|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-239 |
4.63e-179 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 490.66 E-value: 4.63e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAALRSDVG 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFLGKI 239
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-214 |
5.26e-146 |
|
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: 406.15 E-value: 5.26e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAALRSDVGM 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 917391194 162 EPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAI 214
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-236 |
2.14e-127 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 361.04 E-value: 2.14e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL-----------PAEG 69
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgelvPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 70 KELAALRSDVGMVFQSFNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIAR 149
Cdd:COG4598 88 RQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 150 ALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQS 229
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKS 247
|
....*..
gi 917391194 230 ERARDFL 236
Cdd:COG4598 248 ERLRQFL 254
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-236 |
8.99e-121 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 343.61 E-value: 8.99e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAALRSDVG 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFL 236
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-242 |
1.43e-102 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 297.82 E-value: 1.43e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISV------EGRPLPAEGKELAA 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 75 LRSDVGMVFQSFNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAME 154
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 155 PKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARD 234
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
....*...
gi 917391194 235 FLGKILGH 242
Cdd:PRK11264 243 FLEKFLLQ 250
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-242 |
7.10e-102 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 299.30 E-value: 7.10e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHF----GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA-EGKELAAL 75
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 76 RSDVGMVFQSFNLFAHKTILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEP 155
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVAL-PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 156 KVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARD 234
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRR 239
|
....*...
gi 917391194 235 FLGKILGH 242
Cdd:COG1135 240 FLPTVLND 247
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
2-240 |
1.44e-101 |
|
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: 295.20 E-value: 1.44e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL-----------PAEGK 70
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLyhmpgrngplvPADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 71 ELAALRSDVGMVFQSFNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARA 150
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 151 LAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQS 229
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 917391194 230 ERARDFLGKIL 240
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-236 |
7.85e-95 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 277.67 E-value: 7.85e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL----PAEGKELAALRS 77
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfskTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 78 DVGMVFQSFNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKV 157
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 158 MLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSfFDNPQSERARDFL 236
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFKNYL 240
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-236 |
7.71e-94 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 275.35 E-value: 7.71e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGR----PLPAEGKELAALRS 77
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfSQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 78 DVGMVFQSFNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKV 157
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 158 MLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPdSFFDNPQSERARDFL 236
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQTEAFAHYL 240
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-218 |
1.68e-91 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 268.84 E-value: 1.68e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGD----LHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEG-KELAAL 75
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSeRELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 76 RSD-VGMVFQSFNLFAHKTILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAME 154
Cdd:COG1136 84 RRRhIGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917391194 155 PKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARkAADRVIFMADGAIVEDT 218
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAA-RADRVIRLRDGRIVSDE 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-228 |
5.60e-89 |
|
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: 262.52 E-value: 5.60e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGD----LHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA-EGKELAAL 75
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 76 RSDVGMVFQSFNLFAHKTILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEP 155
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917391194 156 KVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQ 228
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-236 |
7.87e-88 |
|
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: 259.91 E-value: 7.87e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLP-AEGKELAALRSDV 79
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITgLSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVML 159
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 160 FDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPqSERARDFL 236
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-237 |
4.55e-86 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 259.26 E-value: 4.55e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRP---LPAEgkelaalRS 77
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvtgLPPE-------KR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 78 DVGMVFQSFNLFAHKTILQNVTLAPtKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKV 157
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAENVAFGL-RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 158 MLFDEPTSALDP----EMVNEVLDVmvsLAKEGMTMLVVTH------EMgfarkaADRVIFMADGAIVEDTDPDSFFDNP 227
Cdd:COG3842 157 LLLDEPLSALDAklreEMREELRRL---QRELGITFIYVTHdqeealAL------ADRIAVMNDGRIEQVGTPEEIYERP 227
|
250
....*....|
gi 917391194 228 QSERARDFLG 237
Cdd:COG3842 228 ATRFVADFIG 237
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
6-236 |
4.01e-85 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 253.74 E-value: 4.01e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 6 DVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLP-----------AEGKELAA 74
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvADKNQLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 75 LRSDVGMVFQSFNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGI-ASQKDKYPAQLSGGQQQRVAIARALAM 153
Cdd:PRK10619 90 LRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 154 EPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERAR 233
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQ 249
|
...
gi 917391194 234 DFL 236
Cdd:PRK10619 250 QFL 252
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-241 |
7.54e-85 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 255.88 E-value: 7.54e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHF----GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA-EGKELAAL 75
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 76 RSDVGMVFQSFNLFAHKTILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEP 155
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 156 KVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARD 234
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTRE 239
|
....*..
gi 917391194 235 FLGKILG 241
Cdd:PRK11153 240 FIQSTLH 246
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-236 |
9.41e-85 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 252.22 E-value: 9.41e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRL-EPID----SGEISVEGRPLPAEGKELAALR 76
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMnDLVPgvriEGKVLFDGQDIYDKKIDVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 SDVGMVFQSFNLFAhKTILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQ-KDK---YPAQLSGGQQQRVAIARALA 152
Cdd:TIGR00972 82 RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEvKDRlhdSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 153 MEPKVMLFDEPTSALDPEMVNEVLDVMVSLaKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERA 232
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQEL-KKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRT 239
|
....
gi 917391194 233 RDFL 236
Cdd:TIGR00972 240 EDYI 243
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
3.50e-84 |
|
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: 249.71 E-value: 3.50e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGD----LHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEG-KELAALR 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSeKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 SD-VGMVFQSFNLFAHKTILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEP 155
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVEL-PLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 156 KVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKaADRVIFMADGAI 214
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-221 |
6.36e-84 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 250.36 E-value: 6.36e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHF-GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA-EGKELAALRSD 78
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQSFNLFAHKTILQNV--------TLAPTKVRKKNKADAEkRALELLERVGIASQKDKYPAQLSGGQQQRVAIARA 150
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagrlgrtSTWRSLLGLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 917391194 151 LAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPD 221
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPA 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
1.67e-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: 1.67e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHF-----GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA-EGKELAA 74
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 75 LRSDVGMVFQ----SFNlfAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGI-ASQKDKYPAQLSGGQQQRVAIAR 149
Cdd:COG1123 340 LRRRVQMVFQdpysSLN--PRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 150 ALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQ 228
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
....*
gi 917391194 229 SERAR 233
Cdd:COG1123 498 HPYTR 502
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-221 |
6.11e-81 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 243.07 E-value: 6.11e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHF----GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaegkelAALR 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-------TGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 SDVGMVFQSFNLFAHKTILQNVTLAPtKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPK 156
Cdd:COG1116 80 PDRGVVFQEPALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 157 VMLFDEPTSALDP----EMVNEVLDVmvsLAKEGMTMLVVTH---EmgfarkA---ADRVIFMAD--GAIVEDTDPD 221
Cdd:COG1116 159 VLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTHdvdE------AvflADRVVVLSArpGRIVEEIDVD 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-218 |
1.14e-80 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 241.11 E-value: 1.14e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHF-GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL-PAEGKELAALRSD 78
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQSFNLFAHKTILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVM 158
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 159 LFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDT 218
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-228 |
8.28e-80 |
|
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: 239.33 E-value: 8.28e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEG-KELAALRSDVG 80
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFF--DNPQ 228
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPL 231
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-228 |
9.63e-80 |
|
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: 238.77 E-value: 9.63e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVqkHF---GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaEGKELAALRSD 78
Cdd:COG1122 1 IELENL--SFsypGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI--TKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQsfN----LFAhKTILQNVTLAPtKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAME 154
Cdd:COG1122 77 VGLVFQ--NpddqLFA-PTVEEDVAFGP-ENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917391194 155 PKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQ 228
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-216 |
1.87e-79 |
|
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: 237.80 E-value: 1.87e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAegkeLAALRSDVGM 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG----VPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVTLAPtKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGL-KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 162 EPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVE 216
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-241 |
1.31e-78 |
|
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: 236.62 E-value: 1.31e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFG----DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPaeGKELAALR 76
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT--RRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 SDVGMVFQ----SFNlfAHKTILQnvTLA-PTKVRKKnkADAEKRALELLERVGI-ASQKDKYPAQLSGGQQQRVAIARA 150
Cdd:COG1124 79 RRVQMVFQdpyaSLH--PRHTVDR--ILAePLRIHGL--PDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 151 LAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQS 229
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
250
....*....|..
gi 917391194 230 ERARDFLGKILG 241
Cdd:COG1124 233 PYTRELLAASLA 244
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-212 |
8.88e-78 |
|
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: 232.08 E-value: 8.88e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAALRSDVGM 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVTLAptkvrkknkadaekralellervgiasqkdkypaqLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 917391194 162 EPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADG 212
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
9.32e-78 |
|
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: 234.00 E-value: 9.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPI-----DSGEISVEGRPLPAEGKELAALR 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 SDVGMVFQSFNLFaHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGI-ASQKDKYPA-QLSGGQQQRVAIARALAME 154
Cdd:cd03260 81 RRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALwDEVKDRLHAlGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 155 PKVMLFDEPTSALDPEMVNEVLDVMVSLAKEgMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSF 223
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-238 |
2.43e-76 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 233.06 E-value: 2.43e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHV-LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaEGKELAALRSDV 79
Cdd:COG1125 1 MIEFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDI--RDLDPVELRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNLFAHKTILQNVTLAPtKVRKKNKADAEKRALELLERVGI--ASQKDKYPAQLSGGQQQRVAIARALAMEPKV 157
Cdd:COG1125 79 GYVIQQIGLFPHMTVAENIATVP-RLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 158 MLFDEPTSALDPeMVNEVL-DVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVE-DTdPDSFFDNPQSERARD 234
Cdd:COG1125 158 LLMDEPFGALDP-ITREQLqDELLRLQRElGKTIVFVTHDIDEALKLGDRIAVMREGRIVQyDT-PEEILANPANDFVAD 235
|
....
gi 917391194 235 FLGK 238
Cdd:COG1125 236 FVGA 239
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-223 |
1.38e-75 |
|
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: 228.99 E-value: 1.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDL-HVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA-EGKELAALRSDV 79
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNLFAHKTILQNV------TLAPTKVRKKNKADAEK-RALELLERVGIASQKDKYPAQLSGGQQQRVAIARALA 152
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgRRSTWRSLFGLFPKEEKqRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 917391194 153 MEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSF 223
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-221 |
1.00e-74 |
|
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: 225.81 E-value: 1.00e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGD----LHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKelaalrs 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 78 DVGMVFQSFNLFAHKTILQNVTLAPtKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKV 157
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGL-ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 158 MLFDEPTSALDP----EMVNEVLDVmvsLAKEGMTMLVVTHEMGFARKAADRVIFMA--DGAIVEDTDPD 221
Cdd:cd03293 153 LLLDEPFSALDAltreQLQEELLDI---WRETGKTVLLVTHDIDEAVFLADRVVVLSarPGRIVAEVEVD 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-221 |
1.14e-74 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 226.10 E-value: 1.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPaegKELAALRSDVGM 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA---RDPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 162 EPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPD 221
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD 216
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-237 |
6.93e-74 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 228.11 E-value: 6.93e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEgkeLAALRSDVGM 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN---LPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVTLAPtKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 162 EPTSALD----PEMVNEVLDVmvsLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFLG 237
Cdd:COG1118 159 EPFGALDakvrKELRRWLRRL---HDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-236 |
1.67e-73 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 224.15 E-value: 1.67e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRL-EPID----SGEISVEGRPLPAEGKELAALR 76
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIPgarvEGEILLDGEDIYDPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 SDVGMVFQSFNLFAhKTILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQ-KDK---YPAQLSGGQQQRVAIARALA 152
Cdd:COG1117 92 RRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEvKDRlkkSALGLSGGQQQRLCIARALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 153 MEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEgMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERA 232
Cdd:COG1117 171 VEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRT 249
|
....
gi 917391194 233 RDFL 236
Cdd:COG1117 250 EDYI 253
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-237 |
3.57e-73 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 226.49 E-value: 3.57e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaegKELAALRSDVG 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV----TDLPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNLFAHKTILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAF-PLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHE----MGFarkaADRVIFMADGAIVEDTDPDSFFDNPQSERARDF 235
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEELYDRPANLFVAGF 233
|
..
gi 917391194 236 LG 237
Cdd:COG3839 234 IG 235
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-241 |
1.42e-72 |
|
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: 221.40 E-value: 1.42e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFG-DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL-PAEGKELAALRSD 78
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQSFNLFAHKTILQNVtLAPTKVRKKN---------KADAEkRALELLERVGIASQKDKYPAQLSGGQQQRVAIAR 149
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENV-LHGRLGYKPTwrsllgrfsEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 150 ALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVedtdpdsfFDNPQ 228
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIV--------FDGAP 230
|
250
....*....|...
gi 917391194 229 SERARDFLGKILG 241
Cdd:TIGR02315 231 SELDDEVLRHIYG 243
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-217 |
7.36e-71 |
|
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: 216.22 E-value: 7.36e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHF----GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL-PAEGKELAAL 75
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 76 RSDVGMVFQ----SFNlfAHKTILQNVTLAPTKVRKKNKADAEKRA-LELLERVGIASQ-KDKYPAQLSGGQQQRVAIAR 149
Cdd:cd03257 81 RKEIQMVFQdpmsSLN--PRMTIGEQIAEPLRIHGKLSKKEARKEAvLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 150 ALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVED 217
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-237 |
1.03e-70 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 216.16 E-value: 1.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHvlKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL----PAEGKelaalr 76
Cdd:COG3840 1 MLRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLtalpPAERP------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 sdVGMVFQSFNLFAHKTILQNVTLAptkVRKKNKADAEKRAL--ELLERVGIASQKDKYPAQLSGGQQQRVAIARALAME 154
Cdd:COG3840 73 --VSMLFQENNLFPHLTVAQNIGLG---LRPGLKLTAEQRAQveQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 155 PKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERAR 233
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALA 227
|
....
gi 917391194 234 DFLG 237
Cdd:COG3840 228 AYLG 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-238 |
3.47e-70 |
|
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: 215.24 E-value: 3.47e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLH-VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRL-EPiDSGEISVEGRPLPAEgkELAALRSDV 79
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLiEP-TSGEIFIDGEDIREQ--DPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNLFAHKTILQNVTLAPtKVRKKNKADAEKRALELLERVGI--ASQKDKYPAQLSGGQQQRVAIARALAMEPKV 157
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 158 MLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFL 236
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
..
gi 917391194 237 GK 238
Cdd:cd03295 237 GA 238
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-222 |
4.96e-70 |
|
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: 214.22 E-value: 4.96e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGD----LHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKE-LAAL 75
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDaRARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 76 RSD-VGMVFQSFNLFAHKTILQNVTLaPTKVRkkNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAME 154
Cdd:COG4181 88 RARhVGFVFQSFQLLPTLTALENVML-PLELA--GRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 155 PKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKaADRVIFMADGAIVEDTDPDS 222
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-228 |
6.63e-70 |
|
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: 216.84 E-value: 6.63e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHF----GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEP---IDSGEISVEGRPL-PAEGKEL 72
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLlKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 73 AALR-SDVGMVFQ----SFN-LFahkTILQNVTLAPTKVRKKNKADAEKRALELLERVGI---ASQKDKYPAQLSGGQQQ 143
Cdd:COG0444 81 RKIRgREIQMIFQdpmtSLNpVM---TVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 144 RVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDS 222
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEE 237
|
....*.
gi 917391194 223 FFDNPQ 228
Cdd:COG0444 238 LFENPR 243
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-235 |
1.54e-68 |
|
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: 211.73 E-value: 1.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 5 RDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA-EGKELAALRS-DVGMV 82
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKELRELRRkKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 83 FQSFNLFAHKTILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDE 162
Cdd:cd03294 108 FQSFALLPHRTVLENVAF-GLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 163 PTSALDP----EMVNEVLDVMvslAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDF 235
Cdd:cd03294 187 AFSALDPlirrEMQDELLRLQ---AELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-212 |
2.33e-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: 209.25 E-value: 2.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 3 VLRDVQKHFGDLH--VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaEGKELAALRSDVG 80
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL--TKLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFN--LFAHkTILQNVTLAPtKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVM 158
Cdd:cd03225 79 LVFQNPDdqFFGP-TVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 917391194 159 LFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADG 212
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-237 |
2.14e-67 |
|
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: 216.31 E-value: 2.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHF--GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPID---SGEISVEGRPLPAEGKELaaL 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL--R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 76 RSDVGMVFQ----SFNLFahkTILQNVTLAPtKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARAL 151
Cdd:COG1123 82 GRRIGMVFQdpmtQLNPV---TVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 152 AMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSE 230
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
....*..
