|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-215 |
2.94e-104 |
|
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: 302.96 E-value: 2.94e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSGMYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTP-LKDARSIRRKIGYLP 82
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDvLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 QQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPT 162
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491943749 163 AGLDPEERIRFRNLLADFANERLVLLSTHIVSDVEATTNRIGILDHGRLVFNG 215
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-230 |
5.00e-100 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 293.12 E-value: 5.00e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-KDARSIRRKIGYL 81
Cdd:COG1131 1 IEVRGLTKRYGDKT--ALDGVSLTVEPGeIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVaRDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 82 PQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEP 161
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 162 TAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAAGHVFV 230
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVFL 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-281 |
1.78e-73 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 227.68 E-value: 1.78e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKdaRSIRRKIGYL 81
Cdd:COG4152 1 MLELKGLTKRFGDKT--AVDDVSFTVPKGeIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD--PEDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 82 PQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEP 161
Cdd:COG4152 77 PEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 162 TAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAAGHVF--VGDLPVAQL 238
Cdd:COG4152 157 FSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLrlEADGDAGWL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 239 KQFktqYQISEQTAHGQHIRVRL-------------LARTPLATWQSVAPTLEEAY 281
Cdd:COG4152 237 RAL---PGVTVVEEDGDGAELKLedgadaqellralLARGPVREFEEVRPSLNEIF 289
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-222 |
9.59e-73 |
|
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: 223.97 E-value: 9.59e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRqqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-KDARSIRRKIGYL 81
Cdd:COG4555 2 IEVENLSKKYGKV--PALKDVSFTAKDGeITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVrKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 82 PQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEP 161
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491943749 162 TAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELID 222
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-211 |
2.06e-70 |
|
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: 215.34 E-value: 2.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRqqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-KDARSIRRKIGYL 81
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGeIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIkKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 82 PQQFGFYPTMKVIDAMTYlailaevpareqkrriewllaavhltaqaktkvkalSGGMLQRLGIAQALVNEPRVLIVDEP 161
Cdd:cd03230 79 PEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491943749 162 TAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRL 211
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-215 |
2.07e-62 |
|
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: 196.28 E-value: 2.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRKIGYLP 82
Cdd:cd03268 1 LKTNDLTKTYGKKR--VLDDISLHVKKGeIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 QQFGFYPTMKVIDAMTYLAILAEVPareqKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPT 162
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491943749 163 AGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRLVFNG 215
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-220 |
2.56e-61 |
|
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: 193.88 E-value: 2.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-KDARSIRRKIGYL 81
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGeIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 82 PQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEP 161
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491943749 162 TAGLDPEERIRFRNLLADFANERLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-220 |
5.73e-60 |
|
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: 190.66 E-value: 5.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDG-TPLKDARSIRRKIGYL 81
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGeIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhDVVREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 82 PQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEP 161
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491943749 162 TAGLDPEERI----RFRNLLADFANErlVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:cd03265 159 TIGLDPQTRAhvweYIEKLKEEFGMT--ILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-221 |
9.40e-59 |
|
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: 187.54 E-value: 9.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGrQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL--KDARSIRRKIGY 80
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGeFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItkKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQ----QFgFYPTmkVID----AMTYLAilaeVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNE 152
Cdd:COG1122 80 VFQnpddQL-FAPT--VEEdvafGPENLG----LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 153 PRVLIVDEPTAGLDPEERIRFRNLLADFANERL-VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELI 221
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKtVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
3-229 |
2.47e-58 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 188.83 E-value: 2.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYRgrQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTP-LKDARSIRRKIGY 80
Cdd:TIGR03522 2 SIRVSSLTKLYG--TQNALDEVSFEAQKGrIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDvLQNPKEVQRNIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDE 160
Cdd:TIGR03522 80 LPEHNPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491943749 161 PTAGLDPEERIRFRNLLADFANERLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAAGHVF 229
Cdd:TIGR03522 160 PTTGLDPNQLVEIRNVIKNIGKDKTIILSTHIMQEVEAICDRVIIINKGKIVADKKLDELSAANKKQVI 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-211 |
2.77e-56 |
|
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: 180.76 E-value: 2.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYR--GRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDAR-----SIR 75
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKGVSLSIEKGeFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 76 RK-IGYLPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPR 154
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491943749 155 VLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDhGRL 211
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRD-GKI 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-215 |
2.07e-55 |
|
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: 178.24 E-value: 2.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDArsIRRKIGYLP 82
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGeIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA--ARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 QQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPT 162
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491943749 163 AGLDPEERIRFRNLLADFA-NERLVLLSTHIVSDVEATTNRIGILDHGRLVFNG 215
Cdd:cd03269 157 SGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-223 |
4.61e-54 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 183.57 E-value: 4.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQ---PALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KDARSI 74
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGeTLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtklsrRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 75 RRKIGYLPQQ-FG-FYPTMKVIDAMTY-LAILAEVPAREQKRRIEWLLAAVHLTAQAKTK-VKALSGGMLQRLGIAQALV 150
Cdd:COG1123 341 RRRVQMVFQDpYSsLNPRMTVGDIIAEpLRLHGLLSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 151 NEPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDA 223
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-221 |
2.29e-53 |
|
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: 173.92 E-value: 2.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHY--RGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KDARSIR 75
Cdd:cd03258 2 IELKNVSKVFgdTGGKVTALKDVSLSVPKGeIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsgKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 76 RKIGYLPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRV 155
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491943749 156 LIVDEPTAGLDPEERIRFRNLLADFaNERL---VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELI 221
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDI-NRELgltIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-225 |
1.62e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 172.20 E-value: 1.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHYRGRqqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARsirRKIG 79
Cdd:COG1121 4 MPAIELENLTVSYGGR--PVLEDVSLTIPPGeFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR---RRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQFGFYPT--MKVID--AMTYLAI--LAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEP 153
Cdd:COG1121 79 YVPQRAEVDWDfpITVRDvvLMGRYGRrgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491943749 154 RVLIVDEPTAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDhGRLVFNGTTDELIDAAA 225
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPEEVLTPEN 230
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
19-228 |
1.88e-52 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 173.73 E-value: 1.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 19 PALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTP-LKDARSIRRKIGYLPQQFGFYPTMKVIDA 96
Cdd:TIGR01188 7 KAVDGVNFKVREGeVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDvVREPRKVRRSIGIVPQYASVDEDLTGREN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 97 MTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNL 176
Cdd:TIGR01188 87 LEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDY 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491943749 177 LADFANERL-VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAAGHV 228
Cdd:TIGR01188 167 IRALKEEGVtILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDT 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-267 |
7.24e-52 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 173.34 E-value: 7.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQP--ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KDARSIR 75
Cdd:COG1135 2 IELENLSKTFPTKGGPvtALDDVSLTIEKGeIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalseRELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 76 RKIGYLPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRV 155
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 156 LIVDEPTAGLDPE--ERIrfRNLLADfANERL---VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELI---DAAAGH 227
Cdd:COG1135 162 LLCDEATSALDPEttRSI--LDLLKD-INRELgltIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFanpQSELTR 238
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 491943749 228 VFVGDLPVAQLKQFKTQyQISEQTAHGQHIRVRLL---ARTPL 267
Cdd:COG1135 239 RFLPTVLNDELPEELLA-RLREAAGGGRLVRLTFVgesADEPL 280
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-210 |
6.48e-51 |
|
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: 166.87 E-value: 6.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 5 QIEQLVKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD--ARSIRRKIGYL 81
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGeFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlsLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 82 PQ----QFgFYPTmkVIDamtYLAILAE---VPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPR 154
Cdd:cd03225 81 FQnpddQF-FGPT--VEE---EVAFGLEnlgLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491943749 155 VLIVDEPTAGLDPEERIRFRNLLADFANERL-VLLSTHIVSDVEATTNRIGILDHGR 210
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-224 |
8.98e-51 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 167.93 E-value: 8.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 2 TTIQIEQLVKHYRGrQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KDARSIR 75
Cdd:COG3638 1 PMLELRNLSKRYPG-GTPALDDVSLEIERGeFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalrgRALRRLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 76 RKIGYLPQQFGFYPTMKVIDA--------MTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQ 147
Cdd:COG3638 80 RRIGMIFQQFNLVPRLSVLTNvlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 148 ALVNEPRVLIVDEPTAGLDPE--ERIrfRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDA 223
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKtaRQV--MDLLRRIAREDgiTVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDA 237
|
.
gi 491943749 224 A 224
Cdd:COG3638 238 V 238
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-212 |
2.05e-50 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 166.00 E-value: 2.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGrQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARS-----IRRK 77
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGeFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreipyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 78 IGYLPQQFGFYPTMKVID----AMtylaILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEP 153
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYEnvalPL----RVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491943749 154 RVLIVDEPTAGLDPEERIRFRNLLADFaNER--LVLLSTHIVSDVEATTNRIGILDHGRLV 212
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEI-NRRgtTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-219 |
9.76e-50 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 164.49 E-value: 9.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRgrQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLkdARSIRRKIGYLP 82
Cdd:TIGR03740 1 LETKNLSKRFG--KQTAVNNISLTVPKNsVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPW--TRKDLHKIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 QQFGFYPTMKVIDAMTYLAILAEVPareqKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPT 162
Cdd:TIGR03740 77 ESPPLYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPT 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 163 AGLDPEERIRFRNLLADFANERL-VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDE 219
Cdd:TIGR03740 153 NGLDPIGIQELRELIRSFPEQGItVILSSHILSEVQQLADHIGIISEGVLGYQGKINK 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-229 |
2.94e-49 |
|
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: 163.51 E-value: 2.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KDARSIRRK 77
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGeFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 78 IGYLPQQFGFYPTMKVID--------AMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQAL 149
Cdd:cd03256 80 IGMIFQQFNLIERLSVLEnvlsgrlgRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 150 VNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAAGH 227
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDE 239
|
..
gi 491943749 228 VF 229
Cdd:cd03256 240 IY 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-212 |
1.20e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 161.36 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTT-IQIEQLVKHYR--GRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL----KDAR 72
Cdd:COG1136 1 MSPlLELRNLTKSYGtgEGEVTALRGVSLSIEAGeFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 73 SI--RRKIGYLPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALV 150
Cdd:COG1136 81 ARlrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 151 NEPRVLIVDEPTAGLDPEERIRFRNLLADFANE--RLVLLSTHivsDVE--ATTNRIGILDHGRLV 212
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTH---DPElaARADRVIRLRDGRIV 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-225 |
3.81e-48 |
|
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: 160.98 E-value: 3.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRqqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD--ARSIRRKIGY 80
Cdd:COG1120 2 LEAENLSVGYGGR--PVLDDVSLSLPPGeVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlsRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQFGFYPTMKVID--AM---TYLAILAEvPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRV 155
Cdd:COG1120 80 VPQEPPAPFGLTVRElvALgryPHLGLFGR-PSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 156 LIVDEPTAGLDPEERIRFRNLLADFANE--RLVLLSTH------IVSDveattnRIGILDHGRLVFNGTTDELIDAAA 225
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHdlnlaaRYAD------RLVLLKDGRIVAQGPPEEVLTPEL 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-212 |
4.84e-48 |
|
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: 159.61 E-value: 4.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGrqQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRKIGYLP 82
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGeFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 QQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPT 162
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491943749 163 AGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLV 212
Cdd:cd03259 159 SALDAKLREELREELKELQRELgiTTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-215 |
1.24e-47 |
|
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: 158.69 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQP--ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDG-TPLKDARSIRRKIG 79
Cdd:cd03266 2 ITADALTKRFRDVKKTvqAVDGVSFTVKPGeVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVD 159
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491943749 160 EPTAGLDpeerIRFRNLLADFANE-----RLVLLSTHIVSDVEATTNRIGILDHGRLVFNG 215
Cdd:cd03266 162 EPTTGLD----VMATRALREFIRQlralgKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-212 |
5.50e-46 |
|
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: 154.59 E-value: 5.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQ--QPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KDARSIR 75
Cdd:cd03257 2 LEVKNLSVSFPTGGgsVKALDDVSFSIKKGeTLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsrRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 76 RKIGYLPQ--QFGFYPTMKVIDAM--TYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTK-VKALSGGMLQRLGIAQALV 150
Cdd:cd03257 82 KEIQMVFQdpMSSLNPRMTIGEQIaePLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRyPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491943749 151 NEPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLV 212
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-223 |
1.15e-45 |
|
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: 154.37 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRqqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KDARSIRRK 77
Cdd:COG1127 6 IEVRNLTKSFGDR--VVLDGVSLDVPRGeILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglseKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 78 IGYLPQQ---FgfyptmkviDAMT-------YLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQ 147
Cdd:COG1127 84 IGMLFQGgalF---------DSLTvfenvafPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491943749 148 ALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFaNERL---VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDA 223
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIREL-RDELgltSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAS 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-197 |
2.34e-45 |
|
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: 153.01 E-value: 2.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQP--ALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARsirRKIGY 80
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFvALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG---PDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDE 160
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 491943749 161 PTAGLDPEERIRFRNLLADFANERL--VLLSTHivsDVE 197
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGktVLLVTH---DID 193
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-210 |
3.35e-45 |
|
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: 151.19 E-value: 3.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSI----RRKI 78
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGeIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpplRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 79 GYLPQQFGFYPTMKVIDAMTYlailaevpareqkrriewllaavhltaqaktkvkALSGGMLQRLGIAQALVNEPRVLIV 158
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 159 DEPTAGLDPEERIRFRNLLADFaNERL---VLLSTHIVSDVEATTNRIGILDHGR 210
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSL-QAQLgitVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-197 |
7.69e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 152.94 E-value: 7.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTT----IQIEQLVKHYRGRQ--QPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARs 73
Cdd:COG1116 1 MSAaapaLELRGVSKRFPTGGggVTALDDVSLTVAAGeFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 74 irRKIGYLPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEP 153
Cdd:COG1116 80 --PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491943749 154 RVLIVDEPTAGLDPEERIRFRNLLAD-FANERL-VLLSTHivsDVE 197
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRlWQETGKtVLFVTH---DVD 200
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-231 |
8.84e-45 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 155.23 E-value: 8.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHYRGrqQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRKIG 79
Cdd:COG3839 1 MASLELENVSKSYGG--VEALKDIDLDIEDGeFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVD 159
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 160 EPTAGLDPEERIRFRNLLADFaNERL---VLLSTHivsD-VEATT--NRIGILDHGRLVFNGTTDELIDAAAgHVFVG 231
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRL-HRRLgttTIYVTH---DqVEAMTlaDRIAVMNDGRIQQVGTPEELYDRPA-NLFVA 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-163 |
3.90e-44 |
|
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: 147.41 E-value: 3.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL--KDARSIRRKIGYLPQQFGFYPTMKVIDAM 97
Cdd:pfam00005 1 LKNVSLTLNPGeILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 98 TYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKV----KALSGGMLQRLGIAQALVNEPRVLIVDEPTA 163
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-229 |
1.08e-43 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 149.37 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KDARSIRRK 77
Cdd:TIGR02315 2 LEVENLSKVYPNGKQ-ALKNINLNINPGeFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklrgKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 78 IGYLPQQFGFYPTMKVID--------AMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQAL 149
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLEnvlhgrlgYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 150 VNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAAGH 227
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLRH 240
|
..
gi 491943749 228 VF 229
Cdd:TIGR02315 241 IY 242
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-199 |
1.16e-43 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 148.01 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRqqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDAR-SIRRKIGYL 81
Cdd:COG4133 3 LEAENLSCRRGER--LLFSGLSFTLAAGeALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAReDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 82 PQQFGFYPTMKVIDAMTYLAILAEVPAREqkRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEP 161
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 491943749 162 TAGLDPEERIRFRNLLADF-ANERLVLLSTHIVSDVEAT 199
Cdd:COG4133 159 FTALDAAGVALLAELIAAHlARGGAVLLTTHQPLELAAA 197
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-215 |
1.38e-43 |
|
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: 148.07 E-value: 1.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 5 QIEQLVKHYRGRqqPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDarsIRRKIGYLPQ 83
Cdd:cd03235 1 EVEDLTVSYGGH--PVLEDVSFEVKPGEFlAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---ERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 84 QFGFYPTM--KVID--AMTYLA--ILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLI 157
Cdd:cd03235 76 RRSIDRDFpiSVRDvvLMGLYGhkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491943749 158 VDEPTAGLDPEERIRFRNLLADF-ANERLVLLSTHIVSDVEATTNRIGILDHgRLVFNG 215
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYFDRVLLLNR-TVVASG 213
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-268 |
4.71e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 149.85 E-value: 4.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQP-------------------ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLV 63
Cdd:COG4586 2 IEVENLSKTYRVYEKEpglkgalkglfrreyreveAVDDISFTIEPGeIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 64 DG-TPLKDARSIRRKIG-----------YLPqqfgfyptmkVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTK 131
Cdd:COG4586 82 LGyVPFKRRKEFARRIGvvfgqrsqlwwDLP----------AIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 132 VKALSGGmlQRL--GIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILD 207
Cdd:COG4586 152 VRQLSLG--QRMrcELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALCDRVIVID 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 208 HGRLVFNGTTDELIDAAAGH-----VFVGDLPVAQLKQFKTQYQISeqtahGQHIRVRLLARTPLA 268
Cdd:COG4586 230 HGRIIYDGSLEELKERFGPYktivlELAEPVPPLELPRGGEVIERE-----GNRVRLEVDPRESLA 290
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-282 |
5.06e-43 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 150.37 E-value: 5.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHYRGRqqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD-ARSIRRKI 78
Cdd:PRK13536 39 TVAIDLAGVSKSYGDK--AVVNGLSFTVASGeCFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPArARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 79 GYLPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIV 158
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 159 DEPTAGLDPEER----IRFRNLLadfANERLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAAG----HVFV 230
Cdd:PRK13536 197 DEPTTGLDPHARhliwERLRSLL---ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGcqviEIYG 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 491943749 231 GDLP--VAQLKQFKTQYQISEQT-----AHGQHIRVRLLARTPLATWQSvAPTLEEAYL 282
Cdd:PRK13536 274 GDPHelSSLVKPYARRIEVSGETlfcyaPDPEQVRVQLRGRAGLRLLQR-PPNLEDVFL 331
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-222 |
5.11e-43 |
|
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: 147.26 E-value: 5.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KDARSIRRK 77
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGeILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglseAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 78 IGYLPQQFGFYPTMKVIDAMTYLaiLAE---VPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPR 154
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFP--LREhtrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491943749 155 VLIVDEPTAGLDPEERIRFRNLLADFaNERL---VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELID 222
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSL-KKELgltSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-221 |
1.32e-42 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 146.29 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIGY 80
Cdd:cd03295 1 IEFENVTKRYGGGK-KAVNNLNLEIAKGeFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQ--AKTKVKALSGGMLQRLGIAQALVNEPRVLIV 158
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 159 DEPTAGLDPEERIRFRNLLADFANE--RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELI 221
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-222 |
1.36e-42 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 146.33 E-value: 1.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD----ARSiR 75
Cdd:COG1137 1 MMTLEAENLVKSYGKRT--VVKDVSLEVNQGeIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmhKRA-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 76 RKIGYLPQQFGFYPTMKVIDAMtyLAIL--AEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEP 153
Cdd:COG1137 78 LGIGYLPQEASIFRKLTVEDNI--LAVLelRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 154 RVLIVDEPTAGLDPEERIRFRNLLADFANERL-VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELID 222
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKERGIgVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-224 |
1.69e-42 |
|
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: 146.49 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYR--GRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL--KDARSIRRKI 78
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGeSFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtrRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 79 GYLPQQ-FG-FYPTMKVIDamtylaILAEvPAR-----EQKRRIEWLLAAVHLTAQAKTKVKA-LSGGMLQRLGIAQALV 150
Cdd:COG1124 82 QMVFQDpYAsLHPRHTVDR------ILAE-PLRihglpDREERIAELLEQVGLPPSFLDRYPHqLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 151 NEPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAA 224
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-223 |
3.34e-42 |
|
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: 154.22 E-value: 3.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIGY 80
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGeRVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqiDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQ-FGFYPTmkVIDAMTylaiLAEVPAREQkrRIEWL--LAAVH-----LTAQAKTKV----KALSGGMLQRLGIAQA 148
Cdd:COG2274 554 VLQDvFLFSGT--IRENIT----LGDPDATDE--EIIEAarLAGLHdfieaLPMGYDTVVgeggSNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 149 LVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTH---IVSDVeattNRIGILDHGRLVFNGTTDELIDA 223
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHrlsTIRLA----DRIIVLDKGRIVEDGTHEELLAR 699
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-219 |
1.05e-41 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 146.87 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYR--GRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDG---TPLKDA--RSIR 75
Cdd:PRK11153 2 IELKNISKVFPqgGRTIHALNNVSLHIPAGeIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdlTALSEKelRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 76 RKIGYLPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRV 155
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491943749 156 LIVDEPTAGLDPEERIRFRNLLADFaNERL---VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDE 219
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDI-NRELgltIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-220 |
1.54e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 146.78 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHYRGrqQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRKIG 79
Cdd:COG3842 3 MPALELENVSKRYGD--VTALDDVSLSIEPGeFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQFGFYPTMKVIDAMTY-LAILAeVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIV 158
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFgLRMRG-VPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491943749 159 DEPTAGLDPEERIRFRNLLADFaNERL---VLLSTH------IVSDveattnRIGILDHGRLVFNGTTDEL 220
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRL-QRELgitFIYVTHdqeealALAD------RIAVMNDGRIEQVGTPEEI 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-251 |
2.21e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 145.33 E-value: 2.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRgrQQPALDHVSLNIQSGM-YGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD-ARSIRRKIGYL 81
Cdd:PRK13537 8 IDFRNVEKRYG--DKLVVDGLSFHVQRGEcFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSrARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 82 PQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEP 161
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 162 TAGLDPEER----IRFRNLLadfANERLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAAGHVFV---GDLP 234
Cdd:PRK13537 166 TTGLDPQARhlmwERLRSLL---ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCDVIeiyGPDP 242
|
250 260
....*....|....*....|
gi 491943749 235 VA---QLKQFKTQYQISEQT 251
Cdd:PRK13537 243 VAlrdELAPLAERTEISGET 262
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-215 |
2.24e-41 |
|
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: 143.24 E-value: 2.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQ-------------------PALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLV 63
Cdd:cd03267 1 IEVSNLSKSYRVYSKepgligslkslfkrkyrevEALKGISFTIEKGeIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 64 DG-TPLKDARSIRRKIGY-LPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQ 141
Cdd:cd03267 81 AGlVPWKRRKKFLRRIGVvFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 142 RLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLVFNG 215
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-210 |
4.98e-41 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 139.69 E-value: 4.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 5 QIEQLVKHYRGRqqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARS--IRRKIGYL 81
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGeIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeeLRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 82 PQqfgfyptmkvidamtylailaevpareqkrriewllaavhltaqaktkvkaLSGGMLQRLGIAQALVNEPRVLIVDEP 161
Cdd:cd00267 79 PQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491943749 162 TAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGR 210
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-211 |
8.44e-41 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 141.01 E-value: 8.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYrGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARS-----IRRK 77
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGeFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraipyLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 78 IGYLPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLI 157
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 158 VDEPTAGLDPEERIRFRNLLADFaNER--LVLLSTHIVSDVEATTNRIGILDHGRL 211
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKI-NKAgtTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-220 |
9.46e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 142.59 E-value: 9.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 17 QQPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KDARSIRRKIGYL--------- 81
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFvAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakkkKKLKDLRKKVGLVfqfpehqlf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 82 -----------PQQFGfyptmkvidamtylailaeVPAREQKRRIEWLLAAVHLTAQAKTKVK-ALSGGMLQRLGIAQAL 149
Cdd:TIGR04521 97 eetvykdiafgPKNLG-------------------LSEEEAEERVKEALELVGLDEEYLERSPfELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491943749 150 VNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-219 |
1.19e-40 |
|
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: 141.04 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDG---TPLKDARSIRRKIG 79
Cdd:cd03219 1 LEVRGLTKRFGGLV--ALDDVSFSVRPGeIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGediTGLPPHEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQFGFYPTMKVIDAM----------TYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQAL 149
Cdd:cd03219 79 RTFQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491943749 150 VNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERL-VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDE 219
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGItVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-221 |
1.35e-40 |
|
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: 140.76 E-value: 1.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK----DARSiRRKI 78
Cdd:cd03218 1 LRAENLSKRYGKRK--VVNGVSLSVKQGeIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITklpmHKRA-RLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 79 GYLPQQFGFYPTMKVIDAMtyLAIL--AEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVL 156
Cdd:cd03218 78 GYLPQEASIFRKLTVEENI--LAVLeiRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 157 IVDEPTAGLDPEERIRFRNLLADFANERL-VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELI 221
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIgVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
8.48e-40 |
|
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: 145.43 E-value: 8.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTT-IQIEQLVKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPT---SGKVLVDGTPLKDARS-- 73
Cdd:COG1123 1 MTPlLEVRDLSVRYPGGDVPAVDGVSLTIAPGeTVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 74 IRRKIGYLPQQFgfyptMKVIDAMTYLAILAE------VPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQ 147
Cdd:COG1123 81 RGRRIGMVFQDP-----MTQLNPVTVGDQIAEalenlgLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 148 ALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAA 225
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
.
