|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-241 |
2.32e-162 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 448.67 E-value: 2.32e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREISRSVG 82
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 83 MVFQSFNLFPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLC 162
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 163 DEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFISSV 241
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-242 |
8.76e-132 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 372.21 E-value: 8.76e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTI---TDRD------- 71
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkPDRDgelvpad 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 72 -SQAREISRSVGMVFQSFNLFPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIA 150
Cdd:COG4598 87 rRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 151 RALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQ 230
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPK 246
|
250
....*....|..
gi 695700954 231 TTELKQFISSVR 242
Cdd:COG4598 247 SERLRQFLSSSL 258
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-216 |
8.58e-131 |
|
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: 367.63 E-value: 8.58e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREISRSVGM 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695700954 164 EITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-242 |
1.07e-116 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 333.21 E-value: 1.07e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREISRSVG 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 83 MVFQSFNLFPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLC 162
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 163 DEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFISSVR 242
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHVS 240
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-243 |
1.41e-100 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 292.81 E-value: 1.41e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTI-TDR-----DSQA 74
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARslsqqKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 75 REISRSVGMVFQSFNLFPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALA 154
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 155 MSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTEL 234
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRT 240
|
....*....
gi 695700954 235 KQFISSVRG 243
Cdd:PRK11264 241 RQFLEKFLL 249
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-241 |
9.84e-99 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 291.21 E-value: 9.84e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYY----GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITD-RDSQAREIS 78
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 79 RSVGMVFQSFNLFPHMTALENVMLaPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPK 158
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVAL-PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 159 VLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQF 237
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
....
gi 695700954 238 ISSV 241
Cdd:COG1135 241 LPTV 244
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-230 |
1.30e-93 |
|
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: 274.46 E-value: 1.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYGDN----HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITD-RDSQAREI 77
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 78 SRSVGMVFQSFNLFPHMTALENVMLaPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSP 157
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695700954 158 KVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQ 230
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-239 |
6.32e-93 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 273.77 E-value: 6.32e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTIT---DRD--------S 72
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrDKDgqlkvadkN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 73 QAREISRSVGMVFQSFNLFPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGDRL-DYYPSSLSGGQQQRVAIAR 151
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 152 ALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQT 231
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
....*...
gi 695700954 232 TELKQFIS 239
Cdd:PRK10619 246 PRLQQFLK 253
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-216 |
1.45e-90 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 266.52 E-value: 1.45e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDN----HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITD-RDSQARE 76
Cdd:COG1136 3 PLLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 77 I-SRSVGMVFQSFNLFPHMTALENVMLaPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAM 155
Cdd:COG1136 83 LrRRHIGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695700954 156 SPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFArEVGDRVVFMHQGKV 216
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELA-ARADRVIRLRDGRI 222
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-242 |
1.94e-90 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 267.08 E-value: 1.94e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQA--------- 74
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNgplvpadek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 75 --REISRSVGMVFQSFNLFPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARA 152
Cdd:TIGR03005 81 hlRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 153 LAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQT 231
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 695700954 232 TELKQFISSVR 242
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-216 |
1.22e-86 |
|
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: 256.26 E-value: 1.22e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDN----HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTIT--DRDSQAREI 77
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 78 SRSVGMVFQSFNLFPHMTALENVMLaPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSP 157
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVEL-PLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 158 KVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREvGDRVVFMHQGKV 216
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-239 |
2.97e-86 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 256.09 E-value: 2.97e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTI----TDRDSQAREISR 79
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 80 SVGMVFQSFNLFPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKV 159
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 160 LLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSkTLFANPQTTELKQFIS 239
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQTEAFAHYLS 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-239 |
1.96e-85 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 254.17 E-value: 1.96e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGG----MTITDRDSQAREISR 79
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdFSKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 80 SVGMVFQSFNLFPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKV 159
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 160 LLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDsKTLFANPQTTELKQFIS 239
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNYLS 241
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-238 |
1.29e-83 |
|
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: 249.13 E-value: 1.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITD-RDSQAREISRS 80
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 VGMVFQSFNLFPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 161 LCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFA--NPqttELKQF 237
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAsdDP---WVRQF 240
|
.
gi 695700954 238 I 238
Cdd:COG1127 241 L 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-230 |
1.60e-83 |
|
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: 257.91 E-value: 1.60e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYY-----GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQA-R 75
Cdd:COG1123 259 PLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 76 EISRSVGMVFQ----SFNlfPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLG-DRLDYYPSSLSGGQQQRVAIA 150
Cdd:COG1123 339 ELRRRVQMVFQdpysSLN--PRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 151 RALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANP 229
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
.
gi 695700954 230 Q 230
Cdd:COG1123 497 Q 497
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-231 |
2.44e-83 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 252.71 E-value: 2.44e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREIsrs 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 vGMVFQSFNLFPHMTALENVMLAPRrVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:COG3842 80 -GMVFQDYALFPHLTVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 161 LCDEITSALDP----ELVGEVLKVLEQLaaeGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQT 231
Cdd:COG3842 158 LLDEPLSALDAklreEMREELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPAT 229
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-231 |
1.81e-79 |
|
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: 238.39 E-value: 1.81e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQ-KYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDsqAREISRSVG 82
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN--LRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 83 MVFQsfN----LFpHMTALENVMLAPRRvLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPK 158
Cdd:COG1122 79 LVFQ--NpddqLF-APTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695700954 159 VLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQT 231
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-216 |
2.89e-79 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 238.42 E-value: 2.89e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQK-YYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTIT-DRDSQAREISR 79
Cdd:COG3638 1 PMLELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTaLRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 80 SVGMVFQSFNLFPHMTALENVML-------APRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARA 152
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAgrlgrtsTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 153 LAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-245 |
8.83e-79 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 240.47 E-value: 8.83e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDN----HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQA-REIS 78
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 79 RSVGMVFQSFNLFPHMTALENVMLaPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPK 158
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 159 VLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQF 237
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
....*...
gi 695700954 238 ISSVRGLN 245
Cdd:PRK11153 241 IQSTLHLD 248
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-211 |
5.24e-77 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 233.06 E-value: 5.24e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYY----GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITdrdsqarE 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-------G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 77 ISRSVGMVFQSFNLFPHMTALENVMLAPRRVlKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMS 156
Cdd:COG1116 78 PGPDRGVVFQEPALLPWLTVLDNVALGLELR-GVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 157 PKVLLCDEITSALDP----ELVGEVLKVLEQlaaEGMTLILVTHEMNFAREVGDRVVFM 211
Cdd:COG1116 157 PEVLLMDEPFGALDAltreRLQDELLRLWQE---TGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-243 |
6.27e-77 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 233.01 E-value: 6.27e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGL----EGYQ-DGSIKLGGMTITDRDSQARE 76
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndliPGARvEGEILLDGEDIYDPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 77 ISRSVGMVFQSFNLFPhMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGL----GDRLDYYPSSLSGGQQQRVAIARA 152
Cdd:COG1117 90 LRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 153 LAMSPKVLLCDEITSALDP-------ELVGEvLKvleqlaaEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTL 225
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDPistakieELILE-LK-------KDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
250
....*....|....*...
gi 695700954 226 FANPQTTELKQFISSVRG 243
Cdd:COG1117 241 FTNPKDKRTEDYITGRFG 258
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-216 |
4.43e-76 |
|
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: 229.33 E-value: 4.43e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREIsrsvGM 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNI----GM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVMLAPRRvLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 164 EITSALDP----ELVGEVLKVLEQLaaeGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:cd03259 156 EPLSALDAklreELREELKELQREL---GITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-218 |
2.51e-75 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 227.63 E-value: 2.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNH-VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITD-RDSQAREISRSV 81
Cdd:COG2884 2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFPHMTALENVMLaPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLL 161
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 162 CDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWE 218
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-225 |
4.62e-75 |
|
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: 227.06 E-value: 4.62e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQ-----DGSIKLGGMTITDRDSQAREIS 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 79 RSVGMVFQSFNLFPhMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGL----GDRLDyyPSSLSGGQQQRVAIARALA 154
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALwdevKDRLH--ALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695700954 155 MSPKVLLCDEITSALDPELVGEVLKVLEQLAAEgMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTL 225
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-215 |
1.05e-73 |
|
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: 222.06 E-value: 1.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREISRSVGM 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVMLAprrvlkksaaecrelaqqmlekvglgdrldyypssLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695700954 164 EITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGK 215
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-240 |
1.18e-73 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 227.65 E-value: 1.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREIsrs 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 vGMVFQSFNLFPHMTALENvMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:COG3839 78 -AMVFQSYALYPHMTVYEN-IAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 161 LCDEITSALDP----ELVGEVLKVLEQLaaeGMTLILVTHE----MNFArevgDRVVFMHQGKVWEQGDSKTLFANPQTT 232
Cdd:COG3839 156 LLDEPLSNLDAklrvEMRAEIKRLHRRL---GTTTIYVTHDqveaMTLA----DRIAVMNDGRIQQVGTPEELYDRPANL 228
|
....*...
gi 695700954 233 ELKQFISS 240
Cdd:COG3839 229 FVAGFIGS 236
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-237 |
3.30e-73 |
|
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: 222.76 E-value: 3.30e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITD-RDSQAREISRSVG 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 83 MVFQSFNLFPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLC 162
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695700954 163 DEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFA--NPQtteLKQF 237
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAsdDPL---VRQF 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-218 |
7.51e-73 |
|
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: 221.54 E-value: 7.51e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDN----HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTIT--DRDSQAR 75
Cdd:COG4181 7 PIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFalDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 76 EISRSVGMVFQSFNLFPHMTALENVML-APRRvlkkSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALA 154
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLpLELA----GRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 155 MSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVgDRVVFMHQGKVWE 218
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAARC-DRVLRLRAGRLVE 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-244 |
1.06e-71 |
|
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: 219.29 E-value: 1.06e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYG----DNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSqaREIS 78
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRR--KAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 79 RSVGMVFQ----SFNlfPHMTaLENVMLAPRRVLKKSAAECRelAQQMLEKVGLGDR-LDYYPSSLSGGQQQRVAIARAL 153
Cdd:COG1124 79 RRVQMVFQdpyaSLH--PRHT-VDRILAEPLRIHGLPDREER--IAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 154 AMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTT 232
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
250
....*....|..
gi 695700954 233 ELKQFISSVRGL 244
Cdd:COG1124 234 YTRELLAASLAF 245
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-231 |
1.18e-71 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 222.71 E-value: 1.18e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGmTITDRDSQAREisRSVGM 83
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG-RDLFTNLPPRE--RRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVMLAPRrVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695700954 164 EITSALD----PELVGEVLKVLEQLaaeGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQT 231
Cdd:COG1118 159 EPFGALDakvrKELRRWLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPAT 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-211 |
2.44e-69 |
|
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: 212.33 E-value: 2.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDN----HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITdrdsqarEISR 79
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-------GPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 80 SVGMVFQSFNLFPHMTALENVMLAPRRVlKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKV 159
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLELQ-GVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 160 LLCDEITSALDP----ELVGEVLKVLEQlaaEGMTLILVTHEMNFAREVGDRVVFM 211
Cdd:cd03293 153 LLLDEPFSALDAltreQLQEELLDIWRE---TGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-225 |
3.32e-69 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 212.62 E-value: 3.32e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDrdsQAREISRSVGM 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR---DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVMLApRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695700954 164 EITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTL 225
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-215 |
1.22e-68 |
|
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: 210.02 E-value: 1.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 14 GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDrdSQAREISRSVGMVFQSFNL-FP 92
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK--LSLKELRRKVGLVFQNPDDqFF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 93 HMTALENVMLAPRRvLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPE 172
Cdd:cd03225 90 GPTVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695700954 173 LVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGK 215
Cdd:cd03225 169 GRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-220 |
6.15e-68 |
|
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: 208.90 E-value: 6.15e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYY----GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREI- 77
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 78 SRSVGMVFQ----SFNlfPHMTALENVMlAPRRVLKKSAAECRELAQQMLEKVGLG---DRLDYYPSSLSGGQQQRVAIA 150
Cdd:cd03257 81 RKEIQMVFQdpmsSLN--PRMTIGEQIA-EPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695700954 151 RALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-230 |
2.65e-67 |
|
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: 210.29 E-value: 2.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYY----GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLE---GYQDGSIKLGGMTITD-RDSQA 74
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKlSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 75 REI-SRSVGMVFQ----SFNlfPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGD---RLDYYPSSLSGGQQQR 146
Cdd:COG0444 81 RKIrGREIQMIFQdpmtSLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 147 VAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTL 225
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*
gi 695700954 226 FANPQ 230
Cdd:COG0444 239 FENPR 243
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-238 |
1.10e-66 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 206.14 E-value: 1.10e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGdnHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREISrsvgM 83
Cdd:COG3840 2 LRLDDLTYRYG--DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVS----M 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVMLAPRRVLKKSAAEcRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLGLRPGLKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 164 EITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFI 238
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-216 |
3.32e-66 |
|
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: 205.11 E-value: 3.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDN-HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTIT-DRDSQAREISRSV 81
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINkLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFPHMTALENVMLA--PRRVLKKSAA-----ECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALA 154
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlGRRSTWRSLFglfpkEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695700954 155 MSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-238 |
1.48e-65 |
|
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: 203.24 E-value: 1.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQareiSRSVGM 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH----KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVMLaPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:cd03300 77 VFQNYALFPHLTVFENIAF-GLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 164 EITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFI 238
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-230 |
3.83e-65 |
|
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: 210.53 E-value: 3.83e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYY--GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGL---EGYQDGSIKLGGMTITDRDSQARe 76
Cdd:COG1123 3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 77 iSRSVGMVFQSF--NLFPhMTALENVMLAPRRvLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALA 154
Cdd:COG1123 82 -GRRIGMVFQDPmtQLNP-VTVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 155 MSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQ 230
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-241 |
2.51e-64 |
|
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: 201.33 E-value: 2.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 22 VDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITD-RDSQAREISR-SVGMVFQSFNLFPHMTALEN 99
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKELRELRRkKISMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 100 VMLaPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLK 179
Cdd:cd03294 123 VAF-GLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQD 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695700954 180 VLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFISSV 241
Cdd:cd03294 202 ELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGV 264
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-216 |
1.63e-63 |
|
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: 198.29 E-value: 1.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYGDNH-VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITD-RDSQAREISRS 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 VGMVFQSFNLFPHMTALENVmLAPRRVLKKSAAEC--------RELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARA 152
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENV-LHGRLGYKPTWRSLlgrfseedKERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 153 LAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-238 |
1.67e-63 |
|
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: 198.33 E-value: 1.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREisrsVGM 83
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN----VGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVMLAPR---RVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 161 LCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFI 238
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-244 |
2.84e-63 |
|
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: 197.52 E-value: 2.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNH-VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDsqAREISRSVG 82
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD--PVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 83 MVFQSFNLFPHMTALENVMLAPRrVLKKSAAECRELAQQMLEKVGLGDR--LDYYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVPK-LLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 161 LCDEITSALDP----ELVGEVLKVLEQLaaeGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQ 236
Cdd:cd03295 158 LMDEPFGALDPitrdQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAE 234
|
....*...
gi 695700954 237 FISSVRGL 244
Cdd:cd03295 235 FVGADRLL 242
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-230 |
4.68e-63 |
|
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: 196.89 E-value: 4.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 6 INQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAReISRSVGMVF 85
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEI-ARLGIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 86 QSFNLFPHMTALENVMLAPRRVLK---------KSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMS 156
Cdd:cd03219 82 QIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695700954 157 PKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQ 230
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
3-240 |
4.38e-62 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 197.80 E-value: 4.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQK--YYGDN--HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITD-RDSQAREI 77
Cdd:TIGR02314 1 MIKLSNITKvfHQGTKtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTlSNSELTKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 78 SRSVGMVFQSFNLFPHMTALENVMLaPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSP 157
Cdd:TIGR02314 81 RRQIGMIFQHFNLLSSRTVFGNVAL-PLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 158 KVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQ 236
Cdd:TIGR02314 160 KVLLCDEATSALDPATTQSILELLKEINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQK 239
|
....
gi 695700954 237 FISS 240
Cdd:TIGR02314 240 FIRS 243
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-228 |
7.66e-62 |
|
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: 193.42 E-value: 7.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAReISRSVGM 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER-ARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKvgLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 164 EITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFAN 228
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-241 |
8.72e-62 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 197.61 E-value: 8.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDrdSQAREisRSVGM 83
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARD--RKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVMLA----PRRVlKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKV 159
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGltvlPRRE-RPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 160 LLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFI 238
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFM 237
|
...
gi 695700954 239 SSV 241
Cdd:PRK10851 238 GEV 240
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-230 |
2.02e-61 |
|
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: 193.33 E-value: 2.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRdsQAREISRS 80
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGL--PPHRIARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 vGMV--FQSFNLFPHMTALENVMLAPRRVLK--------------KSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQ 144
Cdd:COG0411 80 -GIArtFQNPRLFPELTVLENVLVAAHARLGrgllaallrlprarREEREARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 145 QRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSK 223
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
....*..
gi 695700954 224 TLFANPQ 230
Cdd:COG0411 239 EVRADPR 245
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-221 |
2.07e-61 |
|
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: 193.34 E-value: 2.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDsqAREISRSVG 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS--RRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 83 MVFQSFNLFPHMTALENVML--AP-RRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKV 159
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALgrYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695700954 160 LLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGD 221
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-236 |
1.13e-60 |
|
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: 192.28 E-value: 1.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDN-----HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQA-REI 77
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 78 SRSVGMVFQsfnlFPHM-----TALENVMLAPRRvLKKSAAECRELAQQMLEKVGLGDrlDYY---PSSLSGGQQQRVAI 149
Cdd:TIGR04521 81 RKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKN-LGLSEEEAEERVKEALELVGLDE--EYLersPFELSGGQMRRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 150 ARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFAN 228
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSD 233
|
250
....*....|....*....
gi 695700954 229 -----------PQTTELKQ 236
Cdd:TIGR04521 234 vdelekigldvPEITELAR 252
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-230 |
8.72e-60 |
|
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: 188.65 E-value: 8.72e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAReISRS 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRI-ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 VGMVFQSFNLFPHMTALENVMLAPRRVLKKSAAECRelaqqmLEKVG-----LGDRLDYYPSSLSGGQQQRVAIARALAM 155
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRAD------LERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 156 SPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQ 230
Cdd:COG0410 154 RPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-216 |
4.00e-59 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 187.22 E-value: 4.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRdsqareiSRS 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-------RRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 VGMVFQSFNL---FPhMTALENVML---APRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALA 154
Cdd:COG1121 77 IGYVPQRAEVdwdFP-ITVRDVVLMgryGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695700954 155 MSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-236 |
8.71e-59 |
|
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: 186.87 E-value: 8.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNH--VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTiTDRDSQAREISRSV 81
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD-TLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQS-FNLFPHMT-------ALENVMLAPrrvlkksaAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARAL 153
Cdd:TIGR04520 80 GMVFQNpDNQFVGATveddvafGLENLGVPR--------EEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 154 AMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREvGDRVVFMHQGKVWEQGDSKTLFAN---- 228
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQvell 230
|
250
....*....|....*
gi 695700954 229 -------PQTTELKQ 236
Cdd:TIGR04520 231 keigldvPFITELAK 245
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-243 |
1.20e-57 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 183.89 E-value: 1.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 12 YYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGL-----EGYQDGSIKLGGMTITDRDSQAREISRSVGMVFQ 86
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 87 SFNLFPHMTALENVMLAPR-RVLKKSAAECRELAQQMLEKVGL----GDRLDYYPSSLSGGQQQRVAIARALAMSPKVLL 161
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKlNGLVKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 162 CDEITSALDPELVGEVLKVLEQLAAEgMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFISSV 241
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGA 251
|
..