gi 917391194 231 RARDFLG 237
Cdd:COG1123 238 AAVPRLG 244
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
17-235 |
1.47e-64 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 205.34 E-value: 1.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA-EGKELAALR-SDVGMVFQSFNLFAHKTI 94
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKlSKKELRELRrKKMSMVFQHFALLPHRTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 95 LQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP----E 170
Cdd:COG4175 123 LENVAF-GLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrE 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 171 MVNEVLDVMVSLAKegmTMLVVTHEMGFARKAADRVIFMADGAIV-EDTdPDSFFDNPQSERARDF 235
Cdd:COG4175 202 MQDELLELQAKLKK---TIVFITHDLDEALRLGDRIAIMKDGRIVqIGT-PEEILTNPANDYVADF 263
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-237 |
1.61e-64 |
|
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: 200.54 E-value: 1.61e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAegkeLAALRSDVGM 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN----LPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:cd03300 77 VFQNYALFPHLTVFENIAF-GLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 162 EPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFLG 237
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-239 |
1.64e-63 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 201.80 E-value: 1.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAegkeLAALRSDVGM 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITR----LPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYG-LKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 162 EPTSALDPEmvnevldVMVSLAKE--------GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERAR 233
Cdd:TIGR03265 160 EPLSALDAR-------VREHLRTEirqlqrrlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVA 232
|
....*.
gi 917391194 234 DFLGKI 239
Cdd:TIGR03265 233 DFVGEV 238
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-237 |
5.36e-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: 196.79 E-value: 5.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRplpaEGKELAALRSDVGM 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE----DATDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVTLApTKVRKK----NKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKV 157
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFG-LRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 158 MLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFL 236
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
.
gi 917391194 237 G 237
Cdd:cd03296 238 G 238
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-209 |
5.52e-62 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 192.83 E-value: 5.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAA--LRSDVGM 81
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASkfRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:TIGR03608 81 LFQNFALIENETVEENLDL-GLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 917391194 162 EPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFArKAADRVIFM 209
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-214 |
2.07e-61 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 191.57 E-value: 2.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL---PAEgkelaALRSD 78
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLsamPPP-----EWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQSFNLFAhKTILQNVTLAPtkvRKKNKADAEKRALELLERVGI-ASQKDKYPAQLSGGQQQRVAIARALAMEPKV 157
Cdd:COG4619 76 VAYVPQEPALWG-GTVRDNLPFPF---QLRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 158 MLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAI 214
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-221 |
9.20e-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: 191.41 E-value: 9.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA-EGKELAALrsdV 79
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARR---I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQS----FNL----------FAHKTILQNVTlaptkvrkknKADAEKrALELLERVGIASQKDKYPAQLSGGQQQRV 145
Cdd:COG1120 78 AYVPQEppapFGLtvrelvalgrYPHLGLFGRPS----------AEDREA-VEEALERTGLEHLADRPVDELSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 146 AIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPD 221
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-242 |
2.29e-60 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 190.30 E-value: 2.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaegkelAALRSDVG 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-------RRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFN----------------LFAHKTILqnvtlaptkvRKKNKADAEkRALELLERVGIASQKDKYPAQLSGGQQQR 144
Cdd:COG1121 79 YVPQRAEvdwdfpitvrdvvlmgRYGRRGLF----------RRPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 145 VAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTdPDSFF 224
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGP-PEEVL 226
|
250
....*....|....*...
gi 917391194 225 DNPQSERARDFLGKILGH 242
Cdd:COG1121 227 TPENLSRAYGGPVALLAH 244
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-216 |
2.27e-59 |
|
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: 186.69 E-value: 2.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaegKELAALRSDVGM 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV----TDLPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAF-GLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 162 EPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVE 216
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-212 |
1.64e-58 |
|
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: 182.98 E-value: 1.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELaalRSDVGM 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV---KRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVtlaptkvrkknkadaekralellervgiasqkdkypaQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:cd03230 78 LPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 917391194 162 EPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADG 212
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-241 |
1.70e-58 |
|
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: 185.45 E-value: 1.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaeGKELAALRSDVG 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV---RKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNLFAHKTILQNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRYF-AELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFLGKIL 240
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVALI 236
|
.
gi 917391194 241 G 241
Cdd:COG4555 237 G 237
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-228 |
4.15e-58 |
|
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: 184.86 E-value: 4.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRP---LPAEgkELAALrs 77
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitgLPPH--RIARL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 78 dvGMV--FQSFNLFAHKTILQNVTLA--------------PTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQ 141
Cdd:COG0411 80 --GIArtFQNPRLFPELTVLENVLVAaharlgrgllaallRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 142 QQRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDP 220
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
....*...
gi 917391194 221 DSFFDNPQ 228
Cdd:COG0411 238 AEVRADPR 245
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-228 |
5.52e-58 |
|
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: 183.79 E-value: 5.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRP---LPAEgkELAALRsdVG 80
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDitgLPPH--EIARLG--IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNLFAHKTILQNVTLAP---------TKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARAL 151
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMVAAqartgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 152 AMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQ 228
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-228 |
5.70e-58 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 186.86 E-value: 5.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHF-----------GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL-PAEG 69
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 70 KELAALRSDVGMVFQ----SFNlfAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGI-ASQKDKYPAQLSGGQQQR 144
Cdd:COG4608 88 RELRPLRRRMQMVFQdpyaSLN--PRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 145 VAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSF 223
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDEL 245
|
....*
gi 917391194 224 FDNPQ 228
Cdd:COG4608 246 YARPL 250
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-228 |
1.05e-57 |
|
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: 184.58 E-value: 1.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 15 HVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAE-GKELAALRSDVGMVFQsF---NLFA 90
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKkKKKLKDLRKKVGLVFQ-FpehQLFE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 91 hKTILQNVTLAPtKVRKKNKADAEKRALELLERVGI-ASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
Cdd:TIGR04521 98 -ETVYKDIAFGP-KNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 170 EMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQ 228
Cdd:TIGR04521 176 KGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-212 |
1.30e-57 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 182.06 E-value: 1.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHF-GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL-PAEGKELAALRSD 78
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVnRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQSFNLFAHKTILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVM 158
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 917391194 159 LFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADG 212
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
17-239 |
1.40e-57 |
|
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: 186.98 E-value: 1.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL----PAEGKELAalRSDVGMVFQSFNLFAHK 92
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENImkqsPVELREVR--RKKIGMVFQQFALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 93 TILQNVTLAPtKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMV 172
Cdd:TIGR01186 87 TILQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 173 NEVLDVMVSL-AKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFLGKI 239
Cdd:TIGR01186 166 DSMQDELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-239 |
4.72e-57 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 185.29 E-value: 4.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaegKELAALRSDVGM 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV----SRLHARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNV----TLAPTKVRKkNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKV 157
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIafglTVLPRRERP-NAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 158 MLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFL 236
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFM 237
|
...
gi 917391194 237 GKI 239
Cdd:PRK10851 238 GEV 240
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-237 |
1.28e-56 |
|
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: 180.22 E-value: 1.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHvLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGR---PLPAEgkelaalRSD 78
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPE-------KRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQSFNLFAHKTILQNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVM 158
Cdd:cd03299 73 ISYVPQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 159 LFDEPTSALDPEmVNEVLDVMVSLAKE--GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFL 236
Cdd:cd03299 152 LLDEPFSALDVR-TKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
.
gi 917391194 237 G 237
Cdd:cd03299 231 G 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-226 |
1.80e-56 |
|
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: 179.55 E-value: 1.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRP---LPAEgkelAALRSDVG 80
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDitgLPPH----ERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERvgIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDN 226
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
12-224 |
3.69e-55 |
|
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: 177.62 E-value: 3.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 12 GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRpLPAEGKELAALRSDVGMVFQS-FNLFA 90
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGL-DTLDEENLWEIRKKVGMVFQNpDNQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 91 HKTI-------LQNVTLAPTKVRKknkadaekRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEP 163
Cdd:TIGR04520 92 GATVeddvafgLENLGVPREEMRK--------RVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 917391194 164 TSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKaADRVIFMADGAIVEDTDPDSFF 224
Cdd:TIGR04520 164 TSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIF 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-212 |
7.03e-55 |
|
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: 173.20 E-value: 7.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAegKELAALRSDVGMVF 83
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK--LPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 84 QsfnlfahktilqnvtlaptkvrkknkadaekralellervgiasqkdkypaqLSGGQQQRVAIARALAMEPKVMLFDEP 163
Cdd:cd00267 80 Q----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 917391194 164 TSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADG 212
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-230 |
7.88e-54 |
|
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: 181.04 E-value: 7.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 8 QKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPiDSGEISVEGRPLPA-EGKELAALRSDVGMVFQ-- 84
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGlSRRALRPLRRRMQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 85 --SFN------------LFAHKTILqnvtlaptkvrkkNKADAEKRALELLERVGI-ASQKDKYPAQLSGGQQQRVAIAR 149
Cdd:COG4172 372 fgSLSprmtvgqiiaegLRVHGPGL-------------SAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 150 ALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQ 228
Cdd:COG4172 439 ALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQ 518
|
..
gi 917391194 229 SE 230
Cdd:COG4172 519 HP 520
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-237 |
1.42e-53 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 176.06 E-value: 1.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGrplpaegkELAALRS---- 77
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG--------EDVTHRSiqqr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 78 DVGMVFQSFNLFAHKTILQNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKV 157
Cdd:PRK11432 79 DICMVFQSYALFPHMSLGENVGYG-LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 158 MLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFL 236
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFM 237
|
.
gi 917391194 237 G 237
Cdd:PRK11432 238 G 238
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-215 |
1.87e-53 |
|
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: 170.31 E-value: 1.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaegkelaalrsdvgmvf 83
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 84 qsfNLFAHKTILQNVTLAPTkvrkknkadaekraleLLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEP 163
Cdd:cd03214 64 ---ASLSPKELARKIAYVPQ----------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 917391194 164 TSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIV 215
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-228 |
2.84e-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: 179.50 E-value: 2.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 12 GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEP----IDSGEISVEGRPL-PAEGKELAALR-SDVGMVFQ- 84
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLlGLSERELRRIRgNRIAMIFQe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 85 ---SFNlfAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGI---ASQKDKYPAQLSGGQQQRVAIARALAMEPKVM 158
Cdd:COG4172 101 pmtSLN--PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEPDLL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917391194 159 LFDEPTSALDPEMVNEVLDVMVSL-AKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQ 228
Cdd:COG4172 179 IADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-214 |
3.80e-53 |
|
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: 170.67 E-value: 3.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHF-GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA-EGKELAALRSDV 79
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNLFAHKTILQNVTLAPTKVRKKNKaDAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVML 159
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPR-EIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 917391194 160 FDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAI 214
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-237 |
4.00e-53 |
|
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: 171.32 E-value: 4.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRP---LPAEgkELAALRs 77
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDitgLPPH--RIARLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 78 dVGMVFQSFNLFAHKTILQNVTLA--PTKVRKKNKADAEkRALE----LLERvgiASQkdkyPA-QLSGGQQQRVAIARA 150
Cdd:COG0410 80 -IGYVPEGRRIFPSLTVEENLLLGayARRDRAEVRADLE-RVYElfprLKER---RRQ----RAgTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 151 LAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPqsE 230
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP--E 228
|
....*..
gi 917391194 231 RARDFLG 237
Cdd:COG0410 229 VREAYLG 235
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-221 |
8.44e-53 |
|
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: 181.19 E-value: 8.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLH--VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaEGKELAALRSDV 79
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL--RQIDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNLFaHKTILQNVTLAptkvrkknKADA-EKRALELLERVGIASQKDKYP-----------AQLSGGQQQRVAI 147
Cdd:COG2274 552 GVVLQDVFLF-SGTIRENITLG--------DPDAtDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917391194 148 ARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKeGMTMLVVTHEMGFARKaADRVIFMADGAIVEDTDPD 221
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHE 694
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-214 |
2.10e-52 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 170.24 E-value: 2.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEisvegrpLPAEGKELAALRSDVGM 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-------LLAGTAPLAEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVTLAPtkvrkknKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:PRK11247 86 MFQDARLLPWKKVIDNVGLGL-------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 917391194 162 EPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAI 214
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-239 |
3.72e-52 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 173.21 E-value: 3.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRP---LPAEgkelaalRSD 78
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDithVPAE-------NRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQSFNLFAHKTILQNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVM 158
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 159 LFDEPTSALD----PEMVNEvldvMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERAR 233
Cdd:PRK09452 167 LLDESLSALDyklrKQMQNE----LKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVA 242
|
....*.
gi 917391194 234 DFLGKI 239
Cdd:PRK09452 243 RFIGEI 248
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
16-212 |
4.03e-52 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 168.36 E-value: 4.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLP--AEGKELAALRSDVGMVFQSFNLFAHKT 93
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTnlSYSQKIILRRELIGYIFQSFNLIPHLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 94 ILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVN 173
Cdd:NF038007 100 IFDNVAL-PLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNAR 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 917391194 174 EVLDVMVSLAKEGMTMLVVTHEMGfARKAADRVIFMADG 212
Cdd:NF038007 179 AVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDG 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-212 |
6.50e-52 |
|
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: 166.02 E-value: 6.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGD--LHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEgkELAALRSDV 79
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL--DLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNLFaHKTILQNVtlaptkvrkknkadaekralellervgiasqkdkypaqLSGGQQQRVAIARALAMEPKVML 159
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 917391194 160 FDEPTSALDPEMVNEVLDVMVSLAKeGMTMLVVTHEMGFARKaADRVIFMADG 212
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-239 |
8.51e-51 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 165.86 E-value: 8.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRL-----EPIDSGEISVEGRPLPAegKELAALR 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFK--MDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 SDVGMVFQSFNLFAHKTILQNVTLAPTKVR-KKNKADAEKRALELLERVGIASQ-KDKYPA---QLSGGQQQRVAIARAL 151
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKLNRlVKSKKELQERVRWALEKAQLWDEvKDRLDApagKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 152 AMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEgMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSER 231
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHEL 240
|
....*....
gi 917391194 232 ARDFL-GKI 239
Cdd:PRK14247 241 TEKYVtGRL 249
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-221 |
3.27e-50 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 170.97 E-value: 3.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL----PAEgkelaALR 76
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrsPRD-----AQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 SDVGMVFQSFNLFAHKTILQNVTLA--PTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAME 154
Cdd:COG1129 79 AGIAIIHQELNLVPNLSVAENIFLGrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 917391194 155 PKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIV-----EDTDPD 221
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVgtgpvAELTED 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-210 |
4.21e-50 |
|
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: 162.70 E-value: 4.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 11 FGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaegkelAALRSDVGMVFQSFNL-- 88
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-------EKERKRIGYVPQRRSIdr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 89 -FAhKTILQNVTLAPTKVR---KKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
Cdd:cd03235 82 dFP-ISVRDVVLMGLYGHKglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 917391194 165 SALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMA 210
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-216 |
1.24e-49 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 170.73 E-value: 1.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVqkHF---GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaegKE--LAALR 76
Cdd:COG1132 340 IEFENV--SFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI----RDltLESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 SDVGMVFQSFNLFaHKTILQNVTLAptkvrKKNKADAE-KRALEL--LERVgIASQKDKYPAQ-------LSGGQQQRVA 146
Cdd:COG1132 414 RQIGVVPQDTFLF-SGTIRENIRYG-----RPDATDEEvEEAAKAaqAHEF-IEALPDGYDTVvgergvnLSGGQRQRIA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917391194 147 IARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKeGMTMLVVTHemgfaR----KAADRVIFMADGAIVE 216
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAH-----RlstiRNADRILVLDDGRIVE 554
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-242 |
1.36e-49 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 163.71 E-value: 1.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAALRSDVGMVFQSFN--LFAhKT 93
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVGIVFQNPDdqLFA-PT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 94 ILQNVTLAPTKVrKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVN 173
Cdd:PRK13639 96 VEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 174 EVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFLGKILGH 242
Cdd:PRK13639 175 QIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKANLRLPRVAH 243
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-165 |
1.39e-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: 159.35 E-value: 1.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPaeGKELAALRSDVGMVFQSFNLFAHKTILQ 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT--DDERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917391194 97 NVTLAPTkVRKKNKADAEKRALELLERVGIASQKD----KYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTS 165
Cdd:pfam00005 79 NLRLGLL-LKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-239 |
2.16e-49 |
|
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: 164.59 E-value: 2.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 32 VLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaegKELAALRSDVGMVFQSFNLFAHKTILQNVTLaPTKVRKKNKA 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV----TNVPPHLRHINMVFQSYALFPHMTVEENVAF-GLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 112 DAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD----PEMVNEVLDVMVSLakeGM 187
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQL---GI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 917391194 188 TMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFLGKI 239
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
6-215 |
2.42e-49 |
|
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: 165.27 E-value: 2.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 6 DVQKHFGDLHVlkDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL--PAEGKELAALRSDVGMVF 83
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLPPHRRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 84 QSFNLFAHKTILQNVTLAptkvRKKNKADAEKRAL-ELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDE 162
Cdd:COG4148 84 QEARLFPHLSVRGNLLYG----RKRAPRAERRISFdEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 917391194 163 PTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIV 215
Cdd:COG4148 160 PLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
6-215 |
4.06e-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: 160.54 E-value: 4.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 6 DVQKHFGDLHVlkDIDLEVPaGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKE--LAALRSDVGMVF 83
Cdd:cd03297 5 DIEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinLPPQQRKIGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 84 QSFNLFAHKTILQNVTLAptkvrKKNKADAEKRAL--ELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:cd03297 82 QQYALFPHLNVRENLAFG-----LKRKRNREDRISvdELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 917391194 162 EPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIV 215
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
19-217 |
4.78e-49 |
|
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: 160.35 E-value: 4.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 19 DIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAegkeLAALRSDVGMVFQSFNLFAHKTILQNV 98
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA----APPADRPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 99 TLAPTKVRKKNKADAEKRAlELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDV 178
Cdd:cd03298 92 GLGLSPGLKLTAEDRQAIE-VALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 917391194 179 MVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVED 217
Cdd:cd03298 171 VLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-241 |
8.41e-49 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 160.78 E-value: 8.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPID-----SGEISVEGRPLPAEGKELAALR 76
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 SDVGMVFQSFNLFAHKTILQNVTLAptkvRKKNKADAEKRalELLERVGIASQK-----------DKYPAQLSGGQQQRV 145
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIG----VKLNGLVKSKK--ELDERVEWALKKaalwdevkdrlNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 146 AIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEgMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFD 225
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
250
....*....|....*.