gi 491943749 226 G 226
Cdd:COG1123 236 A 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-210 |
8.71e-40 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 136.74 E-value: 8.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDA--RSIRRKIGY 80
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGeKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLdlESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQFgfyptmkVIDAMTylaiLAEVpareqkrrIewllaavhltaqaktkvkaLSGGMLQRLGIAQALVNEPRVLIVDE 160
Cdd:cd03228 81 VPQDP-------FLFSGT----IREN--------I-------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491943749 161 PTAGLDPEERIRFRNLLADFANERLVLLSTHIVSDVEAtTNRIGILDHGR 210
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-220 |
1.15e-39 |
|
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: 139.49 E-value: 1.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARS---IRRKIG 79
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFvAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENlweIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQ----QFgfyptmkvidamtyLAILAE-----------VPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLG 144
Cdd:TIGR04520 81 MVFQnpdnQF--------------VGATVEddvafglenlgVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 145 IAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVeATTNRIGILDHGRLVFNGTTDEL 220
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREI 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-238 |
1.49e-39 |
|
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: 139.32 E-value: 1.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 17 QQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KDARSIRRK-IGYLPQQFGFYP 89
Cdd:cd03294 36 QTVGVNDVSLDVREGeIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsrKELRELRRKkISMVFQSFALLP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 90 TMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEE 169
Cdd:cd03294 116 HRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491943749 170 RIRFRNLLADFANE--RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAAG-HV--FVGDLPVAQL 238
Cdd:cd03294 196 RREMQDELLRLQAElqKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANdYVreFFRGVDRAKV 269
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-211 |
5.47e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.10 E-value: 5.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLvkHYRGRQQPALDHVSLNIQSGM-YGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIGY 80
Cdd:COG4619 1 LELEGL--SFRVGGKPILSPVSLTLEAGEcVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSamPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQFGFYPtMKVIDAMTYLAILAEVPAREQkrRIEWLLAAVHLTAQAKTK-VKALSGGMLQRLGIAQALVNEPRVLIVD 159
Cdd:COG4619 79 VPQEPALWG-GTVRDNLPFPFQLRERKFDRE--RALELLERLGLPPDILDKpVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491943749 160 EPTAGLDPEERIRFRNLLADFANE--RLVLLSTHIVSDVEATTNRIGILDHGRL 211
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEegRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-219 |
1.52e-38 |
|
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: 136.32 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDG---TPLKDARSIRR 76
Cdd:COG0411 2 DPLLEVRGLTKRFGGLV--AVDDVSLEVERGeIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrdiTGLPPHRIARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 77 KIGY---LPQQFgfyPTMKVIDAM----------TYLAILAEVPA-----REQKRRIEWLLAAVHLTAQAKTKVKALSGG 138
Cdd:COG0411 80 GIARtfqNPRLF---PELTVLENVlvaaharlgrGLLAALLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 139 MLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERL--VLLSTHIVSDVEATTNRIGILDHGRLVFNGT 216
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGitILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
...
gi 491943749 217 TDE 219
Cdd:COG0411 237 PAE 239
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-223 |
2.11e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 138.36 E-value: 2.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIR-RKIGY 80
Cdd:COG1118 2 SIEVRNISKRFGSFT--LLDDVSLEIASGeLVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPReRRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQFGFYPTMKVID----AMTYLAilaeVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVL 156
Cdd:COG1118 80 VFQHYALFPHMTVAEniafGLRVRP----PSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 157 IVDEPTAGLD----PEERIRFRNLLADFanERLVLLSTHivsDVE-----AttNRIGILDHGRLVFNGTTDELIDA 223
Cdd:COG1118 156 LLDEPFGALDakvrKELRRWLRRLHDEL--GGTTVFVTH---DQEealelA--DRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-225 |
3.56e-38 |
|
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: 137.11 E-value: 3.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQP--ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKP---TSGKVLVDGTPL-----KDAR 72
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvkAVDGVSFDVRRGeTLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklseKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 73 SIR-RKIGYLPQqfgfyptmkviDAMTYL-------AILAEV-------PAREQKRRIEWLLAAVHLTAQAKTKVK---A 134
Cdd:COG0444 82 KIRgREIQMIFQ-----------DPMTSLnpvmtvgDQIAEPlrihgglSKAEARERAIELLERVGLPDPERRLDRyphE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 135 LSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER-L-VLLSTHIVSDVEATTNRIGILDHGRLV 212
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELgLaILFITHDLGVVAEIADRVAVMYAGRIV 230
|
250
....*....|...
gi 491943749 213 FNGTTDELIDAAA 225
Cdd:COG0444 231 EEGPVEELFENPR 243
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-232 |
1.36e-37 |
|
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: 133.13 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGrqQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRKIGYLP 82
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGeFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 QQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPT 162
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491943749 163 AGLDPEER----IRFRNLladfaNERL---VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAAgHVFVGD 232
Cdd:cd03300 159 GALDLKLRkdmqLELKRL-----QKELgitFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA-NRFVAD 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-220 |
1.70e-37 |
|
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: 132.69 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSGM-YGLLGKNGAGKSTLMKILTTLEK-----PTSGKVLVDGTPLKDAR----S 73
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEiTALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDvdvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 74 IRRKIGYLPQQfgfyPT---MKVIDAMTY-LAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKA--LSGGMLQRLGIAQ 147
Cdd:cd03260 79 LRRRVGMVFQK----PNpfpGSIYDNVAYgLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491943749 148 ALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-221 |
4.66e-37 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 131.69 E-value: 4.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpaLDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRKIGYLP 82
Cdd:cd03299 1 LKVENLSKDWKEFK---LKNVSLEVERGDYfVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 QQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPT 162
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491943749 163 AGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELI 221
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-215 |
1.06e-36 |
|
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: 129.09 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 5 QIEQLVKHYRGRqqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIGYL 81
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGeIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAslSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 82 PQqfgfyptmkvidAMTYLAILaevpareqkrriewllaavHLtaqAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEP 161
Cdd:cd03214 79 PQ------------ALELLGLA-------------------HL---ADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491943749 162 TAGLDPEERIRFRNLLADFANER--LVLLSTH------IVSDveattnRIGILDHGRLVFNG 215
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERgkTVVMVLHdlnlaaRYAD------RVILLKDGRIVAQG 180
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-215 |
1.62e-36 |
|
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: 130.02 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIGY 80
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGeKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQFG-FYPTMKviDAMTYLAILAEVPAREQKRRIEWL--LAAVH---LTAQAKTKVKALSGGMLQRLGIAQALVNEPR 154
Cdd:cd03245 83 VPQDVTlFYGTLR--DNITLGAPLADDERILRAAELAGVtdFVNKHpngLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 155 VLIVDEPTAGLD--PEERI--RFRNLLADfaneRLVLLSTHIVSdVEATTNRIGILDHGRLVFNG 215
Cdd:cd03245 161 ILLLDEPTSAMDmnSEERLkeRLRQLLGD----KTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-223 |
4.43e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 129.34 E-value: 4.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL----KDARSIRRKI 78
Cdd:COG1126 2 IEIENLHKSFGDLE--VLKGISLDVEKGeVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdskKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 79 GYLPQQFGFYPTMKVIDAMTY-LAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLI 157
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 158 VDEPTAGLDPE---ERIrfrNLLADFANERL-VLLSTH------IVSDveattnRIGILDHGRLVFNGTTDELIDA 223
Cdd:COG1126 160 FDEPTSALDPElvgEVL---DVMRDLAKEGMtMVVVTHemgfarEVAD------RVVFMDGGRIVEEGPPEEFFEN 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-222 |
8.26e-36 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 128.67 E-value: 8.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRgrQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDG----TPLKDARSIRRKI 78
Cdd:PRK09493 2 IEFKNVSKHFG--PTQVLHNIDLNIDQGeVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvnDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 79 GYLPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRI-EWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLI 157
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQaRELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 158 VDEPTAGLDPEERIRFRNLLADFANERLVL-LSTHIVSDVEATTNRIGILDHGRLVFNGTTDELID 222
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMvIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-212 |
3.58e-35 |
|
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: 124.46 E-value: 3.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGrqQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK---DARSIRRKIG 79
Cdd:cd03216 1 LELRGITKRFGG--VKALDGVSLSVRRGeVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfasPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQqfgfyptmkvidamtylailaevpareqkrriewllaavhltaqaktkvkaLSGGMLQRLGIAQALVNEPRVLIVD 159
Cdd:cd03216 79 MVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491943749 160 EPTAGLDPEERIRFRNLLADFANERL-VLLSTHIVSDVEATTNRIGILDHGRLV 212
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVaVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-225 |
4.72e-35 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 126.68 E-value: 4.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYRgrQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRKIGYL 81
Cdd:cd03296 2 SIEVRNVSKRFG--DFVALDDVSLDIPSGeLVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 82 PQQFGFYPTMKVIDAMTY-LAI---LAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLI 157
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFgLRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 158 VDEPTAGLDPEERIRFRNLLADFANERLV--LLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAA 225
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVttVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-211 |
2.96e-34 |
|
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: 123.79 E-value: 2.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL----KDARSIRRKI 78
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGeVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddkKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 79 GYLPQQFGFYPTMKVIDAMTYLAILAE-VPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLI 157
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLAPIKVKgMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 158 VDEPTAGLDPEERIRFRNLLADFANERL-VLLSTHIVSDVEATTNRIGILDHGRL 211
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMtMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-219 |
3.36e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 129.76 E-value: 3.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KDArsIRRK 77
Cdd:COG3845 6 LELRGITKRFGGVV--ANDDVSLTVRPGeIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirspRDA--IALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 78 IGYLPQQFGFYPTMKVIDAMtylaILAEVPA-------REQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALV 150
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENI----VLGLEPTkggrldrKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 151 NEPRVLIVDEPTAGLDPEERIRFRNLLADFANERL-VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDE 219
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAAEGKsIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-212 |
4.19e-34 |
|
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: 123.52 E-value: 4.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRqqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRKIGYLP 82
Cdd:cd03301 1 VELENVTKRFGNV--TALDDLNLDIADGeFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 QQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPT 162
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 163 AGLDPEERIRFRNLLADFaNERL---VLLSTHivSDVEATT--NRIGILDHGRLV 212
Cdd:cd03301 159 SNLDAKLRVQMRAELKRL-QQRLgttTIYVTH--DQVEAMTmaDRIAVMNDGQIQ 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-220 |
6.71e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 127.26 E-value: 6.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGrqQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRKIGYLP 82
Cdd:PRK11607 20 LEIRNLTKSFDG--QHAVDDVSLTIYKGeIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 QQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPT 162
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491943749 163 AGLDPEERIRFRNLLADFAnERL---VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK11607 178 GALDKKLRDRMQLEVVDIL-ERVgvtCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-215 |
7.19e-34 |
|
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: 122.79 E-value: 7.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 24 VSLNIQSGMYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDAR------SIRRKIGYLPQQFGFYPTMKVIDAM 97
Cdd:cd03297 17 IDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkinlpPQQRKIGLVFQQYALFPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 98 TYlaILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLL 177
Cdd:cd03297 97 AF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491943749 178 ADFAnERL---VLLSTHIVSDVEATTNRIGILDHGRLVFNG 215
Cdd:cd03297 175 KQIK-KNLnipVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-223 |
1.38e-33 |
|
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: 128.73 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIG 79
Cdd:COG4987 333 SLELEDVSFRYPGAGRPVLDGLSLTLPPGeRVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdlDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQ---FgfyptmkvidAMTY---LAIlaevpAREQ--KRRIEWLLAAVHLTAQAK-------TKV----KALSGGML 140
Cdd:COG4987 413 VVPQRphlF----------DTTLrenLRL-----ARPDatDEELWAALERVGLGDWLAalpdgldTWLgeggRRLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 141 QRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTHIVSDVEATTNRIgILDHGRLVFNGTTDEL 220
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRIL-VLEDGRIVEQGTHEEL 556
|
...
gi 491943749 221 IDA 223
Cdd:COG4987 557 LAQ 559
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
13-221 |
5.69e-33 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 121.34 E-value: 5.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 13 YRGRqqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVL-VDGTPLK--DARSIRRKIGY----LPQQ 84
Cdd:COG1119 13 RGGK--TILDDISWTVKPGeHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGERRGgeDVWELRKRIGLvspaLQLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 85 FgfYPTMKVIDA-MT--YLAI-LAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDE 160
Cdd:COG1119 91 F--PRDETVLDVvLSgfFDSIgLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491943749 161 PTAGLDPEERIRFRNLLADFANERL--VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELI 221
Cdd:COG1119 169 PTAGLDLGARELLLALLDKLAAEGAptLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-223 |
8.22e-33 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 127.55 E-value: 8.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLkDARSI--RRKIGYLPQQFGFYPTMKVIDA 96
Cdd:NF033858 281 AVDHVSFRIRRGeIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DAGDIatRRRVGYMSQAFSLYGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 97 MTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNL 176
Cdd:NF033858 360 LELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491943749 177 LADFANERLV--LLSTHIVSdvEAT-TNRIGILDHGRLVFNGTTDELIDA 223
Cdd:NF033858 440 LIELSREDGVtiFISTHFMN--EAErCDRISLMHAGRVLASDTPAALVAA 487
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-197 |
9.46e-33 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 121.12 E-value: 9.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHY--RGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRrk 77
Cdd:COG4525 1 MSMLTVRHVSVRYpgGGQPQPALQDVSLTIESGeFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 78 iGYLPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLI 157
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491943749 158 VDEPTAGLDPEERIRFRNLLADFANE--RLVLLSTHivsDVE 197
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRtgKGVFLITH---SVE 196
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-221 |
1.11e-32 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 126.41 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYRGRQqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIG 79
Cdd:COG4988 336 SIELEDVSFSYPGGR-PALDGLSLTIPPGeRVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSdlDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQ-FGFYPTmkVIDAMTylaiLAEVPAREQkrRIEWLLAAVHLTAQAK-------TKV----KALSGGMLQRLGIAQ 147
Cdd:COG4988 415 WVPQNpYLFAGT--IRENLR----LGRPDASDE--ELEAALEAAGLDEFVAalpdgldTPLgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491943749 148 ALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTHIVSDVEAtTNRIGILDHGRLVFNGTTDELI 221
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELL 559
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-216 |
2.23e-32 |
|
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: 126.67 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 6 IEQLVKHYRGRQQPALDHVSLNI-QSGMYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK-DARSIRRKIGYLPQ 83
Cdd:TIGR01257 931 VKNLVKIFEPSGRPAVDRLNITFyENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 84 QFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTA 163
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491943749 164 GLDPEERIRFRNLLADFANERLVLLSTHIVSDVEATTNRIGILDHGRLVFNGT 216
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-232 |
1.49e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 117.69 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGT-----PLKdARSi 74
Cdd:PRK10895 1 MATLTAKNLAKAYKGRR--VVEDVSLTVNSGeIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLH-ARA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 75 RRKIGYLPQQFGFYPTMKVID-AMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEP 153
Cdd:PRK10895 77 RRGIGYLPQEASIFRRLSVYDnLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 154 RVLIVDEPTAGLDPEERIRFRNLLADFANERL-VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDE-LIDAAAGHVFVG 231
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRDSGLgVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEiLQDEHVKRVYLG 236
|
.
gi 491943749 232 D 232
Cdd:PRK10895 237 E 237
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-222 |
1.90e-31 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 116.76 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARS---IRRKIG 79
Cdd:cd03224 1 LEVENLNAGYGKSQ--ILFGVSLTVPEGeIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPherARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQFGFYPTMKVIDAMTyLAILAEVPAREqKRRIEWLLAAV-HLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIV 158
Cdd:cd03224 79 YVPEGRRIFPELTVEENLL-LGAYARRRAKR-KARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491943749 159 DEPTAGLDP--EERIrFRnLLADFANERL-VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELID 222
Cdd:cd03224 157 DEPSEGLAPkiVEEI-FE-AIRELRDEGVtILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-220 |
2.29e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.05 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KDARsiRRK 77
Cdd:COG1129 5 LEMRGISKSFGGVK--ALDGVSLELRPGeVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrspRDAQ--AAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 78 IGYLPQQFGFYPTMKVIDAMtYLailaevpAREQKRR--IEW---------LLAAVHLTAQAKTKVKALSGGMLQRLGIA 146
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENI-FL-------GREPRRGglIDWramrrrareLLARLGLDIDPDTPVGDLSVAQQQLVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 147 QALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERL-VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVaIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-223 |
4.57e-31 |
|
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: 116.05 E-value: 4.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIGY 80
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGeVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAlaDPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQFGFYpTMKVIDAmtylaILAEVPAREQKRRIEWL-LAAVH-----LTAQAKTKV----KALSGGMLQRLGIAQALV 150
Cdd:cd03252 81 VLQENVLF-NRSIRDN-----IALADPGMSMERVIEAAkLAGAHdfiseLPEGYDTIVgeqgAGLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491943749 151 NEPRVLIVDEPTAGLDPE-ERIRFRNLLADFANeRLVLLSTHIVSDVEaTTNRIGILDHGRLVFNGTTDELIDA 223
Cdd:cd03252 155 HNPRILIFDEATSALDYEsEHAIMRNMHDICAG-RTVIIIAHRLSTVK-NADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-215 |
4.82e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 121.33 E-value: 4.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 6 IEQLVKHYRGRqqPALDHVSLNIQSGM-YGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDgtplKDARsirrkIGYLPQQ 84
Cdd:COG0488 1 LENLSKSFGGR--PLLDDVSLSINPGDrIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP----KGLR-----IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 85 FGFYPTMKVIDAM-----TYLAILAEVPAREQK---------------------------RRIEWLLAAVHLT-AQAKTK 131
Cdd:COG0488 70 PPLDDDLTVLDTVldgdaELRALEAELEELEAKlaepdedlerlaelqeefealggweaeARAEEILSGLGFPeEDLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 132 VKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANerLVLLSTHivsDVE---ATTNRIGILDH 208
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG--TVLVVSH---DRYfldRVATRILELDR 224
|
....*...
gi 491943749 209 GRL-VFNG 215
Cdd:COG0488 225 GKLtLYPG 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-223 |
6.07e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 115.95 E-value: 6.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTT-IQIEQLVKHYRGRQQP--------------------ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTS 58
Cdd:COG1134 1 MSSmIEVENVSKSYRLYHEPsrslkelllrrrrtrreefwALKDVSFEVERGeSVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 59 GKVLVDG--TPLkdarsirrkIGYlpqQFGFYPTMKVID-AMTYLAIL----AEVPAREqkRRIEW---LLAAVHltaqa 128
Cdd:COG1134 81 GRVEVNGrvSAL---------LEL---GAGFHPELTGREnIYLNGRLLglsrKEIDEKF--DEIVEfaeLGDFID----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 129 kTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILD 207
Cdd:COG1134 142 -QPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRLCDRAIWLE 220
|
250
....*....|....*.
gi 491943749 208 HGRLVFNGTTDELIDA 223
Cdd:COG1134 221 KGRLVMDGDPEEVIAA 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-220 |
7.16e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 116.72 E-value: 7.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK-DARS---IRRKIGYL---PQQFGFYPTM 91
Cdd:PRK13639 17 ALKGINFKAEKGeMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSlleVRKTVGIVfqnPDDQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 92 KVIDAMTYLAIlaEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERI 171
Cdd:PRK13639 97 EEDVAFGPLNL--GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491943749 172 RFRNLLADFANERL-VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK13639 175 QIMKLLYDLNKEGItIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-253 |
1.49e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 115.88 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDAR--SIRRKIGY 80
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWvAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQ----QF-GfyptMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRV 155
Cdd:PRK13635 86 VFQnpdnQFvG----ATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 156 LIVDEPTAGLDPEERIRFRNLLADFANE-RLVLLS-THivsDVE--ATTNRIGILDHGRLVFNGTTDELIDAAAGHVFVG 231
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQkGITVLSiTH---DLDeaAQADRVIVMNKGEILEEGTPEEIFKSGHMLQEIG 238
|
250 260
....*....|....*....|....
gi 491943749 232 -DLPVA-QLKQFKTQYQISEQTAH 253
Cdd:PRK13635 239 lDVPFSvKLKELLKRNGILLPNTY 262
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-225 |
1.76e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 116.75 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQP---------ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL----- 68
Cdd:COG4608 8 LEVRDLKKHFPVRGGLfgrtvgvvkAVDGVSFDIRRGeTLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglsg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 69 KDARSIRRKIgylpqQFGF---Y----PTMKVIDamtylaILAE-------VPAREQKRRIEWLLAAVHLTAQAKTKV-K 133
Cdd:COG4608 88 RELRPLRRRM-----QMVFqdpYaslnPRMTVGD------IIAEplrihglASKAERRERVAELLELVGLRPEHADRYpH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 134 ALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER-LVLL-STHIVSDVEATTNRIGILDHGRL 211
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELgLTYLfISHDLSVVRHISDRVAVMYLGKI 236
|
250
....*....|....