gi 695700954 242 RG 243
Cdd:PRK14267 252 LG 253
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-238 |
1.27e-57 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 187.46 E-value: 1.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREisrs 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 VGMVFQSFNLFPHMTALENVMLApRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 161 LCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFI 238
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFI 245
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-216 |
1.23e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 179.63 E-value: 1.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDsqAREISRSVGM 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP--PPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPhMTALENvMLAPRRVLKKSAAecRELAQQMLEKVGLGDR-LDYYPSSLSGGQQQRVAIARALAMSPKVLLC 162
Cdd:COG4619 79 VPQEPALWG-GTVRDN-LPFPFQLRERKFD--RERALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 163 DEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-238 |
1.60e-56 |
|
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: 180.44 E-value: 1.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAReisRSVG 82
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR---RQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 83 MVFQSFNLFPHMTALENV-MLAPRRVLKKSAAECRelAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLL 161
Cdd:COG4555 78 VLPDERGLYDRLTVRENIrYFAELYGLFDEELKKR--IEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 162 CDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFI 238
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAF 232
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-241 |
6.00e-56 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 183.38 E-value: 6.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQA-REISRS-VGMVFQSFNLFPHMTA 96
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElRELRRKkMSMVFQHFALLPHRTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 97 LENVM--LAPRRVlkkSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDP--- 171
Cdd:COG4175 123 LENVAfgLEIQGV---PKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlir 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695700954 172 -ELVGEVLKVLEQLaaeGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFISSV 241
Cdd:COG4175 200 rEMQDELLELQAKL---KKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDV 267
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-216 |
1.28e-55 |
|
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: 175.66 E-value: 1.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRdsqAREISRSVGM 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKE---PEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVMLaprrvlkksaaecrelaqqmlekvglgdrldyypsslSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:cd03230 78 LPEEPSLYENLTVRENLKL-------------------------------------SGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695700954 164 EITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
2.40e-55 |
|
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: 176.29 E-value: 2.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREIsrsvGM 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDI----AM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENvMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:cd03301 77 VFQNYALYPHMTVYDN-IAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695700954 164 EITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-230 |
5.47e-55 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 179.16 E-value: 5.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYY---------GDNHV--LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDR 70
Cdd:COG4608 6 PLLEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 71 DSQA-REISRSVGMVFQ----SFNlfPHMTaLENVMLAPRRVLK-KSAAECRELAQQMLEKVGLG-DRLDYYPSSLSGGQ 143
Cdd:COG4608 86 SGRElRPLRRRMQMVFQdpyaSLN--PRMT-VGDIIAEPLRIHGlASKAERRERVAELLELVGLRpEHADRYPHEFSGGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 144 QQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDS 222
Cdd:COG4608 163 RQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPR 242
|
....*...
gi 695700954 223 KTLFANPQ 230
Cdd:COG4608 243 DELYARPL 250
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-229 |
7.27e-55 |
|
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: 179.53 E-value: 7.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 22 VDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRdsqAREIS-----RSVGMVFQSFNLFPHMTA 96
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDS---ARGIFlpphrRRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 97 LENVMLAPRRVlkkSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGE 176
Cdd:COG4148 95 RGNLLYGRKRA---PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695700954 177 VLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANP 229
Cdd:COG4148 172 ILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-245 |
3.33e-54 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 177.30 E-value: 3.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 34 IIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQareiSRSVGMVFQSFNLFPHMTALENVMLaPRRVLKKSAA 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH----LRHINMVFQSYALFPHMTVEENVAF-GLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 114 ECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVG----EVLKVLEQLaaeGM 189
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDqmqlELKTIQEQL---GI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 190 TLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFISSVRGLN 245
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFE 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-231 |
1.46e-53 |
|
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: 180.65 E-value: 1.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYY-----------GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQdGSIKLGGMTITDR 70
Cdd:COG4172 274 PLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 71 DSQA-REISRSVGMVFQ----SFNlfPHMTALENVMlAPRRVL--KKSAAECRELAQQMLEKVGL-GDRLDYYPSSLSGG 142
Cdd:COG4172 353 SRRAlRPLRRRMQVVFQdpfgSLS--PRMTVGQIIA-EGLRVHgpGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 143 QQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGD 221
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGP 509
|
250
....*....|
gi 695700954 222 SKTLFANPQT 231
Cdd:COG4172 510 TEQVFDAPQH 519
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-239 |
4.28e-53 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 171.88 E-value: 4.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGL-----EGYQDGSIKLGGMTITDRDSQARE 76
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 77 ISRSVGMVFQSFNLFPhMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGL----GDRLDYYPSSLSGGQQQRVAIARA 152
Cdd:PRK14239 84 LRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 153 LAMSPKVLLCDEITSALDPELVGEVLKVLEQLaAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTT 232
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHK 241
|
....*..
gi 695700954 233 ELKQFIS 239
Cdd:PRK14239 242 ETEDYIS 248
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-230 |
3.76e-52 |
|
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: 176.80 E-value: 3.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDN----HVLKGVDLDIDMGQVISIIGRSGSGKS----TLLRCINGLEGYQDGSIKLGGMTITD-RD 71
Cdd:COG4172 4 MPLLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGlSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 72 SQAREI-SRSVGMVFQ----SFNlfPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGD---RLDYYPSSLSGGQ 143
Cdd:COG4172 84 RELRRIrGNRIAMIFQepmtSLN--PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 144 QQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDS 222
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPT 241
|
....*...
gi 695700954 223 KTLFANPQ 230
Cdd:COG4172 242 AELFAAPQ 249
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-238 |
1.27e-51 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 171.06 E-value: 1.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 9 VQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREISrsvgMVFQSF 88
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDIC----MVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 89 NLFPHMTALENVMLApRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSA 168
Cdd:PRK11432 88 ALFPHMSLGENVGYG-LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695700954 169 LDPEL---VGEVLKVLEQlaAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFI 238
Cdd:PRK11432 167 LDANLrrsMREKIRELQQ--QFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFM 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-230 |
1.29e-51 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 168.17 E-value: 1.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGL-----EGYQDGSIKLGGMTITDRDsqAR 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD--VI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 76 EISRSVGMVFQSFNLFPHMTALENVMLAPR-RVLKKSAAECRELAQQMLEKVGL----GDRLDYYPSSLSGGQQQRVAIA 150
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIPNLSIFENVALGLKlNRLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 151 RALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEgMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQ 230
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-242 |
1.43e-51 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 171.57 E-value: 1.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 11 KYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRD-SQAREISR-SVGMVFQSF 88
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSpVELREVRRkKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 89 NLFPHMTALENVMLAPRrVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSA 168
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPE-LLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695700954 169 LDP----ELVGEVLKVLEQLaaeGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFISSVR 242
Cdd:TIGR01186 160 LDPlirdSMQDELKKLQATL---QKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVD 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-216 |
1.71e-51 |
|
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: 166.55 E-value: 1.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 13 YGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMtitdrdsQAREISRSVGMVFQSFNL-- 90
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-------PLEKERKRIGYVPQRRSIdr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 91 -FPhMTALENVML---APRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEIT 166
Cdd:cd03235 82 dFP-ISVRDVVLMglyGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695700954 167 SALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-239 |
2.01e-51 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 166.93 E-value: 2.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 5 TINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAReISRSVGMV 84
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHER-ARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 85 FQSFNLFPHMTALENVML---APRRVLKKSAAECREL---AQQMLEKVGlGDrldyypssLSGGQQQRVAIARALAMSPK 158
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTglaALPRRSRKIPDEIYELfpvLKEMLGRRG-GD--------LSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 159 VLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLfanpQTTELKQF 237
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRRY 227
|
..
gi 695700954 238 IS 239
Cdd:TIGR03410 228 LA 229
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-215 |
5.84e-51 |
|
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: 163.18 E-value: 5.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 5 TINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSqaREISRSVGMV 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL--EELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 85 FQsfnlfphmtalenvmlaprrvlkksaaecrelaqqmlekvglgdrldyypssLSGGQQQRVAIARALAMSPKVLLCDE 164
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695700954 165 ITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGK 215
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-239 |
1.05e-49 |
|
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: 162.89 E-value: 1.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHvLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREISrsvgM 83
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDIS----Y 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVMLApRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 164 EITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFIS 239
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-167 |
1.25e-49 |
|
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: 159.74 E-value: 1.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAReiSRSVGMVFQSFNLFPHMTALE 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL--RKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695700954 99 NVMLaPRRVLKKSAAECRELAQQMLEKVGLGD----RLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITS 167
Cdd:pfam00005 79 NLRL-GLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-240 |
1.92e-49 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 163.08 E-value: 1.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDN---------HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRD 71
Cdd:COG4167 2 SALLEVRNLSKTFKYRtglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 72 SQAReiSRSVGMVFQ----SFNlfPHMTA---LEnvmlAP-RRVLKKSAAECRELAQQMLEKVGL-GDRLDYYPSSLSGG 142
Cdd:COG4167 82 YKYR--CKHIRMIFQdpntSLN--PRLNIgqiLE----EPlRLNTDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 143 QQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGD 221
Cdd:COG4167 154 QKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGK 233
|
250
....*....|....*....
gi 695700954 222 SKTLFANPQTTELKQFISS 240
Cdd:COG4167 234 TAEVFANPQHEVTKRLIES 252
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-220 |
2.03e-49 |
|
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: 161.31 E-value: 2.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDM---GQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDrDSQAREIS---RSVGMVFQSFNLFP 92
Cdd:cd03297 10 LPDFTLKIDFdlnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD-SRKKINLPpqqRKIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 93 HMTALENVMLAPRRvlkKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPE 172
Cdd:cd03297 89 HLNVRENLAFGLKR---KRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695700954 173 LVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:cd03297 166 LRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
4-238 |
2.15e-49 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 165.56 E-value: 2.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDN----HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTItdrdSQAREI-- 77
Cdd:NF040933 3 VRVENVTKIFKKGkkevVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLV----ASPGKIiv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 78 ---SRSVGMVFQSFNLFPHMTALENVMLaPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALA 154
Cdd:NF040933 79 ppeDRNIGMVFQNWALYPNMTVFDNIAF-PLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 155 MSPKVLLCDEITSALDP-------ELVGEVLKVLeqlaaeGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFA 227
Cdd:NF040933 158 KNPQVLLLDEPFSNLDArirdsarALVKKIQREL------KITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYD 231
|
250
....*....|.
gi 695700954 228 NPQTTELKQFI 238
Cdd:NF040933 232 NPANIFVARLI 242
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-220 |
2.75e-49 |
|
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: 159.91 E-value: 2.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 5 TINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDsqAREISRSVGMV 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS--PKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 85 fqsfnlfphmtalenvmlaprrvlkksaaecrelaQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDE 164
Cdd:cd03214 79 -----------------------------------PQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 165 ITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-216 |
4.31e-49 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 161.77 E-value: 4.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLiTINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTItdrdSQAREISRsv 81
Cdd:PRK11247 12 PL-LLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL----AEAREDTR-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 gMVFQSFNLFPHMTALENVMLAPRrvlkksaAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLL 161
Cdd:PRK11247 85 -LMFQDARLLPWKKVIDNVGLGLK-------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 162 CDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-216 |
6.82e-49 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 167.50 E-value: 6.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGG--MTITD-RDSQAREI 77
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSpRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 78 SrsvgMVFQSFNLFPHMTALENVMLA--PRR--VLKKSAAecRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARAL 153
Cdd:COG1129 82 A----IIHQELNLVPNLSVAENIFLGrePRRggLIDWRAM--RRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695700954 154 AMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:COG1129 156 SRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-230 |
8.50e-49 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 162.11 E-value: 8.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDN-----HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITD--RDSQARE 76
Cdd:PRK13634 3 ITFQKVEHRYQYKtpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 77 ISRSVGMVFQsfnlFP-HM----TALENVMLAPRRvLKKSAAECRELAQQMLEKVGLG-DRLDYYPSSLSGGQQQRVAIA 150
Cdd:PRK13634 83 LRKKVGIVFQ----FPeHQlfeeTVEKDICFGPMN-FGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 151 RALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANP 229
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
.
gi 695700954 230 Q 230
Cdd:PRK13634 238 D 238
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-216 |
3.16e-48 |
|
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: 158.34 E-value: 3.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHV-LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITD-RDSQAREISRSV 81
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFPHMTALENVMLApRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLL 161
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 162 CDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-219 |
5.58e-48 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 158.02 E-value: 5.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MP---LITINQVQKYYGDNH----VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQ 73
Cdd:PRK10584 1 MPaenIVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 74 AREISRS--VGMVFQSFNLFPHMTALENVMLaPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIAR 151
Cdd:PRK10584 81 ARAKLRAkhVGFVFQSFMLIPTLNALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 152 ALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVgDRVVFMHQGKVWEQ 219
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARC-DRRLRLVNGQLQEE 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-220 |
3.86e-47 |
|
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: 155.34 E-value: 3.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGdnHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREISrsvgM 83
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVS----M 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVMLA--PRRVLKksaAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLL 161
Cdd:cd03298 75 LFQENNLFAHLTVEQNVGLGlsPGLKLT---AEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 162 CDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-227 |
8.21e-47 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 156.71 E-value: 8.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDN--HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDrdSQAREISR 79
Cdd:PRK13635 4 EIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE--ETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 80 SVGMVFQS-FNLFPHMT-------ALENVMLaPRrvlkksaAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIAR 151
Cdd:PRK13635 82 QVGMVFQNpDNQFVGATvqddvafGLENIGV-PR-------EEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 152 ALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGM-TLILVTHEMNFAREvGDRVVFMHQGKVWEQGDSKTLFA 227
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-215 |
1.90e-46 |
|
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: 152.15 E-value: 1.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNH--VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTItdRDSQAREISRSV 81
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL--RDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFpHMTALENVmlaprrvlkksaaecrelaqqmlekvglgdrldyypssLSGGQQQRVAIARALAMSPKVLL 161
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695700954 162 CDEITSALDPELVGEVLKVLEQLaAEGMTLILVTHEMNFAREVgDRVVFMHQGK 215
Cdd:cd03228 120 LDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-225 |
1.06e-45 |
|
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: 151.89 E-value: 1.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGD--NHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGmtiTDRDSQAREISRSV 81
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING---YSIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFPHMTALENVMLAPRrvLK-KSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYAR--LKgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 161 LCDEITSALDPELVGEVLKVLEQLaAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTL 225
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-214 |
1.08e-45 |
|
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: 152.23 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQareisRSVgmVFQSFNLFPHMTALE 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD-----RMV--VFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 99 NVMLAPRRVLKK-SAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEV 177
Cdd:TIGR01184 74 NIALAVDRVLPDlSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 695700954 178 LKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQG 214
Cdd:TIGR01184 154 QEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-216 |
1.21e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 153.32 E-value: 1.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYG-----DNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAReiS 78
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKR--A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 79 RSVGMVFQ--SFNLFPHMTALENVMLAPRRVLKKS-----AAECRELAQQMLEKVGLG--DRLDYYPSSLSGGQQQrvai 149
Cdd:COG1101 80 KYIGRVFQdpMMGTAPSMTIEENLALAYRRGKRRGlrrglTKKRRELFRELLATLGLGleNRLDTKVGLLSGGQRQ---- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695700954 150 ARALAMS----PKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:COG1101 156 ALSLLMAtltkPKLLLLDEHTAALDPKTAALVLELTEKIVEEnNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-242 |
1.44e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 153.22 E-value: 1.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNH--VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDrdSQAREISR 79
Cdd:PRK13632 6 VMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK--ENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 80 SVGMVFQS-FNLFPHMTA-------LENVMLAPrrvlKKSAAECRELAQqmleKVGLGDRLDYYPSSLSGGQQQRVAIAR 151
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVeddiafgLENKKVPP----KKMKDIIDDLAK----KVGMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 152 ALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGM-TLILVTHEMNfarEV--GDRVVFMHQGKVWEQGDSKTLFAN 228
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMD---EAilADKVIVFSEGKLIAQGKPKEILNN 232
|
250
....*....|....
gi 695700954 229 pqttelKQFISSVR 242
Cdd:PRK13632 233 ------KEILEKAK 240
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-242 |
1.71e-45 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 160.66 E-value: 1.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYY----GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREI 77
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 78 SRS--VGMVFQSFNLFPHMTALENVMLaPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAM 155
Cdd:PRK10535 83 LRRehFGFIFQRYHLLSHLTAAQNVEV-PAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 156 SPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREvGDRVVFMHQGKVW--------EQGDSKTLFA 227
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVrnppaqekVNVAGGTEPV 240
|
250
....*....|....*
gi 695700954 228 NPQTTELKQFISSVR 242
Cdd:PRK10535 241 VNTASGWRQFVSGFR 255
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-227 |
2.25e-45 |
|
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: 160.77 E-value: 2.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNH--VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDsqAREISRSV 81
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID--PASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFpHMTALENVMLA-P-------RRVLKKSAAEcrELAQQM---LEKVgLGDRldyyPSSLSGGQQQRVAIA 150
Cdd:COG2274 552 GVVLQDVFLF-SGTIRENITLGdPdatdeeiIEAARLAGLH--DFIEALpmgYDTV-VGEG----GSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 151 RALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAeGMTLILVTHEMNFAREVgDRVVFMHQGKVWEQGDSKTLFA 227
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDGTHEELLA 698
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-240 |
2.90e-45 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 155.19 E-value: 2.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQareiSRS 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA----ERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 VGMVFQSFNLFPHMTALENvMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAEN-MSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 161 LCDEITSALDPEL-VG---EVLKVLEQLaaeGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQ 236
Cdd:PRK11000 156 LLDEPLSNLDAALrVQmriEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAG 232
|
....
gi 695700954 237 FISS 240
Cdd:PRK11000 233 FIGS 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-229 |
6.26e-45 |
|
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: 158.01 E-value: 6.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNH--VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAreISR 79
Cdd:COG4987 332 PSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD--LRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 80 SVGMVFQSFNLFpHMTALENVMLAprrvlKKSAAEcRELAqQMLEKVGLGDRLDYYP-----------SSLSGGQQQRVA 148
Cdd:COG4987 410 RIAVVPQRPHLF-DTTLRENLRLA-----RPDATD-EELW-AALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 149 IARALAMSPKVLLCDEITSALDPELVGEVLKVLEQlAAEGMTLILVTHEMNfAREVGDRVVFMHQGKVWEQGDSKTLFAN 228
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
.
gi 695700954 229 P 229
Cdd:COG4987 560 N 560
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-240 |
7.15e-45 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 153.85 E-value: 7.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQK-YYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREISr 79
Cdd:PRK11650 1 MAGLKLQAVRKsYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 80 svgMVFQSFNLFPHMTALENvM---LAPRRVLKKSAAECRELAQQMLEkvgLGDRLDYYPSSLSGGQQQRVAIARALAMS 156
Cdd:PRK11650 80 ---MVFQNYALYPHMSVREN-MaygLKIRGMPKAEIEERVAEAARILE---LEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 157 PKVLLCDEITSALDPELVG----EVLKVLEQLAAegmTLILVTHEMNFAREVGDRVVFMHQGKVwEQ-GDSKTLFANPQT 231
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKLRVqmrlEIQRLHRRLKT---TSLYVTHDQVEAMTLADRVVVMNGGVA-EQiGTPVEVYEKPAS 228
|
....*....
gi 695700954 232 TELKQFISS 240
Cdd:PRK11650 229 TFVASFIGS 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-241 |
7.68e-45 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 154.22 E-value: 7.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTItdrdSQAREISRS 80
Cdd:PRK11607 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----SHVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 VGMVFQSFNLFPHMTALENVMLAPRRVlKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQD-KLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 161 LCDEITSALDPELVG----EVLKVLEQLaaeGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQ 236
Cdd:PRK11607 172 LLDEPMGALDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAE 248
|
....*
gi 695700954 237 FISSV 241
Cdd:PRK11607 249 FIGSV 253
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-241 |
9.93e-45 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 152.94 E-value: 9.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 20 KGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITD-RDSQAREISRSVGMVFQ----SFNlfPHM 94
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmKDDEWRAVRSDIQMIFQdplaSLN--PRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 95 TALEnVMLAPRRVL--KKSAAECRELAQQMLEKVGLGDRL-DYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDP 171
Cdd:PRK15079 116 TIGE-IIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695700954 172 ELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFISSV 241
Cdd:PRK15079 195 SIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-204 |
1.42e-44 |
|
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: 148.40 E-value: 1.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAReisRSV 81
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR---RRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFPHMTALENVMLApRRVLKKSAAecRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLL 161
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRFW-AALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695700954 162 CDEITSALDPELVGEVLKVLEQLAAEGMTLILVTH---EMNFAREV 204
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqplELAAARVL 200
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-219 |
1.75e-44 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 150.01 E-value: 1.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDN----HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTIT----DRds 72
Cdd:COG4525 1 MSMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgaDR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 73 qareisrsvGMVFQSFNLFPHMTALENVMLAPRrvLKK-SAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIAR 151
Cdd:COG4525 79 ---------GVVFQKDALLPWLNVLDNVAFGLR--LRGvPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695700954 152 ALAMSPKVLLCDEITSALDP---ELVGEVLkvLEQLAAEGMTLILVTHEMNFAREVGDRVVFM--HQGKVWEQ 219
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDAltrEQMQELL--LDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVER 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-216 |
1.89e-44 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 155.57 E-value: 1.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLegYQ--DGSIKLGG--MTITD-RDSqar 75
Cdd:COG3845 3 PPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGL--YQpdSGEILIDGkpVRIRSpRDA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 76 eISRSVGMVFQSFNLFPHMTALENVMLA--PRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARAL 153
Cdd:COG3845 78 -IALGIGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695700954 154 AMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
8-235 |
2.62e-44 |
|
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: 152.19 E-value: 2.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 8 QVQKYYGDnHVLKgVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTItdRDSQAREI----SRSVGM 83
Cdd:TIGR02142 4 RFSKRLGD-FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL--FDSRKGIFlppeKRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVMLAPRRVlkkSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:TIGR02142 80 VFQEARLFPHLSVRGNLRYGMKRA---RPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 164 EITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKV---------WEQGDSKTLFANPQTTE 233
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVaaagpiaevWASPDLPWLAREDQGSL 236
|
..