gi 917391194 226 NPQSERARDFLGKILG 241
Cdd:PRK14267 238 NPEHELTEKYVTGALG 253
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-221 |
8.81e-49 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 167.13 E-value: 8.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL----PAEgkelaALR 76
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirsPRD-----AIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 SDVGMVFQSFNLFAHKTILQNVTLA--PTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAME 154
Cdd:COG3845 80 LGIGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 155 PKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPD 221
Cdd:COG3845 160 ARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-215 |
2.12e-48 |
|
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: 158.19 E-value: 2.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAegkelAALRSDVGMVFQS--FNLFAhKT 93
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-----KERRKSIGYVMQDvdYQLFT-DS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 94 ILQNVTLaptkvRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVN 173
Cdd:cd03226 89 VREELLL-----GLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 917391194 174 EVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIV 215
Cdd:cd03226 164 RVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-222 |
5.33e-48 |
|
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: 166.09 E-value: 5.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHF--GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEgkELAALRSDV 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDL--DEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNLFAHkTILQNVTLAptkvrkknKADA-EKRALELLERVG----IASQKDKY-------PAQLSGGQQQRVAI 147
Cdd:COG4987 412 AVVPQRPHLFDT-TLRENLRLA--------RPDAtDEELWAALERVGlgdwLAALPDGLdtwlgegGRRLSGGERRRLAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 148 ARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKeGMTMLVVTHEM-GFARkaADRVIFMADGAIVEDTDPDS 222
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLaGLER--MDRILVLEDGRIVEQGTHEE 555
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
1.67e-47 |
|
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: 154.51 E-value: 1.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL----PAEgkelaALRS 77
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVsfasPRD-----ARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 78 DVGMVFQsfnlfahktilqnvtlaptkvrkknkadaekralellervgiasqkdkypaqLSGGQQQRVAIARALAMEPKV 157
Cdd:cd03216 76 GIAMVYQ----------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 158 MLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIV 215
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-221 |
1.73e-47 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 157.72 E-value: 1.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFG----DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGkelaalr 76
Cdd:COG4525 3 MLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 SDVGMVFQSFNLFAHKTILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPK 156
Cdd:COG4525 76 ADRGVVFQKDALLPWLNVLDNVAF-GLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917391194 157 VMLFDEPTSALDP---EMVNE-VLDVMvslAKEGMTMLVVTHEMGFARKAADRVIFMAD--GAIVEDTDPD 221
Cdd:COG4525 155 FLLMDEPFGALDAltrEQMQElLLDVW---QRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVERLELD 222
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-221 |
1.62e-46 |
|
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: 162.23 E-value: 1.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQ-KHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEgkELAALRSDVG 80
Cdd:COG4988 337 IELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL--DPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNLFaHKTILQNVTLAptkvrkknKADAEKRAL-ELLERVG----IASQKDKYP-------AQLSGGQQQRVAIA 148
Cdd:COG4988 415 WVPQNPYLF-AGTIRENLRLG--------RPDASDEELeAALEAAGldefVAALPDGLDtplgeggRGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917391194 149 RALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKeGMTMLVVTHEMGFARkAADRVIFMADGAIVEDTDPD 221
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLA-QADRILVLDDGRIVEQGTHE 556
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-228 |
3.68e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 155.18 E-value: 3.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAE--GKELAALRSDVGMVFQ--SFNLFaHK 92
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkkNKKLKPLRKKVGIVFQfpEHQLF-EE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 93 TILQNVTLAPTKVRKKnKADAEKRALELLERVGI-ASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEM 171
Cdd:PRK13634 102 TVEKDICFGPMNFGVS-EEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 172 VNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQ 228
Cdd:PRK13634 181 RKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
4.06e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 155.27 E-value: 4.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKE--------- 71
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigylpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 72 --------------LAALRsdvGMvfqsfnlfahktilqnvtlaptkvrkkNKADAEKRALELLERVGIASQKDKYPAQL 137
Cdd:COG4152 81 glypkmkvgeqlvyLARLK---GL---------------------------SKAEAKRRADEWLERLGLGDRANKKVEEL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 138 SGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVED 217
Cdd:COG4152 131 SKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-213 |
6.29e-46 |
|
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: 151.86 E-value: 6.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaeGKELAALRSDVG 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI---RDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNLFAHKTILQNVTLAptkVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFW---AALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTH-EMGFarkAADRVIFMADGA 213
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqPLEL---AAARVLDLGDFK 206
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-238 |
1.11e-45 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 153.01 E-value: 1.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRL-----EPIDSGEISVEGRPLPAEGKELAAL 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 76 RSDVGMVFQSFNLFAHkTILQNVT--LAPTKVRKKNKADAekrALEL-LERVGIASQ-KDKYPAQ---LSGGQQQRVAIA 148
Cdd:PRK14239 85 RKEIGMVFQQPNPFPM-SIYENVVygLRLKGIKDKQVLDE---AVEKsLKGASIWDEvKDRLHDSalgLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 149 RALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLaKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQ 228
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
250
....*....|.
gi 917391194 229 SERARDFL-GK 238
Cdd:PRK14239 240 HKETEDYIsGK 250
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-237 |
1.53e-45 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 155.57 E-value: 1.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL----PAEgkelaalRS 77
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMndvpPAE-------RG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 78 dVGMVFQSFNLFAHKTILQNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKV 157
Cdd:PRK11000 77 -VGMVFQSYALYPHLSVAENMSFG-LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 158 MLFDEPTSALDP----EMVNEVLDVMVSLakeGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERAR 233
Cdd:PRK11000 155 FLLDEPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVA 231
|
....
gi 917391194 234 DFLG 237
Cdd:PRK11000 232 GFIG 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-242 |
2.14e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 153.08 E-value: 2.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGD-LHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAALRSDV 79
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQS--FNLFAhKTILQNVTLAPTKVrKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKV 157
Cdd:PRK13636 85 GMVFQDpdNQLFS-ASVYQDVSFGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 158 MLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFL 236
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKVNLR 242
|
....*.
gi 917391194 237 GKILGH 242
Cdd:PRK13636 243 LPRIGH 248
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-220 |
2.55e-45 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 160.27 E-value: 2.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHF----GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA-EGKELAALRSD 78
Cdd:PRK10535 7 LKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADALAQLRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 -VGMVFQSFNLFAHKTILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKV 157
Cdd:PRK10535 87 hFGFIFQRYHLLSHLTAAQNVEV-PAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917391194 158 MLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKaADRVIFMADGAIVEDTDP 220
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPA 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-237 |
5.72e-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: 5.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHF-GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL----PAEgkelaal 75
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnelePAD------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 76 rSDVGMVFQSFNLFAHKTILQNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEP 155
Cdd:PRK11650 76 -RDIAMVFQNYALYPHMSVRENMAYG-LKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 156 KVMLFDEPTSALDP----EMVNEVLDVMVSLakeGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSER 231
Cdd:PRK11650 154 AVFLFDEPLSNLDAklrvQMRLEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTF 230
|
....*.
gi 917391194 232 ARDFLG 237
Cdd:PRK11650 231 VASFIG 236
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-226 |
2.92e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 150.20 E-value: 2.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAALRSDVGMVFQ--SFNLFaHKTI 94
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQypEYQLF-EETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 95 LQNVTLAPTKvRKKNKADAEKRALELLERVGIASQ--KDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMV 172
Cdd:PRK13637 102 EKDIAFGPIN-LGLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 917391194 173 NEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDN 226
Cdd:PRK13637 181 DEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-216 |
8.68e-44 |
|
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: 147.29 E-value: 8.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAAlRSDVGMVF 83
Cdd:TIGR03410 3 VSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA-RAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 84 QSFNLFAHKTILQNV-TLAPTKVRKKNKADAEKRAL-----ELLERVGiasqkdkypAQLSGGQQQRVAIARALAMEPKV 157
Cdd:TIGR03410 82 QGREIFPRLTVEENLlTGLAALPRRSRKIPDEIYELfpvlkEMLGRRG---------GDLSGGQQQQLAIARALVTRPKL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 158 MLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVE 216
Cdd:TIGR03410 153 LLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVA 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-220 |
1.18e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 149.08 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFG-----DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEIS----------------- 59
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 60 -----VEGRPLPAEGKELAALRSDVGMVFQ--SFNLFaHKTILQNVTLAPTKVRKKnKADAEKRALELLERVGI-ASQKD 131
Cdd:PRK13651 83 vleklVIQKTRFKKIKKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVS-KEEAKKRAAKYIELVGLdESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 132 KYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMAD 211
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
....*....
gi 917391194 212 GAIVEDTDP 220
Cdd:PRK13651 241 GKIIKDGDT 249
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-223 |
1.24e-43 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 147.91 E-value: 1.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA-EGKELAALRSDVGMVFQ----SFNlfA 90
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRAQRKAFRRDIQMVFQdsisAVN--P 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 91 HKTILQNVTLAPTKVRKKNKADAEKRALELLERVGIA-SQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
Cdd:PRK10419 105 RKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 170 EMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVED---TDPDSF 223
Cdd:PRK10419 185 VLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETqpvGDKLTF 242
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
1.45e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 147.83 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLH--VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEgkELAALRSD 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKE--NLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQS-FNLFAHKTI-------LQNVTLAPTKVRKKnkadaekrALELLERVGIASQKDKYPAQLSGGQQQRVAIARA 150
Cdd:PRK13632 85 IGIIFQNpDNQFIGATVeddiafgLENKKVPPKKMKDI--------IDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 151 LAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGM-TMLVVTHEMGFARKaADRVIFMADGAIVEDTDPDSFFDNPQ 228
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-232 |
1.86e-43 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 146.65 E-value: 1.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLkdIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEG----RPLPAegkelaalR 76
Cdd:PRK10771 1 MLKLTDITWLYHHLPMR--FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtTTPPS--------R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 SDVGMVFQSFNLFAHKTILQNVTLAPTKVRKKNkaDAEKRALE-LLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEP 155
Cdd:PRK10771 71 RPVSMLFQENNLFSHLTVAQNIGLGLNPGLKLN--AAQREKLHaIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 156 KVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERA 232
Cdd:PRK10771 149 PILLLDEPFSALDPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASA 226
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-218 |
7.95e-43 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 146.77 E-value: 7.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 9 KHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPaegKELAALRSDVGMVFQSFNL 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV---REPRKVRRSIGIVPQYASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 89 FAHKTILQNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
Cdd:TIGR01188 78 DEDLTGRENLEMM-GRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 917391194 169 PEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIV-EDT 218
Cdd:TIGR01188 157 PRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIaEGT 207
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-217 |
8.04e-43 |
|
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: 143.90 E-value: 8.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGrplPAEGKELAALRSdVGM 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG---KSYQKNIEALRR-IGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVTLAPTKVRKKNKadaekRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLARLLGIRKK-----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 162 EPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVED 217
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-239 |
9.41e-43 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 148.83 E-value: 9.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaegKELAALRSDVGMVF 83
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----SHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 84 QSFNLFAHKTILQNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEP 163
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 164 TSALDPE----MVNEVLDVmvsLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFLGKI 239
Cdd:PRK11607 177 MGALDKKlrdrMQLEVVDI---LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSV 253
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-215 |
2.13e-42 |
|
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: 143.19 E-value: 2.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGkelaalRSDVGMVF 83
Cdd:cd03269 3 VENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA------RNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 84 QSFNLFAHKTIL-QNVTLAptKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDE 162
Cdd:cd03269 77 EERGLYPKMKVIdQLVYLA--QLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 917391194 163 PTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIV 215
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
7-218 |
3.51e-42 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 143.00 E-value: 3.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 7 VQKHFGD----LHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKE-LAALRS-DVG 80
Cdd:PRK10584 12 LKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaRAKLRAkHVG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNLFAHKTILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:PRK10584 92 FVFQSFMLIPTLNALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKaADRVIFMADGAIVEDT 218
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEEA 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-222 |
9.13e-42 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 142.95 E-value: 9.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA-EGKELAALRsdv 79
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwSPWELARRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNL-FAHkTILQNVTLAPTKVRKKNKADAEkRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALA------ 152
Cdd:COG4559 78 AVLPQHSSLaFPF-TVEEVVALGRAPHGSSAAQDRQ-IVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepv 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917391194 153 -MEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDS 222
Cdd:COG4559 156 dGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-211 |
1.08e-41 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 141.08 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTIN-RLEPI--DSGEISVEGRPLPAegkeLAALRS 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRLTA----LPAEQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 78 DVGMVFQSFNLFAHKTILQNVTLA-PTKVRKKNKADaekRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPK 156
Cdd:COG4136 77 RIGILFQDDLLFPHLSVGENLAFAlPPTIGRAQRRA---RVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 157 VMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGfARKAADRVIFMAD 211
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREFVFEQIRQrGIPALLVTHDEE-DAPAAGRVLDLGN 208
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-239 |
1.74e-41 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 142.11 E-value: 1.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 10 HFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpAEGKEL-----AALRSDVGMVFQ 84
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVL-YFGKDIfqidaIKLRKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 85 SFNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQ---KDKYPA-QLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:PRK14246 98 QPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEvydRLNSPAsQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKEgMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDF-LGKI 239
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYvIGRI 256
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-226 |
1.98e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 142.53 E-value: 1.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEgKELAALRSDVGMVFQSFNLFAHKTIL 95
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDE-ENLWDIRNKAGMVFQNPDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 Q--------NVTLAPTKVRKknkadaekRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSAL 167
Cdd:PRK13633 104 EedvafgpeNLGIPPEEIRE--------RVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 168 DPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKaADRVIFMADGAIVEDTDPDSFFDN 226
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-212 |
2.78e-41 |
|
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: 140.68 E-value: 2.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGkelaalrSDVGMVFQSFNLFAHKTILQ 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-------PDRMVVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 97 NVTLAPTKV-RKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEV 175
Cdd:TIGR01184 74 NIALAVDRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 917391194 176 LDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADG 212
Cdd:TIGR01184 154 QEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-236 |
3.39e-41 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 141.46 E-value: 3.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLR--DVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRL-EPIDS----GEISVEGRPLPAEGKELAA 74
Cdd:PRK14243 9 TVLRteNLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLnDLIPGfrveGKVTFHGKNLYAPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 75 LRSDVGMVFQSFNLFAhKTILQNVTLAPTKVRKKNKADaekralELLER-----VGIASQKDKYPAQ---LSGGQQQRVA 146
Cdd:PRK14243 89 VRRRIGMVFQKPNPFP-KSIYDNIAYGARINGYKGDMD------ELVERslrqaALWDEVKDKLKQSglsLSGGQQQRLC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 147 IARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLaKEGMTMLVVTHEMGFARKAADRVIFMA---------DGAIVED 217
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEF 240
|
250
....*....|....*....