gi 491943749 212 VFNGTTDELIDAAA 225
Cdd:COG4608 237 VEIAPRDELYARPL 250
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
3-219 |
2.68e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 115.53 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYRGR---QQPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDAR----SI 74
Cdd:PRK13637 2 SIKIENLTHIYMEGtpfEKKALDNVNIEIEDGEFvGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklsDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 75 RRKIGYLPQqfgfYPTMKVIDAMTYLAIlAEVPAR------EQKRRIEWLLAAVHLTAQaKTKVKA---LSGGMLQRLGI 145
Cdd:PRK13637 82 RKKVGLVFQ----YPEYQLFEETIEKDI-AFGPINlglseeEIENRVKRAMNIVGLDYE-DYKDKSpfeLSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 146 AQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDE 219
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-215 |
2.76e-30 |
|
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: 113.91 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTL---EKPTSGKVLVDGTPLKDARSiRRKIGYLPQQFGFYPTMKVIDA 96
Cdd:cd03234 23 LNDVSLHVESGqVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKPDQF-QKCVAYVRQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 97 MTYLAILA---EVPAREQKRRIE-WLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIR 172
Cdd:cd03234 102 LTYTAILRlprKSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491943749 173 FRNLLADFANE-RLVLLSTHI-VSDVEATTNRIGILDHGRLVFNG 215
Cdd:cd03234 182 LVSTLSQLARRnRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-218 |
2.88e-30 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 114.34 E-value: 2.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDG--------TPLKDARS 73
Cdd:PRK11124 2 SIQLNGINCFYGAHQ--ALFDITLDCPQGeTLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 74 IRRKIGYLPQQFGFYPTMKVIDAmtylaiLAEVPAR-------EQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIA 146
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPHLTVQQN------LIEAPCRvlglskdQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491943749 147 QALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLV-LLSTHIVSDVEATTNRIGILDHGRLVFNGTTD 218
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITqVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
20-193 |
1.46e-29 |
|
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: 110.98 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL----KDARSIRRKIGYL---PQQFGFYPTm 91
Cdd:TIGR01166 7 VLKGLNFAAERGeVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysrKGLLERRQRVGLVfqdPDDQLFAAD- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 92 kVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERI 171
Cdd:TIGR01166 86 -VDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGRE 164
|
170 180
....*....|....*....|...
gi 491943749 172 RFRNLLADFANE-RLVLLSTHIV 193
Cdd:TIGR01166 165 QMLAILRRLRAEgMTVVISTHDV 187
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-220 |
1.60e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 112.54 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHYRGrqQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSI----- 74
Cdd:PRK11264 1 MSAIEVKNLVKKFHG--QTVLHGIDLEVKPGeVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqqkg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 75 -----RRKIGYLPQQFGFYPTMKVID-AMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQA 148
Cdd:PRK11264 79 lirqlRQHVGFVFQNFNLFPHRTVLEnIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491943749 149 LVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-220 |
2.64e-29 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 117.53 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDAR---SIRRKIG 79
Cdd:NF033858 2 ARLEGVSHRYGKTV--ALDDVSLDIPAGcMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARhrrAVCPRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQFG--FYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLI 157
Cdd:NF033858 80 YMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 158 VDEPTAGLDPEERIRFRNLLADFANERL---VLLST----------HIVSdveattnrigiLDHGRLVFNGTTDEL 220
Cdd:NF033858 160 LDEPTTGVDPLSRRQFWELIDRIRAERPgmsVLVATaymeeaerfdWLVA-----------MDAGRVLATGTPAEL 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-220 |
3.53e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 112.01 E-value: 3.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDA--RSIRRKIGY 80
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYvAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnlKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQ----QFgfyptmkvidamtyLAILAE-----------VPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGI 145
Cdd:PRK13632 88 IFQnpdnQF--------------IGATVEddiafglenkkVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491943749 146 AQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERL-VLLS-THivsDVEATTN--RIGILDHGRLVFNGTTDEL 220
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISiTH---DMDEAILadKVIVFSEGKLIAQGKPKEI 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-168 |
6.27e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 110.87 E-value: 6.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYrGRQQpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL--------KDARS 73
Cdd:COG4161 2 SIQLKNINCFY-GSHQ-ALFDINLECPSGeTLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpseKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 74 IRRKIGYLPQQFGFYPTMKVIDAmtylaiLAEVPAR-------EQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIA 146
Cdd:COG4161 80 LRQKVGMVFQQYNLWPHLTVMEN------LIEAPCKvlglskeQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIA 153
|
170 180
....*....|....*....|..
gi 491943749 147 QALVNEPRVLIVDEPTAGLDPE 168
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDPE 175
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-220 |
8.12e-29 |
|
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: 116.27 E-value: 8.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGtplkdaRSIRRKIGYLP 82
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGeCFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG------KSILTNISDVH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 QQFGFYPTMKVIDAMT------YL-AILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRV 155
Cdd:TIGR01257 2012 QNMGYCPQFDAIDDLLtgrehlYLyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 156 LIVDEPTAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREgRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-212 |
9.68e-29 |
|
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: 109.27 E-value: 9.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 15 GRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKdARSIRRKIGYLPQQFGFYPTMKV 93
Cdd:cd03226 10 KKGTEILDDLSLDLYAGeIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-AKERRKSIGYVMQDVDYQLFTDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 94 IDAMTYLAiLAEVPAREQKrrIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRF 173
Cdd:cd03226 89 VREELLLG-LKELDAGNEQ--AETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491943749 174 RNLLADFANE-RLVLLSTHivsDVE---ATTNRIGILDHGRLV 212
Cdd:cd03226 166 GELIRELAAQgKAVIVITH---DYEflaKVCDRVLLLANGAIV 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-212 |
1.27e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 109.19 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARS-----IRRK 77
Cdd:PRK10908 2 IRFEHVSKAYLGGRQ-ALQGVTFHMRPGeMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNrevpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 78 IGYLPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLI 157
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 158 VDEPTAGLDPEERIRFRNLLADFANERL-VLLSTHIVSDVEATTNRIGILDHGRLV 212
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVtVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-223 |
1.50e-28 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 109.63 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD--ARSIRRKIGY 80
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGeTVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDytLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQ-FGFYPTmkVIDAMTYLAILAEvpaREQkrrIEWLLAAVHL------------TAQAKTKVKaLSGGMLQRLGIAQ 147
Cdd:cd03251 81 VSQDvFLFNDT--VAENIAYGRPGAT---REE---VEEAARAANAhefimelpegydTVIGERGVK-LSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 148 ALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTHIVSDVEaTTNRIGILDHGRLVFNGTTDELIDA 223
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIE-NADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
6.56e-28 |
|
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: 112.59 E-value: 6.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHY----RGRQQpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKV-------LVDGT---PL 68
Cdd:TIGR03269 280 IKVRNVSKRYisvdRGVVK-AVDNVSLEVKEGeIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTkpgPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 69 KDARSiRRKIGYLPQQFGFYPTMKVIDAMTYlAILAEVPAREQKRRIEWLLAAVHLTAQAKTKV-----KALSGGMLQRL 143
Cdd:TIGR03269 359 GRGRA-KRYIGILHQEYDLYPHRTVLDNLTE-AIGLELPDELARMKAVITLKMVGFDEEKAEEIldkypDELSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 144 GIAQALVNEPRVLIVDEPTAGLDPEERIRFRN--LLADFANERLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELI 221
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsiLKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-215 |
6.88e-28 |
|
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: 106.48 E-value: 6.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQ-PALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILT--TLEKPTSGKVLVDGTPLkDARSIRRKIG 79
Cdd:cd03213 7 RNLTVTVKSSPSKSGkQLLKNVSGKAKPGeLTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL-DKRSFRKIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQFGFYPTMKVIDAMTYLAilaevpareqkrriewllaavhltaqaktKVKALSGGMLQRLGIAQALVNEPRVLIVD 159
Cdd:cd03213 86 YVPQDDILHPTLTVRETLMFAA-----------------------------KLRGLSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 160 EPTAGLDPEERIRFRNLLADFANE-RLVLLSTHIVS-DVEATTNRIGILDHGRLVFNG 215
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRLADTgRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-191 |
9.35e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 106.16 E-value: 9.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 13 YRGRqqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVlvdgtplkdARSIRRKIGYLPQQFGFYPTM 91
Cdd:NF040873 2 YGGR--PVLHGVDLTIPAGsLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------RRAGGARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 92 --KVIDAMTyLAILAEV-----PAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAG 164
Cdd:NF040873 71 plTVRDLVA-MGRWARRglwrrLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180
....*....|....*....|....*...
gi 491943749 165 LDPEERIRFRNLLADFANE-RLVLLSTH 191
Cdd:NF040873 150 LDAESRERIIALLAEEHARgATVVVVTH 177
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-222 |
1.09e-27 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 112.45 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKP---TSGKVLVDGTPLkDARSIRRKIGYLPQQFGFYPTMKVIDA 96
Cdd:TIGR00955 41 LKNVSGVAKPGeLLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI-DAKEMRAISAYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 97 MTYLAIL---AEVPAREQKRRIEWLLAAVHLTAQAKTK------VKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDP 167
Cdd:TIGR00955 120 LMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491943749 168 EERIRFRNLLADFANE-RLVLLSTH-IVSDVEATTNRIGILDHGRLVFNGTTDELID 222
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQKgKTIICTIHqPSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-212 |
1.13e-27 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 107.97 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 2 TTIQIEQLVKHYRG-------RQQPALDHVSLNIQSGM-YGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL----- 68
Cdd:TIGR02769 1 SLLEVRDVTHTYRTgglfgakQRAPVLTNVSLSIEEGEtVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 69 KDARSIRRKIgylpqQFGFYPTMKVIDA-MTYLAILAEvPAR--------EQKRRIEWLLAAVHLTAQAKTKVKA-LSGG 138
Cdd:TIGR02769 81 KQRRAFRRDV-----QLVFQDSPSAVNPrMTVRQIIGE-PLRhltsldesEQKARIAELLDMVGLRSEDADKLPRqLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 139 MLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANE--RLVLLSTHIVSDVEATTNRIGILDHGRLV 212
Cdd:TIGR02769 155 QLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfgTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-166 |
1.48e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 109.65 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHYRGrqQPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRKIG 79
Cdd:PRK09452 12 SPLVELRGISKSFDG--KEVISNLDLTINNGEFlTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVD 159
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
....*..
gi 491943749 160 EPTAGLD 166
Cdd:PRK09452 170 ESLSALD 176
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-220 |
1.63e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 108.01 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 2 TTIQIEQLVKHYRGRQQpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDAR----SIRR 76
Cdd:PRK13636 4 YILKVEELNYNYSDGTH-ALKGININIKKGeVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkglmKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 77 KIGYLPQQfgfyPTMKVIDA-----MTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVN 151
Cdd:PRK13636 83 SVGMVFQD----PDNQLFSAsvyqdVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491943749 152 EPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-215 |
1.83e-27 |
|
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: 105.09 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDAR-SIRRKIGYL 81
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKiALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEkALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 82 PQQFGFYPTmkvidamtylAILAEVPAReqkrriewllaavhltaqaktkvkaLSGGMLQRLGIAQALVNEPRVLIVDEP 161
Cdd:cd03247 81 NQRPYLFDT----------TLRNNLGRR-------------------------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491943749 162 TAGLDPEERIRFRNLLADFANERLVLLSTHIVSDVEAtTNRIGILDHGRLVFNG 215
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-220 |
1.89e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.87 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 15 GRQQPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARS---IRRKIGYLPQQfgfyPt 90
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFlVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwdIRNKAGMVFQN----P- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 91 mkviDAMTYLAILAE----------VPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDE 160
Cdd:PRK13633 95 ----DNQIVATIVEEdvafgpenlgIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491943749 161 PTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVeATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEI 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-221 |
4.59e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 106.31 E-value: 4.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHYR-------GRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL---- 68
Cdd:PRK10419 1 MTLLNVSGLSHHYAhgglsgkHQHQTVLNNVSLSLKSGeTVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLakln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 69 -KDARSIRRKIgylpqQFGFYPTMKVIDA-MTYLAILAEvPAR--------EQKRRIEWLLAAVHLTAQAKTKVKA-LSG 137
Cdd:PRK10419 81 rAQRKAFRRDI-----QMVFQDSISAVNPrKTVREIIRE-PLRhllsldkaERLARASEMLRAVDLDDSVLDKRPPqLSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 138 GMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLVFNG 215
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFgtACLFITHDLRLVERFCQRVMVMDNGQIVETQ 234
|
....*.
gi 491943749 216 TTDELI 221
Cdd:PRK10419 235 PVGDKL 240
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-216 |
5.78e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 106.37 E-value: 5.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 19 PALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL------KDARSIRRKIGYLPQqfgfYPTM 91
Cdd:PRK13649 21 RALFDVNLTIEDGSYtAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsknKDIKQIRKKVGLVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 92 KVIDAmTYLAILA------EVPAREQKRRIEWLLAAVHLTAQAKTKVK-ALSGGMLQRLGIAQALVNEPRVLIVDEPTAG 164
Cdd:PRK13649 97 QLFEE-TVLKDVAfgpqnfGVSQEEAEALAREKLALVGISESLFEKNPfELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 165 LDPEERirfRNLLADFANERL----VLLSTHIVSDVEATTNRIGILDHGRLVFNGT 216
Cdd:PRK13649 176 LDPKGR---KELMTLFKKLHQsgmtIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-225 |
5.83e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 108.58 E-value: 5.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 25 SLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGT---PLKDA--RSIRRK-IGYLPQQFGFYPTMKVIDAM 97
Cdd:PRK10070 48 SLAIEEGeIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiaKISDAelREVRRKkIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 98 TYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLL 177
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491943749 178 ADF--ANERLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAA 225
Cdd:PRK10070 208 VKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-215 |
6.07e-27 |
|
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: 104.92 E-value: 6.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 14 RGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDG--TPLKDarsirrkIGYlpqqfGFYPT 90
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGeRIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLLG-------LGG-----GFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 91 MKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEER 170
Cdd:cd03220 99 LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491943749 171 I----RFRNLLadfANERLVLLSTHIVSDVEATTNRIGILDHGRLVFNG 215
Cdd:cd03220 179 EkcqrRLRELL---KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-223 |
8.26e-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: 8.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 12 HYRGrQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDAR--SIRRKIGYLPQQFGFY 88
Cdd:COG1132 348 SYPG-DRPVLKDISLTIPPGeTVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTleSLRRQIGVVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 89 pTMKVIDAMTYlailaevpAREQKRRIEwLLAAVHLtAQAKTKVKA---------------LSGGMLQRLGIAQALVNEP 153
Cdd:COG1132 427 -SGTIRENIRY--------GRPDATDEE-VEEAAKA-AQAHEFIEAlpdgydtvvgergvnLSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491943749 154 RVLIVDEPTAGLDP--EERIR--FRNLLADfaneRLVLLSTHIVSDVEAtTNRIGILDHGRLVFNGTTDELIDA 223
Cdd:COG1132 496 PILILDEATSALDTetEALIQeaLERLMKG----RTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELLAR 564
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-220 |
8.83e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.48 E-value: 8.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYrGRQQpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRKIGYL 81
Cdd:PRK10851 2 SIEIANIKKSF-GRTQ-VLNDISLDIPSGqMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 82 PQQFGFYPTMKVIDAMTY-LAILaevPAREQ------KRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPR 154
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFgLTVL---PRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491943749 155 VLIVDEPTAGLDPEERIRFRNLLADFANErLVLLSTHIVSDVEATT---NRIGILDHGRLVFNGTTDEL 220
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEE-LKFTSVFVTHDQEEAMevaDRVVVMSQGNIEQAGTPDQV 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-212 |
9.35e-27 |
|
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: 104.44 E-value: 9.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQP--ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL----KDARSI-- 74
Cdd:COG4181 9 IELRGLTKTVGTGAGEltILKGISLEVEAGeSVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldEDARARlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 75 RRKIGYLPQQFGFYPTMKVID-AMTYLAILAEVPAREQKRRiewLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEP 153
Cdd:COG4181 89 ARHVGFVFQSFQLLPTLTALEnVMLPLELAGRRDARARARA---LLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491943749 154 RVLIVDEPTAGLDPEERIRFRNLLADFANER---LVLLsTHivsDVE--ATTNRIGILDHGRLV 212
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERgttLVLV-TH---DPAlaARCDRVLRLRAGRLV 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-211 |
1.22e-26 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 105.14 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 2 TTIQIEQLVKHYRGRQqpALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRkigY 80
Cdd:PRK11247 11 TPLLLNAVSKRYGERT--VLNQLDLHIPAGQFvAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQFGFYPTMKVIDAMTyLAILAEvpAREQKRRIewlLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDE 160
Cdd:PRK11247 86 MFQDARLLPWKKVIDNVG-LGLKGQ--WRDAALQA---LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 161 PTAGLDPEERIRFRNLLadfanERL-------VLLSTHIVSDVEATTNRIGILDHGRL 211
Cdd:PRK11247 160 PLGALDALTRIEMQDLI-----ESLwqqhgftVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-225 |
1.69e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.07 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQpaldHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRKIGYLP 82
Cdd:COG3840 2 LRLDDLTYRYGDFPL----RFDLTIAAGeRVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 QQ--------------FGFYPTMKvidamtylailaevPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQA 148
Cdd:COG3840 78 QEnnlfphltvaqnigLGLRPGLK--------------LTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491943749 149 LVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAA 225
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEP 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-234 |
2.44e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.08 E-value: 2.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 2 TTIQIEQLvkHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD--ARSIRRKI 78
Cdd:PRK13548 1 AMLEARNL--SVRLGGRTLLDDVSLTLRPGeVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwsPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 79 GYLPQQ----FGFypTMKVIDAMTyLAILAEVPAREQkRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALV---- 150
Cdd:PRK13548 79 AVLPQHsslsFPF--TVEEVVAMG-RAPHGLSRAEDD-ALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 151 --NEPRVLIVDEPTAGLDPEERIRFRNLLADFANER----LVLLstHivsDVEATT---NRIGILDHGRLVFNGT----- 216
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglavIVVL--H---DLNLAAryaDRIVLLHQGRLVADGTpaevl 229
|
250
....*....|....*....
gi 491943749 217 TDELIDAAAGH-VFVGDLP 234
Cdd:PRK13548 230 TPETLRRVYGAdVLVQPHP 248
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-211 |
2.96e-26 |
|
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: 101.52 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARS--IRRKIGY 80
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGeSLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPneLGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQqfgfyptmkviDAMTYLAILAEvpareqkrriewllaavhltaqaktkvKALSGGMLQRLGIAQALVNEPRVLIVDE 160
Cdd:cd03246 81 LPQ-----------DDELFSGSIAE---------------------------NILSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491943749 161 PTAGLDPE-ERIRFRNLLADFANERLVLLSTHIVSdVEATTNRIGILDHGRL 211
Cdd:cd03246 123 PNSHLDVEgERALNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-237 |
3.15e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 103.66 E-value: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLvkHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD----ARSIRRki 78
Cdd:COG4559 2 LEAENL--SVRLGGRTLLDDVSLTLRPGeLTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwspwELARRR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 79 GYLPQQ----FGFyPTMKVIdAMTYLAILAevPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALV---- 150
Cdd:COG4559 78 AVLPQHsslaFPF-TVEEVV-ALGRAPHGS--SAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwe 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 151 ---NEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSthIVSDVEATT---NRIGILDHGRLVFNGTTDELIDAA 224
Cdd:COG4559 154 pvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVA--VLHDLNLAAqyaDRILLLHQGRLVAQGTPEEVLTDE 231
|
250
....*....|....
gi 491943749 225 A-GHVFVGDLPVAQ 237
Cdd:COG4559 232 LlERVYGADLRVLA 245
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-191 |
3.45e-26 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 107.76 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYRGRQqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIG 79
Cdd:TIGR02857 321 SLEFSGVSVAYPGRR-PALRPVSFTVPPGeRVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdaDADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQFGFYPtmKVIDAMTYLAiLAEVPAREQKRRIEwlLAAVHLTAQA-----KTKV----KALSGGMLQRLGIAQALV 150
Cdd:TIGR02857 400 WVPQHPFLFA--GTIAENIRLA-RPDASDAEIREALE--RAGLDEFVAAlpqglDTPIgeggAGLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491943749 151 NEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTH 191
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-222 |
3.58e-26 |
|
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: 103.14 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHYrGRQQpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARS---IRR 76
Cdd:COG0410 1 MPMLEVENLHAGY-GGIH-VLHGVSLEVEEGeIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhriARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 77 KIGYLPQQFGFYPTMKVIDAMTyLAILAEVPAREQKRRIEWLLA-----AVHLTAQAKTkvkaLSGGMLQRLGIAQALVN 151
Cdd:COG0410 79 GIGYVPEGRRIFPSLTVEENLL-LGAYARRDRAEVRADLERVYElfprlKERRRQRAGT----LSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491943749 152 EPRVLIVDEPTAGLDPE--ERIrFRnLLADFANERL-VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELID 222
Cdd:COG0410 154 RPKLLLLDEPSLGLAPLivEEI-FE-IIRRLNREGVtILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-212 |
4.90e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.14 E-value: 4.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 17 QQPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDG------TPLKDARSIRRKIG---------- 79
Cdd:PRK13641 19 EKKGLDNISFELEEGSFvALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpeTGNKNLKKLRKKVSlvfqfpeaql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 ----------YLPQQFGFyptmkvidamtylailAEVPAREQKrrIEWLlAAVHLTAQAKTKVK-ALSGGMLQRLGIAQA 148
Cdd:PRK13641 99 fentvlkdveFGPKNFGF----------------SEDEAKEKA--LKWL-KKVGLSEDLISKSPfELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 149 LVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRLV 212
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-220 |
5.80e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 103.95 E-value: 5.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGR---QQPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKV------LVDGTPLKDARS 73
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfERRALYDVNVSIPSGSYvAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervITAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 74 IRRKIGYL--------------------PQQFGfyptmkvidamtylailaeVPAREQKRRIEWLLAAVHLTAQAKTKVK 133
Cdd:PRK13634 83 LRKKVGIVfqfpehqlfeetvekdicfgPMNFG-------------------VSEEDAKQKAREMIELVGLPEELLARSP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 134 -ALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGR 210
Cdd:PRK13634 144 fELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARYADQIVVMHKGT 223
|
250
....*....|
gi 491943749 211 LVFNGTTDEL 220
Cdd:PRK13634 224 VFLQGTPREI 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-223 |
8.62e-26 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 106.72 E-value: 8.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD--ARSIRRKIGY 80
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGeTVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADytLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQ-FGFYPTmkVIDAMTYLAiLAEVPareqKRRIEWLLAAVHLT-----------AQAKTKVKALSGGMLQRLGIAQA 148
Cdd:TIGR02203 411 VSQDvVLFNDT--IANNIAYGR-TEQAD----RAEIERALAAAYAQdfvdklplgldTPIGENGVLLSGGQRQRLAIARA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 149 LVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTHIVSDVEaTTNRIGILDHGRLVFNGTTDELIDA 223
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIE-KADRIVVMDDGRIVERGTHNELLAR 557
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-219 |
2.05e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.53 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRqqPALDHVSLNIQSGM-YGLLGKNGAGKSTLMKILTTLEKPTSGKVLVdGTPLkdarsirrKIGYLP 82
Cdd:COG0488 316 LELEGLSKSYGDK--TLLDDLSLRIDRGDrIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV--------KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 Q-QFGFYPTMKVIDAMTYLAilaevparEQKRRIEW--LLAAVHLT-AQAKTKVKALSGGMLQRLGIAQALVNEPRVLIV 158
Cdd:COG0488 385 QhQEELDPDKTVLDELRDGA--------PGGTEQEVrgYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLL 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 159 DEPTAGLDPEERIRFRNLLADFANErlVLLSTHivsD---VEATTNRIGILDHGRLV-FNGTTDE 219
Cdd:COG0488 457 DEPTNHLDIETLEALEEALDDFPGT--VLLVSH---DryfLDRVATRILEFEDGGVReYPGGYDD 516
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
21-232 |
3.02e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 103.26 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDaRSIR-RKIGYLPQQFGFYPTMKVIDAMT 98
Cdd:PRK11432 22 IDNLNLTIKQGtMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH-RSIQqRDICMVFQSYALFPHMSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 99 YLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLA 178
Cdd:PRK11432 101 YGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIR 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 179 DFaNERLVLLS---THIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAAGHV---FVGD 232
Cdd:PRK11432 181 EL-QQQFNITSlyvTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFmasFMGD 239
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-222 |
3.26e-25 |
|
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: 100.38 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGrQQPALDHVSLNIQSGM-YGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDA--RSIRRKIGY 80
Cdd:cd03254 3 IEFENVNFSYDE-KKPVLKDINFSIKPGEtVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIsrKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQFGFYPTmKVIDAMTYlailaevpAREQKRRIEWLLAA--VHLT-----------AQAKTKVKALSGGMLQRLGIAQ 147
Cdd:cd03254 82 VLQDTFLFSG-TIMENIRL--------GRPNATDEEVIEAAkeAGAHdfimklpngydTVLGENGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 148 ALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTHIVSDVEaTTNRIGILDHGRLVFNGTTDELID 222
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIK-NADKILVLDDGKIIEEGTHDELLA 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
23-211 |
5.25e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 102.80 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 23 HVSLNIQSGMYGL-LGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRKIGYLPQQFGFYPTMKVIDAMTYLA 101
Cdd:PRK11000 21 DINLDIHEGEFVVfVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSYALYPHLSVAENMSFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 102 ILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFA 181
Cdd:PRK11000 101 KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLH 180
|
170 180 190
....*....|....*....|....*....|....
