 DPAARSYILKTILKNYSEDSTLLIATHLISEIEN 201
Cdd:COG4133 163 DAAGVALLAELIAAHLARGGAVLLTTHQPLELAA 196
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-225 |
1.40e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.77 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINgikpsiETKKIvSYLP-ER 91
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG------ETVKI-GYFDqHQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 92 TYLN------DWMK----------VSDLLKFFyDFYSDfdvrranemiksldiDVNEKLKTMSKGTKEKVQLILVMSRNA 155
Cdd:COG0488 388 EELDpdktvlDELRdgapggteqeVRGYLGRF-LFSGD---------------DAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489525288 156 SIYILDEPIGGVDPAARSyILKTILKNYseDSTLLIATH---LiseIENICDEVIFISKGEIV-LQGDVEAIRE 225
Cdd:COG0488 452 NVLLLDEPTNHLDIETLE-ALEEALDDF--PGTVLLVSHdryF---LDRVATRILEFEDGGVReYPGGYDDYLE 519
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-218 |
1.85e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 109.87 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 11 DGIVEFKGVNKSY-GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsIETKKI----- 84
Cdd:COG1132 337 RGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG----VDIRDLtlesl 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 ---VSYLPERTYL-NDwmKVSDLLKFFYDFYSDFDVRRA------NEMIKSLDidvnEKLKTM--SKGTK----EKvQLI 148
Cdd:COG1132 413 rrqIGVVPQDTFLfSG--TIRENIRYGRPDATDEEVEEAakaaqaHEFIEALP----DGYDTVvgERGVNlsggQR-QRI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489525288 149 -----LVmsRNASIYILDEPIGGVDPAARSYILKTiLKNYSEDSTLLIATHLISEIENiCDEVIFISKGEIVLQG 218
Cdd:COG1132 486 aiaraLL--KDPPILILDEATSALDTETEALIQEA-LERLMKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-214 |
2.65e-27 |
|
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: 104.11 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKN----VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPS-IETKKIVSY- 87
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISkLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 88 -------------LPERTYL-NdwmkVSDLLKFFYDFYSDfDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVM 151
Cdd:cd03255 81 rrhigfvfqsfnlLPDLTALeN----VELPLLLAGVPKKE-RRERAEELLERVGLGdrLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489525288 152 SRNASIYILDEPIGGVDPAARSYILKTILK-NYSEDSTLLIATHLIsEIENICDEVIFISKGEI 214
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRElNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-227 |
3.51e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 106.45 E-value: 3.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK-PSIE--TKKIVSYLPE 90
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPvPARArlARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 91 RTYLNDWMKVSDLLkFFYDFYSDFDVRRANEMIKS------LDIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPI 164
Cdd:PRK13536 122 FDNLDLEFTVRENL-LVFGRYFGMSTREIEAVIPSllefarLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525288 165 GGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIREEK 227
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-218 |
4.73e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 105.66 E-value: 4.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGiKP----SIETKKIVSYL 88
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPvpsrARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 PERTYLNDWMKVSDLLKFFYDFYSdFDVRRANEMIKS------LDIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDE 162
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFG-LSAAAARALVPPllefakLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 163 PIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-223 |
1.70e-26 |
|
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: 102.76 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSY-GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK----PSIETKKIVSY- 87
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDireqDPVELRRKIGYv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 88 ------LPERTYLNDWMKVSDLLKffydfYSDFDVR-RANEMIKSLDIDVNEKLK----TMSKGTKEKVQLILVMSRNAS 156
Cdd:cd03295 81 iqqiglFPHMTVEENIALVPKLLK-----WPKEKIReRADELLALVGLDPAEFADryphELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 157 IYILDEPIGGVDPAARSYILKTILKNYSE-DSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-238 |
5.83e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.10 E-value: 5.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKK--------I 84
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaqaagiaI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 V----SYLPERT-----YLN---------DWMKVsdllkffydfysdfdVRRANEMIKSL--DIDVNEKLKTMSKGTKEK 144
Cdd:COG1129 84 IhqelNLVPNLSvaeniFLGreprrggliDWRAM---------------RRRARELLARLglDIDPDTPVGDLSVAQQQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 145 VQLILVMSRNASIYILDEPIGGVDPAARSYILKTI--LKnySEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEA 222
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIrrLK--AQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAE 226
|
250 260
....*....|....*....|..
gi 489525288 223 IREEK------GKSIDALFREE 238
Cdd:COG1129 227 LTEDElvrlmvGRELEDLFPKR 248
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-223 |
1.42e-25 |
|
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: 99.95 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLL-----QPDNGEIMINGI------------- 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKdiydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 76 --------KPSIETKKI---VSYLPeRTYLNDWMKVSDLLkffydfysdfdVRRANEMIkSLDIDVNEKLK--TMSKGTK 142
Cdd:cd03260 81 rrvgmvfqKPNPFPGSIydnVAYGL-RLHGIKLKEELDER-----------VEEALRKA-ALWDEVKDRLHalGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 143 EKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTILKnYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEA 222
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAE-LKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 489525288 223 I 223
Cdd:cd03260 227 I 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
17-224 |
8.57e-25 |
|
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: 97.89 E-value: 8.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 17 KGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIM-----INGIKPSIETKK-------I 84
Cdd:cd03219 4 RGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgedITGLPPHEIARLgigrtfqI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 VSYLPERTYLNDWM-----KVSDLLKFFYDFYSDFDVR-RANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNAS 156
Cdd:cd03219 84 PRLFPELTVLENVMvaaqaRTGSGLLLARARREEREAReRAEELLERVGLAdlADRPAGELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 157 IYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIR 224
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
10-227 |
9.83e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.77 E-value: 9.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 10 QDGIVEFKGVNKSY--GTkNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGiKPSIETKKIVSY 87
Cdd:PRK13636 2 EDYILKVEELNYNYsdGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDG-KPIDYSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 88 LpeRTYLNDWMKVSDLLKFFYDFYSDFDV-------------RRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMS 152
Cdd:PRK13636 80 L--RESVGMVFQDPDNQLFSASVYQDVSFgavnlklpedevrKRVDNALKRTGIEhlKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 153 RNASIYILDEPIGGVDPAARSYILKTILKNYSE-DSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIREEK 227
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-214 |
1.08e-24 |
|
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: 97.22 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKIVSY------ 87
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELrqkvgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 88 -------LPERTYLNDWM----KVSDLLKffydfysDFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRN 154
Cdd:cd03262 81 vfqqfnlFPHLTVLENITlapiKVKGMSK-------AEAEERALELLEKVGLAdkADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 155 ASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEI 214
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
13-223 |
1.27e-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: 97.65 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKN----VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietkKIVSYL 88
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDG--------TDLTLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 PERTYLNDWMKVSDLLKFFYDFYS------------------DFDVRRANEMIKSLDIDVNEKL--KTMSKGTKEKVQLI 148
Cdd:cd03258 73 SGKELRKARRRIGMIFQHFNLLSSrtvfenvalpleiagvpkAEIEERVLELLELVGLEDKADAypAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 149 LVMSRNASIYILDEPIGGVDPAARSYILKTILK-NYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDiNRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-207 |
1.32e-24 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 97.86 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 35 NIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKpsietkkiVSYLPERTYLNDWMKVSDLL-KFFYDFYSD 113
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT--------VSYKPQYIKADYEGTVRDLLsSITKDFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 114 FDVRraNEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTIlKNYSE--DSTL 189
Cdd:cd03237 93 PYFK--TEIAKPLQIEqiLDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI-RRFAEnnEKTA 169
|
170
....*....|....*...
gi 489525288 190 LIATHLISEIENICDEVI 207
Cdd:cd03237 170 FVVEHDIIMIDYLADRLI 187
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
15-223 |
1.36e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.52 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 15 EFKGVNKSYGTKnvLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietKKIVSYLP-ERty 93
Cdd:COG3840 3 RLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG-------QDLTALPPaER-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 94 lndwmKVSDLlkfFYD---F------------------YSDFDVRRANEMIKSLDIDvnEKLK----TMSKGTKEKVQL- 147
Cdd:COG3840 72 -----PVSML---FQEnnlFphltvaqniglglrpglkLTAEQRAQVEQALERVGLA--GLLDrlpgQLSGGQRQRVALa 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 148 -ILVMSRNasIYILDEPIGGVDPAARS---YILKTILKNYseDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:COG3840 142 rCLVRKRP--ILLLDEPFSALDPALRQemlDLVDELCRER--GLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-223 |
1.44e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 97.66 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 21 KSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSI-----ETKKIVSYLPERTYLN 95
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlplhaRARRGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 96 DWMKVSD----LLKFFYDFYSDFDVRRANEMIKSLDID-VNEKL-KTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDP 169
Cdd:PRK10895 91 RRLSVYDnlmaVLQIRDDLSAEQREDRANELMEEFHIEhLRDSMgQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 170 AARSYILKTIlkNYSEDSTL--LIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK10895 171 ISVIDIKRII--EHLRDSGLgvLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-219 |
1.61e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.47 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK---PSIETKKIVS--- 86
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvndPKVDERLIRQeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 87 ------YL-PERTYLNDWMkvsdllkffydfYSDFDVRR-----ANEMIKSLDIDV------NEKLKTMSKGTKEKVQLI 148
Cdd:PRK09493 81 mvfqqfYLfPHLTALENVM------------FGPLRVRGaskeeAEKQARELLAKVglaeraHHYPSELSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489525288 149 LVMSRNASIYILDEPIGGVDPAARSYILKtILKNYSEDS-TLLIATHLISEIENICDEVIFISKGEIVLQGD 219
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPELRHEVLK-VMQDLAEEGmTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGD 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
16-223 |
2.07e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 97.07 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 16 FKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietkKIVSYL------- 88
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--------RVSALLelgagfh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 PERT-----YLN---DWMKVSDLLKFFyDFYSDF-DVRRAnemiksldIDvnEKLKTMSKGTKEKVQLILVMSRNASIYI 159
Cdd:COG1134 101 PELTgreniYLNgrlLGLSRKEIDEKF-DEIVEFaELGDF--------ID--QPVKTYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489525288 160 LDEPIGGVDPA--ARSYilkTILKNYSEDS-TLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:COG1134 170 VDEVLAVGDAAfqKKCL---ARIRELRESGrTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-218 |
2.75e-24 |
|
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: 96.45 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 20 NKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietkKIVSYL-------PERT 92
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--------RVSSLLglgggfnPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 93 -----YLN-DWMKVS-DLLKFFYDFYSDFdvrraNEmiksLDIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIG 165
Cdd:cd03220 101 greniYLNgRLLGLSrKEIDEKIDEIIEF-----SE----LGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489525288 166 GVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
14-223 |
2.96e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.13 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDN-----GEIMINGIKPSIETKKIVSYL 88
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAgtirvGDITIDTARSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 --------------PERTYLNDWMKVSDLLKffyDFYSDFDVRRANEMIKSLDIDVNEKL--KTMSKGTKEKVQLILVMS 152
Cdd:PRK11264 84 rqhvgfvfqnfnlfPHRTVLENIIEGPVIVK---GEPKEEATARARELLAKVGLAGKETSypRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489525288 153 RNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-228 |
4.58e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.18 E-value: 4.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 12 GIVEFKGVNKSYGT---KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGiKPSIET------K 82
Cdd:TIGR00958 477 GLIEFQDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG-VPLVQYdhhylhR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 83 KIVSYLPERTYLNDwmKVSDLLKFFYDFYSDFDVRRA----------NEMIKSLDIDVNEKLKTMSKGTKEKVQLILVMS 152
Cdd:TIGR00958 556 QVALVGQEPVLFSG--SVRENIAYGLTDTPDEEIMAAakaanahdfiMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 153 RNASIYILDEPIGGVDpAARSYILKTILKnySEDSTLLIATHLISEIENiCDEVIFISKGEIVLQGDVEAIREEKG 228
Cdd:TIGR00958 634 RKPRVLILDEATSALD-AECEQLLQESRS--RASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
14-218 |
7.00e-24 |
|
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: 94.87 E-value: 7.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVlkNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGI-----KPSietKKIVSYL 88
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaaPPA---DRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 PERTYL--------NDWMKVSDLLKFfydfySDFDVRRANEMIKSLDIDVNEKLK--TMSKGTKEKVQLILVMSRNASIY 158
Cdd:cd03298 76 FQENNLfahltveqNVGLGLSPGLKL-----TAEDRQAIEVALARVGLAGLEKRLpgELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489525288 159 ILDEPIGGVDPAARSYILKTILKNYSEDS-TLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-221 |
1.05e-23 |
|
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: 94.85 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKN----VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGiKPSIETKKIVSYLP 89
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-EPVTGPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 90 ERTYLNDWMKVSDLLKFFYDF--YSDFDVR-RANEMIKSLDIDVNEKL--KTMSKGTKEKVQLILVMSRNASIYILDEPI 164
Cdd:cd03293 80 QQDALLPWLTVLDNVALGLELqgVPKAEAReRAEELLELVGLSGFENAypHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489525288 165 GGVDPAARSYILKTILKNYSED--STLLIaTHLISEIENICDEVIFISK--GEIVLQGDVE 221
Cdd:cd03293 160 SALDALTREQLQEELLDIWRETgkTVLLV-THDIDEAVFLADRVVVLSArpGRIVAEVEVD 219
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
28-194 |
1.57e-23 |
|
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: 93.64 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 28 VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGiKPSIETKKivSYLPERTYLNDWMKVSDLLKFF 107
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDG-EPLDYSRK--GLLERRQRVGLVFQDPDDQLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 108 YDFYSDFDV-------------RRANEMIKSLDIDVNEK--LKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAAR 172
Cdd:TIGR01166 84 ADVDQDVAFgplnlglseaeveRRVREALTAVGASGLRErpTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGR 163
|
170 180
....*....|....*....|..
gi 489525288 173 SYILKTILKNYSEDSTLLIATH 194
Cdd:TIGR01166 164 EQMLAILRRLRAEGMTVVISTH 185
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
22-218 |
3.00e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.31 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 22 SYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGiKP-----SIETKKIVSYLPERTYLND 96
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD-KPismlsSRQLARRLALLPQHHLTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 97 WMKVSDLLKF-------FYDFYSDFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGV 167
Cdd:PRK11231 90 GITVRELVAYgrspwlsLWGRLSAEDNARVNQAMEQTRINhlADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489525288 168 DPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:PRK11231 170 DINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-215 |
1.03e-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: 91.93 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietkKIVSYLP--ER 91
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG--------RDVTDLPpkDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 92 -------TY-LNDWMKVSDLLKF---FYDFYSDFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIY 158
Cdd:cd03301 73 diamvfqNYaLYPHMTVYDNIAFglkLRKVPKDEIDERVREVAELLQIEhlLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489525288 159 ILDEPIGGVDPAARsYILKTILKNYSE--DSTLLIATHLISEIENICDEVIFISKGEIV 215
Cdd:cd03301 153 LMDEPLSNLDAKLR-VQMRAELKRLQQrlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-215 |
1.23e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.86 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKK--------- 83
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdaialgigm 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 84 ----------------IVSYLPERTYLNdwmkvsdllkffydfysdFDVRRANEMIKS------LDIDVNEKLKTMSKGT 141
Cdd:COG3845 85 vhqhfmlvpnltvaenIVLGLEPTKGGR------------------LDRKAARARIRElserygLDVDPDAKVEDLSVGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 142 KEKVQLILVMSRNASIYILDEPIGGVDPAARSyILKTILKNYSED--STLLIaTHLISEIENICDEVIFISKGEIV 215
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLTPQEAD-ELFEILRRLAAEgkSIIFI-THKLREVMAIADRVTVLRRGKVV 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-207 |
1.29e-22 |
|
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: 95.82 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSY-GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK-PSIETK---KIVSYL 88
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPlADADADswrDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 PERTYLndwmkVSDLLKFFYDFY----SDFDVRRA------NEMIKSL----DIDVNEKLKTMSKGTKEKVQLILVMSRN 154
Cdd:TIGR02857 402 PQHPFL-----FAGTIAENIRLArpdaSDAEIREAleraglDEFVAALpqglDTPIGEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489525288 155 ASIYILDEPIGGVDPAARSYILKTILKnYSEDSTLLIATHLISEIENiCDEVI 207
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRA-LAQGRTVLLVTHRLALAAL-ADRIV 527
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
31-218 |
1.33e-22 |
|
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: 91.59 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 31 NIDLNIPkGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKI--------VSYLPERTYLNDWMKVSD 102
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqqrkIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 103 LLKFFYDFYSDFDVR-RANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYI---L 176
Cdd:cd03297 95 NLAFGLKRKRNREDRiSVDELLDLLGLDhlLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLlpeL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489525288 177 KTILKNYseDSTLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:cd03297 175 KQIKKNL--NIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-218 |
1.86e-22 |
|
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: 90.69 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNK------SYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQP--DNGEIMINGIKPSIET-KKI 84
Cdd:cd03213 4 LSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSfRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 VSYLPERTYLndwmkvsdllkffydfYSDFDVRRAnemiksldIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPI 164
Cdd:cd03213 84 IGYVPQDDIL----------------HPTLTVRET--------LMFAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 165 GGVDPAARSYILKTiLKNYSEDS-TLLIATH-LISEIENICDEVIFISKGEIVLQG 218
Cdd:cd03213 140 SGLDSSSALQVMSL-LRRLADTGrTIICSIHqPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-223 |
2.10e-22 |
|
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: 94.97 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSY--GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPD---NGEIMINGI-----KPSIETK 82
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRdllelSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 83 KIVSYLPE-RTYLNDwMKVSDLLKF---FYDFYSDFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNAS 156
Cdd:COG1123 84 RIGMVFQDpMTQLNP-VTVGDQIAEaleNLGLSRAEARARVLELLEAVGLErrLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 157 IYILDEPIGGVDPAARSYILKTILKNYSE-DSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-225 |
2.62e-22 |
|
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: 91.79 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKN----VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGI----KPSIETKKIV 85
Cdd:COG1124 2 LEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 86 SYLPE--RTYLNDWMKVSDLLKF-FYDFYSDFDVRRANEMIKSLDIDvnEKLKT-----MSKGTKEKVQLILVMSRNASI 157
Cdd:COG1124 82 QMVFQdpYASLHPRHTVDRILAEpLRIHGLPDREERIAELLEQVGLP--PSFLDryphqLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 158 YILDEPIGGVDPAARSYILkTILKNYSEDS--TLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIRE 225
Cdd:COG1124 160 LLLDEPTSALDVSVQAEIL-NLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
13-215 |
2.73e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 91.26 E-value: 2.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKN----VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKpsietkkiVSYL 88
Cdd:COG1136 4 LLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQD--------ISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 PERtylndwmkvsDLLKF--------FYDFY--SDFDVR-------------------RANEMIKSLDID--VNEKLKTM 137
Cdd:COG1136 76 SER----------ELARLrrrhigfvFQFFNllPELTALenvalplllagvsrkerreRARELLERVGLGdrLDHRPSQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 138 SKGTKEKVqLI---LVMsrNASIYILDEPIGGVDPAARSYILKtILKNYSEDS--TLLIATHlISEIENICDEVIFISKG 212
Cdd:COG1136 146 SGGQQQRV-AIaraLVN--RPKLILADEPTGNLDSKTGEEVLE-LLRELNRELgtTIVMVTH-DPELAARADRVIRLRDG 220
|
...