gi 917391194 218 TDPDSFFDNPQSERARDFL 236
Cdd:PRK14243 241 DRTEKIFNSPQQQATRDYV 259
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-199 |
3.86e-41 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 139.10 E-value: 3.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 12 GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAALRSDVGMVFQSFN--LF 89
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQDPDdqLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 90 AhKTILQNVTLAPTKVRKKnKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
Cdd:TIGR01166 83 A-ADVDQDVAFGPLNLGLS-EAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180 190
....*....|....*....|....*....|
gi 917391194 170 EMVNEVLDVMVSLAKEGMTMLVVTHEMGFA 199
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-212 |
4.65e-41 |
|
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: 139.95 E-value: 4.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDL--HVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaeGKELAALRSDV 79
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI---RTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNLFAHKTILQNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVML 159
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFY-ARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 917391194 160 FDEPTSALDPEMVNEVLDvMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADG 212
Cdd:cd03263 157 LDEPTSGLDPASRRAIWD-LILEVRKGRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
6-242 |
1.16e-40 |
|
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: 142.56 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 6 DVQKHFGDLHVlkDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL--PAEGKELAALRSDVGMVF 83
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdSRKGIFLPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 84 QSFNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLervGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEP 163
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 164 TSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNP------QSERARDFL 236
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPdlpwlaREDQGSLIE 238
|
....*.
gi 917391194 237 GKILGH 242
Cdd:TIGR02142 239 GVVAEH 244
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
13-214 |
1.29e-40 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 138.46 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 13 DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRplpaEGKELAALRSDVGMVFQSFNLFAHK 92
Cdd:TIGR01277 10 YEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ----SHTGLAPYQRPVSMLFQENNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 93 TILQNVTLAPTKVRKKNKADAEKrALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMV 172
Cdd:TIGR01277 86 TVRQNIGLGLHPGLKLNAEQQEK-VVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 917391194 173 NEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAI 214
Cdd:TIGR01277 165 EEMLALVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-236 |
2.85e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 139.77 E-value: 2.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEgkELAALRSDVGMVFQS-FNLFAHKTIL 95
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEE--TVWDVRRQVGMVFQNpDNQFVGATVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEV 175
Cdd:PRK13635 101 DDVAFG-LENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREV 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917391194 176 LDVMVSLAKEGM-TMLVVTHEMGFARKaADRVIFMADGAIVEDTDPDSFF-----------DNPQSERARDFL 236
Cdd:PRK13635 180 LETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFksghmlqeiglDVPFSVKLKELL 251
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-226 |
4.89e-40 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 138.61 E-value: 4.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRL---EPIDSGEISVEGRPLPAEGK---ELAA 74
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRlarDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 75 LRSDVGMVFQSFNLFAHKTILQNVTLAP--------TKVRKKNKADaEKRALELLERVGIASQKDKYPAQLSGGQQQRVA 146
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwrTCFSWFTREQ-KQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 147 IARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAK-EGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSfFD 225
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ-FD 241
|
.
gi 917391194 226 N 226
Cdd:PRK09984 242 N 242
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-220 |
5.16e-40 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 138.37 E-value: 5.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTI-NRLEPiDSGEISVEGRPLPA-EGKELAALRsd 78
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGELSP-DSGEVRLNGRPLADwSPAELARRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 vGMVFQSFNL-FAHkTILQNVTLAPTKVRKKNKADAEKrALELLERVGIASQKDKYPAQLSGGQQQRVAIARALA----- 152
Cdd:PRK13548 79 -AVLPQHSSLsFPF-TVEEVVAMGRAPHGLSRAEDDAL-VAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 153 -MEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDP 220
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
8-227 |
1.06e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 139.22 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 8 QKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVE--------------GRPLPAEGKELA 73
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnheliTNPYSKKIKNFK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 74 ALRSDVGMVFQ--SFNLFaHKTILQNVTLAPTKVrKKNKADAEKRALELLERVGIASQ-KDKYPAQLSGGQQQRVAIARA 150
Cdd:PRK13631 113 ELRRRVSMVFQfpEYQLF-KDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 151 LAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNP 227
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-236 |
3.03e-39 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 140.17 E-value: 3.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLP----AEGKELAalRSDVGMVFQSFNLFAHK 92
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVR--RKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 93 TILQNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMV 172
Cdd:PRK10070 122 TVLDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917391194 173 NEVLDVMVSL-AKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFL 236
Cdd:PRK10070 201 TEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-217 |
3.44e-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: 134.63 E-value: 3.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGqVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELaalRSDVGM 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL---RRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNV-TLAPTKvrKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:cd03264 77 LPQEFGVYPNFTVREFLdYIAWLK--GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAkEGMTMLVVTHEMGFARKAADRVIFMADGAIVED 217
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-217 |
5.96e-39 |
|
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: 135.21 E-value: 5.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLE-PIDSGEISVEGRPLpaeGKE-LAALRSD 78
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERR---GGEdVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQSfnlfahktiLQNVTLAPTKVR--------------KKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQR 144
Cdd:COG1119 80 IGLVSPA---------LQLRFPRDETVLdvvlsgffdsiglyREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 145 VAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEG-MTMLVVTH---EM--GFarkaaDRVIFMADGAIVED 217
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGI-----THVLLLKDGRVVAA 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-224 |
6.04e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 136.41 E-value: 6.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA--EGKELAALRSDVGMVFQ--SFNLFAhK 92
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsKNKDIKQIRKKVGLVFQfpESQLFE-E 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 93 TILQNVTLAPTKVrKKNKADAEKRALELLERVGIASQ-KDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEM 171
Cdd:PRK13649 102 TVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 917391194 172 VNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFF 224
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-216 |
7.42e-39 |
|
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: 134.67 E-value: 7.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVqkHFG---DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaEGKELAALRSD 78
Cdd:cd03253 1 IEFENV--TFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI--REVTLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQSFNLFaHKTILQNVTLAPTKVRKKNKADAEKRAlELLERvgIASQKDKYPAQ-------LSGGQQQRVAIARAL 151
Cdd:cd03253 77 IGVVPQDTVLF-NDTIGYNIRYGRPDATDEEVIEAAKAA-QIHDK--IMRFPDGYDTIvgerglkLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917391194 152 AMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKeGMTMLVVTHEMGFArKAADRVIFMADGAIVE 216
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTI-VNADKIIVLKDGRIVE 215
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
8.04e-39 |
|
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: 134.48 E-value: 8.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFgDLH--------VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISV--EGRPLP---A 67
Cdd:COG4778 4 LLEVENLSKTF-TLHlqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDlaqA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 68 EGKELAALRSD-VGMVFQSFNLFAHKTILQnVTLAPTKVRKKNKADAEKRALELLERVGIASQK-DKYPAQLSGGQQQRV 145
Cdd:COG4778 83 SPREILALRRRtIGYVSQFLRVIPRVSALD-VVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 146 AIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGA 213
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
5-228 |
9.18e-39 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 137.02 E-value: 9.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 5 RDVQKHF----------GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKE-LA 73
Cdd:PRK11308 9 IDLKKHYpvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 74 ALRSDVGMVFQ----SFNlfAHKTILQnvTLA-PTKVRKK-NKADAEKRALELLERVGI-ASQKDKYPAQLSGGQQQRVA 146
Cdd:PRK11308 89 LLRQKIQIVFQnpygSLN--PRKKVGQ--ILEePLLINTSlSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 147 IARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFD 225
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFN 244
|
...
gi 917391194 226 NPQ 228
Cdd:PRK11308 245 NPR 247
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-221 |
9.72e-39 |
|
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: 134.03 E-value: 9.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELaalRSDVGM 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREV---RRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIH-ARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917391194 162 EPTSALDPEMVNEVLDVMVSL-AKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPD 221
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-228 |
1.74e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 135.34 E-value: 1.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAE--GKELAALRSDVGMVFQ--SFNLFaHK 92
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgNKNLKKLRKKVSLVFQfpEAQLF-EN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 93 TILQNVTLAPTKVRKKNKaDAEKRALELLERVGIASQ-KDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEM 171
Cdd:PRK13641 102 TVLKDVEFGPKNFGFSED-EAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 172 VNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQ 228
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-221 |
5.46e-38 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 132.90 E-value: 5.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL----PAE-GKELAAL 75
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVattpSRElAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 76 RSDVGMVFQ-------SFNLFAHktilqnvtlapTKVRKkNKADAEK--RALELLERVGIAsqkDKYPAQLSGGQQQRVA 146
Cdd:COG4604 81 RQENHINSRltvrelvAFGRFPY-----------SKGRL-TAEDREIidEAIAYLDLEDLA---DRYLDELSGGQRQRAF 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 147 IARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPD 221
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPE 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-216 |
8.26e-38 |
|
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: 131.89 E-value: 8.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVqkHFG-----DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaegKELA--A 74
Cdd:cd03249 1 IEFKNV--SFRypsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI----RDLNlrW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 75 LRSDVGMVFQSFNLFAhKTILQNVTLAptkvrkKNKADAE--KRALELLERVG-IASQKDKYP-------AQLSGGQQQR 144
Cdd:cd03249 75 LRSQIGLVSQEPVLFD-GTIAENIRYG------KPDATDEevEEAAKKANIHDfIMSLPDGYDtlvgergSQLSGGQKQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917391194 145 VAIARALAMEPKVMLFDEPTSALDPE---MVNEVLDvmvsLAKEGMTMLVVTHEMGFARKaADRVIFMADGAIVE 216
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAEsekLVQEALD----RAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVE 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
12-212 |
1.01e-37 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 131.86 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 12 GDLH--VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA-EGKELAALRS-DVGMVFQSFN 87
Cdd:PRK11629 18 GSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlSSAAKAELRNqKLGFIYQFHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 88 LFAHKTILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSAL 167
Cdd:PRK11629 98 LLPDFTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 917391194 168 DPEMVNEVLDVMVSL-AKEGMTMLVVTHEMGFARKaADRVIFMADG 212
Cdd:PRK11629 177 DARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKR-MSRQLEMRDG 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-217 |
1.72e-37 |
|
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: 131.20 E-value: 1.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGD--LHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaEGKELAALRSDV 79
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV--RDYTLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNLFaHKTILQNVTLAPTKVRKKNKADAEK--RALELLERV--GIASQKDKYPAQLSGGQQQRVAIARALAMEP 155
Cdd:cd03251 79 GLVSQDVFLF-NDTVAENIAYGRPGATREEVEEAARaaNAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 917391194 156 KVMLFDEPTSALDPEMVNEVLDVMVSLAKeGMTMLVVTHEMGFARKaADRVIFMADGAIVED 217
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVER 217
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
15-220 |
2.32e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 131.78 E-value: 2.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 15 HVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKElaALRSDVGMVFQSFN--LFAhK 92
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK--WVRSKVGLVFQDPDdqVFS-S 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 93 TILQNVTLAPTKVRKkNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMV 172
Cdd:PRK13647 96 TVWDDVAFGPVNMGL-DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 917391194 173 NEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDP 220
Cdd:PRK13647 175 ETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-225 |
3.86e-37 |
|
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: 130.30 E-value: 3.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAegKELAALRSDVGMVFQSfNLFAHKTIL 95
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAL--ADPAWLRRQVGVVLQE-NVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNVTLAPT-----KVRKKNK-ADAEKRALELLErvGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
Cdd:cd03252 94 DNIALADPgmsmeRVIEAAKlAGAHDFISELPE--GYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 170 EMVNEVLDVMVSLAKeGMTMLVVTHEMGfARKAADRVIFMADGAIVEDTDPDSFFD 225
Cdd:cd03252 172 ESEHAIMRNMHDICA-GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-227 |
5.63e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 131.08 E-value: 5.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 12 GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEgkELAALRSDVGMVFQSFN--LF 89
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKE--NIREVRKFVGLVFQNPDdqIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 90 AhKTILQNVTLAPTKVrKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
Cdd:PRK13652 93 S-PTVEQDIAFGPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 170 EMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNP 227
Cdd:PRK13652 171 QGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-221 |
1.35e-36 |
|
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: 134.93 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTL---CRTINRLEPiDSGEI----------------SVEG 62
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLmhvLRGMDQYEP-TSGRIiyhvalcekcgyverpSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 63 RPLPAEGKELA---------------ALRSDVGMVFQ-SFNLFAHKTILQNVTLAPTKVRKKNKaDAEKRALELLERVGI 126
Cdd:TIGR03269 80 EPCPVCGGTLEpeevdfwnlsdklrrRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGK-EAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 127 ASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADR 205
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEVIEDLSDK 238
|
250
....*....|....*.
gi 917391194 206 VIFMADGAIVEDTDPD 221
Cdd:TIGR03269 239 AIWLENGEIKEEGTPD 254
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-221 |
2.08e-36 |
|
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: 128.11 E-value: 2.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 15 HVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaEGKELAALRSDVGMVFQSFNLFAhKTI 94
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI--RDISRKSLRSMIGVVLQDTFLFS-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 95 LQNVTLAP--TKVRKKNKADAEKRALELLERV--GIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE 170
Cdd:cd03254 94 MENIRLGRpnATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 917391194 171 MVNEVLDVMVSLaKEGMTMLVVTHEMGFARKaADRVIFMADGAIVEDTDPD 221
Cdd:cd03254 174 TEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHD 222
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-230 |
2.66e-36 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 128.80 E-value: 2.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 5 RDVQKHF---------GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaEGKELAAL 75
Cdd:COG4167 8 RNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL--EYGDYKYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 76 RSDVGMVFQ----SFNlfAHKTILQnvTL-APTKVRKK-NKADAEKRALELLERVGI-ASQKDKYPAQLSGGQQQRVAIA 148
Cdd:COG4167 86 CKHIRMIFQdpntSLN--PRLNIGQ--ILeEPLRLNTDlTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 149 RALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNP 227
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
...