gi 491943749 182 N--ERLVLLSTHivSDVEATT--NRIGILDHGRL 211
Cdd:PRK11000 181 KrlGRTMIYVTH--DQVEAMTlaDKIVVLDAGRV 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-209 |
7.88e-25 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 99.46 E-value: 7.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRKIGylpQQFGFYPTMKVID--AM 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFiSLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVF---QNYSLLPWLTVREniAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 98 TYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLL 177
Cdd:TIGR01184 78 AVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190
....*....|....*....|....*....|....
gi 491943749 178 ADFANER--LVLLSTHIVSDVEATTNRIGILDHG 209
Cdd:TIGR01184 158 MQIWEEHrvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-166 |
8.00e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 99.50 E-value: 8.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYR-GR-QQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARS-----IR 75
Cdd:PRK11629 6 LQCDNLCKRYQeGSvQTDVLHNVSFSIGEGeMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaeLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 76 -RKIGYLPQQFGFYPTMKVID--AMTYLaILAEVPAREQKRRIEwLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNE 152
Cdd:PRK11629 86 nQKLGFIYQFHHLLPDFTALEnvAMPLL-IGKKKPAEINSRALE-MLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170
....*....|....
gi 491943749 153 PRVLIVDEPTAGLD 166
Cdd:PRK11629 164 PRLVLADEPTGNLD 177
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-227 |
1.25e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.17 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 10 VKHYRGRqqPALDHVSLNIQSG----MYGLLGkngAGKSTLMKILTTLEKPTSGKVLVDGTPLK-----DArsIRRKIGY 80
Cdd:COG1129 259 VEGLSVG--GVVRDVSFSVRAGeilgIAGLVG---AGRTELARALFGADPADSGEIRLDGKPVRirsprDA--IRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LP---QQFGFYPTMKVIDAMTyLAILAE------VPAREQKRRIEWLLAAVHL-TAQAKTKVKALSGGMLQRLGIAQALV 150
Cdd:COG1129 332 VPedrKGEGLVLDLSIRENIT-LASLDRlsrgglLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 151 NEPRVLIVDEPTAGLDPEERIRFRNLLADFANERL-VLLsthIVSDVE---ATTNRIGILDHGRLV--FNG---TTDELI 221
Cdd:COG1129 411 TDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKaVIV---ISSELPellGLSDRILVMREGRIVgeLDReeaTEEAIM 487
|
....*.
gi 491943749 222 DAAAGH 227
Cdd:COG1129 488 AAATGG 493
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-215 |
3.04e-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: 97.56 E-value: 3.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 23 HVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRKIGYLPQQFGFYPTMKVIDAMTyla 101
Cdd:cd03298 16 HFDLTFAQGeITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVG--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 102 iLAEVPA----REQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLL 177
Cdd:cd03298 93 -LGLSPGlkltAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491943749 178 ADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLVFNG 215
Cdd:cd03298 172 LDLHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
20-223 |
7.10e-24 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 97.05 E-value: 7.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSG-MYGLLGKNGAGKS-TLMKILTTLEK---PTSGKVLVDGTPLKDARSIRRKIGYLPQ--QFGFYPTMK 92
Cdd:TIGR02770 1 LVQDLNLSLKRGeVLALVGESGSGKSlTCLAILGLLPPgltQTSGEILLDGRPLLPLSIRGRHIATIMQnpRTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 93 VIDAMTYLAILAEVPAREQKRRIEWLLAAVHLtAQAKTKVKA----LSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPE 168
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALILEALEAVGL-PDPEEVLKKypfqLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491943749 169 ERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDA 223
Cdd:TIGR02770 160 NQARVLKLLRELRQLFgtGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYN 216
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-226 |
1.16e-23 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 100.59 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIGY 80
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGeVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQFGFYP-TM-------------KVIDAmtylailaevpAReqkrriewlLAAVH-----LTAQAKTKV----KALSG 137
Cdd:COG4618 411 LPQDVELFDgTIaeniarfgdadpeKVVAA-----------AK---------LAGVHemilrLPDGYDTRIgeggARLSG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 138 GMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADF-ANERLVLLSTHIVSdVEATTNRIGILDHGRLVFNGT 216
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGP 549
|
250
....*....|
gi 491943749 217 TDELIDAAAG 226
Cdd:COG4618 550 RDEVLARLAR 559
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-245 |
1.31e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.13 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL--KDARSIRRKIGY 80
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWtSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItdDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQ----QFgfyptmkVIDAMTY-LAILAE---VPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNE 152
Cdd:PRK13648 88 VFQnpdnQF-------VGSIVKYdVAFGLEnhaVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 153 PRVLIVDEPTAGLDPEERIRFRNLLADFANERLV-LLS-THIVSDVeATTNRIGILDHGRLVFNGTTDELIDAAAGHVFV 230
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNItIISiTHDLSEA-MEADHVIVMNKGTVYKEGTPTEIFDHAEELTRI 239
|
250 260
....*....|....*....|
gi 491943749 231 G-DLP----VAQLKQFKTQY 245
Cdd:PRK13648 240 GlDLPfpikINQMLGHQTSF 259
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-220 |
1.54e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.18 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHYRGRQQpALDHVSLNI-QSGMYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL--KDARSIRRK 77
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKE-ALNNINFIApRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItkENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 78 IGYL---PQQFGFYPTmkVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPR 154
Cdd:PRK13652 80 VGLVfqnPDDQIFSPT--VEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 155 VLIVDEPTAGLDPEERIRFRNLLADFANE--RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-229 |
2.03e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 96.62 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 2 TTIQIEQLVKHYRgrQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTL----EKPTS------GKVLVDGTPLKD 70
Cdd:PRK09984 3 TIIRVEKLAKTFN--QHQALHAVDLNIHHGeMVALLGPSGSGKSTLLRHLSGLitgdKSAGShiellgRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 71 ARSIRRKIGYLPQQFGFYPTMKVIDAMtYLAILAEVP---------AREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQ 141
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENV-LIGALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 142 RLGIAQALVNEPRVLIVDEPTAGLDPEE-RIRFRNLLADFANERL-VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDE 219
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESaRIVMDTLRDINQNDGItVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
250
....*....|
gi 491943749 220 LIDAAAGHVF 229
Cdd:PRK09984 240 FDNERFDHLY 249
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-167 |
2.08e-23 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 98.64 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSG-----MyGLlgkNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KDARSIRR-KIGYLPQQFGFY 88
Cdd:COG4175 42 GVNDASFDVEEGeifviM-GL---SGSGKSTLVRCLNRLIEPTAGEVLIDGEDItklskKELRELRRkKMSMVFQHFALL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 89 PTMKVIDAMTY-LAIlAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDP 167
Cdd:COG4175 118 PHRTVLENVAFgLEI-QGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDP 196
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-221 |
2.91e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.51 E-value: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD--ARSIRRKIGY 80
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKvALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADysEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQFG-FYPTMKvidamTYLAILAEVPAREQKRRIewlLAAVHLTAQAKTKV----------KALSGGMLQRLGIAQAL 149
Cdd:PRK11160 419 VSQRVHlFSATLR-----DNLLLAAPNASDEALIEV---LQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491943749 150 VNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTHIVSDVEAtTNRIGILDHGRLVFNGTTDELI 221
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQ-FDRICVMDNGQIIEQGTHQELL 561
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-222 |
3.03e-23 |
|
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: 95.37 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 18 QPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDAR--SIRRKIGYLPQQfgfypTMKVI 94
Cdd:cd03253 14 RPVLKDVSFTIPAGkKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTldSLRRAIGVVPQD-----TVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 95 DAMTYLAILAEVPAREQKRRIEWLLAAVH-----LTAQAKTKVKA----LSGGMLQRLGIAQALVNEPRVLIVDEPTAGL 165
Cdd:cd03253 89 DTIGYNIRYGRPDATDEEVIEAAKAAQIHdkimrFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 166 DPE-ERIRFRNlLADFANERLVLLSTHIVSDVeATTNRIGILDHGRLVFNGTTDELID 222
Cdd:cd03253 169 DTHtEREIQAA-LRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLA 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-220 |
3.13e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 95.75 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNI-QSGMYGLLGKNGAGKSTLMKILTTL-----EKPTSGKVLVDGTPL--KDARSIRRKIGYLPQQFGFYPTMK 92
Cdd:PRK14247 19 LDGVNLEIpDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIfkMDVIELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 93 VIDAMTYLAILAEV--PAREQKRRIEWLLAAVHLTAQAKTKVKA----LSGGMLQRLGIAQALVNEPRVLIVDEPTAGLD 166
Cdd:PRK14247 99 IFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKDRLDApagkLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491943749 167 PEERIRFRNLLADFANERLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK14247 179 PENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-197 |
3.15e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.92 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRqqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRrkiGYLP 82
Cdd:PRK11248 2 LQISHLYADYGGK--PALEDINLTLESGeLLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 QQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPT 162
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 491943749 163 AGLDPEERIRFRNLLADFANE--RLVLLSTHivsDVE 197
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQEtgKQVLLITH---DIE 190
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
16-198 |
3.99e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.47 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 16 RQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMK-ILTTLEKP--TSGKVLVDGTPLKDARSIRRKIGYLPQQFGFYPTM 91
Cdd:COG4136 12 GGRPLLAPLSLTVAPGeILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 92 KVIDAMTYlAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERI 171
Cdd:COG4136 92 SVGENLAF-ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180
....*....|....*....|....*....
gi 491943749 172 RFRNLLADFANER--LVLLSTHIVSDVEA 198
Cdd:COG4136 171 QFREFVFEQIRQRgiPALLVTHDEEDAPA 199
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-247 |
5.34e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.00 E-value: 5.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 17 QQPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDG------TPLKDARSIRRKIGYLPQqfgfYP 89
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYyAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithkTKDKYIRPVRKRIGMVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 90 TMKVIDAMTYLAILA-----EVPAREQKRRIEWLLAAVHLTAQAKTKVK-ALSGGMLQRLGIAQALVNEPRVLIVDEPTA 163
Cdd:PRK13646 95 ESQLFEDTVEREIIFgpknfKMNLDEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 164 GLDPEERIRFRNLLADFANE--RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDA----AAGHVfvgDLP-VA 236
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDkkklADWHI---GLPeIV 251
|
250
....*....|..
gi 491943749 237 QL-KQFKTQYQI 247
Cdd:PRK13646 252 QLqYDFEQKYQT 263
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-220 |
6.49e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.06 E-value: 6.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARS--IRRK-IGYLPQQFGFYPTMKVID 95
Cdd:PRK11300 20 AVNNVNLEVREQeIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhqIARMgVVRTFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 96 AM----------TYLAILAEVPA-----REQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDE 160
Cdd:PRK11300 100 NLlvaqhqqlktGLFSGLLKTPAfrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491943749 161 PTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-221 |
8.25e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.70 E-value: 8.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 2 TTIQIEQLVKHYRgrQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD--ARSIRRKI 78
Cdd:PRK11231 1 MTLRTENLTVGYG--TKRILNDLSLSLPTGkITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlsSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 79 GYLPQQFGFYPTMKVIDAMTY-----LAILAEVpAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEP 153
Cdd:PRK11231 79 ALLPQHHLTPEGITVRELVAYgrspwLSLWGRL-SAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491943749 154 RVLIVDEPTAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELI 221
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
18-235 |
9.82e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.83 E-value: 9.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 18 QPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIGYLPQQ----FGFypT 90
Cdd:PRK09536 16 TTVLDGVDLSVREGsLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEalSARAASRRVASVPQDtslsFEF--D 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 91 MKVIDAMTYLAILAEV-PAREQKRR-IEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPE 168
Cdd:PRK09536 94 VRQVVEMGRTPHRSRFdTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491943749 169 ERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRLVFNG------TTDELIDAAAGHVFVGDLPV 235
Cdd:PRK09536 174 HQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLADGRVRAAGppadvlTADTLRAAFDARTAVGTDPA 247
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-210 |
1.22e-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: 91.36 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRqqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPlkdarsirrKIGYLP 82
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGdRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV---------KIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 QqfgfyptmkvidamtylailaevpareqkrriewllaavhltaqaktkvkaLSGGMLQRLGIAQALVNEPRVLIVDEPT 162
Cdd:cd03221 70 Q---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491943749 163 AGLDPEERIRFRNLLADFanERLVLLSTHivsD---VEATTNRIGILDHGR 210
Cdd:cd03221 99 NHLDLESIEALEEALKEY--PGTVILVSH---DryfLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-221 |
1.29e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.67 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 19 PALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD---ARSIRRKIGYLPQQfgfyPTMKVI 94
Cdd:PRK13644 16 PALENINLVIKKGEYiGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfskLQGIRKLVGIVFQN----PETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 95 DAMTY--LAILAE---VPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEE 169
Cdd:PRK13644 92 GRTVEedLAFGPEnlcLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491943749 170 RIR-FRNLLADFANERLVLLSTHIVSDVEAtTNRIGILDHGRLVFNGTTDELI 221
Cdd:PRK13644 172 GIAvLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-211 |
1.49e-22 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 92.11 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD---ARSIRRKIGYLP---QQFGFYPTMK 92
Cdd:cd03215 15 AVRDVSFEVRAGeIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRrspRDAIRAGIAYVPedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 93 VIDAMTyLAILaevpareqkrriewllaavhltaqaktkvkaLSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIR 172
Cdd:cd03215 95 VAENIA-LSSL-------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491943749 173 FRNLLADFANERL-VLLsthIVSDVE---ATTNRIGILDHGRL 211
Cdd:cd03215 143 IYRLIRELADAGKaVLL---ISSELDellGLCDRILVMYEGRI 182
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
34-223 |
2.52e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 93.70 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 34 GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIGYLPQQFGFYPTMKVIDamtyLAILAEVP---- 107
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVAYLPQQLPAAEGMTVRE----LVAIGRYPwhga 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 108 ----AREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANE 183
Cdd:PRK10575 117 lgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQE 196
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491943749 184 R--LVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDA 223
Cdd:PRK10575 197 RglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRG 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-221 |
2.65e-22 |
|
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: 92.99 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 17 QQPALDHVSLNIQSGM-YGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD--ARSIRRKIGYLPQQfgfyPT--- 90
Cdd:cd03249 15 DVPILKGLSLTIPPGKtVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlnLRWLRSQIGLVSQE----PVlfd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 91 MKVIDAMTYLAILAEVPAREQKRRiewlLAAVH-----LTAQAKTKVKA----LSGGMLQRLGIAQALVNEPRVLIVDEP 161
Cdd:cd03249 91 GTIAENIRYGKPDATDEEVEEAAK----KANIHdfimsLPDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 162 TAGLDPEERIRFRNLLADFANERLVLLSTHIVSDVEAtTNRIGILDHGRLVFNGTTDELI 221
Cdd:cd03249 167 TSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELM 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-223 |
3.02e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 96.29 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQ---------PALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEkPTSGKVLVDGTPL----- 68
Cdd:COG4172 276 LEARDLKVWFPIKRGlfrrtvghvKAVDGVSLTLRRGeTLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLdglsr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 69 KDARSIRRKIgylpqQ------FG-FYPTMKVIDamtylaILAE--------VPAREQKRRIEWLLAAVHLTAQAKTK-V 132
Cdd:COG4172 355 RALRPLRRRM-----QvvfqdpFGsLSPRMTVGQ------IIAEglrvhgpgLSAAERRARVAEALEEVGLDPAARHRyP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 133 KALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLV--LLSTHIVSDVEATTNRIGILDHGR 210
Cdd:COG4172 424 HEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLayLFISHDLAVVRALAHRVMVMKDGK 503
|
250
....*....|...
gi 491943749 211 LVFNGTTDELIDA 223
Cdd:COG4172 504 VVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-246 |
3.29e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 93.64 E-value: 3.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLV------DGTPLKDARSIRRKIGYLPQqfgfYPTMK 92
Cdd:PRK13643 21 ALFDIDLEVKKGSYtALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsSTSKQKEIKPVRKKVGVVFQ----FPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 93 VIDAmTYLAILAEVP-----AREQKRRIEW-LLAAVHLTAQAKTKVK-ALSGGMLQRLGIAQALVNEPRVLIVDEPTAGL 165
Cdd:PRK13643 97 LFEE-TVLKDVAFGPqnfgiPKEKAEKIAAeKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 166 DPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL---IDAAAGHvfvgDLPVAQLKQF 241
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVfqeVDFLKAH----ELGVPKATHF 251
|
....*
gi 491943749 242 KTQYQ 246
Cdd:PRK13643 252 ADQLQ 256
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-226 |
4.16e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 93.26 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL--KDARSIRRKIGY 80
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGsKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnaENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQfgfyP-----TMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRV 155
Cdd:PRK13647 84 VFQD----PddqvfSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 156 LIVDEPTAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGT----TDELIDAAAG 226
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDksllTDEDIVEQAG 235
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-223 |
4.25e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 96.35 E-value: 4.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYrGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIGY 80
Cdd:TIGR01193 474 IVINDVSYSY-GYGSNILSDISLTIKMNsKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdiDRHTLRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQfgfyPTMKVIDAMTYLAILAEVPAREQKrriewLLAAVHLtAQAKTKVK---------------ALSGGMLQRLGI 145
Cdd:TIGR01193 553 LPQE----PYIFSGSILENLLLGAKENVSQDE-----IWAACEI-AEIKDDIEnmplgyqtelseegsSISGGQKQRIAL 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 146 AQALVNEPRVLIVDEPTAGLD--PEERIrFRNLLadFANERLVLLSTHIVSdVEATTNRIGILDHGRLVFNGTTDELIDA 223
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDtiTEKKI-VNNLL--NLQDKTIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-223 |
6.34e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 95.52 E-value: 6.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHYR--GRQQPALDHVSLNIQSG-MYGLLGKNGAGKS-TLMKILTTLEKP---TSGKVLVDGTPL----- 68
Cdd:COG4172 4 MPLLSVEDLSVAFGqgGGTVEAVKGVSFDIAAGeTLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLlglse 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 69 KDARSIR-RKIGYLPQqfgfyptmkviDAMTYL-------AILAEV-------PAREQKRRIEWLLAAVHLtAQAKTKVK 133
Cdd:COG4172 84 RELRRIRgNRIAMIFQ-----------EPMTSLnplhtigKQIAEVlrlhrglSGAAARARALELLERVGI-PDPERRLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 134 A----LSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTH---IVSDVeatTNRIG 204
Cdd:COG4172 152 AyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHdlgVVRRF---ADRVA 228
|
250
....*....|....*....
gi 491943749 205 ILDHGRLVFNGTTDELIDA 223
Cdd:COG4172 229 VMRQGEIVEQGPTAELFAA 247
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-220 |
6.54e-22 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 94.02 E-value: 6.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 31 GMYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSI------RRKIGYLPQQFGFYPTMKVIDAMTYLAILA 104
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiflppeKRRIGYVFQEARLFPHLSVRGNLRYGMKRA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 105 EVPAREQK-RRIEWLLAAVHLTAQaktKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDpeeRIRFRNLLADFanE 183
Cdd:TIGR02142 104 RPSERRISfERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD---DPRKYEILPYL--E 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491943749 184 RL-------VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:TIGR02142 176 RLhaefgipILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-220 |
6.71e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.42 E-value: 6.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNI-QSGMYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--------DARSIRRKIGYLPQQFGFYPTM 91
Cdd:PRK14246 26 LKDITIKIpNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqiDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 92 KVIDAMTY-LAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKA----LSGGMLQRLGIAQALVNEPRVLIVDEPTAGLD 166
Cdd:PRK14246 106 SIYDNIAYpLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491943749 167 PEERIRFRNLLADFANERLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK14246 186 IVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-221 |
7.88e-22 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 95.11 E-value: 7.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIG 79
Cdd:TIGR01842 316 HLSVENVTIVPPGGKKPTLRGISFSLQAGeALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqwDRETFGKHIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQFGFYPtmkvidamtylAILAEVPAR-----EQKRRIEWL-LAAVH-----LTAQAKTKV----KALSGGMLQRLG 144
Cdd:TIGR01842 396 YLPQDVELFP-----------GTVAENIARfgenaDPEKIIEAAkLAGVHelilrLPDGYDTVIgpggATLSGGQRQRIA 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 145 IAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADF-ANERLVLLSTHIVSdVEATTNRIGILDHGRLVFNGTTDELI 221
Cdd:TIGR01842 465 LARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-220 |
1.63e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.61 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 13 YRGRQQPALDHVSLNIQ-SGMYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDAR----SIRRKIGYL---PQQ 84
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSlSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrgllALRQQVATVfqdPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 85 FGFYPTMKViDAMTYLAILAeVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAG 164
Cdd:PRK13638 89 QIFYTDIDS-DIAFSLRNLG-VPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491943749 165 LDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQgNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-211 |
3.89e-21 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 89.45 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGR-QQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD----------- 70
Cdd:cd03248 12 VKFQNVTFAYPTRpDTLVLQDVSFTLHPGeVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkylhskvs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 71 ---------ARSIRRKIGYLPQQfgfYPTMKVIDAMTYLAILAEVPAREQKRRIEwllaavhltaqAKTKVKALSGGMLQ 141
Cdd:cd03248 92 lvgqepvlfARSLQDNIAYGLQS---CSFECVKEAAQKAHAHSFISELASGYDTE-----------VGEKGSQLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 142 RLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTHIVSDVEaTTNRIGILDHGRL 211
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
12-220 |
5.37e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 89.64 E-value: 5.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 12 HYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL---------------KDARSIR 75
Cdd:PRK10619 12 HKRYGEHEVLKGVSLQANAGdVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvadkNQLRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 76 RKIGYLPQQFGFYPTMKVIDAMTYLAI----LAEVPAREqkrRIEWLLAAVHLTAQAKTKVKA-LSGGMLQRLGIAQALV 150
Cdd:PRK10619 92 TRLTMVFQHFNLWSHMTVLENVMEAPIqvlgLSKQEARE---RAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491943749 151 NEPRVLIVDEPTAGLDPE---ERIRFRNLLADFANERLVLlsTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVV--THEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
8-220 |
6.76e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 90.79 E-value: 6.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 8 QLVKHY---RG-----RQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDA-----RS 73
Cdd:PRK11308 10 DLKKHYpvkRGlfkpeRLVKALDGVSFTLERGkTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdpeaqKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 74 IRRKIGYLPQQ-FG-FYPTMKVIDAMTY-LAILAEVPAREQKRRIEWLLAAVHL-TAQAKTKVKALSGGMLQRLGIAQAL 149
Cdd:PRK11308 90 LRQKIQIVFQNpYGsLNPRKKVGQILEEpLLINTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491943749 150 VNEPRVLIVDEPTAGLDPEERIRFRNLLADFANE---RLVLLStHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK11308 170 MLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElglSYVFIS-HDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-220 |
7.33e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 89.33 E-value: 7.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSGM-YGLLGKNGAGKSTLMKIL-----TTLEKPTSGKVLVDGT----PLKDARS 73
Cdd:COG1117 12 IEVRNLNVYYGDKQ--ALKDINLDIPENKvTALIGPSGCGKSTLLRCLnrmndLIPGARVEGEILLDGEdiydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 74 IRRKIGYLPQQfgfyPT---MKVIDAMTYLAILAEVPAREQ-KRRIEWLLAAVHLTAQAKTKVK----ALSGGMLQRLGI 145
Cdd:COG1117 90 LRRRVGMVFQK----PNpfpKSIYDNVAYGLRLHGIKSKSElDEIVEESLRKAALWDEVKDRLKksalGLSGGQQQRLCI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 146 AQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTHI------VSDveattnRIGILDHGRLVFNGTTDE 219
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNmqqaarVSD------YTAFFYLGELVEFGPTEQ 239
|
.