gi 695700954 234 LK 235
Cdd:TIGR02142 237 IE 238
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
12-239 |
2.81e-44 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 149.55 E-value: 2.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 12 YYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGL----EGYQ-DGSIKLGGMTITDRDSQAREISRSVGMVFQ 86
Cdd:PRK14243 19 YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndliPGFRvEGKVTFHGKNLYAPDVDPVEVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 87 SFNLFPHmTALENVMLAPRrvLKKSAAECRELAQQMLEKVGL----GDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLC 162
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYGAR--INGYKGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 163 DEITSALDPELVGEVLKVLEQLaAEGMTLILVTHEMNFAREVGDRVVFMH---------QGKVWEQGDSKTLFANPQTTE 233
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSPQQQA 254
|
....*.
gi 695700954 234 LKQFIS 239
Cdd:PRK14243 255 TRDYVS 260
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-220 |
4.53e-44 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 148.73 E-value: 4.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCING-LEGYQdGSIKLGGMTItdRDSQAREISRSV 81
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSS-GEVRLNGRPL--AAWSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNL-FPhMTALENVML--APRRvlkKSAAECRELAQQMLEKVGLGDRLD-YYPSsLSGGQQQRVAIARALA--- 154
Cdd:COG4559 78 AVLPQHSSLaFP-FTVEEVVALgrAPHG---SSAAQDRQIVREALALVGLAHLAGrSYQT-LSGGEQQRVQLARVLAqlw 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 155 ----MSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:COG4559 153 epvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQG 222
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-233 |
4.88e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 149.81 E-value: 4.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREISRSVGMVFQ--SFNLFPHmTA 96
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQypEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 97 LENVMLAPRRvLKKSAAECRELAQQMLEKVGLG--DRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELV 174
Cdd:PRK13637 102 EKDIAFGPIN-LGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 175 GEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTE 233
Cdd:PRK13637 181 DEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLE 240
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-228 |
9.07e-44 |
|
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: 154.92 E-value: 9.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQ-KYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAreISRS 80
Cdd:COG4988 335 PSIELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS--WRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 VGMVFQSFNLFpHMTALENVMLAPRRVlkkSAAECRELaqqmLEKVGLGDRLDYYP-----------SSLSGGQQQRVAI 149
Cdd:COG4988 413 IAWVPQNPYLF-AGTIRENLRLGRPDA---SDEELEAA----LEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 150 ARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAeGMTLILVTHEMNFAREVgDRVVFMHQGKVWEQGDSKTLFAN 228
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEELLAK 561
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-225 |
2.11e-43 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 146.27 E-value: 2.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 23 DLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITdRDSQAReisRSVGMVFQSFNLFPHMTALENVML 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT-TTPPSR---RPVSMLFQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 103 APRRVLKKSAAEcRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLE 182
Cdd:PRK10771 95 GLNPGLKLNAAQ-REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695700954 183 QLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTL 225
Cdd:PRK10771 174 QVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-209 |
3.30e-43 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 145.32 E-value: 3.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 5 TINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGL--EGYQ-DGSIKLGGMTITDRDSQAREIsrsv 81
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSaSGEVLLNGRRLTALPAEQRRI---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFPHMTALENVMLA-PRRVlkkSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFAlPPTI---GRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695700954 161 LCDEITSALDPELVGEVLK-VLEQLAAEGMTLILVTHEMNFAREVGdRVV 209
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEEDAPAAG-RVL 204
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-241 |
1.17e-42 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 145.54 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGL---EGYQDGSIKLGGMTITDRDSQAREISR 79
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 80 S---VGMVFQSFNLFPHMTALENVMLAP-------RRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAI 149
Cdd:PRK09984 84 SranTGYIFQQFNLVNRLSVLENVLIGAlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 150 ARALAMSPKVLLCDEITSALDPE---LVGEVLKVLEQlaAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTlF 226
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPEsarIVMDTLRDINQ--NDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ-F 240
|
250
....*....|....*
gi 695700954 227 ANPQTTELKQFISSV 241
Cdd:PRK09984 241 DNERFDHLYRSINRV 255
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-220 |
1.68e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 151.86 E-value: 1.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 12 YYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLegY--QDGSIKLGGMTITDRDSQarEISRSVGMVFQSFN 89
Cdd:COG1132 349 YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF--YdpTSGRILIDGVDIRDLTLE--SLRRQIGVVPQDTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 90 LFpHMTALENVMLAP--------RRVLKksAAECRELAQQMLEKVG--LGDRldyyPSSLSGGQQQRVAIARALAMSPKV 159
Cdd:COG1132 425 LF-SGTIRENIRYGRpdatdeevEEAAK--AAQAHEFIEALPDGYDtvVGER----GVNLSGGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695700954 160 LLCDEITSALDPELVGEVLKVLEQLAAeGMTLILVTHEMNFAREVgDRVVFMHQGKVWEQG 220
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRNA-DRILVLDDGRIVEQG 556
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-216 |
5.04e-42 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 142.01 E-value: 5.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 11 KYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGmtitdRDSQAREISRSVGMVFQS--F 88
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-----KPIKAKERRKSIGYVMQDvdY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 89 NLFPHMTALEnvmlapRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSA 168
Cdd:cd03226 83 QLFTDSVREE------LLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695700954 169 LDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:cd03226 157 LDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-216 |
9.62e-42 |
|
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: 139.87 E-value: 9.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTI---TDRDSQAREIsrs 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVsfaSPRDARRAGI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 vGMVFQsfnlfphmtalenvmlaprrvlkksaaecrelaqqmlekvglgdrldyypssLSGGQQQRVAIARALAMSPKVL 160
Cdd:cd03216 78 -AMVYQ----------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 161 LCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-220 |
1.65e-41 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 142.22 E-value: 1.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCING-LEGYQdGSIKLGGMTITdrDSQAREISRS 80
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDS-GEVRLNGRPLA--DWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 VGMVFQSFNL-FPhMTALENV-M-LAPRRvlkKSAAECRELAQQMLEKVG---LGDRldYYPsSLSGGQQQRVAIARALA 154
Cdd:PRK13548 78 RAVLPQHSSLsFP-FTVEEVVaMgRAPHG---LSRAEDDALVAAALAQVDlahLAGR--DYP-QLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695700954 155 ------MSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-238 |
1.89e-41 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 142.11 E-value: 1.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTIT-DRDS---QAREIS 78
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfGKDIfqiDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 79 RSVGMVFQSFNLFPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLG----DRLDYYPSSLSGGQQQRVAIARALA 154
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 155 MSPKVLLCDEITSALDPELVGEVLKVLEQLAAEgMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTEL 234
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
....
gi 695700954 235 KQFI 238
Cdd:PRK14246 249 EKYV 252
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
1.97e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 142.58 E-value: 1.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQ-KYYGDN-HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDsqAREISR 79
Cdd:PRK13648 6 SIIVFKNVSfQYQSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN--FEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 80 SVGMVFQS-FNLFPHMT-------ALENVMLaprrvlkkSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIAR 151
Cdd:PRK13648 84 HIGIVFQNpDNQFVGSIvkydvafGLENHAV--------PYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 152 ALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREvGDRVVFMHQGKVWEQGDSKTLF 226
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-222 |
2.59e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 143.30 E-value: 2.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLG----------------------GMTITDRDSQAR 75
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkkktkekekvleklviQKTRFKKIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 76 EISRSVGMVFQ--SFNLFpHMTALENVMLAPRRvLKKSAAECRELAQQMLEKVGLG-DRLDYYPSSLSGGQQQRVAIARA 152
Cdd:PRK13651 102 EIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVS-MGVSKEEAKKRAAKYIELVGLDeSYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 153 LAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDS 222
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDT 249
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-233 |
2.61e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 142.52 E-value: 2.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 5 TINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREISRSVGMV 84
Cdd:PRK13639 4 TRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 85 FQSFN--LFPHmTALENVMLAPRRvLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLC 162
Cdd:PRK13639 84 FQNPDdqLFAP-TVEEDVAFGPLN-LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695700954 163 DEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTE 233
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-233 |
3.06e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 142.18 E-value: 3.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGD-NHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSqaREISRSVG 82
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENE--KWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 83 MVFQSFN--LFPhMTALENVMLAPRRvLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:PRK13647 83 LVFQDPDdqVFS-STVWDDVAFGPVN-MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695700954 161 LCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDsKTLFANPQTTE 233
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD-KSLLTDEDIVE 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-234 |
3.76e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 142.15 E-value: 3.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDrDSQAREISRSVGMVFQS-FNLFPHMTA 96
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSD-EENLWDIRNKAGMVFQNpDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 97 LENVMLAPRRvLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGE 176
Cdd:PRK13633 104 EEDVAFGPEN-LGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRRE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 177 VLKVLEQLAAE-GMTLILVTHEMNFAREvGDRVVFMHQGKVWEQGDSKTLFAN-----------PQTTEL 234
Cdd:PRK13633 183 VVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEvemmkkigldvPQVTEL 251
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-229 |
8.90e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 142.30 E-value: 8.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAR--------------EISRSVGM 83
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHElitnpyskkiknfkELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQ--SFNLFPHmTALENVMLAPRrVLKKSAAECRELAQQMLEKVGLGDR-LDYYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMFGPV-ALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 161 LCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANP 229
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-218 |
1.40e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 140.21 E-value: 1.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYY---------GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRD 71
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 72 -SQAREISRSVGMVFQ----SFNlfPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGDR-LDYYPSSLSGGQQQ 145
Cdd:PRK10419 81 rAQRKAFRRDIQMVFQdsisAVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695700954 146 RVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWE 218
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-230 |
2.70e-40 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 141.26 E-value: 2.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYY--------GDNHV--LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDR 70
Cdd:PRK11308 3 QPLLQAIDLKKHYpvkrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 71 DSQAR-EISRSVGMVFQSfnlfPHMTalenvmLAPRrvlKK---------------SAAECRELAQQMLEKVGL-GDRLD 133
Cdd:PRK11308 83 DPEAQkLLRQKIQIVFQN----PYGS------LNPR---KKvgqileepllintslSAAERREKALAMMAKVGLrPEHYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 134 YYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMH 212
Cdd:PRK11308 150 RYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMY 229
|
250
....*....|....*...
gi 695700954 213 QGKVWEQGDSKTLFANPQ 230
Cdd:PRK11308 230 LGRCVEKGTKEQIFNNPR 247
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-243 |
3.67e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 139.46 E-value: 3.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGL----EGYQ-DGSIKLGGMTITD-RDsqAREISRSVGMVFQSFNLF 91
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvSGYRySGDVLLGGRSIFNyRD--VLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 92 PhMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGL----GDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITS 167
Cdd:PRK14271 114 P-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 168 ALDPELVGEVLKVLEQLaAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFISSVRG 243
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSG 267
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-240 |
4.42e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 139.02 E-value: 4.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQ-----DGSIKLGGMTITDRDSQAR 75
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 76 EISRSVGMVFQSFNLFPhMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDY--YPSSL--SGGQQQRVAIAR 151
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHkiHKSALdlSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 152 ALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEG-MTLILVTHEMNFAREVGDRVVFMHQ-----GKVWEQGDSKTL 225
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKI 243
|
250
....*....|....*
gi 695700954 226 FANPQTTELKQFISS 240
Cdd:PRK14258 244 FNSPHDSRTREYVLS 258
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-220 |
9.59e-40 |
|
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: 136.73 E-value: 9.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITdrdSQAREISRSVGM 83
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV---REPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVMLAPRrVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHAR-LYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695700954 164 EITSALDPELVGEVLKVLEQL-AAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-220 |
9.70e-40 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 136.19 E-value: 9.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREIsrsvGM 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRI----GA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVMLApRRVLKKSAAECrelaQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLL-ARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 164 EITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-236 |
1.11e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 138.34 E-value: 1.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTIT--DRDSQAREISRSVGMVFQsfnlFPHM-- 94
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstSKNKDIKQIRKKVGLVFQ----FPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 95 ---TALENVMLAPRRvLKKSAAECRELAQQMLEKVGLGDRL-DYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALD 170
Cdd:PRK13649 99 feeTVLKDVAFGPQN-FGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 171 PELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQ 236
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFLEEKQ 243
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-220 |
1.16e-39 |
|
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: 136.17 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGqVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDrdsQAREISRSVGM 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK---QPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALEnvMLAPRRVLKK-SAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLC 162
Cdd:cd03264 77 LPQEFGVYPNFTVRE--FLDYIAWLKGiPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695700954 163 DEITSALDPELVGEVLKVLEQLAAEgMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-241 |
1.24e-39 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 140.94 E-value: 1.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITD-RDSQAREISRS-VGMVFQSFNLFPHMTA 96
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKiSDAELREVRRKkIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 97 LENVMLApRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGE 176
Cdd:PRK10070 124 LDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 177 VLKVLEQLAAEGM-TLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFISSV 241
Cdd:PRK10070 203 MQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-216 |
2.64e-39 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 135.77 E-value: 2.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQK-YYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITD-RDSQAREISRS 80
Cdd:PRK10908 1 MIRFEHVSKaYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 VGMVFQSFNLFPHMTALENVMLaPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 161 LCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-230 |
4.43e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 136.88 E-value: 4.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQA--REISRSVGMVFQsfnlFPHM-- 94
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlKKLRKKVSLVFQ----FPEAql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 95 ---TALENVMLAPRRvLKKSAAECRELAQQMLEKVGLGDRL-DYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALD 170
Cdd:PRK13641 99 fenTVLKDVEFGPKN-FGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 171 PELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQ 230
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-219 |
6.60e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 134.94 E-value: 6.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNH----VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREI 77
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 78 --SRSVGMVFQSFNLFPHMTALENVMLaPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAM 155
Cdd:PRK11629 84 lrNQKLGFIYQFHHLLPDFTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 156 SPKVLLCDEITSALDPELVGEVLKVLEQL-AAEGMTLILVTHEMNFAREVgDRVVFMHQGKVWEQ 219
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-220 |
2.21e-38 |
|
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: 133.26 E-value: 2.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYGDN----HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMtitDRDSQAREIS 78
Cdd:cd03266 1 MITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF---DVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 79 RSVGMVFQSFNLFPHMTALENVMLAPR-RVLKKSAAECR--ELAQQMlekvGLGDRLDYYPSSLSGGQQQRVAIARALAM 155
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENLEYFAGlYGLKGDELTARleELADRL----GMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 156 SPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-234 |
4.40e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 133.96 E-value: 4.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYGDNH-VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRdSQAREISRSV 81
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF-SKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNL-FPHMTALENVMLAPRRvLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:PRK13644 80 GIVFQNPETqFVGRTVEEDLAFGPEN-LCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695700954 161 LCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNfAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTEL 234
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-216 |
6.08e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 134.08 E-value: 6.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDsqAREIS----- 78
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED--RRRIGylpee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 79 RSvgmvfqsfnLFPHMTALENVM-LAPRRVLKKSAAecRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSP 157
Cdd:COG4152 80 RG---------LYPKMKVGEQLVyLARLKGLSKAEA--KRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 158 KVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-237 |
7.44e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 133.75 E-value: 7.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYG-----DNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDR--DSQARE 76
Cdd:PRK13646 3 IRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 77 ISRSVGMVFQsfnlFPHMTALEN-----VMLAPRRvLKKSAAECRELAQQMLEKVGLG-DRLDYYPSSLSGGQQQRVAIA 150
Cdd:PRK13646 83 VRKRIGMVFQ----FPESQLFEDtvereIIFGPKN-FKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 151 RALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFAnp 229
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK-- 235
|
....*...
gi 695700954 230 QTTELKQF 237
Cdd:PRK13646 236 DKKKLADW 243
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-211 |
2.41e-37 |
|
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: 130.63 E-value: 2.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKL--GGMTITDRDSQAREI----SRSVGMVFQSFNLF 91
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPREIlalrRRTIGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 92 PHMTALENVMlAPRRVLKKSAAECRELAQQMLEKVGLGDRL-DYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALD 170
Cdd:COG4778 106 PRVSALDVVA-EPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695700954 171 PELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFM 211
Cdd:COG4778 185 AANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-227 |
7.38e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 131.01 E-value: 7.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQ-KYYGD--NHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDsqAREISR 79
Cdd:PRK13650 4 IIEVKNLTfKYKEDqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN--VWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 80 SVGMVFQS-FNLFPHMT-------ALENVMLAPRrvlkksaaECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIAR 151
Cdd:PRK13650 82 KIGMVFQNpDNQFVGATveddvafGLENKGIPHE--------EMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 152 ALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNfarEVG--DRVVFMHQGKVWEQGDSKTLFA 227
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD---EVAlsDRVLVMKNGQVESTSTPRELFS 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-230 |
8.10e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 129.76 E-value: 8.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITD-----RdsqAR 75
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmhkR---AR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 76 eisRSVGMVFQSFNLFPHMTALENVMlAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAM 155
Cdd:COG1137 78 ---LGIGYLPQEASIFRKLTVEDNIL-AVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 156 SPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTlILVT-HemNfARE---VGDRVVFMHQGKVWEQGDSKTLFANPQ 230
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIG-VLITdH--N-VREtlgICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-227 |
3.16e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 129.93 E-value: 3.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAReisRSV 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR---QRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFPHMTALENvMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLL 161
Cdd:PRK13537 83 GVVPQFDNLDPDFTVREN-LLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 162 CDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFA 227
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-226 |
3.97e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 129.47 E-value: 3.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 22 VDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQA--REISRSVGMVFQsfnlFPHM----- 94
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeiKPVRKKVGVVFQ----FPESqlfee 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 95 TALENVMLAPRRvLKKSAAECRELAQQMLEKVGLGDRL-DYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPEL 173
Cdd:PRK13643 101 TVLKDVAFGPQN-FGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695700954 174 VGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLF 226
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-220 |
7.77e-36 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 127.51 E-value: 7.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSqaREISRSVGM 83
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPS--RELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQS--FNL------------FPH----MTalenvmlaprrvlkksaAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQ 145
Cdd:COG4604 80 LRQEnhINSrltvrelvafgrFPYskgrLT-----------------AEDREIIDEAIAYLDLEDLADRYLDELSGGQRQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 146 RVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
8-230 |
1.51e-35 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 129.22 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 8 QVQKYYGDnHVLKgVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQareIS-----RSVG 82
Cdd:PRK11144 5 NFKQQLGD-LCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKG---IClppekRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 83 MVFQSFNLFPHMTALENVMLAPRRVLKksaaecrELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLC 162
Cdd:PRK11144 80 YVFQDARLFPHYKVRGNLRYGMAKSMV-------AQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 163 DEITSALDPELVGEVLKVLEQLAAEGMTLIL-VTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQ 230
Cdd:PRK11144 153 DEPLASLDLPRKRELLPYLERLAREINIPILyVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-227 |
2.19e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 127.27 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYGD-NHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREISRSV 81
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQS--FNLFPhMTALENVMLAPRRvLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKV 159
Cdd:PRK13636 85 GMVFQDpdNQLFS-ASVYQDVSFGAVN-LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 160 LLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFA 227
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-230 |
4.75e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 126.45 E-value: 4.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNH--VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGL---EGYQDGSIKLGGMTITDRDsqAREIS 78
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKT--VWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 79 RSVGMVFQS-FNLFPHMTALENVM--LAPRRVlkkSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAM 155
Cdd:PRK13640 84 EKVGIVFQNpDNQFVGATVGDDVAfgLENRAV---PRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 156 SPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFArEVGDRVVFMHQGKVWEQGDSKTLFANPQ 230
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-215 |
5.46e-35 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 125.49 E-value: 5.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQarEISRSv 81
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGH--QIARM- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMV--FQSFNLFPHMTALENVMLAPRRVLK--------------KSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQ 145
Cdd:PRK11300 81 GVVrtFQHVRLFREMTVIENLLVAQHQQLKtglfsgllktpafrRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695700954 146 RVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGK 215
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-220 |
6.68e-35 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 123.93 E-value: 6.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDrdsqarEISRSVGM 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI------AARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVM-LAPRRVLKKSAAecRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLC 162
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVyLAQLKGLKKEEA--RRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695700954 163 DEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-241 |
1.52e-34 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 124.27 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRD------SQA 74
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalseAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 75 REISRSV-GMVFQSF--NLFPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLG-DRLDYYPSSLSGGQQQRVAIA 150
Cdd:PRK11701 84 RRLLRTEwGFVHQHPrdGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 151 RALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANP 229
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDP 243
|
250
....*....|....