gi 489525288 213 EIV 215
Cdd:COG1136 221 RIV 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
17-215 |
5.11e-22 |
|
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: 90.01 E-value: 5.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 17 KGVNKSYG-TKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK-PSIETKKIVSYLPERTYL 94
Cdd:cd03226 3 ENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPiKAKERRKSIGYVMQDVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 95 NDWMK-VSDLLKFFYDFYSDfDVRRANEMIKSLDIDvneKLK-----TMSKGTKEKVQLILVMSRNASIYILDEPIGGVD 168
Cdd:cd03226 83 QLFTDsVREELLLGLKELDA-GNEQAETVLKDLDLY---ALKerhplSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489525288 169 PAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIV 215
Cdd:cd03226 159 YKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
13-224 |
5.19e-22 |
|
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: 90.87 E-value: 5.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIkpSIETKK--------- 83
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGR--DITGLPphriarlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 84 -----IVSYLPERTYL-NdwMKV-----------SDLLKFFYDFYSDFDVR-RANEMIKSLDID--VNEKLKTMSKGTKE 143
Cdd:COG0411 82 artfqNPRLFPELTVLeN--VLVaaharlgrgllAALLRLPRARREEREAReRAEELLERVGLAdrADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 144 KVQLILVMSRNASIYILDEPIGGVDPAARSYILKTILK-NYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEA 222
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRlRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
..
gi 489525288 223 IR 224
Cdd:COG0411 240 VR 241
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-222 |
5.41e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 90.84 E-value: 5.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETK---KIVSYL-- 88
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKpseKAIRLLrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 ------------PERTYLNDW----MKVSDLLKffydfysDFDVRRANEMIKSLDIDvnEKLKT----MSKGTKEKVQLI 148
Cdd:COG4161 83 kvgmvfqqynlwPHLTVMENLieapCKVLGLSK-------EQAREKAMKLLARLRLT--DKADRfplhLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489525288 149 LVMSRNASIYILDEPIGGVDPAARSYILKtILKNYSEDS-TLLIATHLISEIENICDEVIFISKGEIVLQGDVEA 222
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDPEITAQVVE-IIRELSQTGiTQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASH 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-213 |
6.04e-22 |
|
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: 87.89 E-value: 6.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietKKIVSYLPErty 93
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-------TVKIGYFEQ--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 94 lndwmkvsdllkffydfysdfdvrranemiksldidvneklktMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARS 173
Cdd:cd03221 71 -------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIE 107
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489525288 174 yILKTILKNYseDSTLLIATHLISEIENICDEVIFISKGE 213
Cdd:cd03221 108 -ALEEALKEY--PGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
26-218 |
7.11e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 91.26 E-value: 7.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 26 KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPsieTKKIVSylpertyLNDWMKVSDLLk 105
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI---TDKKVK-------LSDIRKKVGLV- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 106 FFYDFYSDFD------------------------VRRANEMIKsLDIdvnEKLKTMSK-----GTKEKVQLILVMSRNAS 156
Cdd:PRK13637 89 FQYPEYQLFEetiekdiafgpinlglseeeienrVKRAMNIVG-LDY---EDYKDKSPfelsgGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489525288 157 IYILDEPIGGVDPAARSYIL---KTILKNYseDSTLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILnkiKELHKEY--NMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
14-223 |
8.64e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 90.14 E-value: 8.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK----PSIETKKIVSYLP 89
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDvattPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 90 ERTYLNDWMKVSDLLKF--FYdfYS-----DFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYIL 160
Cdd:COG4604 82 QENHINSRLTVRELVAFgrFP--YSkgrltAEDREIIDEAIAYLDLEdlADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 161 DEPIGGVDPA-ARSyILKtILKNYSEDS--TLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:COG4604 160 DEPLNNLDMKhSVQ-MMK-LLRRLADELgkTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
12-228 |
8.92e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.54 E-value: 8.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 12 GIVEFKGVNKSYGTKNV--LKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIkpSIETKKIVSyLP 89
Cdd:PRK11176 340 GDIEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH--DLRDYTLAS-LR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 90 ERTYLndwmkVSDLLKFFYD------------FYSDFDVRRA----------NEMIKSLDIDVNEKLKTMSKGTKEKVQL 147
Cdd:PRK11176 417 NQVAL-----VSQNVHLFNDtianniayarteQYSREQIEEAarmayamdfiNKMDNGLDTVIGENGVLLSGGQRQRIAI 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 148 ILVMSRNASIYILDEPIGGVDPAARSYILKTiLKNYSEDSTLLIATHLISEIENiCDEVIFISKGEIVLQGDVEAIREEK 227
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAA-LDELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQN 569
|
.
gi 489525288 228 G 228
Cdd:PRK11176 570 G 570
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-219 |
1.01e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.84 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 23 YGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGiKPSIETKKivSYLPERTYLNDWMKVSD 102
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-KPLDYSKR--GLLALRQQVATVFQDPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 103 LLKFFYDFYSDFD-------------VRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGV 167
Cdd:PRK13638 88 QQIFYTDIDSDIAfslrnlgvpeaeiTRRVDEALTLVDAQhfRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489525288 168 DPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGD 219
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-195 |
1.19e-21 |
|
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: 92.81 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 8 VSQDGIVEFKGVNKSYGTKN-VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSI----ETK 82
Cdd:TIGR02868 329 GLGKPTLELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSldqdEVR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 83 KIVSYLPERTYLNDwMKVSDLLKFFYDFYSDFDVRRANEMIK----------SLDIDVNEKLKTMSKGTKEKVQLILVMS 152
Cdd:TIGR02868 409 RRVSVCAQDAHLFD-TTVRENLRLARPDATDEELWAALERVGladwlralpdGLDTVLGEGGARLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489525288 153 RNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHL 195
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
17-224 |
1.24e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 90.12 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 17 KGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMiNGIKPSIETKKIVSYLPERTYLND 96
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-AGTAPLAEAREDTRLMFQDARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 97 WMKVSD-----LLKFFYDfysdfDVRRANEMIkSLDIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAA 171
Cdd:PRK11247 95 WKKVIDnvglgLKGQWRD-----AALQALAAV-GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489525288 172 RSYILKTILKNYSEDS-TLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIR 224
Cdd:PRK11247 169 RIEMQDLIESLWQQHGfTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDLPR 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-229 |
2.01e-21 |
|
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: 88.83 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYG--TKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIET----KKIVSY 87
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlaslRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 88 LPERTYL-NDwmKVSDLLKFFYDFYSDFDVRRA----------NEMIKSLDIDVNEKLKTMSKGTKEKVQLILVMSRNAS 156
Cdd:cd03251 81 VSQDVFLfND--TVAENIAYGRPGATREEVEEAaraanahefiMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525288 157 IYILDEPIGGVDPAARSYILKTiLKNYSEDSTLLIATHLISEIENIcDEVIFISKGEIVLQGDVEAIREEKGK 229
Cdd:cd03251 159 ILILDEATSALDTESERLVQAA-LERLMKNRTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELLAQGGV 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
17-223 |
2.46e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.93 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 17 KGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietKKI------------ 84
Cdd:COG1137 7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG-------EDIthlpmhkrarlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 VSYLP-ERTYLNDwMKVSD-LLKFFYDFYSDFDVR--RANEMIKSLDIdvnEKLK-----TMSKGTKEKVQLILVMSRNA 155
Cdd:COG1137 80 IGYLPqEASIFRK-LTVEDnILAVLELRKLSKKEReeRLEELLEEFGI---THLRkskaySLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 156 SIYILDEPIGGVDPAARSYILKTI--LKNysEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIrhLKE--RGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
28-223 |
4.27e-21 |
|
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: 88.16 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 28 VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING--IKPSIETKKIVSYLPERTYLNDWMKVSDLLK 105
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkdITNLPPEKRDISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 106 FFYDFYSDFDV---RRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARS---YILK 177
Cdd:cd03299 94 YGLKKRKVDKKeieRKVLEIAEMLGIDhlLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEklrEELK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489525288 178 TILKNYseDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:cd03299 174 KIRKEF--GVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
15-226 |
4.87e-21 |
|
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: 87.49 E-value: 4.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 15 EFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING--IkPSIETKKIV----SYL 88
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrdI-TGLPPHERAragiGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 PERTYLNDWMKVSDLLKFFYDFYSDFDVRRANEMIKSLDIDVNEKLK----TMSKGtkEkvQLILVMSR----NASIYIL 160
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKqlagTLSGG--E--QQMLAIARalmsRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 161 DEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIREE 226
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
13-89 |
5.21e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 89.77 E-value: 5.21e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietkKIVSYLP 89
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG--------RDVTGLP 73
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
14-214 |
6.21e-21 |
|
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: 87.78 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIET--KKIVSYLPER 91
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPvqERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 92 TYLNDWMKVSDLLKFfydfysDFDVRRANEMIKSLDID--VNEKLKTM-------------SKGTKEKVQLILVMSRNAS 156
Cdd:cd03296 83 YALFRHMTVFDNVAF------GLRVKPRSERPPEAEIRakVHELLKLVqldwladrypaqlSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 157 IYILDEPIGGVDPAARSYiLKTILKNYSEDS--TLLIATHLISEIENICDEVIFISKGEI 214
Cdd:cd03296 157 VLLLDEPFGALDAKVRKE-LRRWLRRLHDELhvTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-228 |
6.39e-21 |
|
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: 87.67 E-value: 6.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKN-VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIET----KKIVSYL 88
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTldslRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 PERTYL-NDwmKVSDLLKFFYDFYSDFDVRRA------NEMIKSL----DIDVNEKLKTMSKGTKEKVQLILVMSRNASI 157
Cdd:cd03253 81 PQDTVLfND--TIGYNIRYGRPDATDEEVIEAakaaqiHDKIMRFpdgyDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489525288 158 YILDEPIGGVDPAARSYILKTILKNYSEDSTLLIAtHLISEIENiCDEVIFISKGEIVLQGDVEAIREEKG 228
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKGG 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-226 |
1.11e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.11 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 1 MDKNINNVSQdgIVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING------ 74
Cdd:PRK15439 1 MQTSDTTAPP--LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpcarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 75 ------------------IKPSIETKK-IVSYLPERTylNDWMKVSDLLKffydfysdfdvrranEMIKSLDIDvneklk 135
Cdd:PRK15439 79 tpakahqlgiylvpqeplLFPNLSVKEnILFGLPKRQ--ASMQKMKQLLA---------------ALGCQLDLD------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 136 tMSKGTKEKV--QLILVMS---RNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFIS 210
Cdd:PRK15439 136 -SSAGSLEVAdrQIVEILRglmRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMR 214
|
250
....*....|....*.
gi 489525288 211 KGEIVLQGDVEAIREE 226
Cdd:PRK15439 215 DGTIALSGKTADLSTD 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-194 |
1.57e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.75 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 22 SYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEImingikpSIETKKIVSYLPERTYLNDWM--K 99
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------RRAGGARVAYVPQRSEVPDSLplT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 100 VSDLL-------KFFYDFYSDFDVRRANEMIKSLDIDVNEK--LKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPA 170
Cdd:NF040873 74 VRDLVamgrwarRGLWRRLTRDDRAAVDDALERVGLADLAGrqLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180
....*....|....*....|....
gi 489525288 171 ARSYILKTILKNYSEDSTLLIATH 194
Cdd:NF040873 154 SRERIIALLAEEHARGATVVVVTH 177
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
11-214 |
2.05e-20 |
|
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: 85.99 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 11 DGIVEFKGVNKSYGTK---NVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietKKIVSY 87
Cdd:cd03248 9 KGIVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG-------KPISQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 88 lpERTYLNDWM------------KVSDLLKFFYDFYSDFDVRRA----------NEMIKSLDIDVNEKLKTMSKGTKEKV 145
Cdd:cd03248 82 --EHKYLHSKVslvgqepvlfarSLQDNIAYGLQSCSFECVKEAaqkahahsfiSELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489525288 146 QLILVMSRNASIYILDEPIGGVDPAARSYIlKTILKNYSEDSTLLIATHLISEIENiCDEVIFISKGEI 214
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQV-QQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-214 |
2.45e-20 |
|
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: 85.54 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSY-GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKIVSYLPER- 91
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 92 -TYLNDWMKVSDLLKF----FYDFYSDFDVRRANEMIKS-LD-IDVNEKLKTM----SKGTKEKVQLILVMSRNASIYIL 160
Cdd:cd03292 81 gVVFQDFRLLPDRNVYenvaFALEVTGVPPREIRKRVPAaLElVGLSHKHRALpaelSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489525288 161 DEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEI 214
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
14-218 |
6.36e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 85.99 E-value: 6.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSY--GT---KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKK----- 83
Cdd:PRK13646 3 IRFDNVSYTYqkGTpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 84 ------IVSYLPERTYLNDW-------------MKVSDLLKFFYDFYSDFDVRRaNEMIKSldidvnekLKTMSKGTKEK 144
Cdd:PRK13646 83 vrkrigMVFQFPESQLFEDTvereiifgpknfkMNLDEVKNYAHRLLMDLGFSR-DVMSQS--------PFQMSGGQMRK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489525288 145 VQLILVMSRNASIYILDEPIGGVDPAARSYILKTILKNYSEDS-TLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENkTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-215 |
6.65e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 84.72 E-value: 6.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKN-VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPS-IETKKIVSY--- 87
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrLKRREIPYLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 88 ----------LPERTylndwmkVSDLLKFFYDF--YSDFDVR-RANEMIKSLDIDvnEKLKTM----SKGtkEKvQLI-- 148
Cdd:COG2884 81 igvvfqdfrlLPDRT-------VYENVALPLRVtgKSRKEIRrRVREVLDLVGLS--DKAKALphelSGG--EQ-QRVai 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 149 ---LVMsrNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIV 215
Cdd:COG2884 149 araLVN--RPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-226 |
6.88e-20 |
|
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: 87.94 E-value: 6.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 11 DGIVEFKGVNKSY-----GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEI-------MINGIKPS 78
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 79 IE----TKKIVSYL-------PERTYLNDWMKVSDLlkffyDFYSDFDVRRANEMIKSLDID------VNEKL-KTMSKG 140
Cdd:TIGR03269 357 PDgrgrAKRYIGILhqeydlyPHRTVLDNLTEAIGL-----ELPDELARMKAVITLKMVGFDeekaeeILDKYpDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 141 TKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTILKNYSE-DSTLLIATHLISEIENICDEVIFISKGEIVLQGD 219
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
....*..
gi 489525288 220 VEAIREE 226
Cdd:TIGR03269 512 PEEIVEE 518
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-216 |
7.06e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.81 E-value: 7.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 16 FKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMI-NGIKpsietkkiVSYLPERTYL 94
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLR--------IGYLPQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 95 NDWMKVSD-----------LLKFFYDFYSDFDV------------------------RRANEMIKSLDI---DVNEKLKT 136
Cdd:COG0488 73 DDDLTVLDtvldgdaelraLEAELEELEAKLAEpdedlerlaelqeefealggweaeARAEEILSGLGFpeeDLDRPVSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 137 MSKGTKEKVQL--ILVmsRNASIYILDEPIGGVDPAARSYiLKTILKNYseDSTLLIATH----LiseiENICDEVIFIS 210
Cdd:COG0488 153 LSGGWRRRVALarALL--SEPDLLLLDEPTNHLDLESIEW-LEEFLKNY--PGTVLVVSHdryfL----DRVATRILELD 223
|
....*.