gi 491943749 220 L 220
Cdd:COG1117 240 I 240
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-191 |
8.48e-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: 92.04 E-value: 8.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYRGrQQPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDAR--SIRRKIG 79
Cdd:TIGR02868 334 TLELRDLSAGYPG-APPVLDGVSLDLPPGERvAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqdEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQFGFYPTmkviDAMTYLAILAEVPAREQkrrIEWLLAAVHL-------TAQAKTKV----KALSGGMLQRLGIAQA 148
Cdd:TIGR02868 413 VCAQDAHLFDT----TVRENLRLARPDATDEE---LWAALERVGLadwlralPDGLDTVLgeggARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491943749 149 LVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTH 191
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-221 |
1.34e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 91.62 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 13 YRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDAR--SIRRKIGYLPQQFG-FY 88
Cdd:PRK11176 351 YPGKEVPALRNINFKIPAGkTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTlaSLRNQVALVSQNVHlFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 89 PTmkVIDAMTYlailaevpAREQKRRIEWLLAAVHLtAQAKTKVK---------------ALSGGMLQRLGIAQALVNEP 153
Cdd:PRK11176 431 DT--IANNIAY--------ARTEQYSREQIEEAARM-AYAMDFINkmdngldtvigengvLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 154 RVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTHIVSDVEaTTNRIGILDHGRLVFNGTTDELI 221
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIE-KADEILVVEDGEIVERGTHAELL 566
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-191 |
1.56e-20 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 88.32 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYrGRQQpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK------------ 69
Cdd:COG4598 8 ALEVRDLHKSF-GDLE-VLKGVSLTARKGdVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelvpa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 70 DAR---SIRRKIGYLPQQFGFYPTMKVIDAMTylailaEVPAREQKR-------RIEWLLAAVHLTAQAKTKVKALSGGM 139
Cdd:COG4598 86 DRRqlqRIRTRLGMVFQSFNLWSHMTVLENVI------EAPVHVLGRpkaeaieRAEALLAKVGLADKRDAYPAHLSGGQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 140 LQRLGIAQALVNEPRVLIVDEPTAGLDPE---ERIRfrnLLADFANE-RLVLLSTH 191
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDPElvgEVLK---VMRDLAEEgRTMLVVTH 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-212 |
2.46e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.74 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DAR-SIRRKIGYLPQQFGFYPTMKVID 95
Cdd:PRK11288 19 ALDDISFDCRAGqVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTaALAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 96 AMtYLAILAE----VPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLD-PEER 170
Cdd:PRK11288 99 NL-YLGQLPHkggiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSaREIE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491943749 171 IRFRNLLADFANERLVLLSTHIVSDVEATTNRIGILDHGRLV 212
Cdd:PRK11288 178 QLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYV 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-222 |
3.16e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.59 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 24 VSLNI-QSGMYGLLGKNGAGKSTLMKILTTL-----EKPTSGKVLVDG----TPLKDARSIRRKIGYLPQQFGFYPTMKV 93
Cdd:PRK14267 23 VDLKIpQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGrniySPDVDPIEVRREVGMVFQYPNPFPHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 94 IDAMTYLAILAEV--PAREQKRRIEWLLAAVHLTAQAKTKVK----ALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDP 167
Cdd:PRK14267 103 YDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAMKPKILLMDEPTANIDP 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 168 EERIRFRNLLADFANERLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELID 222
Cdd:PRK14267 183 VGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-174 |
4.55e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 88.75 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHYRGRQQpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRKIG 79
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQ-VIKGIDLDVADGeFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQFGFYPTMKVIDAMTY-LAIlAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIV 158
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYgLKI-RGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170
....*....|....*.
gi 491943749 159 DEPTAGLDPEERIRFR 174
Cdd:PRK11650 159 DEPLSNLDAKLRVQMR 174
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-226 |
6.44e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.46 E-value: 6.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGtplKDARSIRRKIGYlp 82
Cdd:PRK09700 6 ISMAGIGKSFGPVH--ALKSVNLTVYPGeIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN---INYNKLDHKLAA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 qQFG---FYPTMKVIDAMTYLAIL--AEVPAR-----------EQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIA 146
Cdd:PRK09700 79 -QLGigiIYQELSVIDELTVLENLyiGRHLTKkvcgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 147 QALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRLVFNG-----TTDEL 220
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEgTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGmvsdvSNDDI 237
|
....*.
gi 491943749 221 IDAAAG 226
Cdd:PRK09700 238 VRLMVG 243
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-220 |
7.65e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.16 E-value: 7.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTS---GKVLVDGTPL--KDARSIRRK 77
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWtALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLtaKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 78 IGYLPQ----QFgfyPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEP 153
Cdd:PRK13640 86 VGIVFQnpdnQF---VGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491943749 154 RVLIVDEPTAGLDPEERIRFRNLLADFANER-LVLLS-THIVSDVEATTNRIgILDHGRLVFNGTTDEL 220
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNnLTVISiTHDIDEANMADQVL-VLDDGKLLAQGSPVEI 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-224 |
7.76e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.34 E-value: 7.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGrqQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIR-RKIG-Y 80
Cdd:PRK15439 12 LCARSISKQYSG--VEVLKGIDFTLHAGeVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKaHQLGiY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 L-PQQFGFYPTMKVIDamtylAILAEVPAREQ-KRRIEWLLAAvhLTAQAKTKVKAlsgGML-----QRLGIAQALVNEP 153
Cdd:PRK15439 90 LvPQEPLLFPNLSVKE-----NILFGLPKRQAsMQKMKQLLAA--LGCQLDLDSSA---GSLevadrQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 154 RVLIVDEPTAGLDPEERIRF----RNLLADFANerLVLLStHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAA 224
Cdd:PRK15439 160 RILILDEPTASLTPAETERLfsriRELLAQGVG--IVFIS-HKLPEIRQLADRISVMRDGTIALSGKTADLSTDD 231
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-179 |
8.86e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 85.95 E-value: 8.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTT-IQIEQLVKHYR-----GRQQPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLV--DGTPLK-- 69
Cdd:COG4778 1 MTTlLEVENLSKTFTlhlqgGKRLPVLDGVSFSVAAGECvALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 70 --DARSI----RRKIGYLpQQFgfyptMKVIDAMTYLAILAEvPAREQKRRiewllaavhlTAQAKTKVKAL-------- 135
Cdd:COG4778 81 qaSPREIlalrRRTIGYV-SQF-----LRVIPRVSALDVVAE-PLLERGVD----------REEARARARELlarlnlpe 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491943749 136 ----------SGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLAD 179
Cdd:COG4778 144 rlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEE 197
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
24-192 |
9.35e-20 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 85.24 E-value: 9.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 24 VSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDAR-SIRRKIGYLPQQFGFYPTMKVIDAMTYLA 101
Cdd:cd03231 19 LSFTLAAGeALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRdSIARGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 102 ILAevpAREQkrrIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFA 181
Cdd:cd03231 99 ADH---SDEQ---VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHC 172
|
170
....*....|..
gi 491943749 182 NE-RLVLLSTHI 192
Cdd:cd03231 173 ARgGMVVLTTHQ 184
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-222 |
1.40e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.63 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 18 QPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIGYLPQQFGFYpTMKVI 94
Cdd:TIGR00958 494 VPVLKGLTFTLHPGeVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqyDHHYLHRQVALVGQEPVLF-SGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 95 DAMTY---LAILAEVPAREQKrriewllAAVH-----LTAQAKTKVKA----LSGGMLQRLGIAQALVNEPRVLIVDEPT 162
Cdd:TIGR00958 573 ENIAYgltDTPDEEIMAAAKA-------ANAHdfimeFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 163 AGLDPEERIRFRNLLAdfANERLVLLSTHIVSDVEaTTNRIGILDHGRLVFNGTTDELID 222
Cdd:TIGR00958 646 SALDAECEQLLQESRS--RASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLME 702
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
1.44e-19 |
|
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: 88.32 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLE--KPTSGKVLV----------------D 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGeVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYhvalcekcgyverpskV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 65 GTPL-------------------KDARSIRRKIGYLPQQ-FGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHL 124
Cdd:TIGR03269 79 GEPCpvcggtlepeevdfwnlsdKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 125 TAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPE-ERIRFRNLLADFANERLVL-LSTHIVSDVEATTNR 202
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtAKLVHNALEEAVKASGISMvLTSHWPEVIEDLSDK 238
|
250
....*....|....*....
gi 491943749 203 IGILDHGRLVFNGTTDELI 221
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVV 257
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-166 |
2.09e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 88.24 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD------ARSIRRKIGYLPQQFGFYPTMKV 93
Cdd:PRK10535 24 LKGISLDIYAGeMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadalAQLRREHFGFIFQRYHLLSHLTA 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491943749 94 IDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLD 166
Cdd:PRK10535 104 AQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-229 |
2.37e-19 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 86.71 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRgrQQPALDHVSLNIQSG-MYGLLGKNGAGKSTlMKILTTLEKPTSGKVLVD-GTPLKDARSIRRKIG-Y 80
Cdd:NF000106 14 VEVRGLVKHFG--EVKAVDGVDLDVREGtVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRf*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDE 160
Cdd:NF000106 91 RPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491943749 161 PTAGLDPEER----IRFRNLLADFANerlVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAAGHVF 229
Cdd:NF000106 171 PTTGLDPRTRnevwDEVRSMVRDGAT---VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTL 240
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-212 |
5.97e-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: 83.31 E-value: 5.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSGM-YGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIGY 80
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEkVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkiGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQ--------------FGFYPtmkviDAMTYLAiLAEVPAREqkrriEWLLAAVHLTAQAKTKVKALSGGMLQRLGIA 146
Cdd:cd03244 83 IPQDpvlfsgtirsnldpFGEYS-----DEELWQA-LERVGLKE-----FVESLPGGLDTVVEEGGENLSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 147 QALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTHIVSDVeATTNRIGILDHGRLV 212
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTI-IDSDRILVLDKGRVV 216
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-225 |
7.67e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.39 E-value: 7.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHYrGRQQpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD---ARSIRR 76
Cdd:PRK11614 3 KVMLSFDKVSAHY-GKIQ-ALHEVSLHINQGeIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 77 KIGYLPQQFGFYPTMKVIDAMTYLAILAEvpaREQ-KRRIEWLLAAV-HLTAQAKTKVKALSGGMLQRLGIAQALVNEPR 154
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGFFAE---RDQfQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491943749 155 VLIVDEPTAGLDPEERIRFRNLLADFANERL-VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAA 225
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMtIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-223 |
7.76e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.38 E-value: 7.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQS-GMYGLLGKNGAGKSTLMKILTTLEKPTSG-----KVLVDGTPL---KDARSIRRKIGYLPQQFGFYPTM 91
Cdd:PRK14271 37 LDQVSMGFPArAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyRDVLEFRRRVGMLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 92 KVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVK----ALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDP 167
Cdd:PRK14271 117 IMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDP 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 168 EERIRFRNLLADFANERLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDA 223
Cdd:PRK14271 197 TTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-221 |
9.04e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 84.37 E-value: 9.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKV----------------------LVDGTP----LKDAR 72
Cdd:PRK13651 22 ALDNVSVEINQGEFiAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvlekLVIQKTrfkkIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 73 SIRRKIGYLpQQFGFYPTMK--VIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVK-ALSGGMLQRLGIAQAL 149
Cdd:PRK13651 102 EIRRRVGVV-FQFAEYQLFEqtIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRSPfELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491943749 150 VNEPRVLIVDEPTAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELI 221
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-220 |
9.08e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.01 E-value: 9.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQ-QPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL--KDARSIRRKIG 79
Cdd:PRK13650 5 IEVKNLTFKYKEDQeKYTLNDVSFHVKQGEWlSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQ----QFgfyPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRV 155
Cdd:PRK13650 85 MVFQnpdnQF---VGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491943749 156 LIVDEPTAGLDPEERIRFRNLLADFANE-RLVLLS-THIVSDVeATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISiTHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-266 |
1.07e-18 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 84.77 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 30 SGMYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSI------RRKIGYLPQQFGFYPTMKVIDAMTYlail 103
Cdd:COG4148 25 RGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGiflpphRRRIGYVFQEARLFPHLSVRGNLLY---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 104 AEVPAREQKRRIEW-----LLAAVHLTAQaktKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPE---------E 169
Cdd:COG4148 101 GRKRAPRAERRISFdevveLLGIGHLLDR---RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLArkaeilpylE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 170 RIRfrnlladfanERL---VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAAGHVFVGDLPV-----AQLKQF 241
Cdd:COG4148 178 RLR----------DELdipILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAgsvleATVAAH 247
|
250 260
....*....|....*....|....*
gi 491943749 242 KTQYQISEQTAHGQHIRVRLLARTP 266
Cdd:COG4148 248 DPDYGLTRLALGGGRLWVPRLDLPP 272
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-222 |
1.33e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 85.78 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 19 PALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDA--RSIRRKIGYLPQqfgfyptmkviD 95
Cdd:PRK13657 349 QGVEDVSFEAKPGqTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVtrASLRRNIAVVFQ-----------D 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 96 AMTYLAILAE--VPAREQKRRIEWLLAAVhlTAQA-----------KTKV----KALSGGMLQRLGIAQALVNEPRVLIV 158
Cdd:PRK13657 418 AGLFNRSIEDniRVGRPDATDEEMRAAAE--RAQAhdfierkpdgyDTVVgergRQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 159 DEPTAGLDPEERIRFRNLLADFANERLVLLSTHIVSDV-EATtnRIGILDHGRLVFNGTTDELID 222
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVrNAD--RILVFDNGRVVESGSFDELVA 558
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-218 |
2.84e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.60 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLeKPT---SGKVLVDGTPLKdARSIR---RK-IGYLPQQFGFYPTM 91
Cdd:PRK13549 20 ALDNVSLKVRAGeIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQ-ASNIRdteRAgIAIIHQELALVKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 92 KVIDAMtylaILAEVPAR-------EQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAG 164
Cdd:PRK13549 98 SVLENI----FLGNEITPggimdydAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 165 LDPEERIRFRNLLADFANERL--VLLStHIVSDVEATTNRIGILDHGRLVfnGTTD 218
Cdd:PRK13549 174 LTESETAVLLDIIRDLKAHGIacIYIS-HKLNEVKAISDTICVIRDGRHI--GTRP 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-224 |
3.15e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.05 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGrqQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARS--IRRKIGY 80
Cdd:COG4604 2 IEIKNVSKRYGG--KVVLDDVSLTIPKGgITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSreLAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQ--------------FGFYPTMKvidamtylailaEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIA 146
Cdd:COG4604 80 LRQEnhinsrltvrelvaFGRFPYSK------------GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 147 QALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER-----LVL--------LSTHIVSdveattnrigiLDHGRLVF 213
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELgktvvIVLhdinfascYADHIVA-----------MKDGRVVA 216
|
250
....*....|.
gi 491943749 214 NGTTDELIDAA 224
Cdd:COG4604 217 QGTPEEIITPE 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-243 |
8.27e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 81.29 E-value: 8.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLV-KHYRGRQQPALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL--KDARSIRRKIG 79
Cdd:PRK13642 5 LEVENLVfKYEKESDVNQLNGVSFSITKGEWvSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLtaENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQ-FGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIV 158
Cdd:PRK13642 85 MVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 159 DEPTAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAAGHVFVG-DLPVA 236
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEIGlDVPFS 244
|
....*....
gi 491943749 237 Q--LKQFKT 243
Cdd:PRK13642 245 SnlMKDLRK 253
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-218 |
9.44e-18 |
|
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: 82.95 E-value: 9.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTL--EKPTSGKVLVDGTPLKdARSIR----R 76
Cdd:TIGR02633 2 LEMKGIVKTFGGVK--ALDGIDLEVRPGeCVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLK-ASNIRdterA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 77 KIGYLPQQFGFYPTMKVID------AMTYLAILAEVPAreQKRRIEWLLAAVHLTAQAKTK-VKALSGGMLQRLGIAQAL 149
Cdd:TIGR02633 79 GIVIIHQELTLVPELSVAEniflgnEITLPGGRMAYNA--MYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 150 VNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLS-THIVSDVEATTNRIGILDHGRLVfnGTTD 218
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYiSHKLNEVKAVCDTICVIRDGQHV--ATKD 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
17-208 |
1.08e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.54 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 17 QQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLvdgtplkdaRSIRRKIGYLPQQFGFYPTMkvid 95
Cdd:PRK09544 16 QRRVLSDVSLELKPGkILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLRIGYVPQKLYLDTTL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 96 AMTYLAILAEVPAREQKRRIEWL--LAAVHLTAQAKTKvkaLSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRF 173
Cdd:PRK09544 83 PLTVNRFLRLRPGTKKEDILPALkrVQAGHLIDAPMQK---LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 491943749 174 RNLLADFANER--LVLLSTHIVSDVEATTNRIGILDH 208
Cdd:PRK09544 160 YDLIDQLRRELdcAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-220 |
1.29e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.47 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 18 QPALDHVSLNI-QSGMYGLLGKNGAGKSTLMKILTTL-----EKPTSGKVLVDGTPLKDAR----SIRRKIGYLPQQFGF 87
Cdd:PRK14258 20 QKILEGVSMEIyQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRvnlnRLRRQVSMVHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 88 YPtMKVIDAMTY-LAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKA----LSGGMLQRLGIAQALVNEPRVLIVDEPT 162
Cdd:PRK14258 100 FP-MSVYDNVAYgVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 163 AGLDPEERIRFRNLLADFA--NERLVLLSTH------IVSDVEA----TTNRIgildhGRLVFNGTTDEL 220
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRlrSELTMVIVSHnlhqvsRLSDFTAffkgNENRI-----GQLVEFGLTKKI 243
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-220 |
1.55e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 81.29 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KDARSIRRKIGYLPQQfgfyPTMKV 93
Cdd:PRK15079 36 AVDGVTLRLYEGeTLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkdDEWRAVRSDIQMIFQD----PLASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 94 IDAMTYLAILAE--------VPAREQKRRIEWLLAAVHLTAQAKTKV-KALSGGMLQRLGIAQALVNEPRVLIVDEPTAG 164
Cdd:PRK15079 112 NPRMTIGEIIAEplrtyhpkLSRQEVKDRVKAMMLKVGLLPNLINRYpHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491943749 165 LDPEERIRFRNLLADFANE---RLVLLStHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREmglSLIFIA-HDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
35-224 |
2.45e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.50 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 35 LLGKNGAGKSTLMKILTTLEkPTSGKVLVDGTPLKD--ARSIRRKIGYLPQQFGFYPTMKVIDamtYLAIL--AEVPARE 110
Cdd:COG4138 27 LIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwsAAELARHRAYLSQQQSPPFAMPVFQ---YLALHqpAGASSEA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 111 QKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQAL------VN-EPRVLIVDEPTAGLDPEERIRFRNLLADFANE 183
Cdd:COG4138 103 VEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491943749 184 -RLVLLSTHivsDVEAT---TNRIGILDHGRLVFNGTTDELIDAA 224
Cdd:COG4138 183 gITVVMSSH---DLNHTlrhADRVWLLKQGKLVASGETAEVMTPE 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-220 |
5.75e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.84 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 5 QIEQL-VKHYRGRqqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL--KDARSIRRK-IG 79
Cdd:COG3845 259 EVENLsVRDDRGV--PALKDVSLEVRAGeILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItgLSPRERRRLgVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLP---QQFGFYPTMKVIDAMtylaILAEVPAREQKRRIeWL-LAAVHLTAQAK------------TKVKALSGGMLQRL 143
Cdd:COG3845 337 YIPedrLGRGLVPDMSVAENL----ILGRYRRPPFSRGG-FLdRKAIRAFAEELieefdvrtpgpdTPARSLSGGNQQKV 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 144 GIAQALVNEPRVLIVDEPTAGLDPE--ERIrfRNLLADFANERL-VLLsthIVSDVE---ATTNRIGILDHGRLVFNGTT 217
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGaiEFI--HQRLLELRDAGAaVLL---ISEDLDeilALSDRIAVMYEGRIVGEVPA 486
|
...