gi 695700954 230 QT--TELkqFISSV 241
Cdd:PRK11701 244 QHpyTQL--LVSSV 255
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-229 |
1.68e-34 |
|
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: 123.42 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDR--DSQAReisRSV 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmHKRAR---LGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFPHMTALENVMLApRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLL 161
Cdd:cd03218 78 GYLPQEASIFRKLTVEENILAV-LEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695700954 162 CDEITSALDPELVGEVLKVLEQLAAEGMTlILVT-HEmnfARE---VGDRVVFMHQGKVWEQGDSKTLFANP 229
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIG-VLITdHN---VREtlsITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-228 |
2.70e-34 |
|
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: 123.03 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 15 DNHVLKGVDLDIDMGQVISIIGRSGSGKSTllrCINGLEGYQD---GSIKLGGMTItdRDSQAREISRSVGMVFQSFNLF 91
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERFYDptsGEILLDGVDI--RDLNLRWLRSQIGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 92 PhMTALENVML-APRRVLKKSAAECRE-LAQQMLEKvgLGDRLDY----YPSSLSGGQQQRVAIARALAMSPKVLLCDEI 165
Cdd:cd03249 90 D-GTIAENIRYgKPDATDEEVEEAAKKaNIHDFIMS--LPDGYDTlvgeRGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695700954 166 TSALDPELVGEVLKVLEQlAAEGMTLILVTHEMNFAREVgDRVVFMHQGKVWEQGDSKTLFAN 228
Cdd:cd03249 167 TSALDAESEKLVQEALDR-AMKGRTTIVIAHRLSTIRNA-DLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-220 |
3.01e-34 |
|
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: 123.27 E-value: 3.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGlEGYQ--DGSI-----KLGGMTItdrdsq 73
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG-DLPPtyGNDVrlfgeRRGGEDV------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 74 aREISRSVGMVFQSFNLF--PHMTALENVMLA-------PRRVlkkSAAEcRELAQQMLEKVGLGDRLDYYPSSLSGGQQ 144
Cdd:COG1119 74 -WELRKRIGLVSPALQLRfpRDETVLDVVLSGffdsiglYREP---TDEQ-RERARELLELLGLAHLADRPFGTLSQGEQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 145 QRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEG-MTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
4.85e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 123.37 E-value: 4.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLI-TINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDsqAREISR 79
Cdd:PRK13652 1 MHLIeTRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN--IREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 80 SVGMVFQSFN--LFPhMTALENVMLAPRRV-LKKSAAECRelAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMS 156
Cdd:PRK13652 79 FVGLVFQNPDdqIFS-PTVEQDIAFGPINLgLDEETVAHR--VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695700954 157 PKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANP 229
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-211 |
8.88e-34 |
|
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: 127.40 E-value: 8.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQ-KYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREisRSVG 82
Cdd:TIGR02857 322 LEFSGVSvAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWR--DQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 83 MVFQSFNLFPHmTALENVMLAPRRVlkkSAAECRELAQQ--MLEKV-----GLGDRLDYYPSSLSGGQQQRVAIARALAM 155
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLARPDA---SDAEIREALERagLDEFVaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 156 SPKVLLCDEITSALDPELVGEVLKVLEQLaAEGMTLILVTHEMNFAREVgDRVVFM 211
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-230 |
9.99e-34 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 123.70 E-value: 9.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHV-LKGVD---LDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQdGSIKLGGMTITDRDSQA-- 74
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP-GRVMAEKLEFNGQDLQRis 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 75 ----REISRS-VGMVFQ----SFNlfPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGD---RLDYYPSSLSGG 142
Cdd:PRK11022 80 ekerRNLVGAeVAMIFQdpmtSLN--PCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 143 QQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLA-AEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGD 221
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
....*....
gi 695700954 222 SKTLFANPQ 230
Cdd:PRK11022 238 AHDIFRAPR 246
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-220 |
1.12e-33 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 125.34 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDsqAREISRS 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS--ARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 VGMVFQ----SFNL----------FPHMTALENVMLAPRRVLkksaaecrelaQQMLEKVGLGDRLDYYPSSLSGGQQQR 146
Cdd:PRK09536 79 VASVPQdtslSFEFdvrqvvemgrTPHRSRFDTWTETDRAAV-----------ERAMERTGVAQFADRPVTSLSGGERQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695700954 147 VAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-220 |
1.31e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 121.66 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDrdSQAREISRSVGM 83
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM--LSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQsfnlfpHMTALENVMLapRRVLK-----------KSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARA 152
Cdd:PRK11231 81 LPQ------HHLTPEGITV--RELVAygrspwlslwgRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695700954 153 LAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-227 |
1.58e-33 |
|
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: 120.80 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 11 KYYGD-NHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTItdRDSQAREISRSVGMVFQSFN 89
Cdd:cd03251 9 RYPGDgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV--RDYTLASLRRQIGLVSQDVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 90 LFpHMTALENVMLAPRRVLKKS------AAECRELAQQMLEKVG--LGDRldyyPSSLSGGQQQRVAIARALAMSPKVLL 161
Cdd:cd03251 87 LF-NDTVAENIAYGRPGATREEveeaarAANAHEFIMELPEGYDtvIGER----GVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 162 CDEITSALDPELVGEVLKVLEQLaAEGMTLILVTHEMNFAREvGDRVVFMHQGKVWEQGDSKTLFA 227
Cdd:cd03251 162 LDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-216 |
2.18e-33 |
|
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: 119.58 E-value: 2.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCING-LEGYQD-GSIKLGGmtitdRDSQAREISRSVGMVFQSFNLFPHMT 95
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVsGEVLING-----RPLDKRSFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 96 ALENVMLAprrvlkksaAECRelaqqmlekvglgdrldyypsSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVG 175
Cdd:cd03213 99 VRETLMFA---------AKLR---------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695700954 176 EVLKVLEQLAAEGMTLILVTHE-MNFAREVGDRVVFMHQGKV 216
Cdd:cd03213 149 QVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-224 |
4.35e-33 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 120.19 E-value: 4.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 6 INQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGmtitdrdsqarEISR--SVGM 83
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-----------RVSAllELGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQsfnlfPHMTALENVML-AprRVLKKSAAECRELAQQMLEKVGLGDRLD----YYPSslsgGQQQRVAIARALAMSPK 158
Cdd:COG1134 98 GFH-----PELTGRENIYLnG--RLLGLSRKEIDEKFDEIVEFAELGDFIDqpvkTYSS----GMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 159 VLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKT 224
Cdd:COG1134 167 ILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-227 |
4.97e-33 |
|
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: 119.64 E-value: 4.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 12 YYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRD-SQAREisrSVGMVFQSFNL 90
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrKSLRS---MIGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 91 FPHmTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYP----SSLSGGQQQRVAIARALAMSPKVLLCDEIT 166
Cdd:cd03254 89 FSG-TIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLgengGNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695700954 167 SALDPE---LVGEVLKVLeqlaAEGMTLILVTHEMNFAREVgDRVVFMHQGKVWEQGDSKTLFA 227
Cdd:cd03254 168 SNIDTEtekLIQEALEKL----MKGRTSIIIAHRLSTIKNA-DKILVLDDGKIIEEGTHDELLA 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-228 |
5.03e-33 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 119.98 E-value: 5.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSqAREISRS 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT-AKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 VGMVFQSFNLFPHMTALENVMLAprrvlkkSAAECRELAQQMLEKV-----GLGDRLDYYPSSLSGGQQQRVAIARALAM 155
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMG-------GFFAERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695700954 156 SPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFAN 228
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-227 |
7.74e-33 |
|
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: 119.13 E-value: 7.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 11 KYYGDN-HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAreISRSVGMVFQSFN 89
Cdd:cd03252 9 RYKPDGpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW--LRRQVGVVLQENV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 90 LFpHMTALENVMLA----PRRVLKKSA--AECRELAQQMLEKVG--LGDRldyyPSSLSGGQQQRVAIARALAMSPKVLL 161
Cdd:cd03252 87 LF-NRSIRDNIALAdpgmSMERVIEAAklAGAHDFISELPEGYDtiVGEQ----GAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 162 CDEITSALDPELVGEVLKVLEQLAAeGMTLILVTHEMNFAREvGDRVVFMHQGKVWEQGDSKTLFA 227
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-216 |
8.79e-33 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 117.32 E-value: 8.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 14 GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSqaREISRSVGMVFQSFNLFPH 93
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP--NELGDHVGYLPQDDELFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 94 mTALENVmlaprrvlkksaaecrelaqqmlekvglgdrldyypssLSGGQQQRVAIARALAMSPKVLLCDEITSALDPEL 173
Cdd:cd03246 91 -SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695700954 174 VGEVLKVLEQLAAEGMTLILVTHEMNFAREVgDRVVFMHQGKV 216
Cdd:cd03246 132 ERALNQAIAALKAAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-220 |
1.19e-32 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 118.08 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGD--NHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQarEISRSV 81
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPA--DLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFpHMTALENVMLAprrvlkKSAAECRELAQQMlEKVGLGDRLDYYP-----------SSLSGGQQQRVAIA 150
Cdd:cd03245 81 GYVPQDVTLF-YGTLRDNITLG------APLADDERILRAA-ELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 151 RALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAeGMTLILVTHEMNFAREVgDRVVFMHQGKVWEQG 220
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLLDLV-DRIIVMDSGRIVADG 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-196 |
3.77e-32 |
|
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: 122.85 E-value: 3.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 12 YYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQarEISRSVGMVFQSFNLF 91
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD--EVRRRVSVCAQDAHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 92 pHMTALENVMLAprrvlKKSAAEcrELAQQMLEKVGLGDRLDYYP-----------SSLSGGQQQRVAIARALAMSPKVL 160
Cdd:TIGR02868 422 -DTTVRENLRLA-----RPDATD--EELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPIL 493
|
170 180 190
....*....|....*....|....*....|....*.
gi 695700954 161 LCDEITSALDPELVGEVLKVLEQlAAEGMTLILVTH 196
Cdd:TIGR02868 494 LLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-241 |
4.13e-32 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 123.43 E-value: 4.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 17 HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTI-TDRDSQAREISRSVGMVFQS--FNLFPH 93
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLSPGKLQALRRDIQFIFQDpyASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 94 MTALENVMlAPRRV---LKKSAAECRelAQQMLEKVGLGDRLDY-YPSSLSGGQQQRVAIARALAMSPKVLLCDEITSAL 169
Cdd:PRK10261 418 QTVGDSIM-EPLRVhglLPGKAAAAR--VAWLLERVGLLPEHAWrYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695700954 170 DPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFISSV 241
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-211 |
4.49e-32 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 117.88 E-value: 4.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAreisrsvG 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-------G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 83 MVFQSFNLFPHMTALENVMLApRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLC 162
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695700954 163 DEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFArevgdrvVFM 211
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEA-------VFM 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-227 |
5.67e-32 |
|
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: 122.22 E-value: 5.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYG--DNHVLKGVD---LDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGS--IKLG----GMTITDR 70
Cdd:TIGR03269 278 PIIKVRNVSKRYIsvDRGVVKAVDnvsLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGdewvDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 71 DSQAReISRSVGMVFQSFNLFPHMTALENVMLAPRRVLKKSAAECRelAQQMLEKVGLGDR-----LDYYPSSLSGGQQQ 145
Cdd:TIGR03269 358 DGRGR-AKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMK--AVITLKMVGFDEEkaeeiLDKYPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 146 RVAIARALAMSPKVLLCDEITSALDP----ELVGEVLKVLEQLaaeGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGD 221
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPitkvDVTHSILKAREEM---EQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
....*.
gi 695700954 222 SKTLFA 227
Cdd:TIGR03269 512 PEEIVE 517
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-216 |
5.95e-32 |
|
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: 116.60 E-value: 5.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEgyQDGSIKLGGMTITDRDSQAREISRSVGMVFQSFNLFPHMTAL 97
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 98 ENVMLAPR---RVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELV 174
Cdd:cd03234 100 ETLTYTAIlrlPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695700954 175 GEVLKVLEQLAAEGMTLILVTH----EMnFarEVGDRVVFMHQGKV 216
Cdd:cd03234 180 LNLVSTLSQLARRNRIVILTIHqprsDL-F--RLFDRILLLSSGEI 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-227 |
1.11e-31 |
|
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: 121.45 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKL--------------------- 62
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 63 ------GGMTITDRD------SQAREISRSVGMVFQ-SFNLFPHMTALENVMLAPRRvLKKSAAECRELAQQMLEKVGLG 129
Cdd:TIGR03269 81 pcpvcgGTLEPEEVDfwnlsdKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEE-IGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 130 DRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLA-AEGMTLILVTHEMNFAREVGDRV 208
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*....
gi 695700954 209 VFMHQGKVWEQGDSKTLFA 227
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVVA 258
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-239 |
1.70e-31 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 120.97 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 14 GDNHVLKGVDLDIDMGQVISIIGRSGSGKST----LLRCINglegyQDGSIKLGGMTITDRD-SQAREISRSVGMVFQSF 88
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNrRQLLPVRHRIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 89 N--LFPHMTALEnVMLAPRRVLKK--SAAECRELAQQMLEKVGLGDRLDY-YPSSLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:PRK15134 372 NssLNPRLNVLQ-IIEEGLRVHQPtlSAAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 164 EITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFIS 239
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-240 |
2.92e-31 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 116.04 E-value: 2.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAReiSRSVGMVFQ--SFNLFPHMTa 96
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYR--SQRIRMIFQdpSTSLNPRQR- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 97 LENVMLAPRRVLKKSAAECRELA-QQMLEKVGL-GDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELV 174
Cdd:PRK15112 106 ISQILDFPLRLNTDLEPEQREKQiIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 175 GEVLKV-LEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFISS 240
Cdd:PRK15112 186 SQLINLmLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAG 252
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-209 |
3.54e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 113.48 E-value: 3.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 13 YGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIklggmtitdrdsqAREISRSVGMVFQSFNL-- 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------------RRAGGARVAYVPQRSEVpd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 91 -FPhMTALENVML---APRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEIT 166
Cdd:NF040873 69 sLP-LTVRDLVAMgrwARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695700954 167 SALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREvGDRVV 209
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCV 189
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-227 |
1.42e-30 |
|
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: 113.48 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 12 YYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTItdRDSQAREISRSVGMVFQSFNLF 91
Cdd:cd03253 10 YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI--REVTLDSLRRAIGVVPQDTVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 92 pHMTALENVMLAPrrvLKKSAAECRELAqqmlEKVGLGDRLDYYPSS-----------LSGGQQQRVAIARALAMSPKVL 160
Cdd:cd03253 88 -NDTIGYNIRYGR---PDATDEEVIEAA----KAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 161 LCDEITSALDPELVGEVLKVLEQLAAeGMTLILVTHEMnfaREV--GDRVVFMHQGKVWEQGDSKTLFA 227
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRL---STIvnADKIIVLKDGRIVERGTHEELLA 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-240 |
1.52e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 118.27 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQV----QKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKS-TLLRCINGLEG----YQDGSIKLGGMTITDRD 71
Cdd:PRK15134 3 QPLLAIENLsvafRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvYPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 72 SQA-REI-SRSVGMVFQS--FNLFPHMTaLENVM---LAPRRVLKKSAAecRELAQQMLEKVGL---GDRLDYYPSSLSG 141
Cdd:PRK15134 83 EQTlRGVrGNKIAMIFQEpmVSLNPLHT-LEKQLyevLSLHRGMRREAA--RGEILNCLDRVGIrqaAKRLTDYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 142 GQQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQN 239
|
250 260
....*....|....*....|
gi 695700954 221 DSKTLFANPQTTELKQFISS 240
Cdd:PRK15134 240 RAATLFSAPTHPYTQKLLNS 259
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-228 |
2.18e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 118.00 E-value: 2.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDN--HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREISR 79
Cdd:PRK11160 337 VSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 80 SVgmVFQSFNLFPHmTALENVMLAprrvlKKSAAEcrELAQQMLEKVGLGDRLDYYPS----------SLSGGQQQRVAI 149
Cdd:PRK11160 417 SV--VSQRVHLFSA-TLRDNLLLA-----APNASD--EALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 150 ARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAeGMTLILVTHEMNfAREVGDRVVFMHQGKVWEQGDSKTLFAN 228
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-220 |
6.93e-30 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 117.07 E-value: 6.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 17 HVLKGVDLDIDMGQVISIIGRSGSGKSTLL-----RCINGLEGyqDGSIKLGGMTITdrdsqAREISRSVGMVFQSFNLF 91
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVKG--SGSVLLNGMPID-----AKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 92 PHMTALENVMLA-----PRRVLKKsaaECRELAQQMLEKVGLGDRLD------YYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:TIGR00955 112 PTLTVREHLMFQahlrmPRRVTKK---EKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695700954 161 LCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMN---FarEVGDRVVFMHQGKVWEQG 220
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSselF--ELFDKIILMAEGRVAYLG 249
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-228 |
1.64e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 112.02 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTI---TDRDSQAREISRSVGMVFQ--SFNLFPH 93
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanLKKIKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 94 mTALENVMLAPRRvLKKSAAECRELAQQMLEKVGLG-DRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPE 172
Cdd:PRK13645 107 -TIEKDIAFGPVN-LGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 173 LVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFAN 228
Cdd:PRK13645 185 GEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-214 |
1.87e-29 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 115.27 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTItDRDSQAREISRSV 81
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINY-NKLDHKLAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFPHMTALENVMLApRRVLKK-------SAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALA 154
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIG-RHLTKKvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 155 MSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQG 214
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-220 |
1.91e-29 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 108.55 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDN--HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQareISRSV 81
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA---LSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFpHMTALENvmlaprrvlkksaaecrelaqqmlekvgLGDRLdyypsslSGGQQQRVAIARALAMSPKVLL 161
Cdd:cd03247 78 SVLNQRPYLF-DTTLRNN----------------------------LGRRF-------SGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 162 CDEITSALDPELVGEVLKVLEQlAAEGMTLILVTHEMNfAREVGDRVVFMHQGKVWEQG 220
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFE-VLKDKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-220 |
2.37e-29 |
|
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: 109.93 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 6 INQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGmtitdRDSQAREIsrsvGMVF 85
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-----RVSSLLGL----GGGF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 86 QsfnlfPHMTALENV-MLAprRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDE 164
Cdd:cd03220 96 N-----PELTGRENIyLNG--RLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 165 ITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-241 |
5.53e-29 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 109.85 E-value: 5.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTI-TDRDSQAREISRSV 81
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpAMSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLL 161
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 162 CDEITSALDPELVGEVLKVLEQL-AAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQtTELKQFISS 240
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD-PRVRQFLDG 245
|
.
gi 695700954 241 V 241
Cdd:PRK11831 246 I 246
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-216 |
7.80e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 113.24 E-value: 7.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 6 INQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIklggmtitDRDSQAReisrsVGMVF 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------SIPKGLR-----IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 86 QSFNLFPHMTALENVM--LAPRRVLKKSAAECREL-----------------------------AQQMLEKVGLGDRLDY 134
Cdd:COG0488 68 QEPPLDDDLTVLDTVLdgDAELRALEAELEELEAKlaepdedlerlaelqeefealggweaearAEEILSGLGFPEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 135 YP-SSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVgevlKVLEQ-LAAEGMTLILVTHEMNFAREVGDRVVFMH 212
Cdd:COG0488 148 RPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESI----EWLEEfLKNYPGTVLVVSHDRYFLDRVATRILELD 223
|
....