gi 917391194 228 QSE 230
Cdd:COG4167 242 QHE 244
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-209 |
5.38e-36 |
|
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: 133.18 E-value: 5.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPaeGKELAALRSDVGMVFQSFNLFAhKTIL 95
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA--DADADSWRDQIAWVPQHPFLFA-GTIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNVTLAptkvRKKNKADAEKRALE---LLERV-----GIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSAL 167
Cdd:TIGR02857 414 ENIRLA----RPDASDAEIREALEragLDEFVaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 917391194 168 DPEMVNEVLDVMVSLAkEGMTMLVVTHEMGFARkAADRVIFM 209
Cdd:TIGR02857 490 DAETEAEVLEALRALA-QGRTVLLVTHRLALAA-LADRIVVL 529
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-239 |
6.99e-36 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 127.96 E-value: 6.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGK-ELAALRSDV 79
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRsRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVML 159
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 160 FDEPTSALDPemvnEVLDVMVSLAKE-----GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSeRARD 234
Cdd:PRK11831 167 FDEPFVGQDP----ITMGVLVKLISElnsalGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP-RVRQ 241
|
....*
gi 917391194 235 FLGKI 239
Cdd:PRK11831 242 FLDGI 246
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-217 |
1.37e-35 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 125.94 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDL----HVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRplpAEGKELAALR 76
Cdd:cd03266 1 MITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF---DVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 SDVGMVFQSFNLFAHKTILQNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPK 156
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENLEYF-AGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917391194 157 VMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVED 217
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-224 |
1.52e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 127.54 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTIN-RLEP----IDSGEISVEGrplPAEGKELAALRSDVGMVFQ--SFNLF 89
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNgLLQPtegkVTVGDIVVSS---TSKQKEIKPVRKKVGVVFQfpESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 90 aHKTILQNVTLAPTKVrKKNKADAEKRALELLERVGIASQ-KDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
Cdd:PRK13643 99 -EETVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 169 PEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFF 224
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-215 |
1.66e-35 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 125.76 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQK-HFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA-EGKELAALRSD 78
Cdd:PRK10908 1 MIRFEHVSKaYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQSFNLFAHKTILQNVTLaPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVM 158
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 159 LFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIV 215
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
13-226 |
2.02e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 127.43 E-value: 2.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 13 DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA---EGKELAALRSDVGMVFQ--SFN 87
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkKIKEVKRLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 88 LFaHKTILQNVTLAPTKVrKKNKADAEKRALELLERVGIASQKDKY-PAQLSGGQQQRVAIARALAMEPKVMLFDEPTSA 166
Cdd:PRK13645 103 LF-QETIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917391194 167 LDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDN 226
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-221 |
3.48e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 125.97 E-value: 3.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELaalrsdvG 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-------G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNLFAHKTILQNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMA--DGAIVEDTDPD 221
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSpgPGRVVERLPLN 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-237 |
3.66e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 126.36 E-value: 3.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 11 FGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRL-EPID----SGEISVEGRPLpAEGKELAALRSDVGMVFQS 85
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSgyrySGDVLLGGRSI-FNYRDVLEFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 86 FNLFAhKTILQNVtLAPTKV-----RKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:PRK14271 110 PNPFP-MSIMDNV-LAGVRAhklvpRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAkEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQ-SERARDFLG 237
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKhAETARYVAG 264
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-214 |
6.72e-35 |
|
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: 122.71 E-value: 6.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGkeLAALRSDVGMVFQSFNLFAhKTIL 95
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD--PNELGDHVGYLPQDDELFS-GSIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNVtlaptkvrkknkadaekralellervgiasqkdkypaqLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEmvNE- 174
Cdd:cd03246 94 ENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE--GEr 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 917391194 175 -VLDVMVSLAKEGMTMLVVTHEMGFARkAADRVIFMADGAI 214
Cdd:cd03246 134 aLNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-215 |
8.43e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 129.37 E-value: 8.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 9 KHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL----PAEgkelaALRSdvGMVF- 83
Cdd:COG1129 260 EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrirsPRD-----AIRA--GIAYv 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 84 ----QSFNLFAHKTILQNVTLAPTKVRKK----NKADAEKRALELLERVGIASQKDKYPAQ-LSGGQQQRVAIARALAME 154
Cdd:COG1129 333 pedrKGEGLVLDLSIRENITLASLDRLSRggllDRRRERALAEEYIKRLRIKTPSPEQPVGnLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917391194 155 PKVMLFDEPTSALDpemV---NEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIV 215
Cdd:COG1129 413 PKVLILDEPTRGID---VgakAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-224 |
1.43e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 124.84 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEgkELAALRSDVGMVFQS-FNLFAHKTIL 95
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEE--NVWDIRHKIGMVFQNpDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNVTLAptkvrKKNKA----DAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEM 171
Cdd:PRK13650 101 DDVAFG-----LENKGipheEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 917391194 172 VNEVLDVMVSLAKE-GMTMLVVTHEMGfARKAADRVIFMADGAIVEDTDPDSFF 224
Cdd:PRK13650 176 RLELIKTIKGIRDDyQMTVISITHDLD-EVALSDRVLVMKNGQVESTSTPRELF 228
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-216 |
2.24e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 129.17 E-value: 2.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVqkHFG----DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA--EgkelAAL 75
Cdd:PRK11160 339 LTLNNV--SFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADysE----AAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 76 RSDVGMVFQSFNLFAHkTILQNVTLAptkvrkKNKADAEKrALELLERVGIASQKDKYPA----------QLSGGQQQRV 145
Cdd:PRK11160 413 RQAISVVSQRVHLFSA-TLRDNLLLA------APNASDEA-LIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917391194 146 AIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKeGMTMLVVTHEMgFARKAADRVIFMADGAIVE 216
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRL-TGLEQFDRICVMDNGQIIE 553
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
14-228 |
2.61e-34 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 125.20 E-value: 2.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 14 LHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEG-KELAALRSDVGMVFQ----SFNl 88
Cdd:PRK15079 34 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRAVRSDIQMIFQdplaSLN- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 89 fAHKTIlQNVTLAPTKVR--KKNKADAEKRALELLERVGI-ASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTS 165
Cdd:PRK15079 113 -PRMTI-GEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917391194 166 ALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQ 228
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-227 |
3.51e-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: 122.65 E-value: 3.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGR---PLPAEGkelaalRSD 78
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditKLPMHK------RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVF--QSFNLFAHKTILQNVtLAPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPK 156
Cdd:cd03218 75 LGIGYlpQEASIFRKLTVEENI-LAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917391194 157 VMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNP 227
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-215 |
4.86e-34 |
|
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: 121.99 E-value: 4.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 3 VLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTI-NRLE--PIDSGEISVEGRPLPAegkelAALRSDV 79
Cdd:cd03234 9 VGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEggGTTSGQILFNGQPRKP-----DQFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNLFAHKTILQNVTLAPT---KVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPK 156
Cdd:cd03234 84 AYVRQDDILLPGLTVRETLTYTAIlrlPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 917391194 157 VMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMG---FarKAADRVIFMADGAIV 215
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIV 223
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
16-216 |
4.98e-34 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 128.92 E-value: 4.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaEGKELAALRSDVGMVFQSFNLFAhKTIL 95
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL--AGLDVQAVRRQLGVVLQNGRLMS-GSIF 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNVTL-APTKVrkknkadaeKRALELLERVGIASQKDKYP-----------AQLSGGQQQRVAIARALAMEPKVMLFDEP 163
Cdd:TIGR03797 545 ENIAGgAPLTL---------DEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRILLFDEA 615
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 917391194 164 TSALDPEMvNEVldVMVSLAKEGMTMLVVTHEMGFARKaADRVIFMADGAIVE 216
Cdd:TIGR03797 616 TSALDNRT-QAI--VSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQ 664
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-228 |
1.17e-33 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 121.96 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 5 RDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTIN-RLEPiDSGEISVEGRPlpAEGKELAAL-------- 75
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSaRLAP-DAGEVHYRMRD--GQLRDLYALseaerrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 76 -RSDVGMVFQSF--NLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQK-DKYPAQLSGGQQQRVAIARAL 151
Cdd:PRK11701 87 lRTEWGFVHQHPrdGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAARiDDLPTTFSGGMQQRLQIARNL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 152 AMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQ 228
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQ 244
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-222 |
1.95e-33 |
|
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: 126.07 E-value: 1.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHF-----GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEgrpLPAEGKELAAL 75
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR---VGDEWVDMTKP 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 76 RSD--------VGMVFQSFNLFAHKTILQNVTLA-----PTKVrkknkadAEKRALELLERVGIASQK-----DKYPAQL 137
Cdd:TIGR03269 356 GPDgrgrakryIGILHQEYDLYPHRTVLDNLTEAiglelPDEL-------ARMKAVITLKMVGFDEEKaeeilDKYPDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 138 SGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVE 216
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
....*.
gi 917391194 217 DTDPDS 222
Cdd:TIGR03269 509 IGDPEE 514
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-228 |
2.32e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.83 E-value: 2.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRL---EPIDSGEISVEGRPLPAegKELAALRSDVGMVFQS-FNLFAH 91
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTA--KTVWDIREKVGIVFQNpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 92 KTILQNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEM 171
Cdd:PRK13640 100 ATVGDDVAFG-LENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 172 VNEVLDVMVSLAKE-GMTMLVVTHEMGFArKAADRVIFMADGAIVEDTDPDSFFDNPQ 228
Cdd:PRK13640 179 KEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-238 |
2.75e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 120.52 E-value: 2.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGrplpaegKELAAL----R 76
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG-------EDITHLpmhkR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 SDVGMVF--QSFNLFAHKTILQNVtLAPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAME 154
Cdd:COG1137 76 ARLGIGYlpQEASIFRKLTVEDNI-LAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 155 PKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEmgfARKA---ADRVIFMADGAIVEDTDPDSFFDNPQser 231
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHN---VRETlgiCDRAYIISEGKVLAEGTPEEILNNPL--- 228
|
....*...
gi 917391194 232 ARDF-LGK 238
Cdd:COG1137 229 VRKVyLGE 236
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-217 |
2.97e-33 |
|
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: 118.57 E-value: 2.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFG--DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINR-LEPiDSGEISVEGRPLPAEGKelaALRSD 78
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKP-QQGEITLDGVPVSDLEK---ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQSFNLFAhKTILQNVTlaptkvrkknkadaekralellervgiasqkdkypAQLSGGQQQRVAIARALAMEPKVM 158
Cdd:cd03247 77 ISVLNQRPYLFD-TTLRNNLG-----------------------------------RRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 159 LFDEPTSALDPEMVNEVLDVMVSLAKEgMTMLVVTHEMGfARKAADRVIFMADGAIVED 217
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLT-GIEHMDKILFLENGKIIMQ 177
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-224 |
3.07e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 121.43 E-value: 3.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAE--GKELAALRSDVGMVFQ--SFNLFaHK 92
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkDKYIRPVRKRIGMVFQfpESQLF-ED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 93 TILQNVTLAPtKVRKKNKADAEKRALELLERVGIASQ-KDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEM 171
Cdd:PRK13646 102 TVEREIIFGP-KNFKMNLDEVKNYAHRLLMDLGFSRDvMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 917391194 172 VNEVLDVMVSLA-KEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFF 224
Cdd:PRK13646 181 KRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-194 |
4.01e-33 |
|
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: 125.55 E-value: 4.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHF-GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGrpLPAEGKELAALRSDVG 80
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG--VPVSSLDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNLFAhKTILQNVTLAptkvrKKNKADAEkrALELLERVGIASQKDKYP-----------AQLSGGQQQRVAIAR 149
Cdd:TIGR02868 413 VCAQDAHLFD-TTVRENLRLA-----RPDATDEE--LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 917391194 150 ALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSlAKEGMTMLVVTH 194
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-225 |
5.37e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 122.25 E-value: 5.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKelaALRSDVGM 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR---LARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVTLAPTKVRKKNKaDAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLLVFGRYFGMSTR-EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917391194 162 EPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFD 225
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-227 |
7.19e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 120.48 E-value: 7.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGD-LHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPlPAEGKELAALRSDV 79
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-TGDFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNL-FAHKTILQ-------NVTLAPTKVRKK-NKADAEkralellerVGIASQKDKYPAQLSGGQQQRVAIARA 150
Cdd:PRK13644 80 GIVFQNPETqFVGRTVEEdlafgpeNLCLPPIEIRKRvDRALAE---------IGLEKYRHRSPKTLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 151 LAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGfARKAADRVIFMADGAIVEDTDPDSFFDNP 227
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-215 |
7.47e-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: 118.04 E-value: 7.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTIN--RLEPIDSGEISVEGRPLPAEgkelaALRSDVGMVFQSFNLFAHKT 93
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDKR-----SFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 94 ILQNVTLAptkvrkknkadAEKRalellervgiasqkdkypaQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVN 173
Cdd:cd03213 99 VRETLMFA-----------AKLR-------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 917391194 174 EVLDVMVSLAKEGMTMLVVTH----EMgFarKAADRVIFMADGAIV 215
Cdd:cd03213 149 QVMSLLRRLADTGRTIICSIHqpssEI-F--ELFDKLLLLSQGRVI 191
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-236 |
8.51e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 119.76 E-value: 8.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 6 DVQKhfgdlhVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDsGEISVEGR------PLPAEGKELAALRSDV 79
Cdd:PRK14258 18 DTQK------ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRveffnqNIYERRVNLNRLRRQV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNLFAhKTILQNVTLAPT------KVRKKNKADAEKRALELLERvgIASQKDKYPAQLSGGQQQRVAIARALAM 153
Cdd:PRK14258 91 SMVHPKPNLFP-MSVYDNVAYGVKivgwrpKLEIDDIVESALKDADLWDE--IKHKIHKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 154 EPKVMLFDEPTSALDPEMVNEVLDVMVSLA-KEGMTMLVVTHEMGFARKAADRVIFMAD-----GAIVEDTDPDSFFDNP 227
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSP 247
|
....*....
gi 917391194 228 QSERARDFL 236
Cdd:PRK14258 248 HDSRTREYV 256
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
13-216 |
9.34e-33 |
|
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: 124.83 E-value: 9.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 13 DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaEGKELAALRSDVGMVFQSFNLFaHK 92
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL--ADYTLASLRRQVALVSQDVVLF-ND 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 93 TILQNVTLAPTKVRKKNKADAEKRALELLERV-----GIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSAL 167
Cdd:TIGR02203 421 TIANNIAYGRTEQADRAEIERALAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSAL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 917391194 168 DPEMVNEVLDVMVSLaKEGMTMLVVTHEMGFARKaADRVIFMADGAIVE 216
Cdd:TIGR02203 501 DNESERLVQAALERL-MQGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVE 547
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
1.06e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 119.42 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFG-----DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRP---LPAEGkel 72
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 73 aalRS-DVGMVFQ------SFNLfahkTILQNVTLAPTKVRKK------NKADAE--KRALELLE---------RVGias 128
Cdd:COG1101 78 ---RAkYIGRVFQdpmmgtAPSM----TIEENLALAYRRGKRRglrrglTKKRRElfRELLATLGlglenrldtKVG--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 129 qkdkypaQLSGGQQQrvaiARALAM----EPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAA 203
Cdd:COG1101 148 -------LLSGGQRQ----ALSLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEEnNLTTLMVTHNMEQALDYG 216
|
250
....*....|....