gi 489525288 211 KGEIVL 216
Cdd:COG0488 224 RGKLTL 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
14-74 |
1.46e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 85.90 E-value: 1.46e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING 74
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG 64
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-218 |
1.88e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 85.54 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 9 SQDGIVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING---IKPSIETKKIV 85
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvTHRSIQQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 86 ----SYLpertyLNDWMKVSDLLKF---FYDFYSDFDVRRANEMIKSLDIDVNEK--LKTMSKGTKEKVQLILVMSRNAS 156
Cdd:PRK11432 82 mvfqSYA-----LFPHMSLGENVGYglkMLGVPKEERKQRVKEALELVDLAGFEDryVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525288 157 IYILDEPIGGVDPAARSYILKTILK-NYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRElQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIG 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-74 |
2.28e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 85.77 E-value: 2.28e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489525288 4 NINNVSQDGIVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING 74
Cdd:PRK09452 5 NKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG 75
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-225 |
2.53e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 84.05 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 7 NVSQDGIVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK-PSI------ 79
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENiPAMsrsrly 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 80 ETKKIVSYLPERTYLNDWMKVSDLLKFFYDFYSDF--DVRRANEMIKSLDIDVNEKLKTM----SKGTKEKVQLILVMSR 153
Cdd:PRK11831 81 TVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLpaPLLHSTVMMKLEAVGLRGAAKLMpselSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525288 154 NASIYILDEPIGGVDPAARSYILKTILK-NYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIRE 225
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISElNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-223 |
2.57e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 84.30 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSY--GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIET-----KKI- 84
Cdd:PRK13635 5 IIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwdvrRQVg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 -VSYLPERTYLNdwMKVSDLLKFFYDfysDFDVRRaNEMIKSLDIDVNEKLKT---------MSKGTKEKVQLILVMSRN 154
Cdd:PRK13635 85 mVFQNPDNQFVG--ATVQDDVAFGLE---NIGVPR-EEMVERVDQALRQVGMEdflnrephrLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489525288 155 ASIYILDEPIGGVDPAARSYILKTI--LKNySEDSTLLIATHLISEIENiCDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVrqLKE-QKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-227 |
2.78e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.02 E-value: 2.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 11 DGIVEFKGVNKSY--GTKnVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKK----- 83
Cdd:PRK13647 2 DNIIEVEDLHFRYkdGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvrsk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 84 --IVSYLPERTYLNdwMKVSDLLKF---FYDFYSDFDVRRANEMIKSLDI-DVNEKLKT-MSKGTKEKVQLILVMSRNAS 156
Cdd:PRK13647 81 vgLVFQDPDDQVFS--STVWDDVAFgpvNMGLDKDEVERRVEEALKAVRMwDFRDKPPYhLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489525288 157 IYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIREEK 227
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-218 |
3.36e-19 |
|
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: 82.70 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 18 GVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPD---NGEIMINGIKPSIET-KKIVSYLPERTY 93
Cdd:cd03234 12 KAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQfQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 94 LNDWMKVSDLLKffydFYSDFDVRR--ANEMIKSLDIDV-----------NEKLKTMSKGTKEKVQLILVMSRNASIYIL 160
Cdd:cd03234 92 LLPGLTVRETLT----YTAILRLPRksSDAIRKKRVEDVllrdlaltrigGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489525288 161 DEPIGGVDPAArSYILKTILKNYSEDSTLLIAThlI----SEIENICDEVIFISKGEIVLQG 218
Cdd:cd03234 168 DEPTSGLDSFT-ALNLVSTLSQLARRNRIVILT--IhqprSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-226 |
3.82e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.01 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKN-----VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING-----------IK 76
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 77 PSIETKKIVSYLPERTYLNDwmkvsDLLKFFYDFYSDFDVRRAN---------EMIkSLDIDVNEKLK-TMSKGTKEKVQ 146
Cdd:PRK13643 81 PVRKKVGVVFQFPESQLFEE-----TVLKDVAFGPQNFGIPKEKaekiaaeklEMV-GLADEFWEKSPfELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 147 LILVMSRNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIREE 226
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
9-223 |
4.05e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 83.70 E-value: 4.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 9 SQDGIVEFKGVNKSY--GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPD---NGEIMINGIKPSIETK- 82
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 83 ------KIVSYLPERTYLNdwMKVSDLLKFFYDfysDFDVRRaNEMIKSL-----DIDVNEKLKT----MSKGTKEKVQL 147
Cdd:PRK13640 81 direkvGIVFQNPDNQFVG--ATVGDDVAFGLE---NRAVPR-PEMIKIVrdvlaDVGMLDYIDSepanLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489525288 148 ILVMSRNASIYILDEPIGGVDPAARSYILKTILKNYSEDS-TLLIATHLISEiENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNlTVISITHDIDE-ANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
11-223 |
4.20e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 83.65 E-value: 4.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 11 DGIVEFKGVNKSYGTKN--VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKK----- 83
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEklrkh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 84 --IVSYLPERTYLNDWMK--VSDLLKFFYDFYSDFdVRRANEMIKSLDI--DVNEKLKTMSKGTKEKVQLILVMSRNASI 157
Cdd:PRK13648 85 igIVFQNPDNQFVGSIVKydVAFGLENHAVPYDEM-HRRVSEALKQVDMleRADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489525288 158 YILDEPIGGVDPAARSYILKTILK-NYSEDSTLLIATHLISEIENiCDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKvKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
14-227 |
4.94e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 83.50 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGT--KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKK-------I 84
Cdd:PRK13632 8 IKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeirkkigI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 VSYLPERTYLNdwMKVSDLLKFFYDfYSDFDVRRANEMIKSLDIDVN--EKLK----TMSKGTKEKVQLILVMSRNASIY 158
Cdd:PRK13632 88 IFQNPDNQFIG--ATVEDDIAFGLE-NKKVPPKKMKDIIDDLAKKVGmeDYLDkepqNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 159 ILDEPIGGVDPAARSYILKTILKNYSE-DSTLLIATHLISEIENiCDEVIFISKGEIVLQGDVEAIREEK 227
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTrKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-223 |
5.24e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.22 E-value: 5.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKI--------- 84
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaaqlgigii 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 ---VSYLPERTYLNDwMKVSDLL--KFFYDFYSDFDV--RRANEMIKSLDI--DVNEKLKTMSKGTKEKVQLILVMSRNA 155
Cdd:PRK09700 86 yqeLSVIDELTVLEN-LYIGRHLtkKVCGVNIIDWREmrVRAAMMLLRVGLkvDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 156 SIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-225 |
5.30e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 83.20 E-value: 5.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSY--GTKnVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGiKPSIETKKivSYLPE 90
Cdd:PRK13639 1 ILETRDLKYSYpdGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG-EPIKYDKK--SLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 91 RTYLNDWMKVSDLLKFFYDFYSDF------------DV-RRANEMIKSLDIDVNEKLKT--MSKGTKEKVQLILVMSRNA 155
Cdd:PRK13639 77 RKTVGIVFQNPDDQLFAPTVEEDVafgplnlglskeEVeKRVKEALKAVGMEGFENKPPhhLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489525288 156 SIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQG-------DVEAIRE 225
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGtpkevfsDIETIRK 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
14-223 |
6.26e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.53 E-value: 6.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSY--GT---KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING--IKPSIETKK--- 83
Cdd:PRK13634 3 ITFQKVEHRYqyKTpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvITAGKKNKKlkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 84 ------IVSYLP-----ERTYLND--------WMKVSDLLKffydfysdfdvrRANEMIK--SLDIDVNEKLK-TMSKGT 141
Cdd:PRK13634 83 lrkkvgIVFQFPehqlfEETVEKDicfgpmnfGVSEEDAKQ------------KAREMIElvGLPEELLARSPfELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 142 KEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTILKNYSE-DSTLLIATHLISEIENICDEVIFISKGEIVLQGDV 220
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTP 230
|
...
gi 489525288 221 EAI 223
Cdd:PRK13634 231 REI 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
12-215 |
8.41e-19 |
|
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: 81.77 E-value: 8.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 12 GIVEFKGVNKSY--GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPS-IETKKI---V 85
Cdd:cd03244 1 GDIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkIGLHDLrsrI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 86 SYLPERTYLndwmkVSDLLKF---FYDFYSDFDVRRA----------NEMIKSLDIDVNEKLKTMSKGTKEKVQLILVMS 152
Cdd:cd03244 81 SIIPQDPVL-----FSGTIRSnldPFGEYSDEELWQAlervglkefvESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525288 153 RNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIEniCDEVIFISKGEIV 215
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIID--SDRILVLDKGRVV 216
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
13-223 |
8.67e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.73 E-value: 8.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSY--GTKnVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGI---KPSI--ETKKIV 85
Cdd:PRK13644 1 MIRLENVSYSYpdGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgDFSKlqGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 86 SYL---PERTYLNdwMKVSDLLKFFYD--FYSDFDVRRANEMIKS---LDIDVNEKLKTMSKGTKEKVQLILVMSRNASI 157
Cdd:PRK13644 80 GIVfqnPETQFVG--RTVEEDLAFGPEnlCLPPIEIRKRVDRALAeigLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 158 YILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIEnICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENV 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-226 |
1.03e-18 |
|
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: 81.51 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietkKIVSYLP--ER 91
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG--------KDITNLPphKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 92 T------------YLNDWMKVSDLLKFFYDFYSDFDvRRANEMIKSLDIDVNEKLKT--MSKGTKEKVQLILVMSRNASI 157
Cdd:cd03300 73 PvntvfqnyalfpHLTVFENIAFGLRLKKLPKAEIK-ERVAEALDLVQLEGYANRKPsqLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489525288 158 YILDEPIGGVDPAARSYI---LKTILKNYSedSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIREE 226
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMqleLKRLQKELG--ITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
14-223 |
1.43e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.74 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGI----KPSIETKKIVSYLP 89
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdveaLSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 90 ERTYLNDWMKVSDLLKF-------FYDFYSDFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYIL 160
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMgrtphrsRFDTWTETDRAAVERAMERTGVAqfADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525288 161 DEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
34-218 |
2.73e-18 |
|
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: 83.52 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 34 LNIP--KGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikPSIET-----KKIVSYLPERTYLNDWMKVSDLLKF 106
Cdd:TIGR01257 949 LNITfyENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG--KDIETnldavRQSLGMCPQHNILFHHLTVAEHILF 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 107 FYDFYSDFDVRRANEMIKSLDiDV------NEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTIL 180
Cdd:TIGR01257 1027 YAQLKGRSWEEAQLEMEAMLE-DTglhhkrNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190
....*....|....*....|....*....|....*...
gi 489525288 181 KnYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:TIGR01257 1106 K-YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-213 |
3.84e-18 |
|
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: 79.44 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKN-----VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietkkIVSYL 88
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG---------SIAYV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 PERTYLndwmkVSDLLKffyD---FYSDFDVRRANEMIK--SLDID-----------VNEKLKTMSKGTKEKVQLILVMS 152
Cdd:cd03250 72 SQEPWI-----QNGTIR---EnilFGKPFDEERYEKVIKacALEPDleilpdgdlteIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489525288 153 RNASIYILDEPIGGVDPAARSYIL-KTILKNYSEDSTLLIATHLISEIENiCDEVIFISKGE 213
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
13-74 |
5.08e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 81.28 E-value: 5.08e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 13 IVEFKGVNKSYGTKN----VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING 74
Cdd:COG1135 1 MIELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDG 66
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-163 |
5.14e-18 |
|
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: 82.29 E-value: 5.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 11 DGIVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINgikpsiETKKIVSYLPE 90
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG------ETVKLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 91 RTYLND----WMKVSDLLKFF----YDFYSDFDVRRANEMikslDIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDE 162
Cdd:TIGR03719 394 RDALDPnktvWEEISGGLDIIklgkREIPSRAYVGRFNFK----GSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDE 469
|
.
gi 489525288 163 P 163
Cdd:TIGR03719 470 P 470
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
15-206 |
6.97e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.88 E-value: 6.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 15 EFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING-------IKPSIETKKIVSY 87
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrfasTTAALAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 88 -----LPERT-----YLND------WMKVSDLlkffydfysdfdVRRANEMIKSL--DIDVNEKLKTMSKGTKEKVQLIL 149
Cdd:PRK11288 86 qelhlVPEMTvaenlYLGQlphkggIVNRRLL------------NYEAREQLEHLgvDIDPDTPLKYLSIGQRQMVEIAK 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489525288 150 VMSRNASIYILDEPIGGVdpAAR-SYILKTILKNY-SEDSTLLIATHLISEIENICDEV 206
Cdd:PRK11288 154 ALARNARVIAFDEPTSSL--SAReIEQLFRVIRELrAEGRVILYVSHRMEEIFALCDAI 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
14-219 |
9.44e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.52 E-value: 9.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTK-----NVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEI--MINGIKPSIETKKIVS 86
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 87 YLPE----RTYLNDWMKVSDLLK-----FFYDFYSDFD---------------------VRRANEMIKSLDIDVNEKLKT 136
Cdd:PRK13651 83 VLEKlviqKTRFKKIKKIKEIRRrvgvvFQFAEYQLFEqtiekdiifgpvsmgvskeeaKKRAAKYIELVGLDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 137 ---MSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGE 213
Cdd:PRK13651 163 pfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
....*.
gi 489525288 214 IVLQGD 219
Cdd:PRK13651 243 IIKDGD 248
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-219 |
9.81e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.79 E-value: 9.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 12 GIVEFKGVNKSY--GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING--IKPSIET--KKIV 85
Cdd:PRK11160 337 VSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpIADYSEAalRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 86 SYLPERTYL-NDWMKvsDLLKFFYDFYSDfdvrraNEMIKSLD-------IDVNEKLKT--------MSKGTKEKVQLIL 149
Cdd:PRK11160 417 SVVSQRVHLfSATLR--DNLLLAAPNASD------EALIEVLQqvgleklLEDDKGLNAwlgeggrqLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 150 VMSRNASIYILDEPIGGVDPAARSYILKTILKnYSEDSTLLIATHLISEIENIcDEVIFISKGEIVLQGD 219
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAE-HAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGT 556
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
10-215 |
1.46e-17 |
|
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: 78.22 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 10 QDGIVEFKGVNKSYGTK--NVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK----PSIETKK 83
Cdd:cd03369 3 EHGEIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDistiPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 84 IVSYLPERTYLNDWMKVSDLLKFfyDFYSDFDVRRAnemiksldIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEP 163
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLDPF--DEYSDEEIYGA--------LRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489525288 164 IGGVDPAARSYILKTILKNYSeDSTLLIATHLISEIENiCDEVIFISKGEIV 215
Cdd:cd03369 153 TASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIID-YDKILVMDAGEVK 202
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-219 |
1.97e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 78.52 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING----IKPSIETKKIVS--- 86
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdFSKTPSDKAIRElrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 87 --------Y--LPERTYLNDW----MKVSDLLKffydfysDFDVRRANEMIKSLDIdvNEKLKT----MSKGTKEKVQLI 148
Cdd:PRK11124 83 nvgmvfqqYnlWPHLTVQQNLieapCRVLGLSK-------DQALARAEKLLERLRL--KPYADRfplhLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489525288 149 LVMSRNASIYILDEPIGGVDPAARSYILKtILKNYSEDS-TLLIATHLISEIENICDEVIFISKGEIVLQGD 219
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVS-IIRELAETGiTQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
7-221 |
2.80e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.77 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 7 NVSQDGIVeFKGVNKSY-GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKK-I 84
Cdd:PRK15056 1 MMQQAGIV-VNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKnL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 VSYLPERTYLnDW---MKVSDLLKF-------FYDFYSDFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMS 152
Cdd:PRK15056 80 VAYVPQSEEV-DWsfpVLVEDVVMMgryghmgWLRRAKKRDRQIVTAALARVDMVefRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489525288 153 RNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFIsKGEIVLQGDVE 221
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTE 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-219 |
2.98e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.12 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 5 INNVSQDGIVEFKGVNKSYGTKN-----VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGI--KP 77
Cdd:PRK13631 13 PNPLSDDIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyiGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 78 SIETKKIVSYLPERTyLNDWMKVSDLLKFFYDF--YSDF------DVRRANEMIKSLDIDVNEKLK-------------- 135
Cdd:PRK13631 93 KKNNHELITNPYSKK-IKNFKELRRRVSMVFQFpeYQLFkdtiekDIMFGPVALGVKKSEAKKLAKfylnkmglddsyle 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 136 ----TMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISK 211
Cdd:PRK13631 172 rspfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDK 251
|
....*...