gi 695700954 213 QGKV 216
Cdd:COG0488 224 RGKL 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-216 |
8.98e-29 |
|
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: 107.13 E-value: 8.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAReISRSVGMV---FQSFNLFPHM 94
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA-IRAGIAYVpedRKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 95 TALENVMLaprrvlkksaaecrelaqqmlekvglgdrldyyPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELV 174
Cdd:cd03215 94 SVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695700954 175 GEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:cd03215 141 AEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-215 |
1.42e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 110.31 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAReisRSVGM 83
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLAR---ARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENvMLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:PRK13536 119 VPQFDNLDLEFTVREN-LLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695700954 164 EITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGK 215
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-216 |
3.85e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.26 E-value: 3.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 14 GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAReISRSVGMV---FQSFNL 90
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDA-IRAGIAYVpedRKGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 91 FPHMTALENVMLAPRRVLKK----SAAECRELAQQMLEKVGL-GDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEI 165
Cdd:COG1129 342 VLDLSIRENITLASLDRLSRggllDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695700954 166 TSALDpelVG---EVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:COG1129 422 TRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-218 |
7.07e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 111.05 E-value: 7.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIklggmtitDRDSQAReisrsvgMVF--QSfnlfPHMT 95
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGAR-------VLFlpQR----PYLP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 96 A--LENVMLAPRRVLKKSAAECRELaqqmLEKVGLG---DRLDY---YPSSLSGGQQQRVAIARALAMSPKVLLCDEITS 167
Cdd:COG4178 439 LgtLREALLYPATAEAFSDAELREA----LEAVGLGhlaERLDEeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695700954 168 ALDPELVGEVLKVLEQlAAEGMTLILVTHE---MNFArevgDRVVFMHQGKVWE 218
Cdd:COG4178 515 ALDEENEAALYQLLRE-ELPGTTVISVGHRstlAAFH----DRVLELTGDGSWQ 563
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-221 |
7.15e-28 |
|
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: 110.99 E-value: 7.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 14 GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQarEISRSVGMVFQSFNLFPH 93
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDRE--ELGRHIGYLPQDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 94 mTALENV----MLAPRRVLKksAAE---CRELAQQMLEkvGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEIT 166
Cdd:COG4618 421 -TIAENIarfgDADPEKVVA--AAKlagVHEMILRLPD--GYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 167 SALDPElvGE--VLKVLEQLAAEGMTLILVTHEMNFAREVgDRVVFMHQGKVWEQGD 221
Cdd:COG4618 496 SNLDDE--GEaaLAAAIRALKARGATVVVITHRPSLLAAV-DKLLVLRDGRVQAFGP 549
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
7-230 |
8.28e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.10 E-value: 8.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 7 NQVQKYYGDNHV--LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDsqAREISRSVGMV 84
Cdd:PRK13642 9 NLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN--VWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 85 FQS-FNLFPHMTALENVMLAprrvLKKSAAECRELAQQMLEKVGLGDRLDYY---PSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:PRK13642 87 FQNpDNQFVGATVEDDVAFG----MENQGIPREEMIKRVDEALLAVNMLDFKtrePARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695700954 161 LCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREvGDRVVFMHQGKVWEQGDSKTLFANPQ 230
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-216 |
2.93e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.00 E-value: 2.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLG-GMTIT--DrdsQAREis 78
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGeTVKIGyfD---QHQE-- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 79 rsvgmvfqsfNLFPHMTALENVM-LAPrrvlKKSAAECRELAQQMLEKvglGDRLDYYPSSLSGGQQQRVAIARALAMSP 157
Cdd:COG0488 389 ----------ELDPDKTVLDELRdGAP----GGTEQEVRGYLGRFLFS---GDDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695700954 158 KVLLCDEITSALDPelvgEVLKVLEQ-LAA-EGmTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:COG0488 452 NVLLLDEPTNHLDI----ETLEALEEaLDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-229 |
4.15e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 106.35 E-value: 4.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 14 GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGL---EGYQDGSIKLGGMTITDRDS------QAREISrsvgMV 84
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEkelnklRAEQIS----MI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 85 FQ----SFNlfPHMTALENVMlaprRVL----KKSAAECRELAQQMLEKVGLGD---RLDYYPSSLSGGQQQRVAIARAL 153
Cdd:PRK09473 103 FQdpmtSLN--PYMRVGEQLM----EVLmlhkGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 154 AMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANP 229
Cdd:PRK09473 177 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-223 |
5.30e-27 |
|
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: 102.99 E-value: 5.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQ--DGSIKLGGMTITDR--DSQAReisR 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLppEERAR---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 80 SVGMVFQSfnlfphmtalenvmlaPRRVlkksaaecrelaqqmlEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKV 159
Cdd:cd03217 78 GIFLAFQY----------------PPEI----------------PGVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 160 LLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREV-GDRVVFMHQGKVWEQGDSK 223
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKE 190
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-233 |
1.14e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 103.93 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 13 YGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREISRSVGMVFQSFNLFP 92
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 93 HMTALENVMLAPRRVLKKSAAEcreLAQQMLEKVGLGD--RLDYYP-SSLSGGQQQRVAIARALAMSPKVLLCDEITSAL 169
Cdd:PRK13638 91 FYTDIDSDIAFSLRNLGVPEAE---ITRRVDEALTLVDaqHFRHQPiQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695700954 170 DPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTE 233
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAME 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-241 |
3.79e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 106.48 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREISR------------SVGMVFQ 86
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEqsaaqmrhvrgaDMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 87 S--FNLFPHMTALENVMLAPRRVLKKSAAECRELAQQMLEKVGLGDR---LDYYPSSLSGGQQQRVAIARALAMSPKVLL 161
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 162 CDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQTTELKQFISS 240
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAA 271
|
.
gi 695700954 241 V 241
Cdd:PRK10261 272 V 272
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-229 |
6.00e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 105.70 E-value: 6.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 15 DNHVLKG-VDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQdGSIKLGGMTITDRD-SQAReisRSVGMVFQSFNLFp 92
Cdd:PRK11174 361 DGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDpESWR---KHLSWVGQNPQLP- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 93 HMTALENVMLAprrvlKKSAAEcrELAQQMLEKVGLGDRLDYYP-----------SSLSGGQQQRVAIARALAMSPKVLL 161
Cdd:PRK11174 436 HGTLRDNVLLG-----NPDASD--EQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695700954 162 CDEITSALDPELVGEVLKVLEQlAAEGMTLILVTHEMNFAREVgDRVVFMHQGKVWEQGDSKTLFANP 229
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-227 |
1.01e-25 |
|
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: 104.80 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTItdRDSQAREISRSVGMVFQSFNLFPHmTAL 97
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL--ADYTLASLRRQVALVSQDVVLFND-TIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 98 ENVMLAPRRvlKKSAAECRELAQQmlekVGLGDRLDYYP-----------SSLSGGQQQRVAIARALAMSPKVLLCDEIT 166
Cdd:TIGR02203 424 NNIAYGRTE--QADRAEIERALAA----AYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695700954 167 SALDPELVGEVLKVLEQLaAEGMTLILVTHEMNfAREVGDRVVFMHQGKVWEQGDSKTLFA 227
Cdd:TIGR02203 498 SALDNESERLVQAALERL-MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLA 556
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-230 |
1.60e-25 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 100.54 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 20 KGVDLDIDMGQVISIIGRSGSGKStlLRCINGLEGYQDGSIKLGGMTITDRDSQAREI--SRSVGMVFQ----SFNLFPH 93
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCAlrGRKIATIMQnprsAFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 94 MT--ALENVmlaprRVLKKSAAECRELAqqMLEKVGLGDR---LDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSA 168
Cdd:PRK10418 98 MHthARETC-----LALGKPADDATLTA--ALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695700954 169 LDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQ 230
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-215 |
1.52e-24 |
|
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: 96.77 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCInglegyqdgsikLGGMTITdrdSQAREISRSVGMVFQS---FNlfphM 94
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL------------LGELEKL---SGSVSVPGSIAYVSQEpwiQN----G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 95 TALEN-VMLAP------RRVLKKSAAEcRELaqQMLEK---VGLGDRldyyPSSLSGGQQQRVAIARALAMSPKVLLCDE 164
Cdd:cd03250 81 TIRENiLFGKPfdeeryEKVIKACALE-PDL--EILPDgdlTEIGEK----GINLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695700954 165 ITSALDPElVGEVL--KVLEQLAAEGMTLILVTHEMNFAREVgDRVVFMHQGK 215
Cdd:cd03250 154 PLSAVDAH-VGRHIfeNCILGLLLNNKTRILVTHQLQLLPHA-DQIVVLDNGR 204
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-230 |
2.39e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 97.27 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREiSRS 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA-RRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 VGMVFQSFNLFPHMTALENVM--LAPRRVLKKSAAECRelAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPK 158
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMavLQIRDDLSAEQREDR--ANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695700954 159 VLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFANPQ 230
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-215 |
3.01e-24 |
|
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: 94.05 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTitdrdsqareisrsvgm 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 vfqsfnlfphmtalenvmlaprrvlkksaaecrelaqqmleKVGlgdrldYYPsSLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:cd03221 64 -----------------------------------------KIG------YFE-QLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695700954 164 EITSALDPELVgEVLKvlEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGK 215
Cdd:cd03221 96 EPTNHLDLESI-EALE--EALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
4-218 |
3.90e-24 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 96.18 E-value: 3.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKyygdnHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLggmtitdrDSQAREISRSVgm 83
Cdd:COG2401 36 VELRVVER-----YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV--------DVPDNQFGREA-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 vfqsfnlfphmTALENVmlaPRRVLKKSAAEcrelaqqMLEKVGLGDRLDYY--PSSLSGGQQQRVAIARALAMSPKVLL 161
Cdd:COG2401 101 -----------SLIDAI---GRKGDFKDAVE-------LLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 162 CDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVG-DRVVFMHQGKVWE 218
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-215 |
6.01e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 99.62 E-value: 6.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGL--EGYQDGSIKLGGMTI---TDRDSQAR 75
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELqasNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 76 EISrsvgMVFQSFNLFPHMTALENVMLA----PRRVLKKSAAECRelAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIAR 151
Cdd:PRK13549 83 GIA----IIHQELALVKELSVLENIFLGneitPGGIMDYDAMYLR--AQKLLAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695700954 152 ALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGK 215
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-216 |
1.36e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 98.58 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITdRDSQAREISRSV 81
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA-RLTPAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFPHMTALENVMLAprrvLKKSAAECRELaQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLL 161
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENILFG----LPKRQASMQKM-KQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 162 CDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-225 |
2.14e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 95.24 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAreISRSVGMVFQSFNLFPHMTAL 97
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA--FARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 98 ENVMLA--P-RRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELV 174
Cdd:PRK10575 104 ELVAIGryPwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695700954 175 GEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTL 225
Cdd:PRK10575 184 VDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-220 |
2.94e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 97.72 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 11 KYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLlrcINGLEGYQD---GSIKLGGMTItdRDSQAREISRSVGMVFQS 87
Cdd:PRK13657 343 SYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRVFDpqsGRILIDGTDI--RTVTRASLRRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 88 FNLFPHMTAlENVmlaprRVLKKSA--AECRELAQ--QMLEKV-----GLGDRLDYYPSSLSGGQQQRVAIARALAMSPK 158
Cdd:PRK13657 418 AGLFNRSIE-DNI-----RVGRPDAtdEEMRAAAEraQAHDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695700954 159 VLLCDEITSALDPELVGEVLKVLEQLaAEGMTLILVTHEMNFAREVgDRVVFMHQGKVWEQG 220
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRNA-DRILVFDNGRVVESG 551
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-223 |
3.23e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 94.14 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQdGSIKLGGMTItdRDSQAREISRSVGMVFQSFNLFPHMTALE 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPL--SDWSAAELARHRAYLSQQQSPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 99 NVMLAPRRVLkkSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAM-------SPKVLLCDEITSALDP 171
Cdd:COG4138 89 YLALHQPAGA--SSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695700954 172 ELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSK 223
Cdd:COG4138 167 AQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-229 |
3.49e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.87 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 15 DNHVLKGVDLDIDMGQVISIIGRSGSGKSTllrCINGLEG-YQ--DGSIKLGGMTITDRDSqaREISRSVGMVFQSFNLF 91
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNlYQptGGQVLLDGVPLVQYDH--HYLHRQVALVGQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 92 PHmTALENVMLAPRRvlkKSAAECRELAQQ-------MLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDE 164
Cdd:TIGR00958 568 SG-SVRENIAYGLTD---TPDEEIMAAAKAanahdfiMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 165 ITSALDpelvGEVLKVLEQL-AAEGMTLILVTHEMNFAREVgDRVVFMHQGKVWEQGDSKTLFANP 229
Cdd:TIGR00958 644 ATSALD----AECEQLLQESrSRASRTVLLIAHRLSTVERA-DQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-210 |
1.01e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.13 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQArEISRSVGMVFQSFNLFPHMTALE 98
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA-ALAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 99 NVMLA--PRR--VLKKSAAecRELAQQMLEKvgLGDRLDyyPS----SLSGGQQQRVAIARALAMSPKVLLCDEITSALD 170
Cdd:PRK11288 99 NLYLGqlPHKggIVNRRLL--NYEAREQLEH--LGVDID--PDtplkYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695700954 171 PELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRV-VF 210
Cdd:PRK11288 173 AREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAItVF 213
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-215 |
1.49e-22 |
|
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: 95.66 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGL--EGYQDGSIKLGGMTITD---RDSQAREI 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKAsniRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 78 SrsvgMVFQSFNLFPHMTALENVMLAPRRVLKKSAAECREL---AQQMLEKVGLGDRLDYYP-SSLSGGQQQRVAIARAL 153
Cdd:TIGR02633 81 V----IIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMylrAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695700954 154 AMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGK 215
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-220 |
1.68e-22 |
|
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: 96.24 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 30 QVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGmtiTDRDSQAREISRSVGMVFQSFNLFPHMTALENVMLAPRrvLK 109
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG---KDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQ--LK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 110 -KSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAeG 188
Cdd:TIGR01257 1032 gRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-G 1110
|
170 180 190
....*....|....*....|....*....|..
gi 695700954 189 MTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:TIGR01257 1111 RTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-216 |
6.10e-22 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 90.22 E-value: 6.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 15 DNHVLKGVDLDIDMGQVISIIGRSGSGKSTllrCINGLEGY---QDGSIKLGGMTITDRDSqaREISRSVGMVFQSFNLF 91
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENFyqpQGGQVLLDGKPISQYEH--KYLHSKVSLVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 92 PHmTALENVMLAprrVLKKSAAECRELAQ--------QMLEKvGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:cd03248 101 AR-SLQDNIAYG---LQSCSFECVKEAAQkahahsfiSELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695700954 164 EITSALDPELVGEVLKVLEQlAAEGMTLILVTHEMNFArEVGDRVVFMHQGKV 216
Cdd:cd03248 176 EATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-229 |
6.73e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 92.28 E-value: 6.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPL-------ITINQVQkyyGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQ-----D----GSIKLGG 64
Cdd:COG4170 1 MPLldirnltIEIDTPQ---GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtaDrfrwNGIDLLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 65 MTITDRdsqaREI-SRSVGMVFQ--SFNLFPHMTALENVMLA-PRRVLK----KSAAECRELAQQMLEKVGLGDRLDY-- 134
Cdd:COG4170 78 LSPRER----RKIiGREIAMIFQepSSCLDPSAKIGDQLIEAiPSWTFKgkwwQRFKWRKKRAIELLHRVGIKDHKDImn 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 135 -YPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAA-EGMTLILVTHEMNFAREVGDRVVFMH 212
Cdd:COG4170 154 sYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLY 233
|
250
....*....|....*..
gi 695700954 213 QGKVWEQGDSKTLFANP 229
Cdd:COG4170 234 CGQTVESGPTEQILKSP 250
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-216 |
1.05e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.17 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAReisRSVGMVF-----QSFNLFP 92
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER---RRLGVAYipedrLGRGLVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 93 HMTALENVML--------APRRVLKKSAAecRELAQQMLEK-----VGLGDRLdyypSSLSGGQQQRVAIARALAMSPKV 159
Cdd:COG3845 350 DMSVAENLILgryrrppfSRGGFLDRKAI--RAFAEELIEEfdvrtPGPDTPA----RSLSGGNQQKVILARELSRDPKL 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 160 LLCDEITSALDpelVG---EVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:COG3845 424 LIAAQPTRGLD---VGaieFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-242 |
2.50e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 89.66 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 13 YGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSqaREISRSVGMVFQSFNLFP 92
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS--KEVARRIGLLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 93 HMTALENVMLA--PRRVL-KKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSAL 169
Cdd:PRK10253 95 DITVQELVARGryPHQPLfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695700954 170 DPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFanpqTTELKQFISSVR 242
Cdd:PRK10253 175 DISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV----TAELIERIYGLR 244
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-227 |
2.66e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.39 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYY--GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTItdRDSQAREISRSV 81
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL--RDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFPHMTALENVMLAPRRVLKKSAAECRELAQQM--LEKV--GLGDRLDYYPSSLSGGQQQRVAIARALAMSP 157
Cdd:PRK11176 420 ALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMdfINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 158 KVLLCDEITSALDPELVGEVLKVLEQLAAEgMTLILVTHEMNfAREVGDRVVFMHQGKVWEQGDSKTLFA 227
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELLA 567
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-220 |
5.86e-21 |
|
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: 87.55 E-value: 5.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNH--VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDsqAREISRSV 81
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG--LHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFPHmTALENvmLAP---------RRVLKKSAaeCRELAQQMLEkvGLGDRLDYYPSSLSGGQQQRVAIARA 152
Cdd:cd03244 81 SIIPQDPVLFSG-TIRSN--LDPfgeysdeelWQALERVG--LKEFVESLPG--GLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 153 LAMSPKVLLCDEITSALDPE---LVGEVLKvlEQLAaeGMTLILVTHE----MNFarevgDRVVFMHQGKVWEQG 220
Cdd:cd03244 154 LLRKSKILVLDEATASVDPEtdaLIQKTIR--EAFK--DCTVLTIAHRldtiIDS-----DRILVLDKGRVVEFD 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-196 |
7.63e-21 |
|
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: 85.67 E-value: 7.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVL-KGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIklggmtitdrdsqareisrsvg 82
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 83 mvfqsfnlfpHMTALENVMLAPRRVLKKSAAecreLAQQMLekvglgdrldyYPSS--LSGGQQQRVAIARALAMSPKVL 160
Cdd:cd03223 59 ----------GMPEGEDLLFLPQRPYLPLGT----LREQLI-----------YPWDdvLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....*.
gi 695700954 161 LCDEITSALDPELVGEVLKVLEQlaaEGMTLILVTH 196
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKE---LGITVISVGH 146
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-208 |
2.77e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 89.08 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGL--EGYQDGSIKLGGMTI---TDRDSQAREISrsvgMVFQSFNLFPH 93
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGEVCrfkDIRDSEALGIV----IIHQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 94 MTALENVML----APRRVLKKSAAECRelAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSAL 169
Cdd:NF040905 93 LSIAENIFLgnerAKRGVIDWNETNRR--ARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 695700954 170 DPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRV 208
Cdd:NF040905 171 NEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSI 209
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-227 |
5.14e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 88.62 E-value: 5.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQ-KYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAreISRSVG 82
Cdd:PRK10790 341 IDIDNVSfAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV--LRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 83 MVFQ-----SFNLFPHMT------------ALENVMLAprrvlkksaaecrELAQQMLEkvGLGDRLDYYPSSLSGGQQQ 145
Cdd:PRK10790 419 MVQQdpvvlADTFLANVTlgrdiseeqvwqALETVQLA-------------ELARSLPD--GLYTPLGEQGNNLSVGQKQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 146 RVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLeQLAAEGMTLILVTHEMNFAREvGDRVVFMHQGKVWEQGDSKTL 225
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
..