gi 917391194 204 DRVIFMADGAIVED 217
Cdd:COG1101 217 NRLIMMHEGRIILD 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-214 |
1.33e-32 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 122.26 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPlpAEGKELAALRSDVG 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDD--VEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQ----SFNLFAHKTILQNVTlaPTKVRKKNKADAEKRALE-LLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEP 155
Cdd:PRK09536 81 SVPQdtslSFEFDVRQVVEMGRT--PHRSRFDTWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 156 KVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAI 214
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-214 |
1.96e-32 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 117.89 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAegKELaalrSDVGM 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR--KDL----HKIGS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVtlaptKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:TIGR03740 75 LIESPPLYENLTARENL-----KVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 917391194 162 EPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAI 214
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-216 |
2.02e-32 |
|
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: 123.78 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVqkHFG---DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAegKELAALRSD 78
Cdd:COG5265 358 VRFENV--SFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRD--VTQASLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQSFNLFaHKTILQNVTLAptkvrkknKADAEKRALELLERVG-----IASQKDKYPAQ-------LSGGQQQRVA 146
Cdd:COG5265 434 IGIVPQDTVLF-NDTIAYNIAYG--------RPDASEEEVEAAARAAqihdfIESLPDGYDTRvgerglkLSGGEKQRVA 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917391194 147 IARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKeGMTMLVVTHemgfaRKA----ADRVIFMADGAIVE 216
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAH-----RLStivdADEILVLEAGRIVE 572
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
16-216 |
3.67e-32 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 123.70 E-value: 3.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAegKELAALRSDVGMVFQSFNLFAhKTIL 95
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAI--ADPAWLRRQMGVVLQENVLFS-RSIR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNVTLAP-----TKVRKKNK-ADAEKRALELleRVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
Cdd:TIGR01846 549 DNIALCNpgapfEHVIHAAKlAGAHDFISEL--PQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDY 626
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 917391194 170 EMVNEVLDVMVSLAKeGMTMLVVTHEMGfARKAADRVIFMADGAIVE 216
Cdd:TIGR01846 627 ESEALIMRNMREICR-GRTVIIIAHRLS-TVRACDRIIVLEKGQIAE 671
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-215 |
5.09e-32 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 119.59 E-value: 5.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLrDVQKHFGDLHVlkDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL--PAEGKELAALRSD 78
Cdd:PRK11144 1 MLEL-NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdAEKGICLPPEKRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQSFNLFAHKTILQNVTLAptkVRKKNKADAEKrALELLervGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVM 158
Cdd:PRK11144 78 IGYVFQDARLFPHYKVRGNLRYG---MAKSMVAQFDK-IVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 159 LFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIV 215
Cdd:PRK11144 151 LMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-217 |
5.09e-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: 116.53 E-value: 5.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGD--LHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL----PAEgkelaaL 75
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrqldPAD------L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 76 RSDVGMVFQSFNLFAhKTILQNVTLAPTKVrkknkadAEKRALELLERVGIASQKDKYP-----------AQLSGGQQQR 144
Cdd:cd03245 77 RRNIGYVPQDVTLFY-GTLRDNITLGAPLA-------DDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917391194 145 VAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAkEGMTMLVVTHEMGFArKAADRVIFMADGAIVED 217
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLL-DLVDRIIVMDSGRIVAD 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-214 |
5.16e-32 |
|
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: 115.22 E-value: 5.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAeGKELAALRSDVGMV---FQSFNLFAHK 92
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR-RSPRDAIRAGIAYVpedRKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 93 TILQNVTLaptkvrkknkadaekralellervgiasqkdkyPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMV 172
Cdd:cd03215 94 SVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 917391194 173 NEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAI 214
Cdd:cd03215 141 AEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
10-228 |
7.51e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 118.69 E-value: 7.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 10 HFGD----LHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLepID-SGEISVEGrpLPAEGKELAALR-------- 76
Cdd:PRK11022 12 HFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL--IDyPGRVMAEK--LEFNGQDLQRISekerrnlv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 -SDVGMVFQS--FNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGI---ASQKDKYPAQLSGGQQQRVAIARA 150
Cdd:PRK11022 88 gAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 151 LAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLA-KEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQ 228
Cdd:PRK11022 168 IACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPR 246
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-236 |
8.56e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 121.74 E-value: 8.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPID-----SGEISVEGRP-LPAEGKELAALRSD-VGMVFQ---- 84
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESlLHASEQTLRGVRGNkIAMIFQepmv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 85 SFN-LFAHKTILQNVtLAPTKVRKKNKADAEkrALELLERVGI---ASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:PRK15134 104 SLNpLHTLEKQLYEV-LSLHRGMRREAARGE--ILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFL 236
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLL 257
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
9-228 |
1.94e-31 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 116.08 E-value: 1.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 9 KHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLP-------AEGKELAALRSDVGM 81
Cdd:TIGR02323 11 KSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAelelyqlSEAERRRLMRTEWGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSF--NLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGI-ASQKDKYPAQLSGGQQQRVAIARALAMEPKVM 158
Cdd:TIGR02323 91 VHQNPrdGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917391194 159 LFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQ 228
Cdd:TIGR02323 171 FMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQ 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-239 |
2.60e-31 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 121.12 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 13 DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPA-EGKELAALRSDVGMVFQS--FNLF 89
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlSPGKLQALRRDIQFIFQDpyASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 90 AHKTILQNVtLAPTKVRKKNKAD-AEKRALELLERVGIASQKD-KYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSAL 167
Cdd:PRK10261 416 PRQTVGDSI-MEPLRVHGLLPGKaAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917391194 168 DPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFLGKI 239
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-208 |
4.84e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 113.10 E-value: 4.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 11 FGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAegkeLAALRSDVGmvfQSFNLfa 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVA----YVPQRSEVP---DSLPL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 91 hkTILQNVTL---APTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSAL 167
Cdd:NF040873 73 --TVRDLVAMgrwARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 917391194 168 DPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIF 208
Cdd:NF040873 151 DAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-221 |
5.09e-31 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 120.36 E-value: 5.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHF--GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEG---RPL-PAEgkelaaL 75
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGvdiRQIdPAD------L 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 76 RSDVGMVFQSFNLFaHKTILQNVTLAptkvrkknKADAEKRA-LELLERVGIASQKDKYP-----------AQLSGGQQQ 143
Cdd:TIGR03375 538 RRNIGYVPQDPRLF-YGTLRDNIALG--------APYADDEEiLRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQ 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 144 RVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAkEGMTMLVVTHEMGFArKAADRVIFMADGAIVEDTDPD 221
Cdd:TIGR03375 609 AVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLL-DLVDRIIVMDNGRIVADGPKD 684
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-221 |
6.07e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 114.73 E-value: 6.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEG-KELAAlrsdv 79
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSsRQLAR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 gmvfqsfnlfaHKTILQNVTLAP--TKVRK--------------KNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQ 143
Cdd:PRK11231 77 -----------RLALLPQHHLTPegITVRElvaygrspwlslwgRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 144 RVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPD 221
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-215 |
1.75e-30 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 117.96 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAAlRSDVG 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAA-QLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNLFAHKTILQNVTLA--PTK----VRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAME 154
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGrhLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917391194 155 PKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIV 215
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-216 |
2.30e-30 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 118.20 E-value: 2.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaEGKELAALRSDVGMVFQSFNLFaHKTILQ 96
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL--RDYTLASLRNQVALVSQNVHLF-NDTIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 97 NVTLAPTKvrKKNKADAEK-----RALELLERV--GIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
Cdd:PRK11176 436 NIAYARTE--QYSREQIEEaarmaYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 917391194 170 E---MVNEVLDVMvslaKEGMTMLVVTHEMGFARKaADRVIFMADGAIVE 216
Cdd:PRK11176 514 EserAIQAALDEL----QKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVE 558
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-215 |
4.07e-30 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 116.69 E-value: 4.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL----PAEGKELAalr 76
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltPAKAHQLG--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 sdVGMVFQSFNLFAHKTILQNVTLaptkvRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPK 156
Cdd:PRK15439 88 --IYLVPQEPLLFPNLSVKENILF-----GLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 157 VMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIV 215
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-236 |
5.72e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 116.73 E-value: 5.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 15 HVLKDIDLEVPAGQVVVVLGPSGSGKST----LCRTINrlepiDSGEISVEGRPLPAEG-KELAALRSDVGMVFQSFN-- 87
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNrRQLLPVRHRIQVVFQDPNss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 88 LFAHKTILQNVTLApTKVRKK--NKADAEKRALELLERVGI-ASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
Cdd:PRK15134 375 LNPRLNVLQIIEEG-LRVHQPtlSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917391194 165 SALDPEMVNEVLDVMVSL-AKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFL 236
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-214 |
8.00e-30 |
|
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: 111.02 E-value: 8.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 13 DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELaaLRSDVGMVFQSFNLFAhK 92
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY--LHSKVSLVGQEPVLFA-R 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 93 TILQNVTLAPTKVRKKNKADAEKRA-----LELLERvGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSAL 167
Cdd:cd03248 103 SLQDNIAYGLQSCSFECVKEAAQKAhahsfISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 917391194 168 DPEMvNEVLDVMVSLAKEGMTMLVVTHEMGFARKaADRVIFMADGAI 214
Cdd:cd03248 182 DAES-EQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-229 |
9.47e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.77 E-value: 9.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKElaALRSDVGMVFQS-FNLFAHKTIL 95
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE--KLRKHIGIVFQNpDNQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNVT------LAPTKvrkknkaDAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
Cdd:PRK13648 103 YDVAfglenhAVPYD-------EMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917391194 170 EMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKaADRVIFMADGAIVEDTDPDSFFDNPQS 229
Cdd:PRK13648 176 DARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-216 |
2.58e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.06 E-value: 2.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGrpLPAEGKELAALRSDVGMVFQSFNLFAhKTILQ 96
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG--TDIRTVTRASLRRNIAVVFQDAGLFN-RSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 97 NVtlaptKVRKKNKADAEKR-------ALELLERvgiasQKDKYPA-------QLSGGQQQRVAIARALAMEPKVMLFDE 162
Cdd:PRK13657 428 NI-----RVGRPDATDEEMRaaaeraqAHDFIER-----KPDGYDTvvgergrQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 163 PTSALDPEM---VNEVLD-VMvslakEGMTMLVVTHEMGFARKaADRVIFMADGAIVE 216
Cdd:PRK13657 498 ATSALDVETeakVKAALDeLM-----KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVE 549
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-216 |
3.00e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.39 E-value: 3.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVegrplpaeGK---------E 71
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL--------GEtvkigyfdqH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 72 LAALRSDvgmvfqsfnlfahKTILQNVtlaptkvRKKNKADAEKRALELLERVGIASQK-DKYPAQLSGGQQQRVAIARA 150
Cdd:COG0488 387 QEELDPD-------------KTVLDEL-------RDGAPGGTEQEVRGYLGRFLFSGDDaFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 151 LAMEPKVMLFDEPTSALDPEMVNEVLDvmvSLAK-EGmTMLVVTHEMGFARKAADRVIFMADGAIVE 216
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEE---ALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-225 |
5.80e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 110.67 E-value: 5.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELaalRSDVGM 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA---RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVtLAPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:PRK13537 85 VPQFDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917391194 162 EPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFD 225
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-212 |
2.06e-28 |
|
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: 106.78 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTI-NRLEPIdSGEISVEGRplpaegkelaalrsdVGMVFQ-SFNLFAhkT 93
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALlGELEKL-SGSVSVPGS---------------IAYVSQePWIQNG--T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 94 ILQNVTLA----PTKVRKKNKADAEKRALELL---------ERvGIAsqkdkypaqLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:cd03250 82 IRENILFGkpfdEERYEKVIKACALEPDLEILpdgdlteigEK-GIN---------LSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 917391194 161 DEPTSALDPEMVNEVLD-VMVSLAKEGMTMLVVTHEMGFARKaADRVIFMADG 212
Cdd:cd03250 152 DDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-218 |
2.19e-28 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 107.66 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpAEGKELAALRSDVG 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-TDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERvgIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIV-EDT 218
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVlEDT 220
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-236 |
3.12e-28 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 107.48 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 18 KDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEP----IDSGEISVEGRPLPAegkelAALRS-DVGMVFQ----SFN- 87
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPVAP-----CALRGrKIATIMQnprsAFNp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 88 ---LFAHktilqnvtlAPTKVRKKNKADAEKRALELLERVGIASQK---DKYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:PRK10418 95 lhtMHTH---------ARETCLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 162 EPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFL 236
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-215 |
4.20e-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: 111.38 E-value: 4.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKElaALRSDVGMVFQSFNLFAhKTIL 95
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDRE--ELGRHIGYLPQDVELFD-GTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNVTLAPtkvrkknKADAEKrALELLERVG----IASQKDKY-------PAQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
Cdd:COG4618 424 ENIARFG-------DADPEK-VVAAAKLAGvhemILRLPDGYdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 917391194 165 SALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARkAADRVIFMADGAIV 215
Cdd:COG4618 496 SNLDDEGEAALAAAIRALKARGATVVVITHRPSLLA-AVDKLLVLRDGRVQ 545
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-227 |
7.69e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 111.35 E-value: 7.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 13 DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAegKELAALRSDVGMVFQSFNLFAhK 92
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQ--YDHHYLHRQVALVGQEPVLFS-G 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 93 TILQNVTLAPTKVRKKNKADAEKRA------LELLErvGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSA 166
Cdd:TIGR00958 570 SVRENIAYGLTDTPDEEIMAAAKAAnahdfiMEFPN--GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917391194 167 LDPEMVNEVLDvmvSLAKEGMTMLVVTHEMGFARKaADRVIFMADGAIVEDTDPDSFFDNP 227
Cdd:TIGR00958 648 LDAECEQLLQE---SRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-224 |
1.06e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 106.72 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 13 DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEgkELAALRSDVGMVFQS-FNLFAH 91
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAE--NVWNLRRKIGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 92 KTILQNVTLApTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEM 171
Cdd:PRK13642 97 ATVEDDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 917391194 172 VNEVLDVMVSLA-KEGMTMLVVTHEMGFArKAADRVIFMADGAIVEDTDPDSFF 224
Cdd:PRK13642 176 RQEIMRVIHEIKeKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELF 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-237 |
1.38e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 105.84 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRP---LPaeGKELAalRS 77
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiegLP--GHQIA--RM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 78 DVGMVFQSFNLFAHKTILQNVTLA--------------PTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQ 143
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVAqhqqlktglfsgllKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 144 RVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDS 222
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
250
....*....|....*
gi 917391194 223 FFDNPQSERArdFLG 237
Cdd:PRK11300 241 IRNNPDVIKA--YLG 253
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-238 |
1.20e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 103.05 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGR-----PLPAEGkelaalR 76
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHARA------R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 SDVGMVFQSFNLFAHKTILQNVtLAPTKVRKK-NKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEP 155
Cdd:PRK10895 78 RGIGYLPQEASIFRRLSVYDNL-MAVLQIRDDlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 156 KVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERArdF 235
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRV--Y 234
|
...
gi 917391194 236 LGK 238
Cdd:PRK10895 235 LGE 237
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
13-221 |
1.28e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 102.84 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 13 DLHV-------LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTI--NRLEPIDSGEISVEGR---PLPAEgkELAalRSDVG 80
Cdd:COG0396 5 NLHVsvegkeiLKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEdilELSPD--ERA--RAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQS---------FNLFahKTILQNVTLAPTKVRkknkaDAEKRALELLERVGIAsqkDKYpAQ------LSGGQQQRV 145
Cdd:COG0396 81 LAFQYpveipgvsvSNFL--RTALNARRGEELSAR-----EFLKLLKEKMKELGLD---EDF-LDryvnegFSGGEKKRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 146 AIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHemgFAR----KAADRVIFMADGAIVEDTDPD 221
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH---YQRildyIKPDFVHVLVDGRIVKSGGKE 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-214 |
1.63e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.69 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRplpaegkelaaLRsdVGMVF 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LR--IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 84 QSFNLFAHKTILQNVTLAPTKVRKKNKA-------------------------------DAEKRALELLERVGI-ASQKD 131
Cdd:COG0488 68 QEPPLDDDLTVLDTVLDGDAELRALEAEleeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFpEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 132 KYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVN--EVLdvmvsLAKEGMTMLVVTHEMGFARKAADRVIFM 209
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEwlEEF-----LKNYPGTVLVVSHDRYFLDRVATRILEL 222
|
....*
gi 917391194 210 ADGAI 214
Cdd:COG0488 223 DRGKL 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-221 |
2.97e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 102.08 E-value: 2.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRplpaegkeLAALrSDVGM 81
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR--------VSAL-LELGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSfNLfahkTILQNVTLAPTkVRKKNKADAEKRALELLERVGIASQKDK----YpaqlSGGQQQRVAIARALAMEPKV 157
Cdd:COG1134 98 GFHP-EL----TGRENIYLNGR-LLGLSRKEIDEKFDEIVEFAELGDFIDQpvktY----SSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917391194 158 MLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPD 221
Cdd:COG1134 168 LLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
14-216 |
3.84e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 102.56 E-value: 3.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 14 LHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAALRsdVGMVFQ--SFNLFAH 91
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQR--IRMIFQdpSTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 92 KTILQNVTLaPTKVRKKNKADA-EKRALELLERVGI-ASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
Cdd:PRK15112 104 QRISQILDF-PLRLNTDLEPEQrEKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 917391194 170 EMVNEVLDVMVSL-AKEGMTMLVVTHEMGFARKAADRVIFMADGAIVE 216
Cdd:PRK15112 183 SMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-207 |
6.40e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 100.94 E-value: 6.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKElaALRSDVGMVF 83
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE--IYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 84 QSFNLFAhKTILQNVTLaPTKVRkkNKADAEKRALELLERVGIASQK-DKYPAQLSGGQQQRVAIARALAMEPKVMLFDE 162
Cdd:PRK10247 88 QTPTLFG-DTVYDNLIF-PWQIR--NQQPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 917391194 163 PTSALDP---EMVNEVLDVMVSlaKEGMTMLVVTHEMGfARKAADRVI 207
Cdd:PRK10247 164 ITSALDEsnkHNVNEIIHRYVR--EQNIAVLWVTHDKD-EINHADKVI 208
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-220 |
1.13e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 101.22 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 11 FGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAALRsdVGMVFQSFNLFA 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR--IGLLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 91 HKTILQNVTLA-----PTKVR-KKNKADAEKRALElleRVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
Cdd:PRK10253 95 DITVQELVARGryphqPLFTRwRKEDEEAVTKAMQ---ATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 165 SALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDP 220
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-214 |
2.70e-25 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 103.58 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKElaALRSDVGMVFQSFNLFAhKTIL 95
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRE--TFGKHIGYLPQDVELFP-GTVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNVTlaptkvRKKNKADAEK--------RALELlervgIASQKDKYP-------AQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:TIGR01842 410 ENIA------RFGENADPEKiieaaklaGVHEL-----ILRLPDGYDtvigpggATLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGfARKAADRVIFMADGAI 214
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-217 |
3.65e-25 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 103.28 E-value: 3.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFG-DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKElaALRSDVG 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRH--TLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNLFAhKTILQNVTLAptkVRKKNKADAEKRALELLErvgIASQKDKYP-----------AQLSGGQQQRVAIAR 149
Cdd:TIGR01193 552 YLPQEPYIFS-GSILENLLLG---AKENVSQDEIWAACEIAE---IKDDIENMPlgyqtelseegSSISGGQKQRIALAR 624
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 150 ALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEgmTMLVVTHEMGFARKaADRVIFMADGAIVED 217
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQ 689
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-216 |
6.88e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 102.62 E-value: 6.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 20 IDLEVPAGQVVVVLGPSGSGKSTLcrtINRLepidSGEISVEGRpLPAEGKELAAL-----RSDVGMVFQSFNLFaHKTI 94
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSL---LNAL----LGFLPYQGS-LKINGIELRELdpeswRKHLSWVGQNPQLP-HGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 95 LQNVTLAptkvrkknKADA-EKRALELLERVGIASQKDKYP-----------AQLSGGQQQRVAIARALAMEPKVMLFDE 162
Cdd:PRK11174 440 RDNVLLG--------NPDAsDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 163 PTSALDpeMVNEVLdVMVSL--AKEGMTMLVVTHEMGFArKAADRVIFMADGAIVE 216
Cdd:PRK11174 512 PTASLD--AHSEQL-VMQALnaASRRQTTLMVTHQLEDL-AQWDQIWVMQDGQIVQ 563
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-219 |
1.02e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 101.53 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpAEGKELAALRSDVGMVF 83
Cdd:PRK11288 7 FDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-RFASTTAALAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 84 QSFNLFAHKTILQNVTLA--PTKVRKKNKADAEKRALELLERVGI---ASQKDKYpaqLSGGQQQRVAIARALAMEPKVM 158
Cdd:PRK11288 86 QELHLVPEMTVAENLYLGqlPHKGGIVNRRLLNYEAREQLEHLGVdidPDTPLKY---LSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917391194 159 LFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTD 219
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFD 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-239 |
2.54e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 101.09 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAALR------------SDVGMVFQ 84
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSeqsaaqmrhvrgADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 85 ----SFN-LFA-HKTILQNVTLAPTKVRKKNKADAeKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVM 158
Cdd:PRK10261 112 epmtSLNpVFTvGEQIAESIRLHQGASREEAMVEA-KRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 159 LFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDNPQSERARDFLG 237
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLA 270
|
..