gi 489525288 212 GEIVLQGD 219
Cdd:PRK13631 252 GKILKTGT 259
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
14-74 |
3.48e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 79.04 E-value: 3.48e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING 74
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG 63
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
13-207 |
5.22e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.47 E-value: 5.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGtknvlkNIDLN-----IPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINgIKpsietkkiVSY 87
Cdd:PRK13409 340 LVEYPDLTKKLG------DFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LK--------ISY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 88 LPERTYLNDWMKVSDLLKFFYDFYSDFDVRraNEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIG 165
Cdd:PRK13409 405 KPQYIKPDYDGTVEDLLRSITDDLGSSYYK--SEIIKPLQLErlLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489525288 166 GVDPAARSYILKTIlKNYSE--DSTLLIATHLISEIENICDEVI 207
Cdd:PRK13409 483 HLDVEQRLAVAKAI-RRIAEerEATALVVDHDIYMIDYISDRLM 525
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-223 |
5.70e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 78.69 E-value: 5.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTK----NVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIkpsietkkivsylp 89
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQ-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 90 ERTYLNDwmkvSDLLKFfydfysdfdvRRANEMI-------------------------KSLDID--VNEKLKT------ 136
Cdd:PRK11153 68 DLTALSE----KELRKA----------RRQIGMIfqhfnllssrtvfdnvalplelagtPKAEIKarVTELLELvglsdk 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 137 -------MSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKtILKNYSED--STLLIATHLISEIENICDEVI 207
Cdd:PRK11153 134 adrypaqLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE-LLKDINRElgLTIVLITHEMDVVKRICDRVA 212
|
250
....*....|....*.
gi 489525288 208 FISKGEIVLQGDVEAI 223
Cdd:PRK11153 213 VIDAGRLVEQGTVSEV 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-228 |
8.28e-17 |
|
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: 76.81 E-value: 8.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTK---NVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK----PSIETKKIVS 86
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDirdlNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 87 YLPERTYLNDwMKVSDLLKffydfYSDFDV---------RRAN--EMIKSL----DIDVNEKLKTMSKGTKEKVQLILVM 151
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIR-----YGKPDAtdeeveeaaKKANihDFIMSLpdgyDTLVGERGSQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489525288 152 SRNASIYILDEPIGGVDpAARSYILKTILKNYSEDSTLLIATHLISEIENiCDEVIFISKGEIVLQGDVEAIREEKG 228
Cdd:cd03249 155 LRNPKILLLDEATSALD-AESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQKG 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
24-194 |
9.45e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.68 E-value: 9.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 24 GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGiKPSIETKKIVS--YLPERTYLNDWMKVS 101
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG-GDIDDPDVAEAchYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 102 DLLKFFYDFY--SDFDVRRANEMIKSLDIdVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTI 179
Cdd:PRK13539 92 ENLEFWAAFLggEELDIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
170
....*....|....*
gi 489525288 180 LKNYSEDSTLLIATH 194
Cdd:PRK13539 171 RAHLAQGGIVIAATH 185
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-238 |
9.64e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 78.69 E-value: 9.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGL--LQPDNGEIMIN-GIKP------------- 77
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvALCEkcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 78 -------SIETKKIVSYLPERTYLNDWMK-VSDLLKFFYDFYSDFDV-------------------RRANEMIKSLDID- 129
Cdd:TIGR03269 81 pcpvcggTLEPEEVDFWNLSDKLRRRIRKrIAIMLQRTFALYGDDTVldnvlealeeigyegkeavGRAVDLIEMVQLSh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 130 -VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTILKNY-SEDSTLLIATHLISEIENICDEVI 207
Cdd:TIGR03269 161 rITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270
....*....|....*....|....*....|.
gi 489525288 208 FISKGEIVLQGDVEAIREEKGKSIDALFREE 238
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVAVFMEGVSEVEKEC 271
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-227 |
1.01e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.18 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSY--GT---KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIET------- 81
Cdd:PRK13641 3 IKFENVDYIYspGTpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 82 -KKIVSY--------LPERTYLNDWMKVSDLLKFfydfySDFDVR-RANEMIKS--LDIDVNEKLK-TMSKGTKEKVQLI 148
Cdd:PRK13641 83 lRKKVSLvfqfpeaqLFENTVLKDVEFGPKNFGF-----SEDEAKeKALKWLKKvgLSEDLISKSPfELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 149 LVMSRNASIYILDEPIGGVDPAARSYILKtILKNY-SEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIREEK 227
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQ-LFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-194 |
1.02e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 75.76 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 19 VNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING--IKPSIET-KKIVSYLPERTYLN 95
Cdd:PRK13540 7 LDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsIKKDLCTyQKQLCFVGHRSGIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 96 DWMKVSDllKFFYDFYSDFDVRRANEMIK--SLDIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARS 173
Cdd:PRK13540 87 PYLTLRE--NCLYDIHFSPGAVGITELCRlfSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|.
gi 489525288 174 YILKTILKNYSEDSTLLIATH 194
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSH 185
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-228 |
1.37e-16 |
|
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: 75.99 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYG--TKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING-----IKPSIETKKIVS 86
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlalADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 87 YLPERTYLN----DWMKVSDllkffydfySDFDVRR---------ANEMIKSL----DIDVNEKLKTMSKGTKEKVQLIL 149
Cdd:cd03252 81 VLQENVLFNrsirDNIALAD---------PGMSMERvieaaklagAHDFISELpegyDTIVGEQGAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489525288 150 VMSRNASIYILDEPIGGVDPAARSYILKTiLKNYSEDSTLLIATHLISEIENiCDEVIFISKGEIVLQGDVEAIREEKG 228
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRN-MHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-214 |
1.84e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 77.43 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietkKIVSYLPERT- 92
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG--------TDVSRLHARDr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 93 --------Y-LNDWMKVSDLLKFFYDF----------YSDFDVRRANEMIKsLDIDVNEKLKTMSKGTKEKVQLILVMSR 153
Cdd:PRK10851 75 kvgfvfqhYaLFRHMTVFDNIAFGLTVlprrerpnaaAIKAKVTQLLEMVQ-LAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525288 154 NASIYILDEPIGGVDPAARSYiLKTILKNYSED--STLLIATHLISEIENICDEVIFISKGEI 214
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKE-LRRWLRQLHEElkFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-223 |
1.89e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.36 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 6 NNVSQDGIVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGiKP--SIETK- 82
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA-QPleSWSSKa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 83 --KIVSYLPERTYLNDWMKVSDLLKF-FYDF------YSDFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVM 151
Cdd:PRK10575 83 faRKVAYLPQQLPAAEGMTVRELVAIgRYPWhgalgrFGAADREKVEEAISLVGLKplAHRLVDSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525288 152 SRNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIAT-HLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVlHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-72 |
2.04e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.85 E-value: 2.04e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMI 72
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-238 |
3.34e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.28 E-value: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLqPD---NGEIMING-------IKPSiETK 82
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGeelqasnIRDT-ERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 83 KIV------SYLPERTYL------NDWMKVSdllkffydfYSDFD--VRRANEMIKSLDIDVNEKLKTMSKGTKEKvQLI 148
Cdd:PRK13549 83 GIAiihqelALVKELSVLeniflgNEITPGG---------IMDYDamYLRAQKLLAQLKLDINPATPVGNLGLGQQ-QLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 149 LV---MSRNASIYILDEPIGGVDpAARSYILKTILKNY-SEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIR 224
Cdd:PRK13549 153 EIakaLNKQARLLILDEPTASLT-ESETAVLLDIIRDLkAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMT 231
|
250 260
....*....|....*....|
gi 489525288 225 EEK------GKSIDALFREE 238
Cdd:PRK13549 232 EDDiitmmvGRELTALYPRE 251
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
15-74 |
4.75e-16 |
|
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: 74.63 E-value: 4.75e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 15 EFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING 74
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG 64
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-226 |
4.98e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.17 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSY--GT---KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING-----------IKP 77
Cdd:PRK13649 3 INLQNVSYTYqaGTpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 78 SIETKKIVSYLPERTYLNDwmkvsDLLKFFYDFYSDFDV------RRANEMIKSLDIDVNEKLKT---MSKGTKEKVQLI 148
Cdd:PRK13649 83 IRKKVGLVFQFPESQLFEE-----TVLKDVAFGPQNFGVsqeeaeALAREKLALVGISESLFEKNpfeLSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489525288 149 LVMSRNASIYILDEPIGGVDPAARSYiLKTILKNYSEDS-TLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIREE 226
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKE-LMTLFKKLHQSGmTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-223 |
8.15e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.45 E-value: 8.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSY-GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKIVsylpeR 91
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV-----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 92 TYLNDWMKVSDLLKFFYDFYSDFDV-------------RRANEMIKSLDIdvnEKLKT-----MSKGTKEKVQLILVMSR 153
Cdd:PRK13652 78 KFVGLVFQNPDDQIFSPTVEQDIAFgpinlgldeetvaHRVSSALHMLGL---EELRDrvphhLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489525288 154 NASIYILDEPIGGVDPAARSYILKtILKNYSED--STLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELID-FLNDLPETygMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-74 |
1.25e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 73.61 E-value: 1.25e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 489525288 22 SYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING 74
Cdd:COG4559 10 RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNG 62
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
13-168 |
1.38e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietKKIVSYLPERT 92
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-------KLRIGYVPQKL 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 93 YLNDWM--KVSDLLKFFYDFYSDfDVRRANEMIKSLDIdVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVD 168
Cdd:PRK09544 77 YLDTTLplTVNRFLRLRPGTKKE-DILPALKRVQAGHL-IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
29-218 |
1.59e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.89 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 29 LKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMIN------GIKPSIETKK------IVSYLPERTYLND 96
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKKIKEVKRlrkeigLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 97 --------------------WMKVSDLLKFfydfysdfdVRRANEMIKSLDIDvneklktMSKGTKEKVQLILVMSRNAS 156
Cdd:PRK13645 107 tiekdiafgpvnlgenkqeaYKKVPELLKL---------VQLPEDYVKRSPFE-------LSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525288 157 IYILDEPIGGVDPAARSYILKTILK-NYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERlNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
26-228 |
2.11e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.79 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 26 KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIK-LM-NGLLQPDNGEIMINGikpsietKKIVSYLP-ERTYLNDWM---- 98
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKvLMgHPKYEVTSGSILLDG-------EDILELSPdERARAGIFLafqy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 99 -------KVSDLLKFFY-----DFYSDFD-VRRANEMIKSLDID-------VNEKLktmSKGTKEKVQLILVMSRNASIY 158
Cdd:COG0396 86 pveipgvSVSNFLRTALnarrgEELSAREfLKLLKEKMKELGLDedfldryVNEGF---SGGEKKRNEILQMLLLEPKLA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489525288 159 ILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATH---LISEIEniCDEVIFISKGEIVLQGDVEAIR--EEKG 228
Cdd:COG0396 163 ILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHyqrILDYIK--PDFVHVLVDGRIVKSGGKELALelEEEG 235
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-223 |
2.87e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 72.69 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 19 VNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPS----------IETKKIVSYL 88
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 PER-----TYLNDWMKVSDLLKFFYD-----FYSDFDVR-RANEMIKSLDIDVNEKLK---TMSKGTKEKVQLILVMSRN 154
Cdd:PRK10619 91 RTRltmvfQHFNLWSHMTVLENVMEApiqvlGLSKQEAReRAVKYLAKVGIDERAQGKypvHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489525288 155 ASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-223 |
3.57e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 72.25 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGL--LQPD---NGEIMINGIK----PSIETKKI 84
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDifkmDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 VSY-------LPERTYLND---WMKVSDLLKFFYDFYSdfDVRRANEMIKSLDiDVNEKLK----TMSKGTKEKVQLILV 150
Cdd:PRK14247 84 VQMvfqipnpIPNLSIFENvalGLKLNRLVKSKKELQE--RVRWALEKAQLWD-EVKDRLDapagKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525288 151 MSRNASIYILDEPIGGVDPAARSYILKTILKnYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLE-LKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-238 |
3.68e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 74.09 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGlLQPD---NGEIMING--IKPS----IETKK 83
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGspLKASnirdTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 84 IV------SYLPERTYLNDWMKVSDLLKFFYDFYSDFDVRRANEMIKSLDIDVNEKLKTMSK---GTKEKVQLILVMSRN 154
Cdd:TIGR02633 80 IViihqelTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDyggGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 155 ASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIREEK------G 228
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDiitmmvG 239
|
250
....*....|
gi 489525288 229 KSIDALFREE 238
Cdd:TIGR02633 240 REITSLYPHE 249
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
13-236 |
3.77e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.74 E-value: 3.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNG-----EIMINGIKPS-------IE 80
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiELLGRTVQREgrlardiRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 81 TKKIVSYLPERTYLNDWMKV-----------SDLLKFFYDFYSDFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQL 147
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVlenvligalgsTPFWRTCFSWFTREQKQRALQALTRVGMVhfAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 148 ILVMSRNASIYILDEPIGGVDPAARSYILKTILK-NYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIREE 226
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNE 243
|
250
....*....|
gi 489525288 227 KgksIDALFR 236
Cdd:PRK09984 244 R---FDHLYR 250
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
17-74 |
4.10e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.50 E-value: 4.10e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 17 KGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING 74
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG 63
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
28-214 |
4.42e-15 |
|
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: 70.71 E-value: 4.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 28 VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING-----IKPSiETKKIVSYLPERtylndwmkvsD 102
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisqWDPN-ELGDHVGYLPQD----------D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 103 LLkffydfysdfdvrranemiksLDIDVNEKLktMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTILKN 182
Cdd:cd03246 86 EL---------------------FSGSIAENI--LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL 142
|
170 180 190
....*....|....*....|....*....|..
gi 489525288 183 YSEDSTLLIATHLISEIEnICDEVIFISKGEI 214
Cdd:cd03246 143 KAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-218 |
4.63e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.33 E-value: 4.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 23 YGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK----PSIETKKIVSYLPERTYLNDWM 98
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqhyASKEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 99 KVSDLL-------KFFYDFYSDFDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDP 169
Cdd:PRK10253 97 TVQELVargryphQPLFTRWRKEDEEAVTKAMQATGIThlADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489525288 170 AARSYILKTILK-NYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:PRK10253 177 SHQIDLLELLSElNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
13-207 |
4.68e-15 |
|
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: 73.67 E-value: 4.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGtknvlkNIDLNIPKGKI-----VGLLGPNGSGKSTMIKLMNGLLQPDNGEimingikpsIETKKIVSY 87
Cdd:COG1245 341 LVEYPDLTKSYG------GFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGE---------VDEDLKISY 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 88 LPErtYLND--WMKVSDLLKFFYdfYSDFDVRRAN-EMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDE 162
Cdd:COG1245 406 KPQ--YISPdyDGTVEEFLRSAN--TDDFGSSYYKtEIIKPLGLEklLDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489525288 163 PIGGVDPAARSYILKTIlKNYSE--DSTLLIATHLISEIENICDEVI 207
Cdd:COG1245 482 PSAHLDVEQRLAVAKAI-RRFAEnrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-214 |
9.15e-15 |
|
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: 69.77 E-value: 9.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 25 TKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING--IKPSIETKKI---VSYLPErtylnDWMK 99
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpVTRRSPRDAIragIAYVPE-----DRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 100 VSDLLkffydfysDFDVRRaNEMIKSLdidvneklktMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTI 179
Cdd:cd03215 87 EGLVL--------DLSVAE-NIALSSL----------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLI 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 489525288 180 LKnYSED--STLLIATHLiSEIENICDEVIFISKGEI 214
Cdd:cd03215 148 RE-LADAgkAVLLISSEL-DELLGLCDRILVMYEGRI 182
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
8-74 |
1.37e-14 |
|
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: 70.54 E-value: 1.37e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489525288 8 VSQDGIVEFKGVNKSYGTK----NVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING 74
Cdd:COG4181 3 SSSAPIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG 73
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
13-235 |
1.74e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.79 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSI--ETKKIVSYLPE 90
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvpPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 91 RTYLNDWMKVSDLLKFFY--DFYSDFDVR-RANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIG 165
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLkqDKLPKAEIAsRVNEMLGLVHMQefAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525288 166 GVDPAARSYI---LKTILKNYSedSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIREEKGKSIDALF 235
Cdd:PRK11607 179 ALDKKLRDRMqleVVDILERVG--VTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEF 249
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-227 |
2.36e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.68 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 17 KGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKK------------I 84
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealengismvhqE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 VSYLPERTYL-NDWMKVSDLLKFFYDfySDFDVRRANEMIKSLDIDVN--EKLKTMSKGTKEKVQLILVMSRNASIYILD 161
Cdd:PRK10982 82 LNLVLQRSVMdNMWLGRYPTKGMFVD--QDKMYRDTKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 162 EPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIREEK 227
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDK 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
23-212 |
2.39e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.11 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 23 YGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK---PSIEtKKIV----SYLPertyln 95
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegPGAE-RGVVfqneGLLP------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 96 dWMKVSDLLKFFYDFYSDFDVRR---ANEMIKSLDIDVNEK--LKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPA 170
Cdd:PRK11248 84 -WRNVQDNVAFGLQLAGVEKMQRleiAHQMLKKVGLEGAEKryIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489525288 171 ARSYILKTILKNYSE--DSTLLIaTHLISEIENICDEVIFISKG 212
Cdd:PRK11248 163 TREQMQTLLLKLWQEtgKQVLLI-THDIEEAVFMATELVLLSPG 205
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
39-228 |
3.66e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 71.58 E-value: 3.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 39 GKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING--IKPSI-ETKKIVSYLPERTYLNDWMKVSDLLKFFYDFY---S 112
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksILTNIsDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRgvpA 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 113 DFDVRRANEMIKSLDIDV--NEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLL 190
Cdd:TIGR01257 2045 EEIEKVANWSIQSLGLSLyaDRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVV 2124
|
170 180 190
....*....|....*....|....*....|....*...