gi 491943749 218 DEL 220
Cdd:COG3845 487 AEA 489
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
3-223 |
6.15e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.59 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHyrgRQQPALDHVSLNIQSG-MYGLLGKNGAGKS----TLMKILTTLEKPTSGKVLVDGTPLKDARSIRRK 77
Cdd:PRK10418 4 QIELRNIALQ---AAQPLVHGVSLTLQRGrVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 78 IGYLPQ--QFGFYP--TMKViDAMTYLAILAEVPAREQKRRIewlLAAVHLtAQAKTKVKA----LSGGMLQRLGIAQAL 149
Cdd:PRK10418 81 IATIMQnpRSAFNPlhTMHT-HARETCLALGKPADDATLTAA---LEAVGL-ENAARVLKLypfeMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 150 VNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERL--VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDA 223
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-228 |
2.90e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 78.68 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILT------TLEkptsGKVLVDGTP--LKDAR-SIRRKIGYLPQQFGFYP 89
Cdd:NF040905 16 ALDDVNLSVREGeIHALCGENGAGKSTLMKVLSgvyphgSYE----GEILFDGEVcrFKDIRdSEALGIVIIHQELALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 90 tmkvidamtYLAIlAE--VPAREQKRR--IEW---------LLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVL 156
Cdd:NF040905 92 ---------YLSI-AEniFLGNERAKRgvIDWnetnrrareLLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491943749 157 IVDEPTAGLDPEERIRFRNLLADFANERL--VLLStHIVSDVEATTNRIGILDHGRLVfngttdELIDAAAGHV 228
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLELKAQGItsIIIS-HKLNEIRRVADSITVLRDGRTI------ETLDCRADEV 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-220 |
3.19e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 76.35 E-value: 3.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRgrQQPALDHVSLNIQ-SGMYGLLGKNGAGKSTLMKILTTL-----EKPTSGKVLVDG----TPLKDARS 73
Cdd:PRK14239 6 LQVSDLSVYYN--KKKALNSVSLDFYpNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGhniySPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 74 IRRKIGYLPQQFGFYPtMKVIDAMTY---------LAILAEVPAREQKRRIEWLLAAVHLTAQAKtkvkALSGGMLQRLG 144
Cdd:PRK14239 84 LRKEIGMVFQQPNPFP-MSIYENVVYglrlkgikdKQVLDEAVEKSLKGASIWDEVKDRLHDSAL----GLSGGQQQRVC 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 145 IAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-213 |
3.27e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 76.66 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDG---TPLKDARSIRRkIGYLPQQfgfyPTMKVID 95
Cdd:COG1101 21 ALDGLNLTIEEGDFvTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvTKLPEYKRAKY-IGRVFQD----PMMGTAP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 96 AMTYLAILAEVPAREQKRRIEW------------LLAAVH--LTAQAKTKVKALSGGmlQRlgiaQAL------VNEPRV 155
Cdd:COG1101 96 SMTIEENLALAYRRGKRRGLRRgltkkrrelfreLLATLGlgLENRLDTKVGLLSGG--QR----QALsllmatLTKPKL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 156 LIVDEPTAGLDP----------EERIRFRNLLAdfanerlvLLSTHIVSDVEATTNRIGILDHGRLVF 213
Cdd:COG1101 170 LLLDEHTAALDPktaalvleltEKIVEENNLTT--------LMVTHNMEQALDYGNRLIMMHEGRIIL 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-220 |
4.55e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.20 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLV------------------DGTPLKDARSIRRKIGY 80
Cdd:PRK13631 41 ALNNISYTFEKNkIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhelitnpYSKKIKNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LpQQFGFYPTMK--VIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVK-ALSGGMLQRLGIAQALVNEPRVLI 157
Cdd:PRK13631 121 V-FQFPEYQLFKdtIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491943749 158 VDEPTAGLDPE-ERIRFRNLLADFANERLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK13631 200 FDEPTAGLDPKgEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-179 |
1.42e-15 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 73.43 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTtlEKPTSGKV----LVDGTPLKDarSIRRKIGYLPQQFGFYPTMKVID 95
Cdd:cd03232 23 LNNISGYVKPGtLTALMGESGAGKTTLLDVLA--GRKTAGVItgeiLINGRPLDK--NFQRSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 96 AMTYLAILAEVPAREQKrriewllaavhltaqaktkvkalsggmlqRLGIAQALVNEPRVLIVDEPTAGLDPE---ERIR 172
Cdd:cd03232 99 ALRFSALLRGLSVEQRK-----------------------------RLTIGVELAAKPSILFLDEPTSGLDSQaayNIVR 149
|
....*..
gi 491943749 173 FRNLLAD 179
Cdd:cd03232 150 FLKKLAD 156
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-177 |
1.58e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.05 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHY-RGRQQPA-LDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL----KDARSIRR 76
Cdd:PRK10584 7 VEVHHLKKSVgQGEHELSiLTGVELVVKRGeTIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdEEARAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 77 --KIGYLPQQFGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPR 154
Cdd:PRK10584 87 akHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180
....*....|....*....|...
gi 491943749 155 VLIVDEPTAGLDPEERIRFRNLL 177
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLL 189
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-222 |
2.27e-15 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 74.10 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKV---LVDGTPL--------KDA 71
Cdd:TIGR02323 4 LQVSGLSKSYGGGK--GCRDVSFDLYPGeVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyiMRSGAELelyqlseaERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 72 RSIRRKIGYLPQQFGFYPTMKVIDAMTYLAILAEVPAREQKR----RIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQ 147
Cdd:TIGR02323 82 RLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNiratAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491943749 148 ALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELID 222
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLglAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLD 238
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-224 |
2.58e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 74.25 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 7 EQLVKHYrGRQQPAlDHVSLNIQSGMY-GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD--ARSIRRKIGYLPQ 83
Cdd:PRK10253 11 EQLTLGY-GKYTVA-ENLTVEIPDGHFtAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaSKEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 84 QfGFYPTMKVIDAMTYLAILAEVPA-----REQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIV 158
Cdd:PRK10253 89 N-ATTPGDITVQELVARGRYPHQPLftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 159 DEPTAGLDPEERIRFRNLLADFANERLVLLST--HIVSDVEATTNRIGILDHGRLVFNGTTDELIDAA 224
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAvlHDLNQACRYASHLIALREGKIVAQGAPKEIVTAE 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-225 |
6.40e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 72.31 E-value: 6.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 23 HVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRKIGYLPQQ--------------FGF 87
Cdd:PRK10771 17 RFDLTVERGeRVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQEnnlfshltvaqnigLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 88 YPTMKVidamtylailaevpAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDP 167
Cdd:PRK10771 97 NPGLKL--------------NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 168 EERIRFRNLLADFANER-LVLLS-THIVSDVEATTNRIGILDHGRLVFNGTTDELIDAAA 225
Cdd:PRK10771 163 ALRQEMLTLVSQVCQERqLTLLMvSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-172 |
7.78e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.46 E-value: 7.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 34 GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDgtplkdarsirRKIGYLPQqfgfYptMKVIDAMTYLAILAEVPAR---- 109
Cdd:PRK13409 369 GIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-----------LKISYKPQ----Y--IKPDYDGTVEDLLRSITDDlgss 431
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491943749 110 ----E--QKRRIEWLLaavhltaqaKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIR 172
Cdd:PRK13409 432 yyksEiiKPLQLERLL---------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-227 |
9.58e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 74.09 E-value: 9.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYRGRQqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDA--RSIRRKIG 79
Cdd:COG5265 357 EVRFENVSFGYDPER-PILKGVSFEVPAGkTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVtqASLRAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQfgfyptmkvidamTYL---------------AILAEV--PAReqkrriewlLAAVH-----LTAQAKTKV----- 132
Cdd:COG5265 436 IVPQD-------------TVLfndtiayniaygrpdASEEEVeaAAR---------AAQIHdfiesLPDGYDTRVgergl 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 133 KaLSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDP--EERIrfRNLLADFANERLVL-----LSTHIVSDveattnRIGI 205
Cdd:COG5265 494 K-LSGGEKQRVAIARTLLKNPPILIFDEATSALDSrtERAI--QAALREVARGRTTLviahrLSTIVDAD------EILV 564
|
250 260
....*....|....*....|..
gi 491943749 206 LDHGRLVFNGTTDELIdAAAGH 227
Cdd:COG5265 565 LEAGRIVERGTHAELL-AQGGL 585
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
35-192 |
9.61e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 9.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 35 LLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRkIGYLPQQFGFYPTMKVIDAmtyLAILAEVPAREQkRR 114
Cdd:PRK13539 33 LTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVAEN---LEFWAAFLGGEE-LD 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491943749 115 IEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER-LVLLSTHI 192
Cdd:PRK13539 108 IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGgIVIAATHI 186
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-166 |
9.70e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 74.76 E-value: 9.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSG-MYGLLGKNGAGKSTLMKIL---TTLEKPTSGKVLVDGTPLKDarSIRRKIGYLPQQFGFYPTMKVIDA 96
Cdd:TIGR00956 779 LNNVDGWVKPGtLTALMGASGAGKTTLLNVLaerVTTGVITGGDRLVNGRPLDS--SFQRSIGYVQQQDLHLPTSTVRES 856
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491943749 97 MTYLAIL---AEVPAREQKRRIEWLLAAVHLTAQAKTKVkALSGGML-----QRLGIAQALVNEPRVLI-VDEPTAGLD 166
Cdd:TIGR00956 857 LRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVV-GVPGEGLnveqrKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-191 |
9.72e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.07 E-value: 9.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 34 GLLGKNGAGKSTLMKILTTLEKPTSGKVLVD-----------GTPLKD------ARSIR--RKIGY---LPQQF-Gfypt 90
Cdd:PRK13409 103 GILGPNGIGKTTAVKILSGELIPNLGDYEEEpswdevlkrfrGTELQNyfkklyNGEIKvvHKPQYvdlIPKVFkG---- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 91 mKVIDamtylaILAEVparEQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEER 170
Cdd:PRK13409 179 -KVRE------LLKKV---DERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQR 248
|
170 180
....*....|....*....|.
gi 491943749 171 IRFRNLLADFANERLVLLSTH 191
Cdd:PRK13409 249 LNVARLIRELAEGKYVLVVEH 269
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-223 |
1.24e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.13 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 2 TTIQIEQLVKHYRGR-------QQPALDHVSLNIQSGM-YGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK---- 69
Cdd:PRK15112 3 TLLEVRNLSKTFRYRtgwfrrqTVEAVKPLSFTLREGQtLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 70 DARSIRRKIGYLPQQFGFYPTMKV---IDAMTYLAILAEVPAREqKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIA 146
Cdd:PRK15112 83 SYRSQRIRMIFQDPSTSLNPRQRIsqiLDFPLRLNTDLEPEQRE-KQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 147 QALVNEPRVLIVDEPTAGLDPEERIRFRNLLadfanerLVLLSTHIVSDVEAT---------TNRIGILDHGRLVFNGTT 217
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLM-------LELQEKQGISYIYVTqhlgmmkhiSDQVLVMHQGEVVERGST 234
|
....*.
gi 491943749 218 DELIDA 223
Cdd:PRK15112 235 ADVLAS 240
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-223 |
3.48e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.44 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYRgRQQPALDHVSLNIQS-GMYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIG 79
Cdd:PRK10790 340 RIDIDNVSFAYR-DDNLVLQNINLSVPSrGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSslSHSVLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQfgfyptmKVIDAMTYLAILAEvpAREQKRRIEW-LLAAVHLTAQAKT-----------KVKALSGGMLQRLGIAQ 147
Cdd:PRK10790 419 MVQQD-------PVVLADTFLANVTL--GRDISEEQVWqALETVQLAELARSlpdglytplgeQGNNLSVGQKQLLALAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 148 ALVNEPRVLIVDEPTAGLDP--EERIRfRNLLADFANERLVLLSTHIVSDVEATTnrIGILDHGRLVFNGTTDELIDA 223
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSgtEQAIQ-QALAAVREHTTLVVIAHRLSTIVEADT--ILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-166 |
3.93e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 69.75 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIGY 80
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGeKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIStiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQQfgfyPTMKVIDAMTYLAILAEVPAREqkrriewLLAAVHLTAQAKTkvkaLSGGMLQRLGIAQALVNEPRVLIVDE 160
Cdd:cd03369 87 IPQD----PTLFSGTIRSNLDPFDEYSDEE-------IYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDE 151
|
....*.
gi 491943749 161 PTAGLD 166
Cdd:cd03369 152 ATASID 157
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-172 |
5.42e-14 |
|
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: 72.12 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 34 GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDgtplkdarsirRKIGYLPQqfgfYPTmkvIDA-MTYLAILAEVPARE-- 110
Cdd:COG1245 370 GIVGPNGIGKTTFAKILAGVLKPDEGEVDED-----------LKISYKPQ----YIS---PDYdGTVEEFLRSANTDDfg 431
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491943749 111 ---------QKRRIEWLLaavhltaqaKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIR 172
Cdd:COG1245 432 ssyykteiiKPLGLEKLL---------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 493
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-191 |
5.80e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.58 E-value: 5.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 18 QPALDHVSLNIQSGM-YGLLGKNGAGKSTLMKILT-----------TL--EKPTSGKVLVDgtplkdarsIRRKIGYLPQ 83
Cdd:PRK10938 273 RPILHNLSWQVNPGEhWQIVGPNGAGKSTLLSLITgdhpqgysndlTLfgRRRGSGETIWD---------IKKHIGYVSS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 84 QF----------------GFYPTMKVIDAmtylailaeVPAREQKRRIEWLlAAVHLTAQ-AKTKVKALSGGMlQRLG-I 145
Cdd:PRK10938 344 SLhldyrvstsvrnvilsGFFDSIGIYQA---------VSDRQQKLAQQWL-DILGIDKRtADAPFHSLSWGQ-QRLAlI 412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491943749 146 AQALVNEPRVLIVDEPTAGLDPEERI---RFRNLLADFANERLVLLSTH 191
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDPLNRQlvrRFVDVLISEGETQLLFVSHH 461
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-209 |
6.37e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 69.36 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 12 HYRGRQQPALDHVSLNIQSGMYGLL-GKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLK--DARSIRRKIGY---LPQQF 85
Cdd:PRK10247 14 GYLAGDAKILNNISFSLRAGEFKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlKPEIYRQQVSYcaqTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 86 GfyptMKVIDAMTY-LAILAEVPareQKRRIEWLLAAVHLTAQAKTK-VKALSGGMLQRLGIAQALVNEPRVLIVDEPTA 163
Cdd:PRK10247 94 G----DTVYDNLIFpWQIRNQQP---DPAIFLDDLERFALPDTILTKnIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491943749 164 GLDPEERIRFRNLLADFANER--LVLLSTHIVSDVEATTNRIGILDHG 209
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-220 |
7.81e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 70.18 E-value: 7.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 14 RGrQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD-ARS----IRRKIGYLPQQFGF 87
Cdd:PRK11831 17 RG-NRCIFDNISLTVPRGkITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmSRSrlytVRKRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 88 YPTMKVIDAMTYlailaevPAREQKRRIEWL--------LAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVD 159
Cdd:PRK11831 96 FTDMNVFDNVAY-------PLREHTQLPAPLlhstvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 160 EPTAGLDPeerIRFRNL--LADFANERL---VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK11831 169 EPFVGQDP---ITMGVLvkLISELNSALgvtCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-212 |
8.93e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.52 E-value: 8.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 19 PALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILttlekptSGKVLVDG----------------TPLKD---------AR 72
Cdd:PRK11147 17 PLLDNAELHIEDNeRVCLVGRNGAGKSTLMKIL-------NGEVLLDDgriiyeqdlivarlqqDPPRNvegtvydfvAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 73 SIRRKIGYLPQ------QFGFYPTMKVIDAMTYL-AILAEVPAREQKRRIEWLLAAVHLTAQakTKVKALSGGMLQRLGI 145
Cdd:PRK11147 90 GIEEQAEYLKRyhdishLVETDPSEKNLNELAKLqEQLDHHNLWQLENRINEVLAQLGLDPD--AALSSLSGGWLRKAAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491943749 146 AQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFaNERLVLLStHIVSDVEATTNRIGILDHGRLV 212
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF-QGSIIFIS-HDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
37-168 |
1.15e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.72 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 37 GKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSIRRkIGYLpqqfGFYPTMKV-IDAMTYLAILAEVPAREQKRRI 115
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRF-MAYL----GHLPGLKAdLSTLENLHFLCGLHGRRAKQMP 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 491943749 116 EWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPE 168
Cdd:PRK13543 119 GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-222 |
1.73e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.80 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 5 QIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLV---DGTPLKDAR---SIRRK 77
Cdd:PRK11701 8 SVRGLTKLYGPRK--GCRDVSFDLYPGeVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYAlseAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 78 I-----GYLPQqfgfYPT----MKV------------IDAMTYLAILAEvpAREQKRRIEwlLAAVHLTAQAKTkvkaLS 136
Cdd:PRK11701 86 LlrtewGFVHQ----HPRdglrMQVsaggnigerlmaVGARHYGDIRAT--AGDWLERVE--IDAARIDDLPTT----FS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 137 GGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRF----RNLLADFaneRL-VLLSTHIVSDVEATTNRIGILDHGRL 211
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLldllRGLVREL---GLaVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
250
....*....|.
gi 491943749 212 VFNGTTDELID 222
Cdd:PRK11701 231 VESGLTDQVLD 241
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-183 |
1.90e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.20 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 34 GLLGKNGAGKSTLMKILTTLEKPTSGKVLVD-----------GTPLKD------ARSIR--RKIGY---LPQQFgfypTM 91
Cdd:COG1245 103 GILGPNGIGKSTALKILSGELKPNLGDYDEEpswdevlkrfrGTELQDyfkklaNGEIKvaHKPQYvdlIPKVF----KG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 92 KVIDamtylaILAEVPAREQKRRIEWLLAAVHLTAQaktKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERI 171
Cdd:COG1245 179 TVRE------LLEKVDERGKLDELAEKLGLENILDR---DISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRL 249
|
170
....*....|..
gi 491943749 172 RFRNLLADFANE 183
Cdd:COG1245 250 NVARLIRELAEE 261
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
35-219 |
1.92e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 35 LLGKNGAGKSTLMKILTTLeKPTSGKVLVDGTPLKD--ARSIRRKIGYLPQQFGFYPTMKVIDamtYLAIL--AEVPARE 110
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAwsAAELARHRAYLSQQQTPPFAMPVFQ---YLTLHqpDKTRTEA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 111 QKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVN-------EPRVLIVDEPTAGLDPEERIRFRNLLADFANE 183
Cdd:PRK03695 103 VASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQ 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 491943749 184 -RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDE 219
Cdd:PRK03695 183 gIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-172 |
2.38e-13 |
|
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: 68.20 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSG------MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDgtplkdarsiRRKIGYLPQQfgfyptMKVI 94
Cdd:cd03237 10 LGEFTLEVEGGsiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE----------LDTVSYKPQY------IKAD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 95 DAMTYLAILAEVPAR--EQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIR 172
Cdd:cd03237 74 YEGTVRDLLSSITKDfyTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-211 |
2.84e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 23 HVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDG---TPLKDARSIRRKIGYLP---QQFGFYptmkvID 95
Cdd:PRK15439 281 NISLEVRAGeILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGkeiNALSTAQRLARGLVYLPedrQSSGLY-----LD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 96 AMTYLAILAEV---------PAREqKRRIEWLLAAVHLT-AQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGL 165
Cdd:PRK15439 356 APLAWNVCALThnrrgfwikPARE-NAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491943749 166 DPEERIRFRNLLADFANERLVLLstHIVSD---VEATTNRIGILDHGRL 211
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVL--FISSDleeIEQMADRVLVMHQGEI 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-174 |
2.85e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTI-QIEQLVKHYRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KDarS 73
Cdd:PRK10762 1 MQALlQLKGIDKAFPGVK--ALSGAALNVYPGrVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpKS--S 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 74 IRRKIGYLPQQFGFYPTMkVIDAMTYLailaevpAREQKR---RIEW---------LLAAVHLTAQAKTKVKALSGGMLQ 141
Cdd:PRK10762 77 QEAGIGIIHQELNLIPQL-TIAENIFL-------GREFVNrfgRIDWkkmyaeadkLLARLNLRFSSDKLVGELSIGEQQ 148
|
170 180 190
....*....|....*....|....*....|....
gi 491943749 142 RLGIAQALVNEPRVLIVDEPTAGL-DPEERIRFR 174
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDALtDTETESLFR 182
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
35-215 |
2.96e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.91 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 35 LLGKNGAGKSTLMKILTTLEKPTS--GKVLVDGTplKDARSIRRKIGYLPQQFGFYPTMKVIDAMTYLAILaEVP---AR 109
Cdd:PLN03211 99 VLGPSGSGKSTLLNALAGRIQGNNftGTILANNR--KPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLL-RLPkslTK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 110 EQKRRI------EWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANE 183
Cdd:PLN03211 176 QEKILVaesvisELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK 255
|
170 180 190
....*....|....*....|....*....|....
gi 491943749 184 -RLVLLSTHIVSD-VEATTNRIGILDHGRLVFNG 215
Cdd:PLN03211 256 gKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-219 |
3.08e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 68.27 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNI-QSGMYGLLGKNGAGKSTLMKILTTLEK--PT---SGKVLVDGTPLKDAR----SIRRKIGYLPQQFGFYP 89
Cdd:PRK14243 25 AVKNVWLDIpKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPDvdpvEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 90 TmKVIDAMTYLAI-------LAEVPAREQKRRIEWllaavhltAQAKTKVK----ALSGGMLQRLGIAQALVNEPRVLIV 158
Cdd:PRK14243 105 K-SIYDNIAYGARingykgdMDELVERSLRQAALW--------DEVKDKLKqsglSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 159 DEPTAGLDPEERIRFRNLLADFANERLVLLSTH------IVSDVEA--------TTNRIGIL---DHGRLVFNGTTDE 219
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHnmqqaaRVSDMTAffnvelteGGGRYGYLvefDRTEKIFNSPQQQ 253
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-229 |
3.24e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.49 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 18 QPALDHVSLNIQSGMY-GLLGKNGAGKSTLMK-ILTTLekPTSGKVLVDGTPLK--DARSIRRKIGYLPQ--QFgFYPTM 91
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRiALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIELRelDPESWRKHLSWVGQnpQL-PHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 92 KviDAMTylaiLAEVPAREQkrRIEWLLAAvhltAQAKTKVKA---------------LSGGMLQRLGIAQALVNEPRVL 156
Cdd:PRK11174 440 R--DNVL----LGNPDASDE--QLQQALEN----AWVSEFLPLlpqgldtpigdqaagLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 157 IVDEPTAGLD--PEERIrfRNLLADFANERLVLLSTHIVSDVEAtTNRIGILDHGRLVFNGTTDELidAAAGHVF 229
Cdd:PRK11174 508 LLDEPTASLDahSEQLV--MQALNAASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAEL--SQAGGLF 577
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-226 |
3.29e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.31 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 16 RQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILT-TLEKP-------TSGKVLVDGTPLK--DARSIRRKIGYLPQQ 84
Cdd:PRK13547 12 RHRAILRDLSLRIEPGrVTALLGRNGAGKSTLLKALAgDLTGGgaprgarVTGDVTLNGEPLAaiDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 85 ----FGFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVN--------- 151
Cdd:PRK13547 92 aqpaFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 152 EPRVLIVDEPTAGLDPEERIRFRNLLADFANE-RLVLLSthIVSDVEAT---TNRIGILDHGRLVFNGT-----TDELID 222
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLA--IVHDPNLAarhADRIAMLADGAIVAHGApadvlTPAHIA 249
|
....