gi 917391194 238 KI 239
Cdd:PRK10261 271 AV 272
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-194 |
4.04e-24 |
|
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: 95.25 E-value: 4.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 12 GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAalrsdvgmvfQSFNLFAH 91
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIA----------RGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 92 KTILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEM 171
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|...
gi 917391194 172 VNEVLDVMVSLAKEGMTMLVVTH 194
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-212 |
8.55e-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: 92.90 E-value: 8.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEIsvegrplpaegkelaalrsdvgm 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 vfqsfnlfahkTILQNVTLAptkvrkknkadaekralellervgiasqkdkYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:cd03221 58 -----------TWGSTVKIG-------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 917391194 162 EPTSALDPEMVNEVLDVMvsLAKEGmTMLVVTHEMGFARKAADRVIFMADG 212
Cdd:cd03221 96 EPTNHLDLESIEALEEAL--KEYPG-TVILVSHDRYFLDQVATKIIELEDG 143
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-194 |
2.32e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.96 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVL-KDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISvegrpLPAEGKelaalrsdv 79
Cdd:COG4178 362 ALALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA-----RPAGAR--------- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 gMVF--QsfnlfahKTILQNVTL--------APTKVrkknkADAEkrALELLERVGIA------SQKDKYPAQLSGGQQQ 143
Cdd:COG4178 428 -VLFlpQ-------RPYLPLGTLreallypaTAEAF-----SDAE--LREALEAVGLGhlaerlDEEADWDQVLSLGEQQ 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 917391194 144 RVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDvMVSLAKEGMTMLVVTH 194
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQ-LLREELPGTTVISVGH 542
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-227 |
2.56e-23 |
|
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: 93.71 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGkeLAALRSDVGMVFQSFNLFAhKTIL 95
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG--LHDLRSRISIIPQDPVLFS-GTIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNvtLAPTKVrkknKADAEkrALELLERVG----IASQKDKYPA-------QLSGGQQQRVAIARALAMEPKVMLFDEPT 164
Cdd:cd03244 96 SN--LDPFGE----YSDEE--LWQALERVGlkefVESLPGGLDTvveeggeNLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 165 SALDPE---MVNEVLDVMVSlakeGMTMLVVTHemgfaR----KAADRVIFMADGAIVEdtdpdsfFDNP 227
Cdd:cd03244 168 ASVDPEtdaLIQKTIREAFK----DCTVLTIAH-----RldtiIDSDRILVLDKGRVVE-------FDSP 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
4-194 |
2.63e-23 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 93.87 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHFG------DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEP--IDSGEISVEGRPLPAEgkelaal 75
Cdd:COG2401 27 VAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGRE------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 76 rsdvgmvfqsfnlfahKTILQNVTlaptkvRKKNKADaekrALELLERVGIAsqkDKY-----PAQLSGGQQQRVAIARA 150
Cdd:COG2401 100 ----------------ASLIDAIG------RKGDFKD----AVELLNAVGLS---DAVlwlrrFKELSTGQKFRFRLALL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 917391194 151 LAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTH 194
Cdd:COG2401 151 LAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATH 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-219 |
3.20e-23 |
|
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: 97.59 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDS--GEISVEGRPLPAEGKELAAlRSD 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTE-RAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQSFNLFAHKTILQNVTLA---PTKVRKKNKADAEKRALELLERVGIASQKDKYP-AQLSGGQQQRVAIARALAME 154
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGneiTLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917391194 155 PKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTD 219
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKD 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-221 |
3.24e-23 |
|
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: 92.98 E-value: 3.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLE--PIDSGEISVEGR---PLPAEgkELAalR 76
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEditDLPPE--ERA--R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 SDVGMVFQSfnlfahktilqnvtlaPTKVRK-KNKadaekralELLERVGiasqkdkypAQLSGGQQQRVAIARALAMEP 155
Cdd:cd03217 77 LGIFLAFQY----------------PPEIPGvKNA--------DFLRYVN---------EGFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 156 KVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTH-EMGFARKAADRVIFMADGAIVEDTDPD 221
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-224 |
3.34e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.69 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAALRSDVG 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFN--LFaHKTILQNVTLAptkVRKKNKADAE-----KRALELLERVGIASQkdkyPAQ-LSGGQQQRVAIARALA 152
Cdd:PRK13638 81 TVFQDPEqqIF-YTDIDSDIAFS---LRNLGVPEAEitrrvDEALTLVDAQHFRHQ----PIQcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 917391194 153 MEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFF 224
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-217 |
1.04e-22 |
|
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: 92.40 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRpLPAEGKElaALRSDVGMVF------------ 83
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRK--KFLRRIGVVFgqktqlwwdlpv 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 84 -QSFNLFAHktilqnvtlaptkVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDE 162
Cdd:cd03267 113 iDSFYLLAA-------------IYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 163 PTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVED 217
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-240 |
1.47e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.88 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 15 HVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTI-NRLEP--IDSGEISVEGRPLpaEGKELAALRSDVgmvfQSFNLF-A 90
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPKgvKGSGSVLLNGMPI--DAKEMRAISAYV----QQDDLFiP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 91 HKTILQNVTLAPTKVRKKNKADAEKRAL--ELLERVGIASQKDK---YPAQ---LSGGQQQRVAIARALAMEPKVMLFDE 162
Cdd:TIGR00955 113 TLTVREHLMFQAHLRMPRRVTKKEKRERvdEVLQALGLRKCANTrigVPGRvkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 163 PTSALDPEMVNEVLDVMVSLAKEGMTMLVVTH-------EMgFarkaaDRVIFMADGAIVEDTDPD---SFFDN-----P 227
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpsselfEL-F-----DKIILMAEGRVAYLGSPDqavPFFSDlghpcP 266
|
250
....*....|...
gi 917391194 228 QSERARDFLGKIL 240
Cdd:TIGR00955 267 ENYNPADFYVQVL 279
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-232 |
1.51e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 93.02 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHV-LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL-PAEGKELAALRSDV 79
Cdd:PRK15056 7 IVVNDVTVTWRNGHTaLRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTrQALQKNLVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNLFAHKTILQNVTLAPTKVRKKNKADAEkRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVML 159
Cdd:PRK15056 87 EEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQ-IVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917391194 160 FDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIfMADGAIVEDTDPDSFFDNPQSERA 232
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTFTAENLELA 237
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-197 |
2.30e-22 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 90.50 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 12 GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAalrsdvgmvfQSFNLFAH 91
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPH----------ENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 92 KTILQNVTLAPTKVRKKNK--ADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAihGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*....
gi 917391194 170 EMVNEVLDVMVS-LAKEGMTMLVVTHEMG 197
Cdd:TIGR01189 161 AGVALLAGLLRAhLARGGIVLLTTHQDLG 189
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-221 |
3.04e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.71 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 14 LHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEG-KELAAL--------RSDVGMVfQ 84
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSpRERRRLgvayipedRLGRGLV-P 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 85 SFNLfAHKTILQNVTLAPtkVRKK---NKADAEKRALELLERVGIASQKDKYPA-QLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:COG3845 350 DMSV-AENLILGRYRRPP--FSRGgflDRKAIRAFAEELIEEFDVRTPGPDTPArSLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPD 221
Cdd:COG3845 427 AQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAA 487
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-212 |
3.31e-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: 95.08 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 28 QVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEgkeLAALRSDVGMVFQSFNLFAHKTILQNVTL-APTKVR 106
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN---LDAVRQSLGMCPQHNILFHHLTVAEHILFyAQLKGR 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 107 KKNKADAEKRALelLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLaKEG 186
Cdd:TIGR01257 1034 SWEEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSG 1110
|
170 180
....*....|....*....|....*.
gi 917391194 187 MTMLVVTHEMGFARKAADRVIFMADG 212
Cdd:TIGR01257 1111 RTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-217 |
3.70e-22 |
|
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: 90.67 E-value: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 12 GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPlpaegkelaALRSDVGMVFQSfNLfah 91
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV---------SSLLGLGGGFNP-EL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 92 kTILQNVTLAPTKVRKKNKADAEKRAlELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEM 171
Cdd:cd03220 100 -TGRENIYLNGRLLGLSRKEIDEKID-EIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 917391194 172 VNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVED 217
Cdd:cd03220 178 QEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-212 |
5.39e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.84 E-value: 5.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDS--GEISVEGRPLPAEG-KELAalRSDVG 80
Cdd:PRK13549 8 MKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNiRDTE--RAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNLFAHKTILQNVTLA--PTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVM 158
Cdd:PRK13549 86 IIHQELALVKELSVLENIFLGneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 917391194 159 LFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADG 212
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-194 |
8.44e-22 |
|
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: 88.36 E-value: 8.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEIsveGRPLpaegkelaalRSDVGMVFQsfnlfahKTIL 95
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPE----------GEDLLFLPQ-------RPYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNVTLAptkvrkknkadaekralELLervgiasqkdKYP--AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVN 173
Cdd:cd03223 76 PLGTLR-----------------EQL----------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|.
gi 917391194 174 EVLDVmvsLAKEGMTMLVVTH 194
Cdd:cd03223 129 RLYQL---LKELGITVISVGH 146
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
16-216 |
1.22e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 93.24 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaEGKELAALRSDVGMVFQSFNLFAhKTIL 95
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL--SSLSHSVLRQGVAMVQQDPVVLA-DTFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNVTLAptkvrkknKADAEKRALELLERVGIASQKDKYPA-----------QLSGGQQQRVAIARALAMEPKVMLFDEPT 164
Cdd:PRK10790 433 ANVTLG--------RDISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 917391194 165 SALDP---EMVNEVLdvmvSLAKEGMTMLVVTHEMGFARKaADRVIFMADGAIVE 216
Cdd:PRK10790 505 ANIDSgteQAIQQAL----AAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVE 554
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-219 |
1.65e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 92.55 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDS--GEISVEGRPLpaegkELAALRS--DV 79
Cdd:NF040905 4 MRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVC-----RFKDIRDseAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVF--QSFNLFAHKTILQNVTLAPTKVRKK--NKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEP 155
Cdd:NF040905 79 GIVIihQELALIPYLSIAENIFLGNERAKRGviDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917391194 156 KVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTD 219
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLD 222
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-227 |
4.99e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 89.58 E-value: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 20 IDLEVPAGQVVVV---------------LGPSGSGKS----TLCRTIN----------RLEPIDSGEISVEGRplpaegK 70
Cdd:COG4170 11 IEIDTPQGRVKAVdrvsltlnegeirglVGESGSGKSliakAICGITKdnwhvtadrfRWNGIDLLKLSPRER------R 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 71 ELaaLRSDVGMVFQ--SFNLFAHKTILQNVTLA-PTKVRK----KNKADAEKRALELLERVGIASQKD---KYPAQLSGG 140
Cdd:COG4170 85 KI--IGREIAMIFQepSSCLDPSAKIGDQLIEAiPSWTFKgkwwQRFKWRKKRAIELLHRVGIKDHKDimnSYPHELTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 141 QQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAK-EGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTD 219
Cdd:COG4170 163 ECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGP 242
|
....*...
gi 917391194 220 PDSFFDNP 227
Cdd:COG4170 243 TEQILKSP 250
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-223 |
6.72e-21 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 89.79 E-value: 6.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSG----------------------------KSTLCRTINRLEPI 53
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**rgalpahv*gpdagrrpwrf*twcanRRALRRTIG*HRPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 54 DSGEisvegrplpaegKELAALRSDVGMVFQSFNLfahktilqnvtlaptkvrkkNKADAEKRALELLERVGIASQKDKY 133
Cdd:NF000106 94 R*GR------------RESFSGRENLYMIGR*LDL--------------------SRKDARARADELLERFSLTEAAGRA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 134 PAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGA 213
Cdd:NF000106 142 AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGR 221
|
250
....*....|
gi 917391194 214 IVEDTDPDSF 223
Cdd:NF000106 222 VIADGKVDEL 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-222 |
2.01e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.29 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKElAALRSDVGMVF 83
Cdd:PRK10762 7 LKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK-SSQEAGIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 84 QSFNLFAHKTILQNVTLAPTKVRKKNKADAEK---RALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:PRK10762 86 QELNLIPQLTIAENIFLGREFVNRFGRIDWKKmyaEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAI-----VEDTDPDS 222
Cdd:PRK10762 166 DEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFiaereVADLTEDS 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-220 |
2.21e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 87.19 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTI--NRLEPIDS------GEISVEGRPLPA-EGKELAALRSDVGMVFQSF 86
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGGGAPrgarvtGDVTLNGEPLAAiDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 87 NLFAHKTIlqnVTLA--PTKVRKKNKADAEKR-ALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAM---------E 154
Cdd:PRK13547 96 FAFSAREI---VLLGryPHARRAGALTHRDGEiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 155 PKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDP 220
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-227 |
2.84e-20 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 87.55 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 12 GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTIN--------------RLEPIDSGEISvegrplPAEGKELaaLRS 77
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICgvtkdnwrvtadrmRFDDIDLLRLS------PRERRKL--VGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 78 DVGMVFQ--------SFNLfaHKTILQNVTLAPTKVRKKNKADAEK-RALELLERVGIASQKD---KYPAQLSGGQQQRV 145
Cdd:PRK15093 90 NVSMIFQepqscldpSERV--GRQLMQNIPGWTYKGRWWQRFGWRKrRAIELLHRVGIKDHKDamrSFPYELTEGECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 146 AIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAK-EGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFF 224
Cdd:PRK15093 168 MIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELV 247
|
...
gi 917391194 225 DNP 227
Cdd:PRK15093 248 TTP 250
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-227 |
3.70e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 87.47 E-value: 3.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 12 GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRL---EPIDSGEISVEGRP---LPAegKELAALRSD-VGMVFQ 84
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREilnLPE--KELNKLRAEqISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 85 ----SFN------------LFAHKTIlqnvtlaptkvrkkNKADAEKRALELLERVGIASQKDK---YPAQLSGGQQQRV 145
Cdd:PRK09473 105 dpmtSLNpymrvgeqlmevLMLHKGM--------------SKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 146 AIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFF 224
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVF 250
|
...