gi 489525288 191 IATHLISEIENICDEVIFISKGEIVLQGDVEAIREEKG 228
Cdd:TIGR01257 2125 LTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
26-228 |
3.76e-14 |
|
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: 68.71 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 26 KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGL--LQPDNGEIMINGikpsietKKIVSYLP-ERTylndwmkvsd 102
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKG-------EDITDLPPeERA---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 103 LLKFFYDFYSDFDVrranEMIKSLDI--DVNEKLktmSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTIL 180
Cdd:cd03217 76 RLGIFLAFQYPPEI----PGVKNADFlrYVNEGF---SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVIN 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489525288 181 KNYSEDSTLLIATHLISEIENI-CDEVIFISKGEIVLQGDVEAIR--EEKG 228
Cdd:cd03217 149 KLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALeiEKKG 199
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
14-218 |
4.33e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 69.73 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGT-KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETkkivsylpert 92
Cdd:PRK13633 10 VSYKYESNEESTeKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE----------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 93 ylNDWmkvsdllkffydfysdfDVRRANEMI---------------------KSLDID-------VNEKLKT-------- 136
Cdd:PRK13633 79 --NLW-----------------DIRNKAGMVfqnpdnqivativeedvafgpENLGIPpeeirerVDESLKKvgmyeyrr 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 137 -----MSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTILK-NYSEDSTLLIATHLISEIENiCDEVIFIS 210
Cdd:PRK13633 140 haphlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElNKKYGITIILITHYMEEAVE-ADRIIVMD 218
|
....*...
gi 489525288 211 KGEIVLQG 218
Cdd:PRK13633 219 SGKVVMEG 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
15-162 |
4.92e-14 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 70.60 E-value: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 15 EFKGVNKSYGTKN-----VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIkpSIETKKIVSYlp 89
Cdd:COG4615 329 ELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ--PVTADNREAY-- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 90 ertylndwmkvSDLlkF---FYDFY---------SDFDVRRANEMIKSLDID-----VNEKLKT--MSKGTKEKVQLILV 150
Cdd:COG4615 405 -----------RQL--FsavFSDFHlfdrllgldGEADPARARELLERLELDhkvsvEDGRFSTtdLSQGQRKRLALLVA 471
|
170
....*....|..
gi 489525288 151 MSRNASIYILDE 162
Cdd:COG4615 472 LLEDRPILVFDE 483
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
28-171 |
5.47e-14 |
|
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: 68.15 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 28 VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGiKPSIETKKI----VSYLPERTYLNDWMKVSDL 103
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG-TPLAEQRDEphenILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 104 LKFFYDFYSDFDvRRANEMIKSLDIDVNEKL--KTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAA 171
Cdd:TIGR01189 94 LHFWAAIHGGAQ-RTIEDALAAVGLTGFEDLpaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-214 |
6.75e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IV-EFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINgikpsieTKKIVSYL--- 88
Cdd:PRK11147 318 IVfEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-------TKLEVAYFdqh 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 -----PERTYLNDwmkVSD-------------LLKFFYDFYsdFDVRRANEMIKSLdidvneklktmSKGTKEKVQLILV 150
Cdd:PRK11147 391 raeldPEKTVMDN---LAEgkqevmvngrprhVLGYLQDFL--FHPKRAMTPVKAL-----------SGGERNRLLLARL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489525288 151 MSRNASIYILDEPIGGVDPAARSyILKTILKNYseDSTLLIATHLISEIENICDEV-IFISKGEI 214
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVETLE-LLEELLDSY--QGTVLLVSHDRQFVDNTVTECwIFEGNGKI 516
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-228 |
7.76e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 70.36 E-value: 7.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 29 LKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietkkIVSYLPERTYL-NDWMKVSDLL--K 105
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG---------SVAYVPQQAWIqNDSLRENILFgkA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 106 FFYDFYSdfDVRRANEMIKSLDI-------DVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKT 178
Cdd:TIGR00957 725 LNEKYYQ--QVLEACALLPDLEIlpsgdrtEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEH 802
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489525288 179 IL--KNYSEDSTLLIATHLISEIENIcDEVIFISKGEIVLQGDVEAIREEKG 228
Cdd:TIGR00957 803 VIgpEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDG 853
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-237 |
8.14e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.26 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 6 NNVSQDGIVEFKGVN---KSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLqPDNGEIMINGI------- 75
Cdd:PRK11174 340 KELASNDPVTIEAEDleiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIelreldp 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 76 ----------------------------KPSIETKKIVSYLpERTYLNDWMkvsdllkffydfysdfdvrraNEMIKSLD 127
Cdd:PRK11174 419 eswrkhlswvgqnpqlphgtlrdnvllgNPDASDEQLQQAL-ENAWVSEFL---------------------PLLPQGLD 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 128 IDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDpaARS--YILKTiLKNYSEDSTLLIATHLISEIENiCDE 205
Cdd:PRK11174 477 TPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD--AHSeqLVMQA-LNAASRRQTTLMVTHQLEDLAQ-WDQ 552
|
250 260 270
....*....|....*....|....*....|..
gi 489525288 206 VIFISKGEIVLQGDVEAIREEKGksidaLFRE 237
Cdd:PRK11174 553 IWVMQDGQIVQQGDYAELSQAGG-----LFAT 579
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
10-229 |
9.13e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.13 E-value: 9.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 10 QDGIVEFKGVNKSYGT-KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGiKPsietkkiVSYL 88
Cdd:PRK10790 337 QSGRIDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG-RP-------LSSL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 PERTYLNDWMKVSD----LLKFFYDF------YSDFDVRRA------NEMIKSLDIDVNEKL----KTMSKGTKEKVQLI 148
Cdd:PRK10790 409 SHSVLRQGVAMVQQdpvvLADTFLANvtlgrdISEEQVWQAletvqlAELARSLPDGLYTPLgeqgNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 149 LVMSRNASIYILDEPIGGVDPAARSYILKTiLKNYSEDSTLLIATHLISEIENiCDEVIFISKGEIVLQGDVEAIREEKG 228
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQA-LAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAAQG 566
|
.
gi 489525288 229 K 229
Cdd:PRK10790 567 R 567
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
12-215 |
1.26e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.00 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 12 GIVEFKGVNKSY--GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPS----IETKKIV 85
Cdd:PLN03232 1233 GSIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfglTDLRRVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 86 SYLPERTYLndwmkVSDLLKFFYDFYS---DFDVRRANEM--IKS--------LDIDVNEKLKTMSKGTKEKVQLILVMS 152
Cdd:PLN03232 1313 SIIPQSPVL-----FSGTVRFNIDPFSehnDADLWEALERahIKDvidrnpfgLDAEVSEGGENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525288 153 RNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIEniCDEVIFISKGEIV 215
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIID--CDKILVLSSGQVL 1448
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
30-214 |
1.28e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 30 KNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIM-----INGIKPSIETKKIVSYLPERT-----YLN---D 96
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMlngkeINALSTAQRLARGLVYLPEDRqssglYLDaplA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 97 WMKVS---DLLKFFYDFYSD---FDVRRANEMIKSLDIDvnEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPA 170
Cdd:PRK15439 360 WNVCAlthNRRGFWIKPAREnavLERYRRALNIKFNHAE--QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489525288 171 ARSYILKtILKNYSEDST--LLIATHLiSEIENICDEVIFISKGEI 214
Cdd:PRK15439 438 ARNDIYQ-LIRSIAAQNVavLFISSDL-EEIEQMADRVLVMHQGEI 481
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
33-223 |
2.04e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.30 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 33 DLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK-----PSietKKIVSYL-------PERTY------- 93
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhtttpPS---RRPVSMLfqennlfSHLTVaqniglg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 94 LNDWMKVSDLLKffydfysDFDVRRANEMikSLDiDVNEKLKT-MSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAAR 172
Cdd:PRK10771 96 LNPGLKLNAAQR-------EKLHAIARQM--GIE-DLLARLPGqLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489525288 173 SYILkTILKNYSEDS--TLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK10771 166 QEML-TLVSQVCQERqlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-227 |
2.22e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.89 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNksygTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIET------KKIVs 86
Cdd:COG1129 256 VLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSprdairAGIA- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 87 YLPE-R--------------TYLNDWMKVSDLLkffydFYSDFDVRR-ANEMIKSLDI---DVNEKLKTMSKGTKEKVQL 147
Cdd:COG1129 331 YVPEdRkgeglvldlsirenITLASLDRLSRGG-----LLDRRRERAlAEEYIKRLRIktpSPEQPVGNLSGGNQQKVVL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 148 ILVMSRNASIYILDEPIGGVDPAARSYILKtILKNYSED--STLLIATHLiSEIENICDEVIFISKGEIVLQGDVEAIRE 225
Cdd:COG1129 406 AKWLATDPKVLILDEPTRGIDVGAKAEIYR-LIRELAAEgkAVIVISSEL-PELLGLSDRILVMREGRIVGELDREEATE 483
|
..
gi 489525288 226 EK 227
Cdd:COG1129 484 EA 485
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-223 |
2.57e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.85 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 25 TKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQP-DNGEIMINGikpsietkkIVSYLPERTYLNDWMKVSDL 103
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRG---------SVAYVPQVSWIFNATVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 104 LkffydFYSDFDVRR------ANEMIKSLDI-------DVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPA 170
Cdd:PLN03232 700 L-----FGSDFESERywraidVTALQHDLDLlpgrdltEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489525288 171 ARSYILKTILKNYSEDSTLLIATHLISEIENIcDEVIFISKGEIVLQGDVEAI 223
Cdd:PLN03232 775 VAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAEL 826
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-195 |
3.54e-13 |
|
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: 65.98 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 15 EFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKIVS---YLPER 91
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARgllYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 92 TYLNDWMKVSDLLKFFYDFYSDFDVRRAnemIKSLDIDVNEKL--KTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDP 169
Cdd:cd03231 82 PGIKTTLSVLENLRFWHADHSDEQVEEA---LARVGLNGFEDRpvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180
....*....|....*....|....*.
gi 489525288 170 AARSYILKTILKNYSEDSTLLIATHL 195
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-225 |
6.96e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.02 E-value: 6.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPD-----NGEIMINGIK------PSIETK 82
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNiyspdvDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 83 KIVSYL-------PERTYLND---WMKVSDLLKffydFYSDFDVRRANEMIKSLDID-----VNEKLKTMSKGTKEKVQL 147
Cdd:PRK14267 85 REVGMVfqypnpfPHLTIYDNvaiGVKLNGLVK----SKKELDERVEWALKKAALWDevkdrLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 148 ILVMSRNASIYILDEPIGGVDPAARSYIlKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIRE 225
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKI-EELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
26-218 |
1.48e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.44 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 26 KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDN--GEIMINGIKPSIETKKIVSYLPERTYLNDWMKVSD- 102
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKRTGFVTQDDILYPHLTVREt 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 103 -----LLKFFYDFYSDFDVRRANEMIKSL-------DIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPA 170
Cdd:PLN03211 161 lvfcsLLRLPKSLTKQEKILVAESVISELgltkcenTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489525288 171 ARSYILKTILKNYSEDSTLLIATHL-ISEIENICDEVIFISKGEIVLQG 218
Cdd:PLN03211 241 AAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
31-228 |
1.64e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.30 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 31 NIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING--IKPS-IETKKIVSYlpertylndwMKVSdllkff 107
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGdIATRRRVGY----------MSQA------ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 108 ydF--YSDFDVR-------------------RANEMIKSLDI-DVNEKL-KTMSKGTKEKVQLILVMSRNASIYILDEPI 164
Cdd:NF033858 348 --FslYGELTVRqnlelharlfhlpaaeiaaRVAEMLERFDLaDVADALpDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489525288 165 GGVDPAARSYILKTILKNYSEDS-TLLIATHLISEIENiCDEVIFISKGEIVLQGDVEAIREEKG 228
Cdd:NF033858 426 SGVDPVARDMFWRLLIELSREDGvTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAARG 489
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
26-228 |
1.86e-12 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 64.59 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 26 KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGllQPD----NGEIMING-----IKPSIETKKIV----SYLPE-- 90
Cdd:TIGR01978 13 KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFKGqdlleLEPDERARAGLflafQYPEEip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 91 --------RTYLN-----DWMKVSDLLKFFydfysdfdvRRANEMIKSLDID-------VNEKLktmSKGTKEKVQLILV 150
Cdd:TIGR01978 91 gvsnleflRSALNarrsaRGEEPLDLLDFE---------KLLKEKLALLDMDeeflnrsVNEGF---SGGEKKRNEILQM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 151 MSRNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFI-SKGEIVLQGDVEAIR--EEK 227
Cdd:TIGR01978 159 ALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKPDYVHVlLDGRIVKSGDVELAKelEAK 238
|
.
gi 489525288 228 G 228
Cdd:TIGR01978 239 G 239
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-96 |
3.01e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.34 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSY-GTKNVLKNIDLN-IPKGKIvGLLGPNGSGKSTMIKLMNGLLQPDNGEIMIN-GIKpsietkkiVSYLP 89
Cdd:TIGR03719 4 IYTMNRVSKVVpPKKEILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIK--------VGYLP 74
|
....*..
gi 489525288 90 ERTYLND 96
Cdd:TIGR03719 75 QEPQLDP 81
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-90 |
4.23e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.95 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSY--GT---KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietkKIVSY 87
Cdd:COG1101 1 MLELKNLSKTFnpGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG--------KDVTK 72
|
...
gi 489525288 88 LPE 90
Cdd:COG1101 73 LPE 75
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-221 |
4.95e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.81 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 19 VNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEI-MINGIKPSIETKKIVSYL-PERTYLND 96
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFLrADESPLQH 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 97 WMKVS--DLLKFFYDFYSDFDVRRANemiksldidVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSY 174
Cdd:PRK10636 398 LARLApqELEQKLRDYLGGFGFQGDK---------VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQA 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489525288 175 ILKTILknySEDSTLLIATHLISEIENICDEVIFISKGEI-VLQGDVE 221
Cdd:PRK10636 469 LTEALI---DFEGALVVVSHDRHLLRSTTDDLYLVHDGKVePFDGDLE 513
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
14-214 |
5.41e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 64.28 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMI-----NGIKPSietKKIVSYL 88
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIgekrmNDVPPA---ERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 PERTYLNDWMKVSDLLKFFYDFY----SDFDvRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDE 162
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAgakkEEIN-QRVNQVAEVLQLAhlLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489525288 163 PIGGVDPAARSYILKTILKNYSE-DSTLLIATHLISEIENICDEVIFISKGEI 214
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
29-223 |
6.57e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 64.28 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 29 LKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPS---------IETKKIVSYLpERTYLNDWMK 99
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdaelreVRRKKIAMVF-QSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 100 VSDLLKFFYDFYSdfdVRRANEMIKSLDIDVNEKLKT--------MSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAA 171
Cdd:PRK10070 123 VLDNTAFGMELAG---INAEERREKALDALRQVGLENyahsypdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489525288 172 RSYILKTILK-NYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK10070 200 RTEMQDELVKlQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-221 |
6.77e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.76 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 22 SYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQP-DNGEIMINGikpsietkkIVSYLPERTYLNDWMKV 100
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRG---------TVAYVPQVSWIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 101 SDLLkffydFYSDFDVRRANEMI------KSLDI-------DVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGV 167
Cdd:PLN03130 697 DNIL-----FGSPFDPERYERAIdvtalqHDLDLlpggdltEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489525288 168 DPAARSYILKTILKNYSEDSTLLIAT---HLISEIenicDEVIFISKGEIVLQGDVE 221
Cdd:PLN03130 772 DAHVGRQVFDKCIKDELRGKTRVLVTnqlHFLSQV----DRIILVHEGMIKEEGTYE 824
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-214 |
8.00e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.58 E-value: 8.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 10 QDGIVEFKGVNKSY--GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSI----ETKK 83
Cdd:TIGR00957 1281 PRGRVEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKiglhDLRF 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 84 IVSYLPErtylnDWMKVSDLLKFFYD---FYSDFDVRRANEMI----------KSLDIDVNEKLKTMSKGTKEKVQLILV 150
Cdd:TIGR00957 1361 KITIIPQ-----DPVLFSGSLRMNLDpfsQYSDEEVWWALELAhlktfvsalpDKLDHECAEGGENLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489525288 151 MSRNASIYILDEPIGGVDPAARSYILKTILKNYsEDSTLLIATHLISEIENICdEVIFISKGEI 214
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDNLIQSTIRTQF-EDCTVLTIAHRLNTIMDYT-RVIVLDKGEV 1497
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
25-228 |
8.36e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 64.35 E-value: 8.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 25 TKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKpsietkkivsyLPeRTYLNDWMK----V 100
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIP-----------LT-KLQLDSWRSrlavV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 101 SDLLKFFYDFYS---------------DFDVRRAN--EMIKSL----DIDVNEKLKTMSKGTKEKVQLILVMSRNASIYI 159
Cdd:PRK10789 395 SQTPFLFSDTVAnnialgrpdatqqeiEHVARLASvhDDILRLpqgyDTEVGERGVMLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489525288 160 LDEPIGGVDPAARSYILKTiLKNYSEDSTLLIATHLISEIENiCDEVIFISKGEIVLQGDVEAIREEKG 228
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHN-LRQWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-223 |
9.29e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.87 E-value: 9.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMN--GLLQPD---NGEIMING---IKPSIETKKI 84
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGhniYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 vsylpeRTYLNdwMKVSDLLKFFYDFYSD--FDVRRANEMIKS-LDIDVNEKLK-----------------TMSKGTKEK 144
Cdd:PRK14239 85 ------RKEIG--MVFQQPNPFPMSIYENvvYGLRLKGIKDKQvLDEAVEKSLKgasiwdevkdrlhdsalGLSGGQQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489525288 145 VQLILVMSRNASIYILDEPIGGVDPAARSYILKTILkNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLL-GLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-163 |
9.79e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 9.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 34 LNIPK-GKIVGLLGPNGSGKSTMIKLMNGLLQPDNG-------------------------EIMINGIKPSIetkKI--V 85
Cdd:PRK13409 93 LPIPKeGKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeepswdevlkrfrgtelqnyfkKLYNGEIKVVH---KPqyV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 86 SYLPErtYLNDwmKVSDLLKffydfysDFDVR-RANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDE 162
Cdd:PRK13409 170 DLIPK--VFKG--KVRELLK-------KVDERgKLDEVVERLGLEniLDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
.