gi 695700954 226 FA 227
Cdd:PRK10790 562 LA 563
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-227 |
6.08e-20 |
|
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: 88.34 E-value: 6.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 12 YYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTItdRDSQAREISRSVGMVFQSFNLF 91
Cdd:COG5265 367 YDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI--RDVTQASLRAAIGIVPQDTVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 92 pHMTALENVmlAPRRvLKKSAAECRE---LAQ-----QMLEKvGL----GDR-LdyypsSLSGGQQQRVAIARALAMSPK 158
Cdd:COG5265 445 -NDTIAYNI--AYGR-PDASEEEVEAaarAAQihdfiESLPD-GYdtrvGERgL-----KLSGGEKQRVAIARTLLKNPP 514
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 159 VLLCDEITSALDPELVGEVLKVLEQLAAEGMTLIL------VTHemnfarevGDRVVFMHQGKVWEQGDSKTLFA 227
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVARGRTTLVIahrlstIVD--------ADEILVLEAGRIVERGTHAELLA 581
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-196 |
1.29e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 83.56 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGmtiTDRDSQAREISRSVGMVFQSFNLFPHMTAL 97
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG---TPLAEQRDEPHENILYLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 98 ENVmlaprRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEV 177
Cdd:TIGR01189 92 ENL-----HFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170
....*....|....*....
gi 695700954 178 LKVLEQLAAEGMTLILVTH 196
Cdd:TIGR01189 167 AGLLRAHLARGGIVLLTTH 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
15-196 |
1.43e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 83.31 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 15 DNHVL-KGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTI-TDRDSQAREIsrsvgmvfqsfnLF- 91
Cdd:PRK13538 12 DERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIrRQRDEYHQDL------------LYl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 92 -------PHMTALENVMLAPRrvlkksAAEC--RELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLC 162
Cdd:PRK13538 80 ghqpgikTELTALENLRFYQR------LHGPgdDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190
....*....|....*....|....*....|....
gi 695700954 163 DEITSALDPELVGEVLKVLEQLAAEGMTLILVTH 196
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-215 |
3.18e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTIT---DRDSQAREIS 78
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngPKSSQEAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 79 rsvgMVFQSFNLFPHMTALENVMLAPRRVLKKSAAECREL---AQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAM 155
Cdd:PRK10762 83 ----IIHQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMyaeADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 156 SPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGK 215
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-216 |
3.24e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 86.33 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 22 VDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAReisRSVGMVFQSFNLFPHMTALENVM 101
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATR---RRVGYMSQAFSLYGELTVRQNLE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 102 L-AprRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDP-------EL 173
Cdd:NF033858 362 LhA--RLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPvardmfwRL 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695700954 174 vgevlkvLEQLAAE-GMTLILVTHEMNFArEVGDRVVFMHQGKV 216
Cdd:NF033858 440 -------LIELSREdGVTIFISTHFMNEA-ERCDRISLMHAGRV 475
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-196 |
4.19e-19 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 85.45 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCING-----------LEGYQDGSiklgGMTITDr 70
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRGS----GETIWD- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 71 dsqareISRSVGMVFQSFnlfpHM-----TALENVMLAP--------RRVLKKSaaecRELAQQMLEKVGLGDRLDYYP- 136
Cdd:PRK10938 334 ------IKKHIGYVSSSL----HLdyrvsTSVRNVILSGffdsigiyQAVSDRQ----QKLAQQWLDILGIDKRTADAPf 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695700954 137 SSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMT-LILVTH 196
Cdd:PRK10938 400 HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSH 460
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-226 |
4.24e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.78 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHV-LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQareisRSVG 82
Cdd:PRK15056 7 IVVNDVTVTWRNGHTaLRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK-----NLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 83 MVFQSFNL---FPHMtaLENVMLAPRR----VLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAM 155
Cdd:PRK15056 82 YVPQSEEVdwsFPVL--VEDVVMMGRYghmgWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695700954 156 SPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVfMHQGKVWEQGDSKTLF 226
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTF 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-227 |
4.24e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAreiSRSVGMVFQSFN-----LFPH 93
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD---GLANGIVYISEDrkrdgLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 94 MTALENVMLAPRRVLKKSAAECRELAQQMLekvgLGDRLDYY----PS------SLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:PRK10762 345 MSVKENMSLTALRYFSRAGGSLKHADEQQA----VSDFIRLFniktPSmeqaigLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695700954 164 EITSALDpelVG---EVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV-----WEQGDSKTLFA 227
Cdd:PRK10762 421 EPTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-216 |
5.28e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 85.39 E-value: 5.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQ--AREIS 78
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQdpPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 79 RSV------GMVFQSFNLFPHMTALENVMLAPR-RVLKKSAA-------------ECRelAQQMLEKVGLGDrlDYYPSS 138
Cdd:PRK11147 81 GTVydfvaeGIEEQAEYLKRYHDISHLVETDPSeKNLNELAKlqeqldhhnlwqlENR--INEVLAQLGLDP--DAALSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 139 LSGGQQQRVAIARALAMSPKVLLCDEITSALDPelvgEVLKVLEQ--LAAEGmTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGflKTFQG-SIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-216 |
5.86e-19 |
|
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: 85.26 E-value: 5.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYGDNHVLKGVD---LDIDMGQVISIIGRSGSGKSTLLRCINGL-EGYQDGSIKLGGMTITDRdSQAREIS 78
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRVDdvsFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIR-NPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 79 RSVGMVFQS---FNLFPHMTALENVMLAprrVLKKSAAECRELAQQMLEKVGLG-DRLDYYPSS-------LSGGQQQRV 147
Cdd:TIGR02633 336 AGIAMVPEDrkrHGIVPILGVGKNITLS---VLKSFCFKMRIDAAAELQIIGSAiQRLKVKTASpflpigrLSGGNQQKA 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 148 AIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:TIGR02633 413 VLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-204 |
5.94e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.45 E-value: 5.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREisRSV 81
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR--QQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFPHmTALENVMLaPRRVLKKSAAECRELAQqmLEKVGLGDR-LDYYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:PRK10247 84 SYCAQTPTLFGD-TVYDNLIF-PWQIRNQQPDPAIFLDD--LERFALPDTiLTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695700954 161 LCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTH---EMNFAREV 204
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHdkdEINHADKV 207
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-196 |
2.38e-18 |
|
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: 80.23 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKL-GGMTITDRDSQAREISrsvgmvfqsfnLFPHMTA 96
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnGGPLDFQRDSIARGLL-----------YLGHAPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 97 LENVmLAPRRVLKKSAAEC-RELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVG 175
Cdd:cd03231 84 IKTT-LSVLENLRFWHADHsDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|.
gi 695700954 176 EVLKVLEQLAAEGMTLILVTH 196
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTH 183
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-222 |
2.63e-18 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 81.23 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQ--DGSIKLGGMTITDRDSQAREiSR 79
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEERA-HL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 80 SVGMVFQSFNLFPHMTALENVMLAPRRVLKK------SAAECRELAQQMLEKVGLGdrldyyPSSL--------SGGQQQ 145
Cdd:CHL00131 85 GIFLAFQYPIEIPGVSNADFLRLAYNSKRKFqglpelDPLEFLEIINEKLKLVGMD------PSFLsrnvnegfSGGEKK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695700954 146 RVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVG-DRVVFMHQGKVWEQGDS 222
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDA 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-196 |
4.57e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 14 GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDrdSQAREISRSVGmvFQSFnLFPH 93
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDD--PDVAEACHYLG--HRNA-MKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 94 MTALENVMLApRRVLkkSAAECRELAQqmLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDP-- 171
Cdd:PRK13539 88 LTVAENLEFW-AAFL--GGEELDIAAA--LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAaa 162
|
170 180
....*....|....*....|....*.
gi 695700954 172 -ELVGEVlkVLEQLAAEGMtLILVTH 196
Cdd:PRK13539 163 vALFAEL--IRAHLAQGGI-VIAATH 185
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-220 |
6.05e-18 |
|
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: 79.68 E-value: 6.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMT-ITDRDSQAREISRSVGM---------VFQS 87
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpWKRRKKFLRRIGVVFGQktqlwwdlpVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 88 FNLFPHMTALEnvmlaPRRvLKKSAAECRELAQqmlekvgLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITS 167
Cdd:cd03267 116 FYLLAAIYDLP-----PAR-FKKRLDELSELLD-------LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695700954 168 ALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-218 |
1.32e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 81.56 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHV-LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQA--REISrs 80
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFS-- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 vgMVFQSFNLFPHMTALENVMLAPrrvlkksaaecrELAQQMLEKVGLGDRLDYYPS-----SLSGGQQQRVAIARALAM 155
Cdd:PRK10522 401 --AVFTDFHLFDQLLGPEGKPANP------------ALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695700954 156 SPKVLLCDEITSALDPELVGEVLKV-LEQLAAEGMTLILVTHEMNFArEVGDRVVFMHQGKVWE 218
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYQVlLPLLQEMGKTIFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-216 |
1.56e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.98 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 15 DNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRdSQAREISRSVGMVFQS---FNLF 91
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPR-SPLDAVKKGMAYITESrrdNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 92 PHMTALENVMLAprRVLKKSA----------AECRELAQQMLEKVGLG-DRLDYYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:PRK09700 354 PNFSIAQNMAIS--RSLKDGGykgamglfheVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 161 LCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-197 |
5.75e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.54 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLrciNGLEGYQDGSIKLGGMTITDRdSQAREISRSVGMVFQSFNLFPHMTAL 97
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLL---NALAGRIQGNNFTGTILANNR-KPTKQILKRTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 98 ENVMLAPRRVLKKSAA--ECRELAQQMLEKVGL---GDRL--DYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALD 170
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTkqEKILVAESVISELGLtkcENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180
....*....|....*....|....*..
gi 695700954 171 PELVGEVLKVLEQLAAEGMTLILVTHE 197
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-216 |
8.95e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.82 E-value: 8.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 29 GQVISIIGRSGSGKSTLLRCINGL-EGYQDGSIKLGGMTITDRdSQAREISRSVGMVFQS---FNLFPHMTALENVMLAp 104
Cdd:PRK13549 288 GEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIR-NPQQAIAQGIAMVPEDrkrDGIVPVMGVGKNITLA- 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 105 rrVLKK--------SAAECRELAQQMlekvglgDRLDYYPSS-------LSGGQQQRVAIARALAMSPKVLLCDEITSAL 169
Cdd:PRK13549 366 --ALDRftggsridDAAELKTILESI-------QRLKVKTASpelaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695700954 170 DpelVG---EVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:PRK13549 437 D---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-200 |
9.82e-17 |
|
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: 78.82 E-value: 9.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 5 TINQVQKYYGDN-HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEgyqdgsiklggmtiTDRDSQAR-EISRSVG 82
Cdd:TIGR03719 6 TMNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVD--------------KDFNGEARpQPGIKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 83 MVFQSFNLFPHMTALENVMLAPRRVLK--------------------KSAAECRELaQQMLEKVGLGD------------ 130
Cdd:TIGR03719 72 YLPQEPQLDPTKTVRENVEEGVAEIKDaldrfneisakyaepdadfdKLAAEQAEL-QEIIDAADAWDldsqleiamdal 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 131 RL---DYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGevlkVLEQLAAE--GmTLILVTHEMNF 200
Cdd:TIGR03719 151 RCppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVA----WLERHLQEypG-TVVAVTHDRYF 220
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-229 |
1.84e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 77.15 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITI-NQVQKYYGDNHVLKGVD---LDIDMGQVISIIGRSGSGKSTLLRCINGLEGyQDGSIKLGGMTITDRD----- 71
Cdd:PRK15093 1 MPLLDIrNLTIEFKTSDGWVKAVDrvsMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDIDllrls 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 72 --SQAREISRSVGMVFQSfnlfphmtalenvmlaPRRVLKKSAAECRELAQ-----------------------QMLEKV 126
Cdd:PRK15093 80 prERRKLVGHNVSMIFQE----------------PQSCLDPSERVGRQLMQnipgwtykgrwwqrfgwrkrraiELLHRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 127 GLGDRLDY---YPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQL-AAEGMTLILVTHEMNFAR 202
Cdd:PRK15093 144 GIKDHKDAmrsFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLS 223
|
250 260
....*....|....*....|....*..
gi 695700954 203 EVGDRVVFMHQGKVWEQGDSKTLFANP 229
Cdd:PRK15093 224 QWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-220 |
2.71e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.35 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 26 IDMGQVISIIGRSGSGKSTLLRCINGLEGYQdGSIKLGGMTItdRDSQAREISRSVGMVFQS----FNLfP--HMTALEn 99
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPL--EAWSAAELARHRAYLSQQqtppFAM-PvfQYLTLH- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 100 vmLAPRRVLKKSAAECRELAQQmlekVGLGDRLDYYPSSLSGGQQQRVAIARA-LAMSP------KVLLCDEITSALDPE 172
Cdd:PRK03695 94 --QPDKTRTEAVASALNEVAEA----LGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPdinpagQLLLLDEPMNSLDVA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695700954 173 LVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASG 215
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-229 |
7.38e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 76.29 E-value: 7.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 15 DNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRdsQAREISRSVGMVFQSFNLFPHM 94
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL--QLDSWRSRLAVVSQTPFLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 95 TAlENVMLAprrvlkksaaeCRELAQQMLEKVG-------------------LGDRldyyPSSLSGGQQQRVAIARALAM 155
Cdd:PRK10789 405 VA-NNIALG-----------RPDATQQEIEHVArlasvhddilrlpqgydteVGER----GVMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695700954 156 SPKVLLCDEITSALDPELVGEVLKVLEQLaAEGMTLILVTHEMNFAREvGDRVVFMHQGKVWEQGDSKTLFANP 229
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-192 |
1.84e-15 |
|
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: 72.30 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNH-VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCING-LEGYQ--DGSIKLGGMTITDRDSQARe 76
Cdd:cd03233 4 LSWRNISFTTGKGRSKIpILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrTEGNVsvEGDIHYNGIPYKEFAEKYP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 77 isRSVGMVFQSFNLFPHMTALENVmlaprrvlkKSAAECRelaqqmlekvglGDRldyYPSSLSGGQQQRVAIARALAMS 156
Cdd:cd03233 83 --GEIIYVSEEDVHFPTLTVRETL---------DFALRCK------------GNE---FVRGISGGERKRVSIAEALVSR 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 695700954 157 PKVLLCDEITSALDPELVGEVLKVLEQLA-AEGMTLI 192
Cdd:cd03233 137 ASVLCWDNSTRGLDSSTALEILKCIRTMAdVLKTTTF 173
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-216 |
2.38e-15 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 74.83 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 22 VDLDIDMGQVISIIGRSGSGKSTLLRCINGLegY--QDGSIKLGGMTITDRDsqaREISR---SVgmVFQSFNLFPHMTA 96
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGL--YrpESGEILLDGQPVTADN---REAYRqlfSA--VFSDFHLFDRLLG 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 97 LENVMLAprrvlkksaaecrELAQQMLEKVGLGDRLDYY-----PSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDP 171
Cdd:COG4615 424 LDGEADP-------------ARARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDP 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695700954 172 --------ELVGEvlkvleqLAAEGMTLILVTHEMNFArEVGDRVVFMHQGKV 216
Cdd:COG4615 491 efrrvfytELLPE-------LKARGKTVIAISHDDRYF-DLADRVLKMDYGKL 535
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-213 |
3.18e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.84 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKlggmtitdRDSQAReisrs 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKLR----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 VGMVFQSFNLFPHMTalenvmLAPRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVL 160
Cdd:PRK09544 69 IGYVPQKLYLDTTLP------LTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695700954 161 LCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQ 213
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-220 |
3.32e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.94 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCingLEGYQDGSIKLGGMTITDRDS---------QAREISRSVGMVFQ-S 87
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKA---LAGDLTGGGAPRGARVTGDVTlngeplaaiDAPRLARLRAVLPQaA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 88 FNLFPhMTALENVMLAPRRVLKKSAA---ECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAM--------- 155
Cdd:PRK13547 93 QPAFA-FSAREIVLLGRYPHARRAGAlthRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 156 SPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-228 |
5.29e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 74.00 E-value: 5.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 14 GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCING-LEGYQDGSIKLGGmtitdrdsqareisrSVGMVFQSFNLFp 92
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRG---------------TVAYVPQVSWIF- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 93 HMTALENVMLA----PRRVLKksAAECRELaQQMLEKVGLGDRLDYYPS--SLSGGQQQRVAIARALAMSPKVLLCDEIT 166
Cdd:PLN03130 692 NATVRDNILFGspfdPERYER--AIDVTAL-QHDLDLLPGGDLTEIGERgvNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695700954 167 SALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVgDRVVFMHQGKVWEQGDSKTLFAN 228
Cdd:PLN03130 769 SALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-239 |
6.06e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.62 E-value: 6.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIK-LGG-MtitdRDSQARE-ISRS 80
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGdM----ADARHRRaVCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 VGMVFQSF--NLFPHMTALENV-MLAprRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSP 157
Cdd:NF033858 78 IAYMPQGLgkNLYPTLSVFENLdFFG--RLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 158 KVLLCDEITSALDP-------ELVgevlkvlEQLAAE--GMTLILVTHEMNFArEVGDRVVFMHQGKVWEQGDSKTLFAN 228
Cdd:NF033858 156 DLLILDEPTTGVDPlsrrqfwELI-------DRIRAErpGMSVLVATAYMEEA-ERFDWLVAMDAGRVLATGTPAELLAR 227
|
250
....*....|..
gi 695700954 229 PQTTELKQ-FIS 239
Cdd:NF033858 228 TGADTLEAaFIA 239
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-220 |
1.23e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 70.13 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAreISRSVGMVFQSFNLFphMTAL 97
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED--LRSSLTIIPQDPTLF--SGTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 98 ENvMLAPRRvlKKSAAECRElaqqMLEKVGLGdrldyypSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEV 177
Cdd:cd03369 99 RS-NLDPFD--EYSDEEIYG----ALRVSEGG-------LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695700954 178 LKVLEQLAAeGMTLILVTHEMnfaREVG--DRVVFMHQGKVWEQG 220
Cdd:cd03369 165 QKTIREEFT-NSTILTIAHRL---RTIIdyDKILVMDAGEVKEYD 205
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-221 |
4.10e-14 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 69.43 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 3 LITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQ--DGSIKLGGMTITDRDSQAREiSRS 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLELSPEDRA-GEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 VGMVFQSFNLFPHMTA---LENVMLAPRRVLKKSAAECRELAQQMLEKVGLGDrldyYPSSL---------SGGQQQRVA 148
Cdd:PRK09580 80 IFMAFQYPVEIPGVSNqffLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLK----MPEDLltrsvnvgfSGGEKKRND 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695700954 149 IARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVG-DRVVFMHQGKVWEQGD 221
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGD 229
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-215 |
6.86e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.53 E-value: 6.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQaREISRSVGMVFQSFNLFPHMTALE 98
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSK-EALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 99 NVMLA--PRRVL----KKSAAECRELAQQMLEKVGLGDRLdyypSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPE 172
Cdd:PRK10982 93 NMWLGryPTKGMfvdqDKMYRDTKAIFDELDIDIDPRAKV----ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695700954 173 LVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGK 215
Cdd:PRK10982 169 EVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-227 |
1.13e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 70.36 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 14 GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGmtitdrdsqareisrSVGMVfqsfnlfPH 93
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG---------------SVAYV-------PQ 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 94 MTALENVMLAPRRVLKKSAAECRelAQQMLEKVGLGDRLDYYPS-----------SLSGGQQQRVAIARALAMSPKVLLC 162
Cdd:TIGR00957 707 QAWIQNDSLRENILFGKALNEKY--YQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLF 784
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 163 DEITSALDPELVGEVLKVLeqLAAEGM----TLILVTHEMNFAREVgDRVVFMHQGKVWEQGDSKTLFA 227
Cdd:TIGR00957 785 DDPLSAVDAHVGKHIFEHV--IGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-228 |
1.62e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 69.53 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 16 NHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGmtitdrdsQAREISRSVGMVFQsfnlfphMT 95
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--------SAALIAISSGLNGQ-------LT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 96 ALENVMLAPRRV-LKKSaaECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELV 174
Cdd:PRK13545 102 GIENIELKGLMMgLTKE--KIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695700954 175 GEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGDSKTLFAN 228
Cdd:PRK13545 180 KKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-216 |
2.18e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 22 VDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDsqAREISRSvGMVF-----QSFNLFPHMTA 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRS--PRDAIRA-GIMLcpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 97 LENVMLAPRRvlKKSAAEC-------RELAQQMLEKVGLGDrldyyPS------SLSGGQQQRVAIARALAMSPKVLLCD 163
Cdd:PRK11288 349 ADNINISARR--HHLRAGClinnrweAENADRFIRSLNIKT-----PSreqlimNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 164 EITSALDpelVG---EVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:PRK11288 422 EPTRGID---VGakhEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-228 |
2.95e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.85 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 15 DNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCING-LEGYQDGSIKLGGmtitdrdsqareisrSVGMVFQSFNLFpH 93
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRG---------------SVAYVPQVSWIF-N 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 94 MTALENVMLAprrvlkkSAAEcRELAQQMLEKVGLGDRLDYYPS-----------SLSGGQQQRVAIARALAMSPKVLLC 162
Cdd:PLN03232 693 ATVRENILFG-------SDFE-SERYWRAIDVTALQHDLDLLPGrdlteigergvNISGGQKQRVSMARAVYSNSDIYIF 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 163 DEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVgDRVVFMHQGKVWEQGDSKTLFAN 228
Cdd:PLN03232 765 DDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-216 |
4.04e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 22 VDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAReisRSVGMVF-----QSFNLFPHMTA 96
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQR---LARGLVYlpedrQSSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 97 LENVMLAPRRVLKKSAAECRELAqqMLEKV--GLGDRL---DYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDP 171
Cdd:PRK15439 359 AWNVCALTHNRRGFWIKPARENA--VLERYrrALNIKFnhaEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695700954 172 ELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:PRK15439 437 SARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-240 |
6.79e-13 |
|
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: 66.42 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 14 GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEgYQDGSIKLGGMTITDRDSQarEISRSVGMVFQSFNLFPH 93
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQ--KWRKAFGVIPQKVFIFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 94 MTalenvmlapRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSL-----------SGGQQQRVAIARALAMSPKVLLC 162
Cdd:cd03289 92 TF---------RKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695700954 163 DEITSALDPELVGEVLKVLEQlAAEGMTLILVTHEMNFAREVgDRVVFMHQGKVWeQGDSKTLFANpQTTELKQFISS 240
Cdd:cd03289 163 DEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLEC-QRFLVIEENKVR-QYDSIQKLLN-EKSHFKQAISP 236
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-214 |
1.68e-12 |
|
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: 64.19 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLE--GYQDGSIKLGGMTITDrdsqarEISRSVGMVFQSFNLFPHMTA 96
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKtaGVITGEILINGRPLDK------NFQRSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 97 lenvmlapRRVLKKSAAeCRELAQQmlekvglgdrldyypsslsggQQQRVAIARALAMSPKVLLCDEITSALDPELVGE 176
Cdd:cd03232 97 --------REALRFSAL-LRGLSVE---------------------QRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695700954 177 VLKVLEQLAAEGMTLILVTHEMN---FarEVGDRVVFMHQG 214
Cdd:cd03232 147 IVRFLKKLADSGQAILCTIHQPSasiF--EKFDRLLLLKRG 185
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-197 |
2.56e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.82 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 13 YGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTItDRDSQAREisRSVGMVFQSFNLFP 92
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQ--KQLCFVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 93 HMTALENVMLAPRrvLKKSAAECRELAQQMlekvGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPE 172
Cdd:PRK13540 88 YLTLRENCLYDIH--FSPGAVGITELCRLF----SLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*
gi 695700954 173 LVGEVLKVLEQLAAEGMTLILVTHE 197
Cdd:PRK13540 162 SLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-198 |
3.18e-12 |
|
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: 65.58 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 29 GQVISIIGRSGSGKSTLLRCINGlegyqdgSIK--LGgmtITDRDSQAREISRSvgmvFQSFNLFPHMTALEN------- 99
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSG-------ELKpnLG---DYDEEPSWDEVLKR----FRGTELQDYFKKLANgeikvah 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 100 ----VMLAPRRV------LKKSAAEcRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSAL 169
Cdd:COG1245 165 kpqyVDLIPKVFkgtvreLLEKVDE-RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190
....*....|....*....|....*....|..