gi 491943749 223 AAAG 226
Cdd:PRK13547 250 RCYG 253
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-250 |
3.96e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.11 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDG-------TPLKDARSIRRKIGYL---PQQFGFY 88
Cdd:PRK13645 26 ALNNTSLTFKKNkVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRLRKEIGLVfqfPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 89 PTMKVIDAMTYLAILAEvpAREQKRRIEWLLAAVHLTAQ-AKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDP 167
Cdd:PRK13645 106 ETIEKDIAFGPVNLGEN--KQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 168 EERIRFRNLLADFANE--RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIdaaAGHVFVGDLPVAQLKQFKTQY 245
Cdd:PRK13645 184 KGEEDFINLFERLNKEykKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF---SNQELLTKIEIDPPKLYQLMY 260
|
....*
gi 491943749 246 QISEQ 250
Cdd:PRK13645 261 KLKNK 265
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-166 |
5.43e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.01 E-value: 5.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEK--PTSGKVLVDGTPLKDA----RSiRRKIGYlpqqfGF-YPT-- 90
Cdd:COG0396 16 LKGVNLTIKPGeVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELspdeRA-RAGIFL-----AFqYPVei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 91 --MKVID----AMTylAI-LAEVPAREQKRRIEWLLAAVHLTAQ-AKTKVKA-LSGGMLQRLGIAQALVNEPRVLIVDEP 161
Cdd:COG0396 90 pgVSVSNflrtALN--ARrGEELSAREFLKLLKEKMKELGLDEDfLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDET 167
|
....*
gi 491943749 162 TAGLD 166
Cdd:COG0396 168 DSGLD 172
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-215 |
6.91e-13 |
|
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: 66.01 E-value: 6.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSGM-YGLLGKNGAGKSTLMKILTTLE--KPTSGKVLVDGTPLKDA----RSiRRKIGYLPQqfgfYPtmkv 93
Cdd:cd03217 16 LKGVNLTIKKGEvHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLppeeRA-RLGIFLAFQ----YP---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 94 idamtylailAEVPAreqkRRIEWLLAAVHltaqaktkvKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDpeerIRF 173
Cdd:cd03217 87 ----------PEIPG----VKNADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD----IDA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491943749 174 RNLLADFANERL-----VLLSTH---IVSDVEAttNRIGILDHGRLVFNG 215
Cdd:cd03217 140 LRLVAEVINKLReegksVLIITHyqrLLDYIKP--DRVHVLYDGRIVKSG 187
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-212 |
9.10e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 9.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 16 RQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGT-----PLKDARSIRRKIGYLPQQ--FGF 87
Cdd:PRK10261 335 REVHAVEKVSFDLWPGeTLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlSPGKLQALRRDIQFIFQDpyASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 88 YPTMKVIDA-MTYLAILAEVPAREQKRRIEWLLAAVHLTAQ-AKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGL 165
Cdd:PRK10261 415 DPRQTVGDSiMEPLRVHGLLPGKAAAARVAWLLERVGLLPEhAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491943749 166 DPEERIRFRNLLADFANERLV--LLSTHIVSDVEATTNRIGILDHGRLV 212
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
12-221 |
9.97e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.20 E-value: 9.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 12 HYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDAR--SIRRKIGYLPQQ-FGF 87
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGqMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldSWRSRLAVVSQTpFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 88 YPTMKVIDAmtylaiLAEVPAREQKrrIEWL--LAAVH-----LTAQAKTKVKA----LSGGMLQRLGIAQALVNEPRVL 156
Cdd:PRK10789 402 SDTVANNIA------LGRPDATQQE--IEHVarLASVHddilrLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 157 IVDEPTAGLDPEERIRFRNLLADFANERLVLLSTHIVSD-VEAttNRIGILDHGRLVFNGTTDELI 221
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSAlTEA--SEILVMQHGHIAQRGNHDQLA 537
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-194 |
1.75e-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: 67.27 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRqqPALDHVSLNI-QSGMYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPlkdarsirrKIGYLP 82
Cdd:TIGR03719 323 IEAENLTKAFGDK--LLIDDLSFKLpPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV---------KLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 QQF-GFYPTMKVIDAMTY-LAIL----AEVPAREQKRRIEWllaavHLTAQAKtKVKALSGGMLQRLGIAQALVNEPRVL 156
Cdd:TIGR03719 392 QSRdALDPNKTVWEEISGgLDIIklgkREIPSRAYVGRFNF-----KGSDQQK-KVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491943749 157 IVDEPTAGLDPEERIRFRNLLADFANERLVL---------LSTHIVS 194
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEALLNFAGCAVVIshdrwfldrIATHILA 512
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
33-225 |
2.31e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.84 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 33 YGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTplkdarsirRKIGYLPQ-QFGfYPTMKVIDA--MTYLAILAevpAR 109
Cdd:PRK15064 30 YGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPN---------ERLGKLRQdQFA-FEEFTVLDTviMGHTELWE---VK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 110 EQKRRIEWL--------LAAVHL----------TAQAKtkvkalSGGMLQRLGI----------------------AQAL 149
Cdd:PRK15064 97 QERDRIYALpemseedgMKVADLevkfaemdgyTAEAR------AGELLLGVGIpeeqhyglmsevapgwklrvllAQAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 150 VNEPRVLIVDEPTAGLDPEErIRFrnlLADFANER---LVLLS----------THiVSDveattnrigiLDHGRL-VFNG 215
Cdd:PRK15064 171 FSNPDILLLDEPTNNLDINT-IRW---LEDVLNERnstMIIIShdrhflnsvcTH-MAD----------LDYGELrVYPG 235
|
250
....*....|
gi 491943749 216 TTDELIDAAA 225
Cdd:PRK15064 236 NYDEYMTAAT 245
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-191 |
3.13e-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: 66.50 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 17 QQPALDHVSLNIQSGM-YGLLGKNGAGKSTLMKILTTLEKPTSGKVLvdgtPLKDArsirrKIGYLPQQFGFYPTMKV-- 93
Cdd:TIGR03719 17 KKEILKDISLSFFPGAkIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR----PQPGI-----KVGYLPQEPQLDPTKTVre 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 94 ---------IDAMTYL----AILAEVPA------REQKRRIEWLLAA--------VHLTAQA------KTKVKALSGGML 140
Cdd:TIGR03719 88 nveegvaeiKDALDRFneisAKYAEPDAdfdklaAEQAELQEIIDAAdawdldsqLEIAMDAlrcppwDADVTKLSGGER 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491943749 141 QRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANErlVLLSTH 191
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGT--VVAVTH 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-225 |
3.97e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.11 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 22 DHVSLNIQSG-MYGLLGKNGAGKSTLMK-ILTTLEKPTSGKVLVDGTPLK---DARSIRRKIGYLPQ---QFGFYPTMKV 93
Cdd:PRK13549 279 DDVSFSLRRGeILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKirnPQQAIAQGIAMVPEdrkRDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 94 IDAMTyLAILAEVP-------AREQKRrIEWLLAAVHL-TAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGL 165
Cdd:PRK13549 359 GKNIT-LAALDRFTggsriddAAELKT-ILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943749 166 DPEERIRFRNLLADFANE--RLVLLSTHIvSDVEATTNRIGILDHGRL----VFNGTTDELIDAAA 225
Cdd:PRK13549 437 DVGAKYEIYKLINQLVQQgvAIIVISSEL-PEVLGLSDRVLVMHEGKLkgdlINHNLTQEQVMEAA 501
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3-196 |
4.82e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYRGrQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSiRRKIGYL 81
Cdd:PRK15056 6 GIVVNDVTVTWRN-GHTALRDASFTVPGGsIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ-KNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 82 PQQ----FGFYPTMKVIDAMTYLAILA--EVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRV 155
Cdd:PRK15056 84 PQSeevdWSFPVLVEDVVMMGRYGHMGwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491943749 156 LIVDEPTAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDV 196
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSV 205
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-212 |
5.17e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.09 E-value: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 10 VKHYRGRQQ------------PALDH-VSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KD 70
Cdd:PRK11288 245 IYGYRPRPLgevrlrldglkgPGLREpISFSVRAGeIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirspRD 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 71 ArsIRRKIGYLPQ---QFGFYPTMKVIDAMTylailaeVPAREQKRRIEWLL--------AAVHL------TAQAKTKVK 133
Cdd:PRK11288 325 A--IRAGIMLCPEdrkAEGIIPVHSVADNIN-------ISARRHHLRAGCLInnrweaenADRFIrslnikTPSREQLIM 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 134 ALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRLV 212
Cdd:PRK11288 396 NLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-225 |
7.32e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.50 E-value: 7.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHYR--GRQQPALDHVSLNIQSG-MYGLLGKNGAGKS-TLMKILTTLEKP----TSGKVLVDGTPLKDA- 71
Cdd:PRK15134 3 QPLLAIENLSVAFRqqQTVRTVVNDVSLQIEAGeTLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHAs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 72 ----RSIR-RKIGYLPQQfgfyPTMKVIDAMTYLAILAEVPA-----REQKRRIEWL--LAAVHLTaQAKTKVKA----L 135
Cdd:PRK15134 83 eqtlRGVRgNKIAMIFQE----PMVSLNPLHTLEKQLYEVLSlhrgmRREAARGEILncLDRVGIR-QAAKRLTDyphqL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 136 SGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANE--RLVLLSTHIVSDVEATTNRIGILDHGRLVF 213
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElnMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
250
....*....|..
gi 491943749 214 NGTTDELIDAAA 225
Cdd:PRK15134 238 QNRAATLFSAPT 249
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-215 |
8.01e-12 |
|
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: 63.05 E-value: 8.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 19 PALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPT---SGKVLVDGTPLKDARSI-RRKIGYLPQQFGFYPTMKV 93
Cdd:cd03233 21 PILKDFSGVVKPGeMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKyPGEIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 94 idamtylailaevpaREqkrriewLLAAVhLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRF 173
Cdd:cd03233 101 ---------------RE-------TLDFA-LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491943749 174 RNLLADFANerlVLLSTHIVS------DVEATTNRIGILDHGRLVFNG 215
Cdd:cd03233 158 LKCIRTMAD---VLKTTTFVSlyqasdEIYDLFDKVLVLYEGRQIYYG 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-225 |
1.63e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.46 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSG-MYGLLGKNGAGKSTLMK-ILTTLEKPTSGKVLVDGTPL---KDARSIRRKIGYLPQ---QFGFYPTMK 92
Cdd:TIGR02633 276 VDDVSFSLRRGeILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVdirNPAQAIRAGIAMVPEdrkRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 93 V-----IDAMTYLAILAEVPAREQKRRIEWLLAAVHL-TAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLD 166
Cdd:TIGR02633 356 VgknitLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 167 PEERIRFRNLLADFANE--RLVLLSTHIvSDVEATTNRIGILDHGRL----VFNGTTDELIDAAA 225
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEgvAIIVVSSEL-AEVLGLSDRVLVIGEGKLkgdfVNHALTQEQVLAAA 499
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-191 |
2.48e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.74 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 22 DHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDAR-SIRRKIGYLPQQFGFYPTMKVIDAMTY 99
Cdd:PRK13538 18 SGLSFTLNAGeLVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRdEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 100 LAILAEVPAREQKRRIewlLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLAD 179
Cdd:PRK13538 98 YQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
170
....*....|....
gi 491943749 180 FAnER--LVLLSTH 191
Cdd:PRK13538 175 HA-EQggMVILTTH 187
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-198 |
1.48e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 59.50 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 37 GKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARsiRRKIGYLPQQFGFYPTMKVIDAMTYLAilaevparEQKRRIE 116
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--KPYCTYIGHNLGLKLEMTVFENLKFWS--------EIYNSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 117 WLLAAVH---LTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANE-RLVLLSTHI 192
Cdd:PRK13541 103 TLYAAIHyfkLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSgGIVLLSSHL 182
|
....*.
gi 491943749 193 VSDVEA 198
Cdd:PRK13541 183 ESSIKS 188
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-179 |
1.48e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 61.75 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQL-VKHYRGRqqPALDHVSLNIQSGMyGLL--GKNGAGKSTLMKILTTLEKPTSGKVLVdgtPlKDARSIrrkig 79
Cdd:COG4178 362 ALALEDLtLRTPDGR--PLLEDLSLSLKPGE-RLLitGPSGSGKSTLLRAIAGLWPYGSGRIAR---P-AGARVL----- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQQfgfyPTMKV---IDAMTYLAILAEVPAREqkrrIEWLLAAV---HLTAQAKTKV---KALSGGMLQRLGIAQALV 150
Cdd:COG4178 430 FLPQR----PYLPLgtlREALLYPATAEAFSDAE----LREALEAVglgHLAERLDEEAdwdQVLSLGEQQRLAFARLLL 501
|
170 180
....*....|....*....|....*....
gi 491943749 151 NEPRVLIVDEPTAGLDPEERIRFRNLLAD 179
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-191 |
1.57e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVdGTPLKdarsirrkIGYLPQqfgfY-----PTMKVI 94
Cdd:PRK11147 335 VKDFSAQVQRGdKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLE--------VAYFDQ----HraeldPEKTVM 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 95 DAmtylaiLAE----VPAREQKRRI-----EWLLAAvhltAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGL 165
Cdd:PRK11147 402 DN------LAEgkqeVMVNGRPRHVlgylqDFLFHP----KRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
170 180
....*....|....*....|....*.
gi 491943749 166 DPEERIRFRNLLADFanERLVLLSTH 191
Cdd:PRK11147 472 DVETLELLEELLDSY--QGTVLLVSH 495
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-225 |
1.60e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 10 VKHYRGrqqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKdARS----IRRKIGYLPQQ 84
Cdd:PRK10762 260 VDNLSG---PGVNDVSFTLRKGeILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV-TRSpqdgLANGIVYISED 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 85 F---GFYPTMKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHL-------TAQAKTKVKALSGGMLQRLGIAQALVNEPR 154
Cdd:PRK10762 336 RkrdGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFirlfnikTPSMEQAIGLLSGGNQQKVAIARGLMTRPK 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491943749 155 VLIVDEPTAGLDPEERIRFRNLLADFANERL--VLLSTHIvSDVEATTNRIGILDHGRLV--FNGT--TDELIDAAA 225
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQLINQFKAEGLsiILVSSEM-PEVLGMSDRILVMHEGRISgeFTREqaTQEKLMAAA 491
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-168 |
2.06e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.29 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 15 GRQQPALDHVSLNIQSGM-YGLLGKNGAGKSTLMKILTTLEKPTSGK-VLVDGTplkdarsirrKIGYLPQ--------- 83
Cdd:PRK11819 17 PPKKQILKDISLSFFPGAkIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGI----------KVGYLPQepqldpekt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 84 -----QFGFYPTMKVID-----------AMTYLAILAEVPAREQK-----------RRIEWLLAAVHLTAqAKTKVKALS 136
Cdd:PRK11819 87 vrenvEEGVAEVKAALDrfneiyaayaePDADFDALAAEQGELQEiidaadawdldSQLEIAMDALRCPP-WDAKVTKLS 165
|
170 180 190
....*....|....*....|....*....|..
gi 491943749 137 GGMLQRLGIAQALVNEPRVLIVDEPTAGLDPE 168
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAE 197
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
30-170 |
2.43e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 60.27 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 30 SGMYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARS-I-----RRKIGYLPQQFGFYPTMKVIDAMTYLaiL 103
Cdd:PRK11144 24 QGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgIclppeKRRIGYVFQDARLFPHYKVRGNLRYG--M 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 104 AEVpAREQKRRIEWLLAAVHLTAQAKTkvkALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLD-PEER 170
Cdd:PRK11144 102 AKS-MVAQFDKIVALLGIEPLLDRYPG---SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKR 165
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-223 |
2.73e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.14 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 1 MTTIQIEQLVKHYRGRQQP--ALDHVSLNIQSG-MYGLLGKNGAGKS----TLMKILTTLEKPTSGKVLVDGTPLKDARS 73
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPfrAVDRISYSVKQGeVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 74 IRRKigylpQQFGFYPTMKVIDAMTYL--------AILAEVPA------REQKRRIEWLLAAVHLTAQA-KTKV--KALS 136
Cdd:PRK11022 81 KERR-----NLVGAEVAMIFQDPMTSLnpcytvgfQIMEAIKVhqggnkKTRRQRAIDLLNQVGIPDPAsRLDVypHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 137 GGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFA---NERLVLLsTHIVSDVEATTNRIGILDHGRLVF 213
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqkeNMALVLI-THDLALVAEAAHKIIVMYAGQVVE 234
|
250
....*....|
gi 491943749 214 NGTTDELIDA 223
Cdd:PRK11022 235 TGKAHDIFRA 244
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-191 |
2.89e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.20 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 13 YRGRQQPALDHVSLNIQSGMYGLL-GKNGAGKSTLMKILTTLEK--PTSGKVLVDGTPlkdarsirrkigylpqqfgFYP 89
Cdd:COG2401 38 LRVVERYVLRDLNLEIEPGEIVLIvGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ-------------------FGR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 90 TMKVIDAmtyLAILAEVPAReqkrrIEwLLAAVHL-TAQA-KTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDP 167
Cdd:COG2401 99 EASLIDA---IGRKGDFKDA-----VE-LLNAVGLsDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180
....*....|....*....|....*..
gi 491943749 168 EERIRFRNLLADFANER---LVLLSTH 191
Cdd:COG2401 170 QTAKRVARNLQKLARRAgitLVVATHH 196
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-223 |
3.21e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.82 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKpTSGKVLVDGTPLKD-------ARSIRRKIG------YLPQQF 85
Cdd:PRK15093 22 AVDRVSMTLTEGeIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDidllrlsPRERRKLVGhnvsmiFQEPQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 86 GFYPT-------MKVIDAMTYLAILAEVPAREQKRRIEwLLAAVHLTAQaKTKVKA----LSGGMLQRLGIAQALVNEPR 154
Cdd:PRK15093 101 CLDPServgrqlMQNIPGWTYKGRWWQRFGWRKRRAIE-LLHRVGIKDH-KDAMRSfpyeLTEGECQKVMIAIALANQPR 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491943749 155 VLIVDEPTAGLDPEERIRFRNLLADF--ANERLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDA 223
Cdd:PRK15093 179 LLIADEPTNAMEPTTQAQIFRLLTRLnqNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTT 249
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-169 |
3.26e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.51 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-----KDArsIRRKIGYLPQQFGFYPTMKV 93
Cdd:PRK10982 13 ALDNVNLKVRPHsIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkssKEA--LENGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 94 IDAMTylaiLAEVPAR-----EQK--RRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLD 166
Cdd:PRK10982 91 MDNMW----LGRYPTKgmfvdQDKmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
...
gi 491943749 167 PEE 169
Cdd:PRK10982 167 EKE 169
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-166 |
4.04e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.10 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSG-MYGLLGKNGAGKST----LMKILttlekPTSGKVLVDGTPL-----KDARSIRRKIGYLPQQfgfyP 89
Cdd:PRK15134 301 VVKNISFTLRPGeTLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLhnlnrRQLLPVRHRIQVVFQD----P 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 90 TMKVIDAMTYLAILAE--------VPAREQKRRIEWLLAAVHLTAQAKTKVKA-LSGGMLQRLGIAQALVNEPRVLIVDE 160
Cdd:PRK15134 372 NSSLNPRLNVLQIIEEglrvhqptLSAAQREQQVIAVMEEVGLDPETRHRYPAeFSGGQRQRIAIARALILKPSLIILDE 451
|
....*.
gi 491943749 161 PTAGLD 166
Cdd:PRK15134 452 PTSSLD 457
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-221 |
4.32e-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: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSGM-YGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGT-----PLKDARSIRRK 77
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQkVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIdisklPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 78 IGYLPQ------QFGFYPTMKVIDAMTYLAIlaEVpareqkrriewllaavhltAQAKTKVKALSGGM------------ 139
Cdd:cd03288 100 ILQDPIlfsgsiRFNLDPECKCTDDRLWEAL--EI-------------------AQLKNMVKSLPGGLdavvteggenfs 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 140 ---LQRLGIAQALVNEPRVLIVDEPTAGLD-PEERIRFRNLLADFAnERLVLLSTHIVSDVeATTNRIGILDHGRLVFNG 215
Cdd:cd03288 159 vgqRQLFCLARAFVRKSSILIMDEATASIDmATENILQKVVMTAFA-DRTVVTIAHRVSTI-LDADLVLVLSRGILVECD 236
|
....*.
gi 491943749 216 TTDELI 221
Cdd:cd03288 237 TPENLL 242
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-233 |
6.38e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.80 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVdgtplkdARSIrrKIGYLPQ-QFGFYPTMKviDAMT 98
Cdd:PRK10636 328 LDSIKLNLVPGsRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-------AKGI--KLGYFAQhQLEFLRADE--SPLQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 99 YLAILAEvpaREQKRRIEWLLAAVHLTAQAKTKVKA-LSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLL 177
Cdd:PRK10636 397 HLARLAP---QELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 178 ADFANErLVLLSthivsdveattnrigildHGRLVFNGTTDELIDAAAGHV--FVGDL 233
Cdd:PRK10636 474 IDFEGA-LVVVS------------------HDRHLLRSTTDDLYLVHDGKVepFDGDL 512
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-211 |
7.98e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 10 VKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDG---TPLKDARSIRRKIGYLPQ-- 83
Cdd:PRK09700 268 VRNVTSRDRKKVRDISFSVCRGeILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdiSPRSPLDAVKKGMAYITEsr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 84 -QFGFYPTMKVIDAMT---------YLAILAEVPAREQKRRIEWLLAAVHLT-AQAKTKVKALSGGMLQRLGIAQALVNE 152
Cdd:PRK09700 348 rDNGFFPNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 153 PRVLIVDEPTAGLDPEERIRFRNLLADFANE-RLVLLSTHIVSDVEATTNRIGILDHGRL 211
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-221 |
8.96e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.75 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQ-SGMYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD--ARSIRRKIGY 80
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISpSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfgLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 81 LPQ---------QFGFYPTMKVIDAMTYLAiLAEVPAREQKRRiewllAAVHLTAQAKTKVKALSGGMLQRLGIAQALVN 151
Cdd:PLN03130 1318 IPQapvlfsgtvRFNLDPFNEHNDADLWES-LERAHLKDVIRR-----NSLGLDAEVSEAGENFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 152 EPRVLIVDEPTAGLDP------EERIR--FRNLLADFANERlvlLSTHIVSDveattnRIGILDHGRLVFNGTTDELI 221
Cdd:PLN03130 1392 RSKILVLDEATAAVDVrtdaliQKTIReeFKSCTMLIIAHR---LNTIIDCD------RILVLDAGRVVEFDTPENLL 1460
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-210 |
1.29e-09 |
|
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: 56.71 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 19 PALDHVSLNIQSG-MYGLLGKNGAGKSTL-MKILTTLEKpTSGKVLVDGTplkdarsirrkIGYLPQQ------------ 84
Cdd:cd03250 19 FTLKDINLEVPKGeLVAIVGPVGSGKSSLlSALLGELEK-LSGSVSVPGS-----------IAYVSQEpwiqngtireni 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 85 -FG--FYPTM--KVIDAMTYLAILAEVPAREQkrriewllaavhltaqakTKVK----ALSGGMLQRLGIAQALVNEPRV 155
Cdd:cd03250 87 lFGkpFDEERyeKVIKACALEPDLEILPDGDL------------------TEIGekgiNLSGGQKQRISLARAVYSDADI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491943749 156 LIVDEPTAGLDP--EERIrFRNLLADF-ANERLVLLSTHIVSDVEAtTNRIGILDHGR 210
Cdd:cd03250 149 YLLDDPLSAVDAhvGRHI-FENCILGLlLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-177 |
1.74e-09 |
|
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: 55.62 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSGMYGLL-GKNGAGKSTLMKILT--------TLEKPTSGKVLvdgtplkdarsirrkigYLPQQfgfyptm 91
Cdd:cd03223 17 LKDLSFEIKPGDRLLItGPSGTGKSSLFRALAglwpwgsgRIGMPEGEDLL-----------------FLPQR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 92 kvidamTYLAI--LAEV---PareqkrrieWLlaavhltaqaktkvKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLD 166
Cdd:cd03223 73 ------PYLPLgtLREQliyP---------WD--------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170
....*....|.