gi 489525288 163 P 163
Cdd:PRK13409 239 P 239
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-218 |
1.01e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.83 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 3 KNINNVSqdGIVEFKGVNKSY-GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIET 81
Cdd:PRK13657 326 IDLGRVK--GAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 82 KK-----IVSYLPERTYLNdwMKVSDLLKFFYDFYSDFDVRRANEMIKSLDI----------DVNEKLKTMSKGTKEKVQ 146
Cdd:PRK13657 404 RAslrrnIAVVFQDAGLFN--RSIEDNIRVGRPDATDEEMRAAAERAQAHDFierkpdgydtVVGERGRQLSGGERQRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489525288 147 LILVMSRNASIYILDEPIGGVDpAARSYILKTILKNYSEDSTLLIATHLISEIENiCDEVIFISKGEIVLQG 218
Cdd:PRK13657 482 IARALLKDPPILILDEATSALD-VETEAKVKAALDELMKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
28-227 |
1.04e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.89 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 28 VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIkpSIETKKI-------VSYLPE---RTYLNDW 97
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE--DITGLSPrerrrlgVAYIPEdrlGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 98 MKVSD--LLKFFYDF-YS-----DFDV--RRANEMIKSLDI---DVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPI 164
Cdd:COG3845 351 MSVAEnlILGRYRRPpFSrggflDRKAirAFAEELIEEFDVrtpGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPT 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489525288 165 GGVDPAARSYILKTILKNYSEDSTLLiathLIS----EIENICDEVIFISKGEIVLQGDVEAIREEK 227
Cdd:COG3845 431 RGLDVGAIEFIHQRLLELRDAGAAVL----LISedldEILALSDRIAVMYEGRIVGEVPAAEATREE 493
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
17-96 |
1.10e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 17 KGVNKSYGT-KNVLKNIDLN-IPKGKIvGLLGPNGSGKSTMIKLMNGLLQPDNGEIMI-NGIKpsietkkiVSYLPERTY 93
Cdd:PRK11819 10 NRVSKVVPPkKQILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIK--------VGYLPQEPQ 80
|
...
gi 489525288 94 LND 96
Cdd:PRK11819 81 LDP 83
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-226 |
1.18e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 1 MDKNINNVSQDGIVEFKGVNkSYGTKNVlKNIDLNIPKGKIVGLLGPNGSGKStmiKLMNGLLQPD---NGEIMINGIK- 76
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRT---ELMNCLFGVDkraGGEIRLNGKDi 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 77 ----PSIETKKIVSYLPERTYLNDW---------MKVSDLLKF------FYDFYSDFDVRRANEMIKSLDI---DVNEKL 134
Cdd:PRK09700 328 sprsPLDAVKKGMAYITESRRDNGFfpnfsiaqnMAISRSLKDggykgaMGLFHEVDEQRTAENQRELLALkchSVNQNI 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 135 KTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEI 214
Cdd:PRK09700 408 TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
250
....*....|....
gi 489525288 215 --VLQGDVEAIREE 226
Cdd:PRK09700 488 tqILTNRDDMSEEE 501
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
36-207 |
1.74e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 61.05 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 36 IPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKIvsylpertylndwmkvsdllkffydfysdfd 115
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 116 vrranemiksldidvneklkTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTIlKNYSEDS--TLLIAT 193
Cdd:cd03222 71 --------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI-RRLSEEGkkTALVVE 129
|
170
....*....|....
gi 489525288 194 HLISEIENICDEVI 207
Cdd:cd03222 130 HDLAVLDYLSDRIH 143
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
13-224 |
2.44e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.43 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK-PSIETKKI----VSY 87
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDiTDWQTAKImreaVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 88 LPERTYLNDWMKVSDLLKfFYDFYSDFD-----VRRANEMIKSLDIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDE 162
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLA-MGGFFAERDqfqerIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 163 PIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQ--GDV----EAIR 224
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEdtGDAllanEAVR 231
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-228 |
2.60e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.45 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 3 KNINNVSQDGiVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMiKLMNGLLQPDNGE---------IMIN 73
Cdd:NF000106 4 KTISNGARNA-VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRrpwrf*twcANRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 74 GIKPSIETKKIVSYLPERTYL---NDWM--KVSDLlkffydfySDFDVR-RANEMIK--SLDIDVNEKLKTMSKGTKEKV 145
Cdd:NF000106 82 ALRRTIG*HRPVR*GRRESFSgreNLYMigR*LDL--------SRKDARaRADELLErfSLTEAAGRAAAKYSGGMRRRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 146 QLILVMSRNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIRE 225
Cdd:NF000106 154 DLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
...
gi 489525288 226 EKG 228
Cdd:NF000106 234 KVG 236
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
13-214 |
2.64e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.06 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYG---TKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIET-----KKI 84
Cdd:PRK13650 4 IIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwdirHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 --VSYLPERTYLNdwMKVSDLLKFFYDF----YSDFD--VRRANEMIKSLDIDVNEKLKtMSKGTKEKVQLILVMSRNAS 156
Cdd:PRK13650 84 gmVFQNPDNQFVG--ATVEDDVAFGLENkgipHEEMKerVNEALELVGMQDFKEREPAR-LSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 157 IYILDEPIGGVDPAARSYILKTIlKNYSEDS--TLLIATHLISEIEnICDEVIFISKGEI 214
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTI-KGIRDDYqmTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-215 |
2.87e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 12 GIVEFKGVNKSYGTK--NVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPS----IETKKIV 85
Cdd:PLN03130 1236 GSIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISkfglMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 86 SYLPERTYLndwmkVSDLLKFFYDFYSDF---------------DVRRANEmiKSLDIDVNEKLKTMSKGTKEKVQLILV 150
Cdd:PLN03130 1316 GIIPQAPVL-----FSGTVRFNLDPFNEHndadlweslerahlkDVIRRNS--LGLDAEVSEAGENFSVGQRQLLSLARA 1388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489525288 151 MSRNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIEniCDEVIFISKGEIV 215
Cdd:PLN03130 1389 LLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIID--CDRILVLDAGRVV 1451
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
46-201 |
3.02e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 60.66 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 46 GPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKIVSYLPERTYLNDWMKVSDLLKFFYDFYSDFDVRRANEMIKS 125
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIHYFK 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 126 LDIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIEN 201
Cdd:PRK13541 113 LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHLESSIKS 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-163 |
3.55e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.49 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 34 LNIPK-GKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEI------------------------MING-IKPSIetkKI--V 85
Cdd:COG1245 93 LPVPKkGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkrfrgtelqdyfkkLANGeIKVAH---KPqyV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 86 SYLPERTYLndwmKVSDLLKffydfysDFDVR-RANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDE 162
Cdd:COG1245 170 DLIPKVFKG----TVRELLE-------KVDERgKLDELAEKLGLEniLDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
.
gi 489525288 163 P 163
Cdd:COG1245 239 P 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-215 |
4.38e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.24 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 17 KGVNKSYGT---------KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGiKPsietkkiVSY 87
Cdd:PRK10419 7 SGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRG-EP-------LAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 88 LP---ERTYLNDWMKVsdllkfFYDFYSDFDVR------------------------RANEMIKSLDIDVN--EKL-KTM 137
Cdd:PRK10419 79 LNraqRKAFRRDIQMV------FQDSISAVNPRktvreiireplrhllsldkaerlaRASEMLRAVDLDDSvlDKRpPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 138 SKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKtILKNYSE--DSTLLIATHLISEIENICDEVIFISKGEIV 215
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIR-LLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
13-226 |
6.20e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIM-------INGIKPSIET---- 81
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILylgkevtFNGPKSSQEAgigi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 82 -KKIVSYLPE----------RTYLNDWMKVsDLLKFFydfysdfdvRRANEMIKSLDIDVNEK--LKTMSKGTKEKVQLI 148
Cdd:PRK10762 84 iHQELNLIPQltiaeniflgREFVNRFGRI-DWKKMY---------AEADKLLARLNLRFSSDklVGELSIGEQQMVEIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 149 LVMSRNASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAIREE 226
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTED 231
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
14-172 |
9.81e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.14 E-value: 9.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNV-LKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKkivsylpert 92
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP---------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 93 ylndwmkvSDLLKFFYDFYSDF--------------DVRRANEMIKSLDIdvNEKLK---------TMSKGTKEKVQLIL 149
Cdd:PRK10522 393 --------EDYRKLFSAVFTDFhlfdqllgpegkpaNPALVEKWLERLKM--AHKLEledgrisnlKLSKGQKKRLALLL 462
|
170 180
....*....|....*....|...
gi 489525288 150 VMSRNASIYILDEPIGGVDPAAR 172
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFR 485
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-196 |
1.41e-10 |
|
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: 60.69 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 12 GIVEFKGVNKSY--GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDnGEIMINGI---KPSIET-KKIV 85
Cdd:TIGR01271 1216 GQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVswnSVTLQTwRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 86 SYLPERTYLNDWMKVSDLLKffYDFYSDFDVRRANEMI--KSLDIDVNEKLK--------TMSKGTKEKVQLILVMSRNA 155
Cdd:TIGR01271 1295 GVIPQKVFIFSGTFRKNLDP--YEQWSDEEIWKVAEEVglKSVIEQFPDKLDfvlvdggyVLSNGHKQLMCLARSILSKA 1372
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489525288 156 SIYILDEPIGGVDPAARSYILKTILKNYSeDSTLLIATHLI 196
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQSFS-NCTVILSEHRV 1412
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-223 |
1.49e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.68 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 26 KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIK----------PSIETKKIVSYLPERTYLN 95
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkdifqiDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 96 DWMKVSDLLKFFYDFYSDFDVRRANEMI----------KSLDIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIG 165
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVeeclrkvglwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 166 GVDpAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK14246 183 MID-IVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
26-215 |
2.30e-10 |
|
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: 59.15 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 26 KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKpsietkkiVSYLPERTY-------LNDWM 98
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGID--------ISKLPLHTLrsrlsiiLQDPI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 99 KVSDLLKFFYD---------FYSDFDVRRANEMIKS----LDIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIG 165
Cdd:cd03288 106 LFSGSIRFNLDpeckctddrLWEALEIAQLKNMVKSlpggLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489525288 166 GVDPAARSYILKTILKNYSeDSTLLIATHLISEIENiCDEVIFISKGEIV 215
Cdd:cd03288 186 SIDMATENILQKVVMTAFA-DRTVVTIAHRVSTILD-ADLVLVLSRGILV 233
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
27-215 |
2.64e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 58.95 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 27 NVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIET-----KKI--VSYLPERTYLNdwMK 99
Cdd:PRK13642 21 NQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrRKIgmVFQNPDNQFVG--AT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 100 VSDLLKFFYD---FYSDFDVRRANE---MIKSLDIDVNEKLKtMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARS 173
Cdd:PRK13642 99 VEDDVAFGMEnqgIPREEMIKRVDEallAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489525288 174 YILKTILKNYSE-DSTLLIATHLISEIENiCDEVIFISKGEIV 215
Cdd:PRK13642 178 EIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEII 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-223 |
3.29e-10 |
|
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: 58.91 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKN----VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQP---DNGEIMINGikpsietKKIV 85
Cdd:COG0444 1 LLEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDG-------EDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 86 SyLPER------------------TYLNDWMKVSDLLKFFYDFYSDFDVR----RANEMIKSLDIDVNEKLKT-----MS 138
Cdd:COG0444 74 K-LSEKelrkirgreiqmifqdpmTSLNPVMTVGDQIAEPLRIHGGLSKAeareRAIELLERVGLPDPERRLDrypheLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 139 KGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKtILKNYSE--DSTLLIATHLISEIENICDEVIFISKGEIVL 216
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILN-LLKDLQRelGLAILFITHDLGVVAEIADRVAVMYAGRIVE 231
|
....*..
gi 489525288 217 QGDVEAI 223
Cdd:COG0444 232 EGPVEEL 238
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
19-227 |
3.45e-10 |
|
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: 58.71 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 19 VNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDnGEIMINGIK----PSIETKKIVSYLPERTYL 94
Cdd:cd03289 10 AKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSwnsvPLQKWRKAFGVIPQKVFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 95 ndwmkVSDLLKFFYDFY---SDFDVRRANEMI--KS--------LDIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILD 161
Cdd:cd03289 89 -----FSGTFRKNLDPYgkwSDEEIWKVAEEVglKSvieqfpgqLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 162 EPIGGVDPAArSYILKTILKNYSEDSTLLIATHLISEIENiCDEVIFISKGEIVLQGDVEAIREEK 227
Cdd:cd03289 164 EPSAHLDPIT-YQVIRKTLKQAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
13-215 |
3.76e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.96 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSY-GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKIVSYLpeR 91
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 92 TYLNDWMKVSDLL--KFFYDFY---------SDFDVRR----ANEMIKSLDIDVNEKLKtMSKGTKEKVQLILVMSRNAS 156
Cdd:PRK10908 79 RQIGMIFQDHHLLmdRTVYDNVaipliiagaSGDDIRRrvsaALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489525288 157 IYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIV 215
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-227 |
5.59e-10 |
|
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: 59.15 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 23 YGTKnVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietkkIVSYLPERTY-LNDWMKVS 101
Cdd:TIGR01271 437 YVTP-VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG---------RISFSPQTSWiMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 102 DLLKFFYDFYSDFDVRRANEMIKSLDIdVNEKLK--------TMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARS 173
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQLEEDIAL-FPEKDKtvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 174 YILKTILKNYSEDSTLLIAThliSEIENI--CDEVIFISKGEIVLQGDVEAIREEK 227
Cdd:TIGR01271 586 EIFESCLCKLMSNKTRILVT---SKLEHLkkADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
29-218 |
6.18e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.88 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 29 LKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETkkiVSYLPER---------TYLNDWMK 99
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD---YSYRSQRirmifqdpsTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 100 VSDLLKFFYDFYSDFDV----RRANEMIKSLDI---DVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAAR 172
Cdd:PRK15112 106 ISQILDFPLRLNTDLEPeqreKQIIETLRQVGLlpdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489525288 173 SYILKTILKnysedstlLIATHLISEI---------ENICDEVIFISKGEIVLQG 218
Cdd:PRK15112 186 SQLINLMLE--------LQEKQGISYIyvtqhlgmmKHISDQVLVMHQGEVVERG 232
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
27-194 |
8.87e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.13 E-value: 8.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 27 NVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKIVSYLPERTylndwmkvsdlLKF 106
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQK-----------LGF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 107 FYDFY---SDFDV-------------------RRANEMIKS--LDIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDE 162
Cdd:PRK11629 92 IYQFHhllPDFTAlenvamplligkkkpaeinSRALEMLAAvgLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|...