gi 695700954 170 DpelVGE---VLKVLEQLAAEGMTLILVTHEM 198
Cdd:COG1245 244 D---IYQrlnVARLIRELAEEGKYVLVVEHDL 272
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-220 |
5.10e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 64.76 E-value: 5.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSG--KSTLLRCINGLEGyqdGSIKLGGMTITdrdSQAREISRSV 81
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDA---GRRPWRF*TWC---ANRRALRRTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GM-------VFQSFnlfphmTALENVMLAPRRvLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALA 154
Cdd:NF000106 88 G*hrpvr*gRRESF------SGRENLYMIGR*-LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 155 MSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQG 220
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-205 |
5.23e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.65 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCING----LEGyqdgsiklggmtitDRDSQARE 76
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGelplLSG--------------ERQSQFSH 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 77 ISRsvgmvfQSFNLFPHMTALE-----NVMLAP---------RRVLK---KSAAECRELAQQMlekvGLGDRLDYYPSSL 139
Cdd:PRK10938 67 ITR------LSFEQLQKLVSDEwqrnnTDMLSPgeddtgrttAEIIQdevKDPARCEQLAQQF----GITALLDRRFKYL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 140 SGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMN----FAREVG 205
Cdd:PRK10938 137 STGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDeipdFVQFAG 206
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-220 |
5.41e-12 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 62.34 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 17 HVLKGVDLDIDMGQVISIIGRSGSGKSTLLrcinglegyQDGSIKLGgmtitdrdsQAREISrsvgmvfqSFNLFPHMTA 96
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLV---------NEGLYASG---------KARLIS--------FLPKFSRNKL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 97 LenvmlaprrVLKKsaaecrelaQQMLEKVGLGD-RLDYYPSSLSGGQQQRVAIARALAMSPK--VLLCDEITSALDPEL 173
Cdd:cd03238 63 I---------FIDQ---------LQFLIDVGLGYlTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695700954 174 VGEVLKVLEQLAAEGMTLILVTHEMNFAREvGDRVVFM------HQGKVWEQG 220
Cdd:cd03238 125 INQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVFSG 176
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-241 |
6.55e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCING-LEGYQ---DGSIKLGGMTITDRDSQAREISRSVGmvfQSFNLFPH 93
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGFHigvEGVITYDGITPEEIKKHYRGDVVYNA---ETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 94 MTALENVMLAPR------RVLKKS----AAECRELAQQML-------EKVGlgdrlDYYPSSLSGGQQQRVAIARALAMS 156
Cdd:TIGR00956 153 LTVGETLDFAARcktpqnRPDGVSreeyAKHIADVYMATYglshtrnTKVG-----NDFVRGVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 157 PKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVT--HEMNFAREVGDRVVFMHQGKVWEQGDS---KTLFAN--- 228
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIYFGPAdkaKQYFEKmgf 307
|
250
....*....|....*
gi 695700954 229 --PQTTELKQFISSV 241
Cdd:TIGR00956 308 kcPDRQTTADFLTSL 322
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-214 |
7.43e-12 |
|
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: 64.65 E-value: 7.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 29 GQVISIIGRSGSGKSTLLRCINGlegyqDGSIKLGGMTITdrdsqAREISRSVGMVFQSFNLFPHMTALENVMLAPR--- 105
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTG-----DTTVTSGDATVA-----GKSILTNISDVHQNMGYCPQFDAIDDLLTGREhly 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 106 ---RVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLE 182
Cdd:TIGR01257 2035 lyaRLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
170 180 190
....*....|....*....|....*....|..
gi 695700954 183 QLAAEGMTLILVTHEMNFAREVGDRVVFMHQG 214
Cdd:TIGR01257 2115 SIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-196 |
9.32e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.56 E-value: 9.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSqareiSRSV 81
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR-----SRFM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFPHMTALENVM----LAPRRvlkksaaecrelAQQM----LEKVGLGDRLDYYPSSLSGGQQQRVAIARaL 153
Cdd:PRK13543 85 AYLGHLPGLKADLSTLENLHflcgLHGRR------------AKQMpgsaLAIVGLAGYEDTLVRQLSAGQKKRLALAR-L 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695700954 154 AMSPKVL-LCDEITSALDPELVGEVLKVLE-QLAAEGMTLiLVTH 196
Cdd:PRK13543 152 WLSPAPLwLLDEPYANLDLEGITLVNRMISaHLRGGGAAL-VTTH 195
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-196 |
1.12e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 5 TINQVQKYYGDN-HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLG-GMTitdrdsqareisrsVG 82
Cdd:PRK11819 8 TMNRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIK--------------VG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 83 MVFQSFNLFPHMTALENVMLAPRRVLKKSA-------------AECRELAQQM------LEKVGLGD------------R 131
Cdd:PRK11819 74 YLPQEPQLDPEKTVRENVEEGVAEVKAALDrfneiyaayaepdADFDALAAEQgelqeiIDAADAWDldsqleiamdalR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 132 L---DYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGevlkVLEQ-LAAEGMTLILVTH 196
Cdd:PRK11819 154 CppwDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA----WLEQfLHDYPGTVVAVTH 218
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-243 |
1.13e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.41 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGmtitdRDSQA---REISRSVGMVFQSFNLFPHm 94
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG-----REIGAyglRELRRQFSMIPQDPVLFDG- 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 95 TALENVmlAPrrVLKKSAAEcrelAQQMLEKVGLGDRLDYYP-----------SSLSGGQQQRVAIARA-LAMSPKVLLC 162
Cdd:PTZ00243 1399 TVRQNV--DP--FLEASSAE----VWAALELVGLRERVASESegidsrvleggSNYSVGQRQLMCMARAlLKKGSGFILM 1470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 163 DEITSALDPELVGEV-LKVLEQLAAegMTLILVTHEMNFAREVgDRVVFMHQGKVWEQGDSKTLFANPQ----------- 230
Cdd:PTZ00243 1471 DEATANIDPALDRQIqATVMSAFSA--YTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQsifhsmvealg 1547
|
250
....*....|...
gi 695700954 231 TTELKQFISSVRG 243
Cdd:PTZ00243 1548 RSEAKRFLQLVGR 1560
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-214 |
1.27e-11 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 61.96 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCING----LEGYQDGSIKL-GGMTITDRDSQAReisRSVGMVFQSFNLFpH 93
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGemqtLEGKVHWSNKNeSEPSFEATRSRNR---YSVAYAAQKPWLL-N 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 94 MTALENVMLAP---RRVLKKSAAECRelAQQMLEKVGLGDRLDYYPS--SLSGGQQQRVAIARALAMSPKVLLCDEITSA 168
Cdd:cd03290 93 ATVEENITFGSpfnKQRYKAVTDACS--LQPDIDLLPFGDQTEIGERgiNLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695700954 169 LDPELVGEVLK--VLEQLAAEGMTLILVTHEMNFAREvGDRVVFMHQG 214
Cdd:cd03290 171 LDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-210 |
1.89e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.51 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 6 INQVQKYYGDNH---VLKGVDldidmgqVISIIGRSGSGK-STLLRcinglegyQDGSIKLGGMTITDRDsqAREISRSV 81
Cdd:PTZ00265 1236 MTNEQDYQGDEEqnvGMKNVN-------EFSLTKEGGSGEdSTVFK--------NSGKILLDGVDICDYN--LKDLRNLF 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSFNLFpHMTALENVMLAPRRVLKKSAAECRELA--QQMLEKvgLGDRLDY----YPSSLSGGQQQRVAIARALAM 155
Cdd:PTZ00265 1299 SIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAaiDEFIES--LPNKYDTnvgpYGKSLSGGQKQRIAIARALLR 1375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 156 SPKVLLCDEITSALDPELVGEVLKVLEQLAAEG-MTLILVTHEMNFAREVGDRVVF 210
Cdd:PTZ00265 1376 EPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKRSDKIVVF 1431
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2-216 |
2.22e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 63.27 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLG-GMTITDRDSQAREISRS 80
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEFLRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 VGMVFQsfnlfpHMtalenVMLAPrrvlkksaaecRELAQQMLEKVG----LGDRLDYYPSSLSGGQQQRVAIARALAMS 156
Cdd:PRK10636 391 DESPLQ------HL-----ARLAP-----------QELEQKLRDYLGgfgfQGDKVTEETRRFSGGEKARLVLALIVWQR 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 157 PKVLLCDEITSALDPELVGEVLKVLeqLAAEGmTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:PRK10636 449 PNLLLLDEPTNHLDLDMRQALTEAL--IDFEG-ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-227 |
5.30e-11 |
|
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: 62.27 E-value: 5.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTIT-----DRDSQAREI-------SRSVGMVF 85
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAkiglhDLRFKITIIpqdpvlfSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 86 QSFNLFPHmtalENVMLAprrvlkksaaecRELAQQMLEKVGLGDRLDYYPS----SLSGGQQQRVAIARALAMSPKVLL 161
Cdd:TIGR00957 1381 DPFSQYSD----EEVWWA------------LELAHLKTFVSALPDKLDHECAeggeNLSVGQRQLVCLARALLRKTKILV 1444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695700954 162 CDEITSALDPElVGEVLKVLEQLAAEGMTLILVTHEMNFAREVgDRVVFMHQGKVWEQGDSKTLFA 227
Cdd:TIGR00957 1445 LDEATAAVDLE-TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-183 |
6.41e-11 |
|
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: 61.49 E-value: 6.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAREISRSVGM 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNlfphmTALENVMLAPRRVlkKSAAEC-----RELAQQmlEKVGlgdrldyypsSLSGGQQQRVAIARALAMSPK 158
Cdd:TIGR03719 403 VWEEIS-----GGLDIIKLGKREI--PSRAYVgrfnfKGSDQQ--KKVG----------QLSGGERNRVHLAKTLKSGGN 463
|
170 180
....*....|....*....|....*
gi 695700954 159 VLLCDEITSALDPelvgEVLKVLEQ 183
Cdd:TIGR03719 464 VLLLDEPTNDLDV----ETLRALEE 484
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-203 |
1.88e-10 |
|
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: 57.38 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 29 GQVISIIGRSGSGKSTLLRCInglegyqdgsiklggmtitdrdsqAREISRSVGMVFqsfnlfphmtalenvmlaprrvl 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARAL------------------------ARELGPPGGGVI----------------------- 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 109 kksAAECRELAQQMLEKVgLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLE------ 182
Cdd:smart00382 35 ---YIDGEDILEEVLDQL-LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllll 110
|
170 180
....*....|....*....|.
gi 695700954 183 QLAAEGMTLILVTHEMNFARE 203
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGP 131
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-239 |
5.99e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.15 E-value: 5.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 14 GDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGyQDGSIKLGGMTITDRDSQarEISRSVGMVFQSFNLFPH 93
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQ--TWRKAFGVIPQKVFIFSG 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 94 MTalenvmlapRRVLKKSAAECRELAQQMLEKVGLGDRLDYYPSSL-----------SGGQQQRVAIARALAMSPKVLLC 162
Cdd:TIGR01271 1307 TF---------RKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 163 DEITSALDPELVGEVLKVLEQlAAEGMTLILVTHEMNFAREVgdRVVFMHQGKVWEQGDSKTLFANpQTTELKQFIS 239
Cdd:TIGR01271 1378 DEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHRVEALLEC--QQFLVIEGSSVKQYDSIQKLLN-ETSLFKQAMS 1450
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-216 |
1.54e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQ---------AREISRSVGMVFQ--- 86
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeainhgfalVTEERRSTGIYAYldi 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 87 SFN-LFPHMTALENVMlaprRVL--KKSAAECRELAQQMLEKVglgdrldyyPS------SLSGGQQQRVAIARALAMSP 157
Cdd:PRK10982 344 GFNsLISNIRNYKNKV----GLLdnSRMKSDTQWVIDSMRVKT---------PGhrtqigSLSGGNQQKVIIGRWLLTQP 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 158 KVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-220 |
2.20e-09 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 55.73 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 17 HVLKGVDLDIDMGQVISIIGRSGSGKSTL----------LRCINGLEGYQDGsiKLGGMTITDRDS----------QARE 76
Cdd:cd03270 9 HNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAYARQ--FLGQMDKPDVDSieglspaiaiDQKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 77 ISRS----VGMVFQSFNLFphmtalenvmlaprRVLKKSAAECRELaqQMLEKVGLGD-RLDYYPSSLSGGQQQRVAIAR 151
Cdd:cd03270 87 TSRNprstVGTVTEIYDYL--------------RLLFARVGIRERL--GFLVDVGLGYlTLSRSAPTLSGGEAQRIRLAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 152 ALAMSPKVLL--CDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEMNFAREvGDRVVFM------HQGKVWEQG 220
Cdd:cd03270 151 QIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVIDIgpgagvHGGEIVAQG 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
8-210 |
2.63e-09 |
|
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: 55.88 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 8 QVQKYYGDNH--VLKGvdlDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTIT--------DRDSQAREI 77
Cdd:cd03237 5 TMKKTLGEFTleVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikaDYEGTVRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 78 SRSVGMVFQSFNLFphmtalENVMLAPrrvlkksaaecrelaqQMLEKVglgdrLDYYPSSLSGGQQQRVAIARALAMSP 157
Cdd:cd03237 82 LSSITKDFYTHPYF------KTEIAKP----------------LQIEQI-----LDREVPELSGGELQRVAIAACLSKDA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 158 KVLLCDEITSALDPELVGEVLKVLEQLAAEG-MTLILVTHEMNFAREVGDRV-VF 210
Cdd:cd03237 135 DIYLLDEPSAYLDVEQRLMASKVIRRFAENNeKTAFVVEHDIIMIDYLADRLiVF 189
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-214 |
4.75e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 8 QVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCingLEGYQDGSIKLGGmtitDRDSQAREI----SRSVGM 83
Cdd:TIGR00956 768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNV---LAERVTTGVITGG----DRLVNGRPLdssfQRSIGY 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 84 VFQSFNLFPHMTALENVMLA-----PRRVLKKSAAECRELAQQMLEKVGLGDRLDYYP-SSLSGGQQQRVAIARALAMSP 157
Cdd:TIGR00956 841 VQQQDLHLPTSTVRESLRFSaylrqPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPgEGLNVEQRKRLTIGVELVAKP 920
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695700954 158 KVLL-CDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHE---MNFarEVGDRVVFMHQG 214
Cdd:TIGR00956 921 KLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsaILF--EEFDRLLLLQKG 979
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-198 |
4.85e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 28 MGQVISIIGRSGSGKSTLLRCINGlegyqdgSIK--LGGmtiTDRDSQAREISRSvgmvFQSFNLFPHMTALEN------ 99
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSG-------ELIpnLGD---YEEEPSWDEVLKR----FRGTELQNYFKKLYNgeikvv 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 100 -----VMLAPRRV-------LKKsaAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITS 167
Cdd:PRK13409 164 hkpqyVDLIPKVFkgkvrelLKK--VDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190
....*....|....*....|....*....|...
gi 695700954 168 ALDpelVGEVLKV--LEQLAAEGMTLILVTHEM 198
Cdd:PRK13409 242 YLD---IRQRLNVarLIRELAEGKYVLVVEHDL 271
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-196 |
4.96e-09 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 54.63 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVlkgvDLDidmGQVISIIGRSGSGKSTLLRCIN-GLEGYQDGSIKLGGMTITDRDSQAR------- 75
Cdd:COG0419 5 LRLENFRSYRDTETI----DFD---DGLNLIVGPNGAGKSTILEAIRyALYGKARSRSKLRSDLINVGSEEASvelefeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 76 -----EISRSVGMVFQSFNLFPH--MTALENVMLAPR-RVLKKSAAECRELAQQMLEKVGLGDRL---------DYYP-S 137
Cdd:COG0419 78 ggkryRIERRQGEFAEFLEAKPSerKEALKRLLGLEIyEELKERLKELEEALESALEELAELQKLkqeilaqlsGLDPiE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 138 SLSGGQQQRVAIARALAmspkvLLCDeiTSALDPELVGEVLKVLEQLAaegmtliLVTH 196
Cdd:COG0419 158 TLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
137-202 |
6.72e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 6.72e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 137 SSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAA-EGMTLILVTHEMNFAR 202
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIAHRLSTIR 644
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-221 |
9.13e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.44 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIklggmtitDRDSQAREISRSVGMVFQsfnlfphMTALE 98
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV--------DRNGEVSVIAISAGLSGQ-------LTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 99 NV---MLaprrVLKKSAAECRELAQQMLEKVGLGDRLdYYP-SSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELV 174
Cdd:PRK13546 105 NIefkML----CMGFKRKEIKAMTPKIIEFSELGEFI-YQPvKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695700954 175 GEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKVWEQGD 221
Cdd:PRK13546 180 QKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-228 |
4.65e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDsqAREISRSVGMVFQSFNLFPHMTAL 97
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG--LTDLRRVLSIIPQSPVLFSGTVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 98 EnvmLAPrrVLKKSAAECRElaqqMLEKVGLGDRLDYYP-----------SSLSGGQQQRVAIARALAMSPKVLLCDEIT 166
Cdd:PLN03232 1329 N---IDP--FSEHNDADLWE----ALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695700954 167 SALDPELVGEVLKVLEQlAAEGMTLILVTHEMNFAREVgDRVVFMHQGKVWEQGDSKTLFAN 228
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-216 |
4.85e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIK------LG------------GM 65
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwsenanIGyyaqdhaydfenDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 66 TITDRDSQAREISRSVGMVfqsfnlfphmTALENVMLAPRRVLKKSAaecrelaqqmleKVglgdrldyypssLSGGQQQ 145
Cdd:PRK15064 400 TLFDWMSQWRQEGDDEQAV----------RGTLGRLLFSQDDIKKSV------------KV------------LSGGEKG 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695700954 146 RVAIARALAMSPKVLLCDEITSALDPELVgEVLKV-LEQLaaEGmTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMDMESI-ESLNMaLEKY--EG-TLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-229 |
5.82e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.24 E-value: 5.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIklggmtitdrdsqarEISRSVGMVFQSFNLFpHMTAL 97
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------------WAERSIAYVPQQAWIM-NATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 98 ENVML-----APRrvLKKSAAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPE 172
Cdd:PTZ00243 739 GNILFfdeedAAR--LADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 173 lVGEvlKVLEQL---AAEGMTLILVTHEMNFArEVGDRVVFMHQGKVWEQGDSKTLFANP 229
Cdd:PTZ00243 817 -VGE--RVVEECflgALAGKTRVLATHQVHVV-PRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-197 |
6.57e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.93 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLE--GYQDGSIKLGGMTiTDRDSQAReISrsvGMVFQSFNLFPHMT 95
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKtgGYIEGDIRISGFP-KKQETFAR-IS---GYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 96 ALENVMLA-----PRRVLKKSAAECRELAQQMLEKVGLGDRLDYYP--SSLSGGQQQRVAIARALAMSPKVLLCDEITSA 168
Cdd:PLN03140 970 VRESLIYSaflrlPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180
....*....|....*....|....*....