gi 491943749 167 PEERIRFRNLL 177
Cdd:cd03223 124 EESEDRLYQLL 134
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-177 |
4.05e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.29 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYrGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDArsirrKIGYL 81
Cdd:PRK10522 322 TLELRNVTFAY-QDNGFSVGPINLTIKRGeLLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE-----QPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 82 PQQFG-----FYPTMKVIDamtylailAEVPAREQKRRIEWLlaaVHLTAQAKTKVK-------ALSGGMLQRLGIAQAL 149
Cdd:PRK10522 396 RKLFSavftdFHLFDQLLG--------PEGKPANPALVEKWL---ERLKMAHKLELEdgrisnlKLSKGQKKRLALLLAL 464
|
170 180
....*....|....*....|....*....
gi 491943749 150 VNEPRVLIVDEPTAGLDPE-ERIRFRNLL 177
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHfRREFYQVLL 493
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-191 |
5.66e-09 |
|
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: 55.84 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 34 GLLGKNGAGKSTLMKILTTLEKPTSGKV--------LVD---GTPL---------KDARSIRrKIGY---LPQQFgfypT 90
Cdd:cd03236 30 GLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDefrGSELqnyftklleGDVKVIV-KPQYvdlIPKAV----K 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 91 MKVIDamtylaILAEVPAREQKrriEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEER 170
Cdd:cd03236 105 GKVGE------LLKKKDERGKL---DELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180
....*....|....*....|..
gi 491943749 171 IRFRNLLADFANE-RLVLLSTH 191
Cdd:cd03236 176 LNAARLIRELAEDdNYVLVVEH 197
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
35-166 |
8.28e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.78 E-value: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 35 LLGKNGAGKSTLMKILTTLEKP--TSGKVLVDGTPlKDARSIRRKIGYLPQQFGFYPTMKVIDAMTYLAIL---AEVPAR 109
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFP-KKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLrlpKEVSKE 989
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491943749 110 EQKRRIEWLLAAVHLTAQAKT-----KVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLD 166
Cdd:PLN03140 990 EKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-223 |
1.10e-08 |
|
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: 56.11 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 11 KHYRGRQQPALD----HVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDA--RSIRRKIGYLPQ 83
Cdd:TIGR00957 1288 RNYCLRYREDLDlvlrHINVTIHGGeKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIglHDLRFKITIIPQ 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 84 Q--------------FGFYPTMKVIDAMTYLAILAEVPAREQKrriewllaavhLTAQAKTKVKALSGGMLQRLGIAQAL 149
Cdd:TIGR00957 1368 DpvlfsgslrmnldpFSQYSDEEVWWALELAHLKTFVSALPDK-----------LDHECAEGGENLSVGQRQLVCLARAL 1436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491943749 150 VNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTHIVSDVEATTnRIGILDHGRLVFNGTTDELIDA 223
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-168 |
1.66e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQqpALDHVSLNI-QSGMYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPlkdarsirrKIGYLP 82
Cdd:PRK11819 325 IEAENLSKSFGDRL--LIDDLSFSLpPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV---------KLAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 QQ--------------FGFYPTMKVIDamtylailAEVPAR------------EQKrriewllaavhltaqaktKVKALS 136
Cdd:PRK11819 394 QSrdaldpnktvweeiSGGLDIIKVGN--------REIPSRayvgrfnfkggdQQK------------------KVGVLS 447
|
170 180 190
....*....|....*....|....*....|..
gi 491943749 137 GGMLQRLGIAQALVNEPRVLIVDEPTAGLDPE 168
Cdd:PRK11819 448 GGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
58-226 |
2.86e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 58 SGKVLVDGTP-----LKDARSIRRKIGYLPQQFgfypTMKVIDAMTYLAilaEVPAREQKRRIEwLLAAV-----HLTAQ 127
Cdd:PTZ00265 1276 SGKILLDGVDicdynLKDLRNLFSIVSQEPMLF----NMSIYENIKFGK---EDATREDVKRAC-KFAAIdefieSLPNK 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 128 AKTKV----KALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFAN--ERLVLLSTHIVSDVEaTTN 201
Cdd:PTZ00265 1348 YDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIK-RSD 1426
|
170 180 190
....*....|....*....|....*....|
gi 491943749 202 RIGILDH----GRLV-FNGTTDELIDAAAG 226
Cdd:PTZ00265 1427 KIVVFNNpdrtGSFVqAHGTHEELLSVQDG 1456
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-193 |
3.40e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.53 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 6 IEQLVKHYRGRQQPALDHVSLNIQSGM-YGLLGKNGAGKSTLMKILTTLEKpTSGKVLVDGTPLKDA--RSIRRKIGYLP 82
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAVLQDLSFSVEGGQrVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVtlQTWRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 QQ-FGFYPTM----------------KVIDAMTYLAILAEVPAReqkrriewllaavhLTAQAKTKVKALSGGMLQRLGI 145
Cdd:TIGR01271 1299 QKvFIFSGTFrknldpyeqwsdeeiwKVAEEVGLKSVIEQFPDK--------------LDFVLVDGGYVLSNGHKQLMCL 1364
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491943749 146 AQALVNEPRVLIVDEPTAGLDP-EERIRFRNLLADFANeRLVLLSTHIV 193
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPvTLQIIRKTLKQSFSN-CTVILSEHRV 1412
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
34-220 |
4.02e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.57 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 34 GLLGKNGAGKS----TLMKILTTLEKpTSGKVLVDGT-----PLKDARSIR-RKIGYLPQQ--FGFYPTMKVIDAMTYLA 101
Cdd:PRK09473 46 GIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGReilnlPEKELNKLRaEQISMIFQDpmTSLNPYMRVGEQLMEVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 102 IL----AEVPAREQKRRiewLLAAVHLtAQAKTKVK----ALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRF 173
Cdd:PRK09473 125 MLhkgmSKAEAFEESVR---MLDAVKM-PEARKRMKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQI 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491943749 174 RNLLADFANE--RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDEL 220
Cdd:PRK09473 201 MTLLNELKREfnTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
114-239 |
5.27e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 114 RIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTH 191
Cdd:PRK10938 115 RCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGitLVLVLNR 194
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 491943749 192 IvSDVEATTNRIGILDHGRLVFNGTTDELIDAAAghvfvgdlpVAQLK 239
Cdd:PRK10938 195 F-DEIPDFVQFAGVLADCTLAETGEREEILQQAL---------VAQLA 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-221 |
5.38e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.21 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 3 TIQIEQLVKHYRGRQQPALDHVSLNIQ-SGMYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKD--ARSIRRKIG 79
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPVLHGLSFFVSpSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 80 YLPQ---------QFGFYPTMKVIDAMTYLAiLAEVPAREQKRRiewllAAVHLTAQAKTKVKALSGGMLQRLGIAQALV 150
Cdd:PLN03232 1314 IIPQspvlfsgtvRFNIDPFSEHNDADLWEA-LERAHIKDVIDR-----NPFGLDAEVSEGGENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 151 NEPRVLIVDEPTAGLDpeerIRFRNLLADFANERL----VLLSTHIVSDVeATTNRIGILDHGRLVFNGTTDELI 221
Cdd:PLN03232 1388 RRSKILVLDEATASVD----VRTDSLIQRTIREEFksctMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-219 |
5.45e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTT----LEKPTSGKVLVDGTPLKD-ARSIRRKIGYLPQQFGFYPTMKVI 94
Cdd:TIGR00956 77 LKPMDGLIKPGeLTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGITPEEiKKHYRGDVVYNAETDVHFPHLTVG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 95 DAMTYLAILAEVPAREQ--------KRRIEWLLAAVHLTAQAKTKV-----KALSGGMLQRLGIAQALVNEPRVLIVDEP 161
Cdd:TIGR00956 157 ETLDFAARCKTPQNRPDgvsreeyaKHIADVYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAKIQCWDNA 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491943749 162 TAGLDPEERIRFRNLLADFANErlvLLSTHIVS------DVEATTNRIGILDHGRLVFNGTTDE 219
Cdd:TIGR00956 237 TRGLDSATALEFIRALKTSANI---LDTTPLVAiyqcsqDAYELFDKVIVLYEGYQIYFGPADK 297
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-211 |
9.85e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPAL-DHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLV-DGTPLKDA--RSIRRKI 78
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEIyKDLNFTLTEGkTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDInlKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 79 GYLPQ-------------QFGFYpTMKVIDAMT----------------------------------------------Y 99
Cdd:PTZ00265 463 GVVSQdpllfsnsiknniKYSLY-SLKDLEALSnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknY 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 100 LAIL-AEVPAREQKRRIEWLLAAvhLTAQAKTKVKA----LSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEerirfr 174
Cdd:PTZ00265 542 QTIKdSEVVDVSKKVLIHDFVSA--LPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNK------ 613
|
250 260 270
....*....|....*....|....*....|....*..
gi 491943749 175 nlladfaNERLVllsTHIVSDVEATTNRIGILDHGRL 211
Cdd:PTZ00265 614 -------SEYLV---QKTINNLKGNENRITIIIAHRL 640
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-211 |
1.17e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 10 VKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLKDARSI-------------R 75
Cdd:PRK10982 253 VRNLTSLRQPSIRDVSFDLHKGeILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeainhgfalvteeR 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 76 RKIG-YLPQQFGFYPTMKVIDAmtYLAILAEVPAREQKRRIEWLLAAVHL-TAQAKTKVKALSGGMLQRLGIAQALVNEP 153
Cdd:PRK10982 333 RSTGiYAYLDIGFNSLISNIRN--YKNKVGLLDNSRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLTQP 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 154 RVLIVDEPTAGLDPEERIRFRNLLADFANER--LVLLSTHIvSDVEATTNRIGILDHGRL 211
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKFEIYQLIAELAKKDkgIIIISSEM-PELLGITDRILVMSNGLV 469
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-166 |
1.58e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 18 QPALDHVSLNI-QSGMYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPL-KDARSIRRKIGYLPQQFGFYPTMKVID 95
Cdd:PRK13540 14 QPLLQQISFHLpAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491943749 96 AMTYlailaEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLD 166
Cdd:PRK13540 94 NCLY-----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-168 |
1.61e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRqqPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVlvdgtplKDARSIrrKIGYLP 82
Cdd:PRK15064 320 LEVENLTKGFDNG--PLFKNLNLLLEAGeRLAIIGENGVGKTTLLRTLVGELEPDSGTV-------KWSENA--NIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 83 QQFG--FYPTMKVIDAMTylailaevpareQKRR-------IEWLLAAVHLTA-QAKTKVKALSGGMLQRLGIAQALVNE 152
Cdd:PRK15064 389 QDHAydFENDLTLFDWMS------------QWRQegddeqaVRGTLGRLLFSQdDIKKSVKVLSGGEKGRMLFGKLMMQK 456
|
170
....*....|....*.
gi 491943749 153 PRVLIVDEPTAGLDPE 168
Cdd:PRK15064 457 PNVLVMDEPTNHMDME 472
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
34-203 |
5.65e-07 |
|
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: 48.72 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 34 GLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTplkdarsirrKIGYLPQqfgfyptmkvidamtylailaevpareqkr 113
Cdd:cd03222 29 GIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI----------TPVYKPQ------------------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 114 riewllaavhltaqaktKVKaLSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFA--NERLVLLSTH 191
Cdd:cd03222 69 -----------------YID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEH 130
|
170
....*....|..
gi 491943749 192 IVSDVEATTNRI 203
Cdd:cd03222 131 DLAVLDYLSDRI 142
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-225 |
1.56e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.47 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 12 HYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTPLkdaRSIRRKIGYLPQQF----- 85
Cdd:PRK10261 23 MQEQQKIAAVRNLSFSLQRGeTLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLL---RRRSRQVIELSEQSaaqmr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 86 ---GFYPTMKVIDAMTYL--------AILAEVPAREQKRRIEWLLAAVHLTAQAKTKVK---------ALSGGMLQRLGI 145
Cdd:PRK10261 100 hvrGADMAMIFQEPMTSLnpvftvgeQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAqtilsryphQLSGGMRQRVMI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 146 AQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERL--VLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELIDA 223
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259
|
..
gi 491943749 224 AA 225
Cdd:PRK10261 260 PQ 261
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-215 |
1.12e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDgtplkdarsirRKIGYLPQQfgfyptMKVIDAMTY 99
Cdd:PTZ00243 676 LRDVSVSVPRGkLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-----------RSIAYVPQQ------AWIMNATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 100 LAIL---AEVPAREQKR-RIEWLLAAV-HLTAQAKTKVKA----LSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPE-- 168
Cdd:PTZ00243 739 GNILffdEEDAARLADAvRVSQLEADLaQLGGGLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvg 818
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491943749 169 ERIRFRNLLADFANERLVlLSTHIVSdVEATTNRIGILDHGRLVFNG 215
Cdd:PTZ00243 819 ERVVEECFLGALAGKTRV-LATHQVH-VVPRADYVVALGDGRVEFSG 863
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
25-180 |
1.58e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 46.28 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 25 SLNIQSGMYGL-LGKNGAGKSTLMKILTTLEkPTSGkvlvdGTPLKDARSirrKIGYLPQQfgfyPTM-------KVIDA 96
Cdd:TIGR00954 472 SFEVPSGNNLLiCGPNGCGKSSLFRILGELW-PVYG-----GRLTKPAKG---KLFYVPQR----PYMtlgtlrdQIIYP 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 97 MTYLailaevparEQKRR------IEWLLAAVHLTAQAKTKV---------KALSGGMLQRLGIAQALVNEPRVLIVDEP 161
Cdd:TIGR00954 539 DSSE---------DMKRRglsdkdLEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170
....*....|....*....
gi 491943749 162 TAGLDPEERIRFRNLLADF 180
Cdd:TIGR00954 610 TSAVSVDVEGYMYRLCREF 628
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-191 |
2.08e-05 |
|
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: 45.23 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 4 IQIEQLVKHYRGRQQPALDHVSLNIQSGM-YGLLGKNGAGKSTLMKILTTLEKpTSGKVLVDGT-----PLKDArsiRRK 77
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQrVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVswnsvPLQKW---RKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 78 IGYLPQQ-FGFYPTM----------------KVIDAMTYLAILAEVPAReqkrriewllaavhLTAQAKTKVKALSGGML 140
Cdd:cd03289 79 FGVIPQKvFIFSGTFrknldpygkwsdeeiwKVAEEVGLKSVIEQFPGQ--------------LDFVLVDGGCVLSHGHK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491943749 141 QRLGIAQALVNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTH 191
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEH 195
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-213 |
2.53e-05 |
|
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: 43.52 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 29 QSGMYGLLGKNGAGKSTLMKILTTLEKPTSGKVL-VDGTPLKDARSIRRKIGYLpqqfgfyptmkvidamtylailaevp 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLIIV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 108 areqkrriewllaavhltaqaKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPE-ERIRFRNLLADFANERLV 186
Cdd:smart00382 55 ---------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqEALLLLLEELRLLLLLKS 113
|
170 180
....*....|....*....|....*..
gi 491943749 187 LLSTHIVsdveATTNRIGILDHGRLVF 213
Cdd:smart00382 114 EKNLTVI----LTTNDEKDLGPALLRR 136
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
135-191 |
3.01e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 44.69 E-value: 3.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491943749 135 LSGGMLQRLGIAQAL---VNEPRVLIVDEPTAGLDPEERIRFRNLLADFANERL-VLLSTH 191
Cdd:pfam13304 237 LSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTH 297
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
9-160 |
3.39e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 9 LVKHYRGRQQPALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGtplkDARSIRRKIGYLPQQFGf 87
Cdd:PRK13546 28 LIPKHKNKTFFALDDISLKAYEGdVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----EVSVIAISAGLSGQLTG- 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491943749 88 yptmkvIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDE 160
Cdd:PRK13546 103 ------IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-220 |
4.70e-05 |
|
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: 44.90 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 19 PALDHVSLNIQSG-MYGLLGKNGAGKST-LMKILTTLEkPTSGKVLVDGtplkdarsirrKIGYLPQQFGFYP-TMK--V 93
Cdd:TIGR01271 440 PVLKNISFKLEKGqLLAVAGSTGSGKSSlLMMIMGELE-PSEGKIKHSG-----------RISFSPQTSWIMPgTIKdnI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 94 IDAMTY--LAILAEVPAREQKRRIEwLLAAVHLTAQAKTKVkALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLD--PEE 169
Cdd:TIGR01271 508 IFGLSYdeYRYTSVIKACQLEEDIA-LFPEKDKTVLGEGGI-TLSGGQRARISLARAVYKDADLYLLDSPFTHLDvvTEK 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491943749 170 RIRFRNLLADFANERLVLLSTHIVSDVEAttNRIGILDHGRLVFNGTTDEL 220
Cdd:TIGR01271 586 EIFESCLCKLMSNKTRILVTSKLEHLKKA--DKILLLHEGVCYFYGTFSEL 634
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
5-191 |
5.89e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.22 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 5 QIEQL-VKHYRGrqqpaLDHVSLNIQSGMYGLLGKNGAGKSTLMKILTTLEKPTS------------------------- 58
Cdd:COG3593 2 KLEKIkIKNFRS-----IKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSsrkfdeedfylgddpdlpeieielt 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 59 -----GKVLVDGTPLKDARSIRRKIGYLPQQF--GFYPTMKVIDAMTYLAIL-AEVPAREQKRRIEWLLAA--VHLTAQA 128
Cdd:COG3593 77 fgsllSRLLRLLLKEEDKEELEEALEELNEELkeALKALNELLSEYLKELLDgLDLELELSLDELEDLLKSlsLRIEDGK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491943749 129 KTKVKALSGGMLQRLGIA--QALV-----NEPRVLIVDEPTAGLDPEERIRFRNLLADFANERL-VLLSTH 191
Cdd:COG3593 157 ELPLDRLGSGFQRLILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNqVIITTH 227
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-191 |
1.61e-04 |
|
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: 41.82 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 37 GKNGAGKSTLM---KILTTLEKPTSGKvlvDGTPLKDARSIRRKIGYLPQQFGFYP--TMKVIDAMTYLAILAEVPAREq 111
Cdd:cd03240 29 GQNGAGKTTIIealKYALTGELPPNSK---GGAHDPKLIREGEVRAQVKLAFENANgkKYTITRSLAILENVIFCHQGE- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 112 krrIEWLLAavhltaqakTKVKALSGG------MLQRLGIAQALVNEPRVLIVDEPTAGLDPEER-------IRFRNLLA 178
Cdd:cd03240 105 ---SNWPLL---------DMRGRCSGGekvlasLIIRLALAETFGSNCGILALDEPTTNLDEENIeeslaeiIEERKSQK 172
|
170
....*....|...
gi 491943749 179 DFanerLVLLSTH 191
Cdd:cd03240 173 NF----QLIVITH 181
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-189 |
2.54e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 21 LDHVSLNIQSGM-YGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDG----------TPLKDARSIR------RKIGYLPQ 83
Cdd:PRK10636 17 LDNATATINPGQkVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqeTPALPQPALEyvidgdREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 84 QFGFYPTMKVIDAMTYL-AILAEVPAREQKRRIEWLLAAVHLT-AQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEP 161
Cdd:PRK10636 97 QLHDANERNDGHAIATIhGKLDAIDAWTIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
170 180
....*....|....*....|....*...
gi 491943749 162 TAGLDPEERIRFRNLLADFANErLVLLS 189
Cdd:PRK10636 177 TNHLDLDAVIWLEKWLKSYQGT-LILIS 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
103-166 |
3.04e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 3.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491943749 103 LAEVPAREQKRRIEWLLAAVHLTAQAKTK-VKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLD 166
Cdd:PLN03073 312 LELIDAYTAEARAASILAGLSFTPEMQVKaTKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-222 |
3.87e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.80 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 20 ALDHVSLNIQSG-MYGLLGKNGAGKSTLMKILTTLEKPTSGKVLVDGTplkdARSIRRKIGYLPQQFGfyptmkvIDAMT 98
Cdd:PRK13545 39 ALNNISFEVPEGeIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS----AALIAISSGLNGQLTG-------IENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 99 YLAILAEVPAREQKRRIEWLLAAVHLTAQAKTKVKALSGGMLQRLGIAQALVNEPRVLIVDEPTAGLDPEerirFRNLLA 178
Cdd:PRK13545 108 LKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQT----FTKKCL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491943749 179 DFANE-----RLVLLSTHIVSDVEATTNRIGILDHGRLVFNGTTDELID 222
Cdd:PRK13545 184 DKMNEfkeqgKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-166 |
1.44e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 10 VKH--YRGRQqpALDHVSLNIQSG-MYGLLGKNGAGKSTL-MKIL-TTLEKPTSGKVLVDGTPLkDARSIRRKIGYlpqq 84
Cdd:NF040905 265 VYHplHPERK--VVDDVSLNVRRGeIVGIAGLMGAGRTELaMSVFgRSYGRNISGTVFKDGKEV-DVSTVSDAIDA---- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 85 fGF-YPT----------MKVIDAMTYLAILAEVPAREQKRRIEWLLAAVHLTAQAKTK-------VKALSGGMLQRLGIA 146
Cdd:NF040905 338 -GLaYVTedrkgyglnlIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKMNIKtpsvfqkVGNLSGGNQQKVVLS 416
|
170 180
....*....|....*....|
gi 491943749 147 QALVNEPRVLIVDEPTAGLD 166
Cdd:NF040905 417 KWLFTDPDVLILDEPTRGID 436
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
93-191 |
3.29e-03 |
|
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: 37.34 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 93 VIDAMTYLAILAEVPAR---EQKRRIEwlLAAVHLTAQakTKVKALSGGMLQRLGIAQALVNE---PRVL-IVDEPTAGL 165
Cdd:cd03227 37 ILDAIGLALGGAQSATRrrsGVKAGCI--VAAVSAELI--FTRLQLSGGEKELSALALILALAslkPRPLyILDEIDRGL 112
|
90 100
....*....|....*....|....*..
gi 491943749 166 DPEERIRFRNLLADFANE-RLVLLSTH 191
Cdd:cd03227 113 DPRDGQALAEAILEHLVKgAQVIVITH 139
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
135-222 |
3.92e-03 |
|
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: 37.30 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943749 135 LSGGMLQRLGIAQALVNEPR--VLIVDEPTAGLDPEERIRFRNLLadfanERLVLLSthivsdveattNRIGILDHGRLV 212
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVI-----KGLIDLG-----------NTVILIEHNLDV 151
|
90
....*....|
gi 491943749 213 FNgTTDELID 222
Cdd:cd03238 152 LS-SADWIID 160
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
132-179 |
4.86e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.34 E-value: 4.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 491943749 132 VKALSGG------MLQRLGIAQALVNEPRVLIVDEPTAGLDpEERirfRNLLAD 179
Cdd:PRK01156 799 IDSLSGGektavaFALRVAVAQFLNNDKSLLIMDEPTAFLD-EDR---RTNLKD 848
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
135-191 |
9.37e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.22 E-value: 9.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 491943749 135 LSGGMLQRLGIAQALV--NEPRVLIVDEPTAGLDPEERIRFRNLLADFANERLVLLSTH 191
Cdd:COG4637 259 LSDGTLRFLALLAALLspRPPPLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTH 317
|
|
| |