gi 489525288 163 PIGGVDPAARSYILKTILK-NYSEDSTLLIATH 194
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGElNRLQGTAFLVVTH 204
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-222 |
9.43e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.25 E-value: 9.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 26 KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMingikpsieTKKIVSYLPERTYLNDWMKVSDLLk 105
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW---------AERSIAYVPQQAWIMNATVRGNIL- 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 106 ffydFYSDFDVRRANEMIK-------------SLDIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAAR 172
Cdd:PTZ00243 743 ----FFDEEDAARLADAVRvsqleadlaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489525288 173 SYILKTILKNYSEDSTLLIATHLIsEIENICDEVIFISKGEIVLQGDVEA 222
Cdd:PTZ00243 819 ERVVEECFLGALAGKTRVLATHQV-HVVPRADYVVALGDGRVEFSGSSAD 867
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
29-223 |
1.12e-09 |
|
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: 57.27 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 29 LKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPS---------IETKKI------VSYLPERTY 93
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamsrkelreLRRKKIsmvfqsFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 94 LND---WMKVSDLLKffydfysDFDVRRANEMIK--SLDIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVD 168
Cdd:cd03294 120 LENvafGLEVQGVPR-------AEREERAAEALElvGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 169 PAARSYILKTILKNYSE-DSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:cd03294 193 PLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
28-227 |
1.28e-09 |
|
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: 57.17 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 28 VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietkkIVSYLPERTY-LNDWMKVSDLLKF 106
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG---------RISFSSQFSWiMPGTIKENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 107 FYDFYSDFDVRRANEMIKSL-------DIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTI 179
Cdd:cd03291 123 SYDEYRYKSVVKACQLEEDItkfpekdNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESC 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489525288 180 LKNYSEDSTLLIATHLISEIEnICDEVIFISKGEIVLQGDVEAIREEK 227
Cdd:cd03291 203 VCKLMANKTRILVTSKMEHLK-KADKILILHEGSSYFYGTFSELQSLR 249
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-221 |
1.34e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 57.75 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 24 GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTmikLMNGLLQPD------NGEIMINGIK-PSIETKKIVSY-------LP 89
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTT---LMNALAFRSpkgvkgSGSVLLNGMPiDAKEMRAISAYvqqddlfIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 90 ERTYLNDWMkVSDLLKFFYDFYSDFDVRRANEMIKSLD--------IDVNEKLKTMSKGTKEKVQLILVMSRNASIYILD 161
Cdd:TIGR00955 113 TLTVREHLM-FQAHLRMPRRVTKKEKRERVDEVLQALGlrkcantrIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489525288 162 EPIGGVDPAARSYILKTILKNYSEDSTLLIATHL-ISEIENICDEVIFISKGEIVLQGDVE 221
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPD 252
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
13-221 |
1.34e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.57 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGllQPD----NGEIMINGikpsietKKIVSYL 88
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKG-------ESILDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 PE-RTYLNDWMKV-----------SDLLKFFYD----FY--SDFDVRRANEMIKS-----------LDIDVNEKLKTMSK 139
Cdd:CHL00131 78 PEeRAHLGIFLAFqypieipgvsnADFLRLAYNskrkFQglPELDPLEFLEIINEklklvgmdpsfLSRNVNEGFSGGEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 140 GTKEKVQLILVMSRNAsiyILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATHLISEIENIC-DEVIFISKGEIVLQG 218
Cdd:CHL00131 158 KRNEILQMALLDSELA---ILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTG 234
|
...
gi 489525288 219 DVE 221
Cdd:CHL00131 235 DAE 237
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-216 |
1.55e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 18 GVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLL--QPDNGEIMINGIKPSIEtKKIVSYLPERTYLN 95
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGRE-ASLIDAIGRKGDFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 96 DWMKVSDLLKffydfYSD-FDVRRanemiksldidvneKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDP--AAR 172
Cdd:COG2401 114 DAVELLNAVG-----LSDaVLWLR--------------RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRqtAKR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489525288 173 -SYILKTILKNYSedSTLLIATHlISEIEN--ICDEVIFISKGEIVL 216
Cdd:COG2401 175 vARNLQKLARRAG--ITLVVATH-HYDVIDdlQPDLLIFVGYGGVPE 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-218 |
1.91e-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: 55.73 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 21 KSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPD---NGEIMINGIkPSIETKKI----VSYLPErty 93
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGI-PYKEFAEKypgeIIYVSE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 94 lNDW----MKVSDLLkffydfysDFDVR-RANEMIKSLdidvneklktmSKGTKEKVQLILVMSRNASIYILDEPIGGVD 168
Cdd:cd03233 91 -EDVhfptLTVRETL--------DFALRcKGNEFVRGI-----------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489525288 169 PAARSYILKTI-LKNYSEDSTLLIATHLIS-EIENICDEVIFISKGEIVLQG 218
Cdd:cd03233 151 SSTALEILKCIrTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-211 |
2.55e-09 |
|
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: 54.67 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 26 KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIK------LMNGLLQPDNGEIMINGIKPSIEtkkivsylPERTYLndwmk 99
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaiglalGGAQSATRRRSGVKAGCIVAAVS--------AELIFT----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 100 vsdllkffydfysdfdvrranemiksldidvnekLKTMSKGTKEKVQLILVMS----RNASIYILDEPIGGVDPAARSYI 175
Cdd:cd03227 75 ----------------------------------RLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQAL 120
|
170 180 190
....*....|....*....|....*....|....*.
gi 489525288 176 LKTILKNYSEDSTLLIATHLiSEIENICDEVIFISK 211
Cdd:cd03227 121 AEAILEHLVKGAQVIVITHL-PELAELADKLIHIKK 155
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-194 |
3.89e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 28 VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGiKPSI--ETKKIVSYLPERTYLNDWMKVSDLLK 105
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG-KTATrgDRSRFMAYLGHLPGLKADLSTLENLH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 106 FFYDFYSdfdvRRANEM------IKSLDIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTI 179
Cdd:PRK13543 105 FLCGLHG----RRAKQMpgsalaIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
170
....*....|....*
gi 489525288 180 LKNYSEDSTLLIATH 194
Cdd:PRK13543 181 SAHLRGGGAALVTTH 195
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
10-207 |
4.14e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.11 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 10 QDGIVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING-----IKPSiETKKI 84
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistLKPE-IYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 VSYLPERTYL-NDwmKVSDLLKFFYDFYSDF--------DVRRANEMIKSLDIDVNEklktMSKGTKEKVQLILVMSRNA 155
Cdd:PRK10247 83 VSYCAQTPTLfGD--TVYDNLIFPWQIRNQQpdpaifldDLERFALPDTILTKNIAE----LSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489525288 156 SIYILDEPIGGVDPAARSyILKTILKNYSEDSTL--LIATHLISEIeNICDEVI 207
Cdd:PRK10247 157 KVLLLDEITSALDESNKH-NVNEIIHRYVREQNIavLWVTHDKDEI-NHADKVI 208
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-213 |
4.25e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.43 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDnGEIMING----IKPSIETKKI----- 84
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrvefFNQNIYERRVnlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 85 ---VSYLPERTYLNDwMKVSDLLKF---FYDFYSDFDVRRANE-MIKSLDI--DVNEKLKT----MSKGTKEKVQLILVM 151
Cdd:PRK14258 87 rrqVSMVHPKPNLFP-MSVYDNVAYgvkIVGWRPKLEIDDIVEsALKDADLwdEIKHKIHKsaldLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489525288 152 SRNASIYILDEPIGGVDPAArSYILKTILKNYSEDS--TLLIATHLISEIENICDEVIFISKGE 213
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIA-SMKVESLIQSLRLRSelTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-194 |
5.89e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEimingIKPSiETKKIvSYLPERTY 93
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT-----VKWS-ENANI-GYYAQDHA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 94 --------LNDWM----KVSDllkffydfySDFDVRRA-NEMIKSLDiDVNEKLKTMSKGtkEKVQLI---LVMSRnASI 157
Cdd:PRK15064 393 ydfendltLFDWMsqwrQEGD---------DEQAVRGTlGRLLFSQD-DIKKSVKVLSGG--EKGRMLfgkLMMQK-PNV 459
|
170 180 190
....*....|....*....|....*....|....*....
gi 489525288 158 YILDEPIGGVDPAArsyI--LKTILKNYseDSTLLIATH 194
Cdd:PRK15064 460 LVMDEPTNHMDMES---IesLNMALEKY--EGTLIFVSH 493
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
31-224 |
6.05e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.00 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 31 NIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGI----KPS--IETKKIVsylpeRTYLN-----DWMK 99
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhiegLPGhqIARMGVV-----RTFQHvrlfrEMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 100 VSDLL---------KFFYDFYSDFDVRRAN-----------EMIKSLDIdVNEKLKTMSKGTKEKVQLILVMSRNASIYI 159
Cdd:PRK11300 98 IENLLvaqhqqlktGLFSGLLKTPAFRRAEsealdraatwlERVGLLEH-ANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489525288 160 LDEPIGGVDPAARSYILKTI--LKNYSEDSTLLIaTHLISEIENICDEVIFISKGEIVLQGDVEAIR 224
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIaeLRNEHNVTVLLI-EHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-61 |
8.55e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.52 E-value: 8.55e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNG 61
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG 49
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
29-223 |
1.29e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.90 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 29 LKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKP----------------SIETKKIVSYLPERt 92
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAliaissglngqltgieNIELKGLMMGLTKE- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 93 ylndwmKVSDLLKffydfysdfdvrranEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPA 170
Cdd:PRK13545 119 ------KIKEIIP---------------EIIEFADIGkfIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489525288 171 ARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK13545 178 FTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-194 |
1.48e-08 |
|
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: 53.91 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 22 SYGtKNVLKNIDLNIPK-GKIVGLLGPNGSGKSTMIKLMNGLLQPDNG------------------------EIMING-I 75
Cdd:cd03236 9 RYG-PNSFKLHRLPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeildefrgselqnyfTKLLEGdV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 76 KPSIETkKIVSYLPERTYlndwMKVSDLLKffydfYSDfDVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSR 153
Cdd:cd03236 88 KVIVKP-QYVDLIPKAVK----GKVGELLK-----KKD-ERGKLDELVDQLELRhvLDRNIDQLSGGELQRVAIAAALAR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489525288 154 NASIYILDEPIGGVDPAARSYILKTILKNYSEDSTLLIATH 194
Cdd:cd03236 157 DADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
29-194 |
1.60e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 53.10 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 29 LKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKI--------VSYLPERTYLNDWMKV 100
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAtrsrnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 101 SDLLkffydFYSDFDVRRANEMIKSL----DID---------VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGV 167
Cdd:cd03290 97 ENIT-----FGSPFNKQRYKAVTDACslqpDIDllpfgdqteIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180
....*....|....*....|....*....
gi 489525288 168 DPAARSYILKT-ILKNYSEDS-TLLIATH 194
Cdd:cd03290 172 DIHLSDHLMQEgILKFLQDDKrTLVLVTH 200
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-210 |
2.60e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 53.25 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLlqpdngeimiNGIKPSIETKKIVSYLPERT 92
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRL----------NDLIPGFRVEGKVTFHGKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 93 YLND-------------WMKVSDLLKFFYD----------FYSDFD--VRRANEMIKSLDiDVNEKLKT----MSKGTKE 143
Cdd:PRK14243 80 YAPDvdpvevrrrigmvFQKPNPFPKSIYDniaygaringYKGDMDelVERSLRQAALWD-EVKDKLKQsglsLSGGQQQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489525288 144 KVQLILVMSRNASIYILDEPIGGVDPAARSYIlKTILKNYSEDSTLLIATHLISEIENICDEVIFIS 210
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRI-EELMHELKEQYTIIIVTHNMQQAARVSDMTAFFN 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-239 |
3.48e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 22 SYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMingikpsIETKKIVSYL---PER------- 91
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRII-------YEQDLIVARLqqdPPRnvegtvy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 92 TYLNDWMK-VSDLLKFFYDF-------YSD--------------------FDvRRANEMIKSLDIDVNEKLKTMSKGTKE 143
Cdd:PRK11147 85 DFVAEGIEeQAEYLKRYHDIshlvetdPSEknlnelaklqeqldhhnlwqLE-NRINEVLAQLGLDPDAALSSLSGGWLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 144 KVQLILVMSRNASIYILDEPIGGVDPAARSYiLKTILKNYSedSTLLIATHLISEIENICDEVIFISKGEIV-------- 215
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIETIEW-LEGFLKTFQ--GSIIFISHDRSFIRNMATRIVDLDRGKLVsypgnydq 240
|
250 260
....*....|....*....|....*
gi 489525288 216 -LQGDVEAIREEkgksidALFREEF 239
Cdd:PRK11147 241 yLLEKEEALRVE------ELQNAEF 259
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-74 |
4.12e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.92 E-value: 4.12e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489525288 14 VEFKGVNKSYGTKN-VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING 74
Cdd:PRK11650 4 LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG 65
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
23-194 |
4.54e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 23 YGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMI-NGIKPSI---------------------- 79
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKlrqdqfafeeftvldtvimght 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 80 -------ETKKIVSyLPERTYlNDWMKVSDLLKFF--YDFYSdfDVRRANEMIKSLDIDVNEKLKTMSK---GTKEKVQL 147
Cdd:PRK15064 91 elwevkqERDRIYA-LPEMSE-EDGMKVADLEVKFaeMDGYT--AEARAGELLLGVGIPEEQHYGLMSEvapGWKLRVLL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489525288 148 ILVMSRNASIYILDEPIGGVDPAARSYiLKTILKNYseDSTLLIATH 194
Cdd:PRK15064 167 AQALFSNPDILLLDEPTNNLDINTIRW-LEDVLNER--NSTMIIISH 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-223 |
5.83e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 5.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 24 GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTmiklmNGL----LQPDNGEIMINGIKPSIETKKivSYLPERTYlndwMK 99
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKST-----TGLallrLINSQGEIWFDGQPLHNLNRR--QLLPVRHR----IQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 100 VsdllkFFYDFYSDFDVRRANEMIKSLDIDVNEKlkTMSKGTKEKvQLILVM--------SRN----------------- 154
Cdd:PRK15134 366 V-----VFQDPNSSLNPRLNVLQIIEEGLRVHQP--TLSAAQREQ-QVIAVMeevgldpeTRHrypaefsggqrqriaia 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489525288 155 ------ASIYILDEPIGGVDPAARSYILkTILKNYSEDSTL--LIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK15134 438 ralilkPSLIILDEPTSSLDKTVQAQIL-ALLKSLQQKHQLayLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
9-223 |
6.06e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.42 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 9 SQDGIVefKGVNKSygtknvlkNIDLNipKGKIVGLLGPNGSGKS-TMIKLMnGLLQPdNGEIminGIKPSIETKKIVSy 87
Cdd:PRK09473 24 TPDGDV--TAVNDL--------NFSLR--AGETLGIVGESGSGKSqTAFALM-GLLAA-NGRI---GGSATFNGREILN- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 88 LPER------------------TYLNDWMKVSDLLKFFYDFYSDFDVRRA-NEMIKSLD-IDVNEKLKTM-------SKG 140
Cdd:PRK09473 86 LPEKelnklraeqismifqdpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAfEESVRMLDaVKMPEARKRMkmyphefSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 141 TKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILkTILKNYSED--STLLIATHLISEIENICDEVIFISKGEIVLQG 218
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIM-TLLNELKREfnTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 244
|
....*
gi 489525288 219 DVEAI 223
Cdd:PRK09473 245 NARDV 249
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
31-74 |
1.88e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.80 E-value: 1.88e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489525288 31 NIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING 74
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG 62
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-234 |
2.42e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.88 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSY----GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKIVSYL 88
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 pERTYLNDWMKVSDLLKFFY--------DFYSDFDVR----RANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRN 154
Cdd:PRK10535 84 -RREHFGFIFQRYHLLSHLTaaqnvevpAVYAGLERKqrllRAQELLQRLGLEdrVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 155 ASIYILDEPIGGVDPAARSYILkTILKNYSEDS-TLLIATHlISEIENICDEVIFISKGEIVLQGDVEAIREEKGKSIDA 233
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVM-AILHQLRDRGhTVIIVTH-DPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTEPV 240
|
.
gi 489525288 234 L 234
Cdd:PRK10535 241 V 241
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
32-215 |
2.50e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 32 IDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMING-----------IKPSI----ETKK---IVSYLPERTY 93
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpidirsprdaIRAGImlcpEDRKaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 94 LNdwmkVS---DLLKFFYDFYSDFDVRRANEMIKSLDI---DVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGV 167
Cdd:PRK11288 352 IN----ISarrHHLRAGCLINNRWEAENADRFIRSLNIktpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489525288 168 DPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIV 215
Cdd:PRK11288 428 DVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-212 |
2.95e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 49.16 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 19 VNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTmikLMNGLLQPDN-----GEIMINGIKPSIETKKIVSYLPERTY 93
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKTagvitGEILINGRPLDKNFQRSTGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 94 LNDWMKVSDLLKFfydfysdfdvrranemiksldidvNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAArS 173
Cdd:cd03232 90 HSPNLTVREALRF------------------------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA-A 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489525288 174 YILKTILKNYSEDS-TLLIATHLISE--IENIcDEVIFISKG 212
Cdd:cd03232 145 YNIVRFLKKLADSGqAILCTIHQPSAsiFEKF-DRLLLLKRG 185
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
29-74 |
6.07e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 49.07 E-value: 6.07e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 489525288 29 LKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLqPDNGEIMING 74
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNG 56
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-223 |
6.15e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 49.32 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 23 YGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQP-----DNGEIMING-----IKPSIETKKIVSYLPERT 92
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGrsifnYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 93 YLNDWMKVSDLLKFFydfysdfdvrRANEMIKSLDID---------------VNEKLKT----MSKGTKEKVQLILVMSR 153
Cdd:PRK14271 111 NPFPMSIMDNVLAGV----------RAHKLVPRKEFRgvaqarltevglwdaVKDRLSDspfrLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 154 NASIYILDEPIGGVDPAARSYIlKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-100 |
9.81e-07 |
|
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: 47.15 E-value: 9.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 28 VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEImingIKPSIETkkiVSYLPERTYLND----------W 97
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----GMPEGED---LLFLPQRPYLPLgtlreqliypW 88
|
...