gi 695700954 169 LDPELVGEVLKVLEQLAAEGMTLILVTHE 197
Cdd:PLN03140 1050 LDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-214 |
1.22e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.22 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGmtitdrdsqarEISRSVgmvfQSFNLFPHmTAL 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------RISFSP----QTSWIMPG-TIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 98 ENVMLAP-------RRVLKksaaecrelAQQMLEKVGLGDRLDYYP-----SSLSGGQQQRVAIARALAMSPKVLLCDEI 165
Cdd:TIGR01271 505 DNIIFGLsydeyryTSVIK---------ACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695700954 166 TSALDPELVGEVL-KVLEQLAAEgMTLILVTHEMNFAREvGDRVVFMHQG 214
Cdd:TIGR01271 576 FTHLDVVTEKEIFeSCLCKLMSN-KTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
11-232 |
1.74e-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: 49.88 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 11 KYYGDNHVLkgVDL-DIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRdsqareisrsvgmvfqsfn 89
Cdd:cd03222 8 KRYGVFFLL--VELgVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYK------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 90 lfphmtalenvmlaPRRVlkksaaecrelaqqmlekvglgdrldyypsSLSGGQQQRVAIARALAMSPKVLLCDEITSAL 169
Cdd:cd03222 67 --------------PQYI------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYL 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 170 DPELVGEVLKVLEQLAAEGM-TLILVTHEMNFAREVGDRV-VFMHQGKVWeqgdskTLFANPQTT 232
Cdd:cd03222 103 DIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIhVFEGEPGVY------GIASQPKGT 161
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-198 |
2.11e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.44 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 29 GQVISIIGRSGSGKSTLLRCING-----LEGYQ-----DGSIK-LGGMTITDRDSQAREISRSVGMVFQSFNLFPHmTAL 97
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGklkpnLGKFDdppdwDEILDeFRGSELQNYFTKLLEGDVKVIVKPQYVDLIPK-AVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 98 ENVmlapRRVLKKsaAECRELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEV 177
Cdd:cd03236 105 GKV----GELLKK--KDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180
....*....|....*....|.
gi 695700954 178 LKVLEQLAAEGMTLILVTHEM 198
Cdd:cd03236 179 ARLIRELAEDDNYVLVVEHDL 199
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-214 |
2.36e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 50.63 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGmtitdRDSQAREISRsvgmvfqsfnLFPHmTAL 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----RISFSSQFSW----------IMPG-TIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 98 ENVMLAP-------RRVLKksAAECRELAQQMLEKvglgdrlDYYPS-----SLSGGQQQRVAIARALAMSPKVLLCDEI 165
Cdd:cd03291 116 ENIIFGVsydeyryKSVVK--ACQLEEDITKFPEK-------DNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695700954 166 TSALDPELVGEVL-KVLEQLAAEgMTLILVTHEMNFAREvGDRVVFMHQG 214
Cdd:cd03291 187 FGYLDVFTEKEIFeSCVCKLMAN-KTRILVTSKMEHLKK-ADKILILHEG 234
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-172 |
2.75e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLG---GMTITDrdsQAREisrs 80
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGetvKLAYVD---QSRD---- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 vgmvfqsfNLFPHMTALENV-------MLAPRRVlkKSAAEC-----RELAQQmlEKVGLgdrldyypssLSGGQQQRVA 148
Cdd:PRK11819 398 --------ALDPNKTVWEEIsggldiiKVGNREI--PSRAYVgrfnfKGGDQQ--KKVGV----------LSGGERNRLH 455
|
170 180
....*....|....*....|....
gi 695700954 149 IARALAMSPKVLLCDEITSALDPE 172
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-196 |
3.17e-07 |
|
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: 50.52 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 1 MPLITINqvqkyyGDNhVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYqdgsikLGGMTITDRDSqareisrs 80
Cdd:TIGR00954 457 IPLVTPN------GDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPV------YGGRLTKPAKG-------- 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 81 vgmvfqsfNLF-----PHMT--ALENVMLAPRRVL--KKSAAECRELaQQMLEKVGLGDRLDY---------YPSSLSGG 142
Cdd:TIGR00954 516 --------KLFyvpqrPYMTlgTLRDQIIYPDSSEdmKRRGLSDKDL-EQILDNVQLTHILEReggwsavqdWMDVLSGG 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695700954 143 QQQRVAIARALAMSPKVLLCDEITSALDPELVGevlKVLEQLAAEGMTLILVTH 196
Cdd:TIGR00954 587 EKQRIAMARLFYHKPQFAILDECTSAVSVDVEG---YMYRLCREFGITLFSVSH 637
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
17-198 |
3.27e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.92 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 17 HVLKGVDLDIDMGQVISIIGRSGSGKSTLL---------RCINGLEGY------QDGSIKLGGMTITDRDSQAREiSRSV 81
Cdd:cd03271 9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLKKEQpgnhdrIEGLEHIDKVIVIDQSPIGRT-PRSN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQSfnLFPHMTALENVMLAPRR-----------------VLKKSAAECRELAQ---------QMLEKVGLGD-RLDY 134
Cdd:cd03271 88 PATYTG--VFDEIRELFCEVCKGKRynretlevrykgksiadVLDMTVEEALEFFEnipkiarklQTLCDVGLGYiKLGQ 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695700954 135 YPSSLSGGQQQRVAIARALAM---SPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHEM 198
Cdd:cd03271 166 PATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL 232
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
138-216 |
5.82e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 138 SLSGGQQQRVAIARALAMSPKVLLCDEITSALDpelVG---EVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQG 214
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEG 480
|
..
gi 695700954 215 KV 216
Cdd:NF040905 481 RI 482
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-228 |
7.93e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.74 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 18 VLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTItdRDSQAREISRSVGMVFQS---------F 88
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI--SKFGLMDLRKVLGIIPQApvlfsgtvrF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 89 NLFP---HMTA-----LENVML--APRRVLKKSAAECRELAQqmlekvglgdrldyypsSLSGGQQQRVAIARALAMSPK 158
Cdd:PLN03130 1332 NLDPfneHNDAdlwesLERAHLkdVIRRNSLGLDAEVSEAGE-----------------NFSVGQRQLLSLARALLRRSK 1394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695700954 159 VLLCDEITSALDPELVGEVLKVL-EQLAAegMTLILVTHEMNFAREVgDRVVFMHQGKVWEQGDSKTLFAN 228
Cdd:PLN03130 1395 ILVLDEATAAVDVRTDALIQKTIrEEFKS--CTMLIIAHRLNTIIDC-DRILVLDAGRVVEFDTPENLLSN 1462
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
17-216 |
8.75e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.35 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 17 HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGmtitdrDSQAREISRSVGMVFQSFNLfphmta 96
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS------GVKAGCIVAAVSAELIFTRL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 97 lenvmlaprrvlkksaaecrelaqqmlekvglgdrldyypsSLSGGQQQRVAIARALAM-----SPKVLLcDEITSALDP 171
Cdd:cd03227 77 -----------------------------------------QLSGGEKELSALALILALaslkpRPLYIL-DEIDRGLDP 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695700954 172 ELVGEVLKVLEQLAAEGMTLILVTHEMNFAREVgdrVVFMHQGKV 216
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIVITHLPELAELA---DKLIHIKKV 156
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-210 |
1.96e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 2 PLITINQVQKYYGDN--HVLKGvdlDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGgMTI--------TDRD 71
Cdd:PRK13409 339 TLVEYPDLTKKLGDFslEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIsykpqyikPDYD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 72 SQAREISRSVGMVFQSfNLFPHmtalenvmlaprrvlkksaaecrELAQQMlekvGLGDRLDYYPSSLSGGQQQRVAIAR 151
Cdd:PRK13409 415 GTVEDLLRSITDDLGS-SYYKS-----------------------EIIKPL----QLERLLDKNVKDLSGGELQRVAIAA 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695700954 152 ALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAE-GMTLILVTHEMNFAREVGDRV-VF 210
Cdd:PRK13409 467 CLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLmVF 527
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-172 |
3.18e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.40 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 34 IIGRSGSGKSTLLRCINGLEGYQDGSIKLggmtitdRDSQAREISRS-VGMVFQSFNLFPHMTALENVMLAPRrvLKKSA 112
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYY-------KNCNINNIAKPyCTYIGHNLGLKLEMTVFENLKFWSE--IYNSA 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 113 aecrELAQQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPE 172
Cdd:PRK13541 102 ----ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
17-209 |
4.16e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 17 HVLKGVDLDIDMGQVISIIGRSGSGKS-----TLLRCINGL-EGYQDGSIKLGGMTIT-----DRD----SQaREISRSV 81
Cdd:PRK00635 609 HNLKDLTISLPLGRLTVVTGVSGSGKSslindTLVPAVEEFiEQGFCSNLSIQWGAISrlvhiTRDlpgrSQ-RSIPLTY 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQ----------------------SFNL----------FPHMTALENVMLAP------RRVL---------KKSAAE 114
Cdd:PRK00635 688 IKAFDdlrelfaeqprskrlgltkshfSFNTplgacaecqgLGSITTTDNRTSIPcpsclgKRFLpqvlevrykGKNIAD 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 115 CRELAQQMLEKVGLGD-------------RLDYYP-----SSLSGGQQQRVAIA-RALAMSPKVLL--CDEITSALDPEL 173
Cdd:PRK00635 768 ILEMTAYEAEKFFLDEpsihekihalcslGLDYLPlgrplSSLSGGEIQRLKLAyELLAPSKKPTLyvLDEPTTGLHTHD 847
|
250 260 270
....*....|....*....|....*....|....*.
gi 695700954 174 VGEVLKVLEQLAAEGMTLILVTHEMNFAReVGDRVV 209
Cdd:PRK00635 848 IKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVL 882
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
108-239 |
5.22e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 108 LKKSAAECRELAQQMLEKVGLGDRLdyypSSLSGGQQQRVAIARALAMSPK---VLLCDEITSALDPELVGEVLKVLEQL 184
Cdd:PRK00635 1673 LKKIQKPLQALIDNGLGYLPLGQNL----SSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTL 1748
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695700954 185 AAEGMTLILVTHEMNFAREvGDRVVFMHQGKvwEQGDSKTLFANP-------QTTELKQFIS 239
Cdd:PRK00635 1749 VSLGHSVIYIDHDPALLKQ-ADYLIEMGPGS--GKTGGKILFSGPpkdisasKDSLLKTYMC 1807
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-227 |
6.26e-06 |
|
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: 46.06 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 4 ITINQVQKYYGDN--HVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLGGMTITDRDSQAreISRSV 81
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT--LRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 82 GMVFQS---------FNLFPHMTALENVMLaprrvlkksaaECRELAQQMLEKVGLGDRLDYYPS----SLSGGQQQRVA 148
Cdd:cd03288 98 SIILQDpilfsgsirFNLDPECKCTDDRLW-----------EALEIAQLKNMVKSLPGGLDAVVTeggeNFSVGQRQLFC 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 149 IARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEgMTLILVTHEMNFAREvGDRVVFMHQGKVWEQGDSKTLFA 227
Cdd:cd03288 167 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLA 243
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
129-196 |
6.79e-06 |
|
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: 46.23 E-value: 6.79e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695700954 129 GDRLDYYPSSLSGGQQQ---RVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTH 196
Cdd:pfam13304 227 GGGGELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-210 |
6.84e-06 |
|
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: 46.70 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 29 GQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKlGGMTI--------TDRDSQAREISRSV-GMVFQSfNLFPHmtalen 99
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKIsykpqyisPDYDGTVEEFLRSAnTDDFGS-SYYKT------ 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 100 vmlaprrvlkksaaecrelaqQMLEKVGLGDRLDYYPSSLSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLK 179
Cdd:COG1245 438 ---------------------EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAK 496
|
170 180 190
....*....|....*....|....*....|...
gi 695700954 180 VLEQLAAE-GMTLILVTHEMNFAREVGDRV-VF 210
Cdd:COG1245 497 AIRRFAENrGKTAMVVDHDIYLIDYISDRLmVF 529
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
138-216 |
8.71e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 8.71e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695700954 138 SLSGGQQQRVAIARALAMSPKVLLCDEITSALDpelVGEVLKVLEQLAAEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKL 419
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
121-198 |
1.71e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 121 QMLEKVGLGD-RLDYYPSSLSGGQQQRVAIARAL---AMSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTH 196
Cdd:TIGR00630 811 QTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
..
gi 695700954 197 EM 198
Cdd:TIGR00630 891 NL 892
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-202 |
3.14e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.36 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 34 IIGRSGSGKSTLLRCIN-GLEGyqDGSIKLGGMTITDRDSQAREISRSVGMVFQSFNlfphmtalENVMLAPRR--VLKk 110
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyALTG--ELPPNSKGGAHDPKLIREGEVRAQVKLAFENAN--------GKKYTITRSlaILE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 111 SAAECR--ELAQQMLEKVGlgdrldyypsSLSGGQQQ------RVAIARALAMSPKVLLCDEITSALDPELVGEVLKVL- 181
Cdd:cd03240 96 NVIFCHqgESNWPLLDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIi 165
|
170 180
....*....|....*....|..
gi 695700954 182 -EQLAAEGMTLILVTHEMNFAR 202
Cdd:cd03240 166 eERKSQKNFQLIVITHDEELVD 187
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-209 |
1.69e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 1.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695700954 137 SSLSGGQQQRVAIARALA--MSPKVLLCDEITSALDPELVGEVLKVLEQLAAEGMTLILVTHE---MNFArevgDRVV 209
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGaeLIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLA----DRII 548
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
121-198 |
2.24e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 121 QMLEKVGLGdrldyY-----PSS-LSGGQQQRVAIARALA--MSPKVL-LCDEITSALDPELVGEVLKVLEQLAAEGMTL 191
Cdd:COG0178 808 QTLQDVGLG-----YiklgqPATtLSGGEAQRVKLASELSkrSTGKTLyILDEPTTGLHFHDIRKLLEVLHRLVDKGNTV 882
|
....*..
gi 695700954 192 ILVTHEM 198
Cdd:COG0178 883 VVIEHNL 889
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
19-46 |
4.38e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 4.38e-04
10 20
....*....|....*....|....*...
gi 695700954 19 LKGVDLDIDMGQVISIIGRSGSGKSTLL 46
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-200 |
4.73e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.09 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 13 YGDNHVLKGVDLDIDMGQVISIIGRSGSGKSTLLRCINGLEGYQDGSIKLG-GMTITDRDsQAREIsrsvgmvfqsfnLF 91
Cdd:PRK11147 329 IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGtKLEVAYFD-QHRAE------------LD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 92 PHMTALEN-------VML--APRRVLKKsaaecrelaqqmlekvgLGDRLdYYP-------SSLSGGQQQRVAIARALAM 155
Cdd:PRK11147 396 PEKTVMDNlaegkqeVMVngRPRHVLGY-----------------LQDFL-FHPkramtpvKALSGGERNRLLLARLFLK 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695700954 156 SPKVLLCDEITSALDPelvgEVLKVLEQLAAE--GmTLILVTHEMNF 200
Cdd:PRK11147 458 PSNLLILDEPTNDLDV----ETLELLEELLDSyqG-TVLLVSHDRQF 499
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
21-46 |
5.89e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.19 E-value: 5.89e-04
10 20
....*....|....*....|....*.
gi 695700954 21 GVDLDIDMGQVISIIGRSGSGKSTLL 46
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
17-45 |
6.63e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 6.63e-04
10 20
....*....|....*....|....*....
gi 695700954 17 HVLKGVDLDIDMGQVISIIGRSGSGKSTL 45
Cdd:PRK00349 14 HNLKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
17-45 |
7.55e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 7.55e-04
10 20
....*....|....*....|....*....
gi 695700954 17 HVLKGVDLDIDMGQVISIIGRSGSGKSTL 45
Cdd:COG0178 619 NNLKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
17-45 |
1.54e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 1.54e-03
10 20
....*....|....*....|....*....
gi 695700954 17 HVLKGVDLDIDMGQVISIIGRSGSGKSTL 45
Cdd:COG0178 14 HNLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
139-220 |
2.04e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.06 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 139 LSGGQQQRVAIARALAMSPKVLLCDEITSALDPELVGEVLKVLEQLA--AEGMTLILVTHEMNFAREVGDRVVFMHQGKV 216
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVhlTEATVLMSLLQPAPETFDLFDDIILLSEGQI 416
|
....
gi 695700954 217 WEQG 220
Cdd:PLN03140 417 VYQG 420
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
17-45 |
2.53e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 2.53e-03
10 20
....*....|....*....|....*....
gi 695700954 17 HVLKGVDLDIDMGQVISIIGRSGSGKSTL 45
Cdd:TIGR00630 10 HNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
32-89 |
3.95e-03 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 37.57 E-value: 3.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695700954 32 ISIIGRSGSGKSTLLRCIngLegYQDGSIK-LG----GMTITDRDSQARE--ISRSVGMVFQSFN 89
Cdd:cd04170 2 IALVGHSGSGKTTLAEAL--L--YATGAIDrLGrvedGNTVSDYDPEEKKrkMSIETSVAPLEWN 62
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
137-216 |
4.20e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 38.03 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 137 SSLSGGQQQRVAIARALAM-----SPKVLLcDEITSALDPELVGEVLKVLEQLaAEGMTLILVTHEMNFArEVGDRV--V 209
Cdd:pfam02463 1076 DLLSGGEKTLVALALIFAIqkykpAPFYLL-DEIDAALDDQNVSRVANLLKEL-SKNAQFIVISLREEML-EKADKLvgV 1152
|
....*..
gi 695700954 210 FMHQGKV 216
Cdd:pfam02463 1153 TMVENGV 1159
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
25-196 |
4.27e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 37.25 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 25 DIDMGQVISIIGRSGSGKSTLLRCInglegyqdgSIKLGGMTITDRDSQAREISR-------SVGMVFQsfnlfphmtal 97
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTILDAI---------TYALYGKTPRYGRQENLRSVFapgedtaEVSFTFQ----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695700954 98 envmLAPR--RVLKKSAAECRELAQQMLEKVGLGDRLDYYP-SSLSGGQQQRVAIARALAMSPKV----------LLCDE 164
Cdd:cd03279 84 ----LGGKkyRVERSRGLDYDQFTRIVLLPQGEFDRFLARPvSTLSGGETFLASLSLALALSEVLqnrggarleaLFIDE 159
|
170 180 190
....*....|....*....|....*....|..
gi 695700954 165 ITSALDPELVGEVLKVLEQLAAEGMTLILVTH 196
Cdd:cd03279 160 GFGTLDPEALEAVATALELIRTENRMVGVISH 191
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