gi 489525288 98 MKV 100
Cdd:cd03223 89 DDV 91
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
17-70 |
1.18e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.00 E-value: 1.18e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 489525288 17 KGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEI 70
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-229 |
1.67e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.49 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKN---VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMI------------------ 72
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndshnlkdinlkwwrski 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 73 ---------------NGIKPSIETKKIVSYLPER-------TYLNDWMKVSDLLKFFYDFYSDFDVRRANEMIK------ 124
Cdd:PTZ00265 463 gvvsqdpllfsnsikNNIKYSLYSLKDLEALSNYynedgndSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEmrknyq 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 125 ----SLDIDVNEKL---------------------KTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTI 179
Cdd:PTZ00265 543 tikdSEVVDVSKKVlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 489525288 180 --LKNYSEDSTLLIAtHLISEIEnICDEVIFISKGEIVLQGDVEAIREEKGK 229
Cdd:PTZ00265 623 nnLKGNENRITIIIA-HRLSTIR-YANTIFVLSNRERGSTVDVDIIGEDPTK 672
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
29-218 |
1.92e-06 |
|
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: 46.55 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 29 LKNIDLNIPKGKIVGLLGPNGSGKSTMIKlmngllqpdngeimiNGIKPSIETkkivsylpertylndwMKVSDLLKFFY 108
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------------EGLYASGKA----------------RLISFLPKFSR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 109 DFYSdfdvrraneMIKSLD--IDV-------NEKLKTMSKGTKEKVQLI--LVMSRNASIYILDEPIGGVDPAARSYILK 177
Cdd:cd03238 60 NKLI---------FIDQLQflIDVglgyltlGQKLSTLSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489525288 178 TILKNYSEDSTLLIATHLISEIENiCDEVIFISK------GEIVLQG 218
Cdd:cd03238 131 VIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPgsgksgGKVVFSG 176
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
29-218 |
4.67e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.10 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 29 LKNIDLNIPKGKIVGLLGPNGSGKSTMI---------------------KLMNGLLQPDNGEimINGIKPSIETK-KIVS 86
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDS--IEGLSPAIAIDqKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 87 YLPERTYlndwMKVSDLLKFFYDFYSDFDVRRANEMIKSLDID---VNEKLKTMSKGTKEKVQLI--LVMSRNASIYILD 161
Cdd:cd03270 89 RNPRSTV----GTVTEIYDYLRLLFARVGIRERLGFLVDVGLGyltLSRSAPTLSGGEAQRIRLAtqIGSGLTGVLYVLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489525288 162 EPIGGVDPAARSYILKTILKNYSEDSTLLIATHlISEIENICDEVIFISK------GEIVLQG 218
Cdd:cd03270 165 EPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEH-DEDTIRAADHVIDIGPgagvhgGEIVAQG 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
39-74 |
5.20e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.08 E-value: 5.20e-06
10 20 30
....*....|....*....|....*....|....*.
gi 489525288 39 GKIVGLLGPNGSGKSTMIKLMNGLLqPDNGEIMING 74
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAG 56
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
31-223 |
1.57e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 45.25 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 31 NIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMIN---------GIKPSIETKKIvSYLPERTYLNDWMKVS 101
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNgrvlfdaekGICLPPEKRRI-GYVFQDARLFPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 102 DLLKFfydFYSDFDVRRANEMIKSLDIdvnEKL-----KTMSKGTKEKVQL---------ILVMsrnasiyilDEPIGGV 167
Cdd:PRK11144 95 GNLRY---GMAKSMVAQFDKIVALLGI---EPLldrypGSLSGGEKQRVAIgralltapeLLLM---------DEPLASL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489525288 168 D-PAARSyiLKTILKNYSEDSTL--LIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK11144 160 DlPRKRE--LLPYLERLAREINIpiLYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-74 |
2.71e-05 |
|
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: 44.68 E-value: 2.71e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489525288 5 INNVSqdgiVEFKGvnkSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKS-TMIKLMnGLLqPDN-----GEIMING 74
Cdd:COG4172 9 VEDLS----VAFGQ---GGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLL-PDPaahpsGSILFDG 75
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
31-219 |
2.85e-05 |
|
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: 44.43 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 31 NIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPD-NGEIMINGIKPSIET--KKI---VSYLPE---RTYLNDWMKVS 101
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpaQAIragIAMVPEdrkRHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 102 D--LLKFFYDFYSDFDVRRANEMiKSLDIDVNE-KLKT---------MSKGTKEKVQLILVMSRNASIYILDEPIGGVDP 169
Cdd:TIGR02633 358 KniTLSVLKSFCFKMRIDAAAEL-QIIGSAIQRlKVKTaspflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489525288 170 AARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEivLQGD 219
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK--LKGD 484
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-223 |
3.15e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.46 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 29 LKNIDLNIPKGKIVGLLGPNGSGKS-TMIKLMNgLLQPDNGEIMINGIKPSIETKKIVSyLPER---------------- 91
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvTALALMR-LLEQAGGLVQCDKMLLRRRSRQVIE-LSEQsaaqmrhvrgadmami 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 92 -----TYLNDWMKV----SDLLKFFYDFYSDFDVRRANEMIKSLDIDVNEKL-----KTMSKGTKEKVQLILVMSRNASI 157
Cdd:PRK10261 110 fqepmTSLNPVFTVgeqiAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTIlsrypHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489525288 158 YILDEPIGGVDPAARSYILKTILKNYSEDSTLLI-ATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIfITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
29-223 |
3.26e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.04 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 29 LKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGikpsietkkIVSYLPERTYLNDWMKVSDLLKF-- 106
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG---------EVSVIAISAGLSGQLTGIENIEFkm 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 107 FYDFYSDFDVRRANEMI---KSLDIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAARSYILKTILKNY 183
Cdd:PRK13546 111 LCMGFKRKEIKAMTPKIiefSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489525288 184 SEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK13546 191 EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
29-54 |
3.61e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 3.61e-05
10 20
....*....|....*....|....*.
gi 489525288 29 LKNIDLNIPKGKIVGLLGPNGSGKST 54
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSS 41
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-208 |
4.17e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 3 KNINNVsqDGIVEFKGVNKSYGTKN---VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLM-------------------- 59
Cdd:PTZ00265 1157 KNKNDI--KGKIEIMDVNFRYISRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtn 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 60 ----------------------------------NGLLQPDNGEIMINGIKPS----IETKKIVSYLPERTYLNDwMKVS 101
Cdd:PTZ00265 1235 dmtneqdyqgdeeqnvgmknvnefsltkeggsgeDSTVFKNSGKILLDGVDICdynlKDLRNLFSIVSQEPMLFN-MSIY 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 102 DLLKFFYDFYSDFDVRRA------NEMIKSL----DIDVNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAA 171
Cdd:PTZ00265 1314 ENIKFGKEDATREDVKRAckfaaiDEFIESLpnkyDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
250 260 270
....*....|....*....|....*....|....*...
gi 489525288 172 RSYILKTILK-NYSEDSTLLIATHLISEIENICDEVIF 208
Cdd:PTZ00265 1394 EKLIEKTIVDiKDKADKTIITIAHRIASIKRSDKIVVF 1431
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
10-212 |
4.47e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.38 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 10 QDGIVEFKGVNKSY--GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSI----ETKK 83
Cdd:PTZ00243 1305 QAGSLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAyglrELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 84 IVSYLPERTYLNDWMKVSDLLKFFYdfYSDFDVRRANEMiksldIDVNEKLKTMSKGTKEKVQ-----------LILVMS 152
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVDPFLE--ASSAEVWAALEL-----VGLRERVASESEGIDSRVLeggsnysvgqrQLMCMA 1457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489525288 153 R----NASIYIL-DEPIGGVDPAARSYILKTILKNYSEDSTLLIA--THLISEieniCDEVIFISKG 212
Cdd:PTZ00243 1458 RallkKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAhrLHTVAQ----YDKIIVMDHG 1520
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
12-56 |
5.49e-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: 43.85 E-value: 5.49e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 489525288 12 GIVEFKGVNKsygtkNVLKNIDLNIPKGKIVGLLGPNGSGKSTMI 56
Cdd:TIGR00630 612 KFLTLKGARE-----NNLKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
25-56 |
5.65e-05 |
|
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: 42.99 E-value: 5.65e-05
10 20 30
....*....|....*....|....*....|..
gi 489525288 25 TKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMI 56
Cdd:cd03271 7 RENNLKNIDVDIPLGVLTCVTGVSGSGKSSLI 38
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
25-65 |
5.68e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 5.68e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 489525288 25 TKNVLKNIDLNIPKGKIVGLLGPNGSGKSTmikLMNGLLQP 65
Cdd:COG0178 617 RENNLKNVDVEIPLGVLTCVTGVSGSGKST---LVNDILYP 654
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-70 |
6.39e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 6.39e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 489525288 24 GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEI 70
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSY 58
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
25-65 |
6.53e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.52 E-value: 6.53e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 489525288 25 TKNVLKNIDLNIPKGKIVGLLGPNGSGKSTmikLMNGLLQP 65
Cdd:PRK00349 621 RENNLKNVDVEIPLGKFTCVTGVSGSGKST---LINETLYK 658
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
7-219 |
7.84e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.56 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 7 NVSQDGIVEFKGVNKSYgTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLM----NGLLQPDNGEIMINGIKPSiETK 82
Cdd:TIGR00956 56 KILTRGFRKLKKFRDTK-TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPE-EIK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 83 K----IVSYLPErtylND----WMKVSDLLKFF---------YDFYSDFDvrRANEM------IKSLDIDVNEK-----L 134
Cdd:TIGR00956 134 KhyrgDVVYNAE----TDvhfpHLTVGETLDFAarcktpqnrPDGVSREE--YAKHIadvymaTYGLSHTRNTKvgndfV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 135 KTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPA-ARSYI--LKTILKnySEDSTLLIATHLISE-IENICDEVIFIS 210
Cdd:TIGR00956 208 RGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAtALEFIraLKTSAN--ILDTTPLVAIYQCSQdAYELFDKVIVLY 285
|
....*....
gi 489525288 211 KGEIVLQGD 219
Cdd:TIGR00956 286 EGYQIYFGP 294
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
28-74 |
8.06e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.89 E-value: 8.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 489525288 28 VLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPD--------NGEIMING 74
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNG 70
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-70 |
1.03e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 1.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489525288 13 IVEFKGVNKSY-GTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEI 70
Cdd:PLN03073 508 IISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
29-55 |
1.89e-04 |
|
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: 42.31 E-value: 1.89e-04
10 20
....*....|....*....|....*..
gi 489525288 29 LKNIDLNIPKGKIVGLLGPNGSGKSTM 55
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
13-194 |
2.05e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 41.30 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 13 IVEFKGVNKSYGTK----NVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKIVSYL 88
Cdd:PRK10584 6 IVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 89 PERT---YLNDWMKVSDL-------LKFFYDFYSDFDVR-RANEMIKSLDIdvNEKLKTM----SKGTKEKVQLILVMSR 153
Cdd:PRK10584 86 RAKHvgfVFQSFMLIPTLnalenveLPALLRGESSRQSRnGAKALLEQLGL--GKRLDHLpaqlSGGEQQRVALARAFNG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489525288 154 NASIYILDEPIGGVDPAARSYILKTILK-NYSEDSTLLIATH 194
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSlNREHGTTLILVTH 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-74 |
2.11e-04 |
|
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: 41.98 E-value: 2.11e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489525288 21 KSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMiklmnGL----LQPDNGEIMING 74
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTL-----GLallrLIPSEGEIRFDG 346
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
29-54 |
2.47e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 2.47e-04
10 20
....*....|....*....|....*.
gi 489525288 29 LKNIDLNIPKGKIVGLLGPNGSGKST 54
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSS 41
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
14-214 |
2.94e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 14 VEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGllqpD------NGEIMINGIKPSIET----KK 83
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DhpqgysNDLTLFGRRRGSGETiwdiKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 84 IVSYLPERTYLNdwMKVSDLLK------FF-----YDFYSDFDVRRANEMIKSLDID---VNEKLKTMSKGTKEKVQLIL 149
Cdd:PRK10938 337 HIGYVSSSLHLD--YRVSTSVRnvilsgFFdsigiYQAVSDRQQKLAQQWLDILGIDkrtADAPFHSLSWGQQRLALIVR 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489525288 150 VMSRNASIYILDEPIGGVDPAARSYILKTILKNYSEDST-LLIATHLISEIEN-ICDEVIFISKGEI 214
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSHHAEDAPAcITHRLEFVPDGDI 481
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
38-72 |
3.43e-04 |
|
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: 39.66 E-value: 3.43e-04
10 20 30
....*....|....*....|....*....|....*
gi 489525288 38 KGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMI 72
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY 35
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
28-94 |
4.58e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 40.95 E-value: 4.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489525288 28 VLKNIDLNIPKGKivGLL--GPNGSGKSTMIKLMNGL--------LQPDNGEIMingikpsietkkivsYLPERTYL 94
Cdd:COG4178 378 LLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLwpygsgriARPAGARVL---------------FLPQRPYL 437
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
33-223 |
4.97e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 33 DLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKP---SIET-KKIVSylpertylNDWMKV-SDLLKFF 107
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHItrlSFEQlQKLVS--------DEWQRNnTDMLSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 108 YDfysDF-------------DVRRANEMIKSLDID--VNEKLKTMSKGTKEKVQLILVMSRNASIYILDEPIGGVDPAAR 172
Cdd:PRK10938 95 ED---DTgrttaeiiqdevkDPARCEQLAQQFGITalLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489525288 173 SYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEIVLQGDVEAI 223
Cdd:PRK10938 172 QQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
13-74 |
6.78e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.77 E-value: 6.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGL--LQPDNGEIMING 74
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKG 64
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
22-65 |
1.13e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 1.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489525288 22 SYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIklmNGLLQP 65
Cdd:PRK00635 604 SKATKHNLKDLTISLPLGRLTVVTGVSGSGKSSLI---NDTLVP 644
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-214 |
2.47e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 38.76 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 26 KNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNGLLQPDN-GEIMINGIKPSIET-----KKIVSYLPE---RTYLND 96
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKIRNpqqaiAQGIAMVPEdrkRDGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 97 WMKVSDLLKF-FYDFYSDFDVRRANEMIKSLDIDVNE-KLKT---------MSKGTKEKVQLILVMSRNASIYILDEPIG 165
Cdd:PRK13549 355 VMGVGKNITLaALDRFTGGSRIDDAAELKTILESIQRlKVKTaspelaiarLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489525288 166 GVDPAARSYILKTILKNYSEDSTLLIATHLISEIENICDEVIFISKGEI 214
Cdd:PRK13549 435 GIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
112-194 |
3.36e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.14 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 112 SDFDVRRANEMIKSLDIDVNEKLKTMSKGTKEKVQLILVMSRNA---SIYILDEPIGGVDPAARSYILKTILKNYSEDST 188
Cdd:pfam13304 212 VDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLSALpkgGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQ 291
|
....*.
gi 489525288 189 LLIATH 194
Cdd:pfam13304 292 LILTTH 297
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
46-211 |
4.19e-03 |
|
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: 37.20 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 46 GPNGSGKSTMIKLMNGLLQPDngeiMINGIKPSIETKKIVSYLPERTYLNdwMKVSDLLKFFYDFYSDFDVRRANEMIKS 125
Cdd:cd03240 29 GQNGAGKTTIIEALKYALTGE----LPPNSKGGAHDPKLIREGEVRAQVK--LAFENANGKKYTITRSLAILENVIFCHQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 126 LDID--VNEKLKTMSKGTKEKVQLIL------VMSRNASIYILDEPIGGVDPAARSYILKTILKNYSEDST--LLIATHl 195
Cdd:cd03240 103 GESNwpLLDMRGRCSGGEKVLASLIIrlalaeTFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSQKNfqLIVITH- 181
|
170
....*....|....*.
gi 489525288 196 ISEIENICDEVIFISK 211
Cdd:cd03240 182 DEELVDAADHIYRVEK 197
|
|
| AAA_14 |
pfam13173 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
38-116 |
5.68e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 463799 [Multi-domain] Cd Length: 128 Bit Score: 36.03 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525288 38 KGKIVGLLGPNGSGKSTMIKLMNGLLQPDNGEIMINGIKPSIETKKIV--------SYLPERTYL--------NDWMKVs 101
Cdd:pfam13173 1 SRKILVITGPRQVGKTTLLLQLIKELLPPENILYINLDDPRLLKLADFellelfleLLYPGKTYLfldeiqrvPDWELA- 79
|
90
....*....|....*
gi 489525288 102 dlLKFFYDFYSDFDV 116
Cdd:pfam13173 80 --LKRLYDDGPNGRV 92
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-61 |
5.99e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.46 E-value: 5.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 489525288 13 IVEFKGVNKSYGTKNVLKNIDLNIPKGKIVGLLGPNGSGKSTMIKLMNG 61
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PrkA |
COG2766 |
Predicted Ser/Thr protein kinase [Signal transduction mechanisms]; |
40-62 |
7.07e-03 |
|
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
Pssm-ID: 442049 [Multi-domain] Cd Length: 675 Bit Score: 37.12 E-value: 7.07e-03
10 20
....*....|....*....|....
gi 489525288 40 KIVGLLGPNGSGKSTMI-KLMNGL 62
Cdd:COG2766 109 RILLLHGPVGSGKSTLArCLKRGL 132
|
|
| |