gi 917391194 225 DNP 227
Cdd:PRK09473 251 YQP 253
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-216 |
4.33e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.30 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 18 KDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEgKELAALRSDVGMVFQS---FNLFAHKTI 94
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPR-SPLDAVKKGMAYITESrrdNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 95 LQNVTLAPT--------------KVRKKNKADAEKRALELLervgiASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:PRK09700 359 AQNMAISRSlkdggykgamglfhEVDEQRTAENQRELLALK-----CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVE 216
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
12-194 |
4.46e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 4.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 12 GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPlpaegkelaalrSDVGMVFQSFNLFAH 91
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD------------IDDPDVAEACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 92 K-------TILQNVTLAptkvrKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
Cdd:PRK13539 81 RnamkpalTVAENLEFW-----AAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 917391194 165 SALDPEMVNEVLDVMVSLAKEGMTMLVVTH 194
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-216 |
1.07e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 87.46 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAegKELAALRSDVGMVFQSFNLFAhKTIL 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK--LQLDSWRSRLAVVSQTPFLFS-DTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNVTLAptkvrkknKADAEKRALELLERvgIASQKDK-------YPAQ-------LSGGQQQRVAIARALAMEPKVMLFD 161
Cdd:PRK10789 407 NNIALG--------RPDATQQEIEHVAR--LASVHDDilrlpqgYDTEvgergvmLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 917391194 162 EPTSALDPEMVNEVLDVMvSLAKEGMTMLVVTHEMGfARKAADRVIFMADGAIVE 216
Cdd:PRK10789 477 DALSAVDGRTEHQILHNL-RQWGEGRTVIISAHRLS-ALTEASEILVMQHGHIAQ 529
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-231 |
2.94e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 84.75 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHF----------GDL-----------HVLKDIDLEVPAGQVVVVLGPSGSGKSTlcrTINRLEPI---DSG 56
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkGALkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKST---TIKMLTGIlvpTSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 57 EISVEGR-PLpaegKELAALRSDVGMVF-------------QSFNLFAHktilqnvtlaptkVRKKNKADAEKRALELLE 122
Cdd:COG4586 78 EVRVLGYvPF----KRRKEFARRIGVVFgqrsqlwwdlpaiDSFRLLKA-------------IYRIPDAEYKKRLDELVE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 123 RVGIASQKDKyPA-QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFAR 200
Cdd:COG4586 141 LLDLGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIE 219
|
250 260 270
....*....|....*....|....*....|.
gi 917391194 201 KAADRVIFMADGAIVEDTDPDSFFDNPQSER 231
Cdd:COG4586 220 ALCDRVIVIDHGRIIYDGSLEELKERFGPYK 250
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-214 |
3.16e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.87 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 18 KDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGkelAALRSDVGMVF-----QSFNLFAHK 92
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS---TAQRLARGLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 93 TILQNV-TLAPTKVRKKNKADAEKRALELLER-VGIA-SQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
Cdd:PRK15439 357 PLAWNVcALTHNRRGFWIKPARENAVLERYRRaLNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 917391194 170 EMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAI 214
Cdd:PRK15439 437 SARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-217 |
4.32e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 85.95 E-value: 4.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 12 GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLcrtinrlepidsgeISVEGRPLPAEGKELAALRSDVGMVFQS---FNL 88
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSL--------------ISAMLGELPPRSDASVVIRGTVAYVPQVswiFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 89 FAHKTILQNVTLAPTKVRKKNKADAEKRALELLERvGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
Cdd:PLN03130 694 TVRDNILFGSPFDPERYERAIDVTALQHDLDLLPG-GDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 917391194 169 PEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKaADRVIFMADGAIVED 217
Cdd:PLN03130 773 AHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQ-VDRIILVHEGMIKEE 820
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
13-215 |
9.89e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.20 E-value: 9.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 13 DLHV---LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPiDSGEISVEGRPLPA-EGKELAALRSDV--------G 80
Cdd:COG4138 5 DVAVagrLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDwSAAELARHRAYLsqqqsppfA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 M-VFQSFNLFAHktilqnvtlaptkvRKKNKADAEKRALELLERVGIAsqkDKYP---AQLSGGQQQRVAIARALAM--- 153
Cdd:COG4138 84 MpVFQYLALHQP--------------AGASSEAVEQLLAQLAEALGLE---DKLSrplTQLSGGEWQRVRLAAVLLQvwp 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 154 ----EPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIV 215
Cdd:COG4138 147 tinpEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-220 |
2.36e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 83.24 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLP-AEGKElaALRSDVGMV 82
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKE--ALENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 83 FQSFNLFAHKTILQNVTLA--PTKVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVeDTDP 220
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI-ATQP 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-217 |
2.86e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 83.49 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTInrlepidSGEISvegrplPAEGKELAaLRSDVGMVFQS---FNLFAHKT 93
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAM-------LGELS------HAETSSVV-IRGSVAYVPQVswiFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 94 ILQNVTLAPTKVRKKNKADAEKRALELL---ERVGIASQKdkypAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE 170
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVTALQHDLDLLpgrDLTEIGERG----VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 917391194 171 MVNEVLDVMVSLAKEGMTMLVVTHEMGFArKAADRVIFMADGAIVED 217
Cdd:PLN03232 775 VAHQVFDSCMKDELKGKTRVLVTNQLHFL-PLMDRIILVSEGMIKEE 820
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-207 |
3.05e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.93 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEIsvegrplpaegKELAALRsdVG 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNLfahktilqNVTLAPTKVRKKNKADAEKRA--LELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVM 158
Cdd:PRK09544 71 YVPQKLYL--------DTTLPLTVNRFLRLRPGTKKEdiLPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 917391194 159 LFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVI 207
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-209 |
4.85e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.86 E-value: 4.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAegKELAAlRSDVGM 81
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA--GDIAT-RRRVGY 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSFNLFAHKTILQNVTL-A-----PtkvrkknKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEP 155
Cdd:NF033858 344 MSQAFSLYGELTVRQNLELhArlfhlP-------AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKP 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 917391194 156 KVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKaADRVIFM 209
Cdd:NF033858 417 ELLILDEPTSGVDPVARDMFWRLLIELSREdGVTIFISTHFMNEAER-CDRISLM 470
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-222 |
1.35e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.45 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 4 LRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpaEGKELAALRSDVGMVF 83
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL--ESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 84 QSFNLFAHKTILQNVTLA--P--TKVRKKNKADAEKrALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVML 159
Cdd:PRK10575 92 QQLPAAEGMTVRELVAIGryPwhGALGRFGAADREK-VEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917391194 160 FDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDS 222
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
13-199 |
1.44e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.92 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 13 DLHVL-KDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGKELAAlrsdvgmvfqsfNLF-- 89
Cdd:PRK13538 12 DERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQ------------DLLyl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 90 AHK-------TILQNVTLAptkVRKKNKADAEkRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDE 162
Cdd:PRK13538 80 GHQpgiktelTALENLRFY---QRLHGPGDDE-ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 917391194 163 PTSALDPEMVNEVLDVMVS-LAKEGMTMLVVTHEMGFA 199
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQhAEQGGMVILTTHQDLPVA 193
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-213 |
1.71e-17 |
|
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: 78.14 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 13 DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLC-RTINRLEPIdSGEISVEGRPLPAEGKELAALRSDVGMVFQSFN-LFA 90
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL-EGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKpWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 91 HKTILQNVTLAPTKVRKKNKADAEKRALEL---LERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSAL 167
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDACSLQPdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 917391194 168 DPEMVNEVLD--VMVSLAKEGMTMLVVTHEMGFARKaADRVIFMADGA 213
Cdd:cd03290 172 DIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDGS 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-216 |
3.27e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 80.02 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGD--LHVlKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGkeLAALRSDV 79
Cdd:PRK10522 323 LELRNVTFAYQDngFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ--PEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNLFAHktilqnvTLAPtkvrkKNKADAEKRALELLERVGIASQ---KDKYPA--QLSGGQQQRVAIARALAME 154
Cdd:PRK10522 400 SAVFTDFHLFDQ-------LLGP-----EGKPANPALVEKWLERLKMAHKlelEDGRISnlKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917391194 155 PKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKaADRVIFMADGAIVE 216
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRREFYQVLLPLLQEmGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-221 |
3.52e-17 |
|
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: 79.84 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 20 IDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEgkELAALRSDVGMVFQSFNLFAHktiLQNVt 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD--NREAYRQLFSAVFSDFHLFDR---LLGL- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 100 laptkvrkkNKADAEKRALELLERVGIAsqkDKYPAQ--------LSGGQQQRVAIARALAMEPKVMLFDEPTSALDP-- 169
Cdd:COG4615 425 ---------DGEADPARARELLERLELD---HKVSVEdgrfsttdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPef 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 170 ------EMVNEvldvmvsLAKEGMTMLVVTH-EMGFArkAADRVIFMADGAIVEDTDPD 221
Cdd:COG4615 493 rrvfytELLPE-------LKARGKTVIAISHdDRYFD--LADRVLKMDYGKLVELTGPA 542
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-215 |
4.73e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.57 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 20 IDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAeGKELAALRSdvGMVF-----QSFNLFAHKTI 94
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI-RSPRDAIRA--GIMLcpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 95 LQNVTLAPTkvRKKNKADA---EKRALELLERVgIASQKDKYPA------QLSGGQQQRVAIARALAMEPKVMLFDEPTS 165
Cdd:PRK11288 349 ADNINISAR--RHHLRAGClinNRWEAENADRF-IRSLNIKTPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 917391194 166 ALDPEMVNEVLDVMVSLAKEGMTMLVVTHE----MGFarkaADRVIFMADGAIV 215
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQGVAVLFVSSDlpevLGV----ADRIVVMREGRIA 475
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-216 |
4.96e-17 |
|
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: 79.99 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 12 GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTInrLEPIDSgeisVEGRplpaegkelAALRSDVGMVFQSF---NL 88
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDK----VEGH---------VHMKGSVAYVPQQAwiqND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 89 FAHKTILQNVTLAPTKVRKKNKADAEKRALELLERvGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
Cdd:TIGR00957 714 SLRENILFGKALNEKYYQQVLEACALLPDLEILPS-GDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 917391194 169 PEMVNEVLDVMVslAKEGM----TMLVVTHEMGFARKaADRVIFMADGAIVE 216
Cdd:TIGR00957 793 AHVGKHIFEHVI--GPEGVlknkTRILVTHGISYLPQ-VDVIIVMSGGKISE 841
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-220 |
5.23e-17 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 76.68 E-value: 5.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGkeLAALRSDVGMVFQSFNLFAhKTIL 95
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP--LEDLRSSLTIIPQDPTLFS-GTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNvtLAPtkvrkKNKADAEkralELLERVGIASQKDkypaQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEV 175
Cdd:cd03369 100 SN--LDP-----FDEYSDE----EIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 917391194 176 LDVMVSLAKeGMTMLVVTHEMgfaRKAA--DRVIFMADGAIVEDTDP 220
Cdd:cd03369 165 QKTIREEFT-NSTILTIAHRL---RTIIdyDKILVMDAGEVKEYDHP 207
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-196 |
1.50e-16 |
|
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: 78.29 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 22 LEVP-AGQVVVVLGPSGSGKSTlcrTINrlepIDSGEI-----SVEGRPLPAE------GKELaalrsdvgmvFQSFNLF 89
Cdd:COG1245 93 LPVPkKGKVTGILGPNGIGKST---ALK----ILSGELkpnlgDYDEEPSWDEvlkrfrGTEL----------QDYFKKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 90 AHKTI-----LQNVTLAPtKVRKKN------KADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVM 158
Cdd:COG1245 156 ANGEIkvahkPQYVDLIP-KVFKGTvrelleKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 917391194 159 LFDEPTSALDpemVNE---VLDVMVSLAKEGMTMLVVTHEM 196
Cdd:COG1245 235 FFDEPSSYLD---IYQrlnVARLIRELAEEGKYVLVVEHDL 272
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
15-213 |
1.79e-16 |
|
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: 74.28 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 15 HVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTInrlepidsgeISVEGRPLPAEGKELAalrsdvgmvfqsfnlFAHKTI 94
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG----------LYASGKARLISFLPKF---------------SRNKLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 95 LQNvtlaptkvrkknkadaekrALELLERVGIASQKDKYPAQ-LSGGQQQRVAIARALAMEPK--VMLFDEPTSALDPEM 171
Cdd:cd03238 64 FID-------------------QLQFLIDVGLGYLTLGQKLStLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 917391194 172 VNEVLDVMVSLAKEGMTMLVVTHEMGFArKAADRVIFMADGA 213
Cdd:cd03238 125 INQLLEVIKGLIDLGNTVILIEHNLDVL-SSADWIIDFGPGS 165
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-196 |
9.99e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.00 E-value: 9.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 27 GQVVVVLGPSGSGKSTLCRtinrlepIDSGEI-----SVEGRPLPAE------GKELaalrsdvgmvfqsFNLF------ 89
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVK-------ILSGELipnlgDYEEEPSWDEvlkrfrGTEL-------------QNYFkklyng 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 90 ----AHKTilQNVTLAPTKVRKK-----NKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:PRK13409 159 eikvVHKP--QYVDLIPKVFKGKvrellKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*....
gi 917391194 161 DEPTSALDpemVNE---VLDVMVSLAkEGMTMLVVTHEM 196
Cdd:PRK13409 237 DEPTSYLD---IRQrlnVARLIRELA-EGKYVLVVEHDL 271
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-194 |
1.15e-15 |
|
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: 75.56 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVegrplPAEGK----------ELAALRSDVGMVFQS 85
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK-----PAKGKlfyvpqrpymTLGTLRDQIIYPDSS 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 86 FNLFAH-------KTILQNVTLAptkvrkknkadaekralELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVM 158
Cdd:TIGR00954 542 EDMKRRglsdkdlEQILDNVQLT-----------------HILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190
....*....|....*....|....*....|....*..
gi 917391194 159 LFDEPTSALDPEMVnevlDVMVSLAKE-GMTMLVVTH 194
Cdd:TIGR00954 605 ILDECTSAVSVDVE----GYMYRLCREfGITLFSVSH 637
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-214 |
1.20e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 75.44 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPID-SGEISVEGRPlPAEGKELAALRSDVG 80
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLFGRR-RGSGETIWDIKKHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFNL-FAHKTILQNVTLA------------PTKVRKKnkadaekrALELLERVGIASQKDKYPAQ-LSGGQQQRVA 146
Cdd:PRK10938 340 YVSSSLHLdYRVSTSVRNVILSgffdsigiyqavSDRQQKL--------AQQWLDILGIDKRTADAPFHsLSWGQQRLAL 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 147 IARALAMEPKVMLFDEPTSALDP---EMVNEVLDVMVSlakEGMT-MLVVTHEmgfARKAAD----RVIFMADGAI 214
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVLIS---EGETqLLFVSHH---AEDAPAcithRLEFVPDGDI 481
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-222 |
1.34e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.43 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 23 EVPAGQVVVVLGPSGSGKSTLCRTINRLEPiDSGEISVEGRPLPA-EGKELAALRS--------DVGM-VFQSFNLFAHK 92
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAwSAAELARHRAylsqqqtpPFAMpVFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 93 tilqnvtlaptkvrKKNKADAEKRALELLERVGIAsqkDKYP---AQLSGGQQQRVAIA-------RALAMEPKVMLFDE 162
Cdd:PRK03695 97 --------------KTRTEAVASALNEVAEALGLD---DKLGrsvNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917391194 163 PTSALDPEMVNeVLDVMVS-LAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDS 222
Cdd:PRK03695 160 PMNSLDVAQQA-ALDRLLSeLCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-229 |
1.67e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.59 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHF--GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGkeLAALRSDV 79
Cdd:PTZ00243 1309 LVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG--LRELRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 GMVFQSFNLFaHKTILQNV----TLAPTKVRkknkadaekRALELL---ERV-----GIASQKDKYPAQLSGGQQQRVAI 147
Cdd:PTZ00243 1387 SMIPQDPVLF-DGTVRQNVdpflEASSAEVW---------AALELVglrERVaseseGIDSRVLEGGSNYSVGQRQLMCM 1456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 148 ARALAME-PKVMLFDEPTSALDPEMVNEVLDVMVSlAKEGMTMLVVTHEMGFARKaADRVIFMADGAIVEDTDPDSFFDN 226
Cdd:PTZ00243 1457 ARALLKKgSGFILMDEATANIDPALDRQIQATVMS-AFSAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMGSPRELVMN 1534
|
...
gi 917391194 227 PQS 229
Cdd:PTZ00243 1535 RQS 1537
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-214 |
2.92e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPL----PAEGkeLAAlrsdvGMVFQSFN----- 87
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtrsPQDG--LAN-----GIVYISEDrkrdg 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 88 LFAHKTILQNVTL-APTKVRKKN---KADAEKRALE---LLERVGIASQkDKYPAQLSGGQQQRVAIARALAMEPKVMLF 160
Cdd:PRK10762 341 LVLGMSVKENMSLtALRYFSRAGgslKHADEQQAVSdfiRLFNIKTPSM-EQAIGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 917391194 161 DEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAI 214
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-215 |
3.15e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.53 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 6 DVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTInrlepidSGEI---SVEGRPLPAEGKELAALRSDVGMV 82
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIqgnNFTGTILANNRKPTKQILKRTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 83 FQSFNLFAHKTILQNVTLA-----PTKVRKKNKAD-AEKRALEL-LERVGIASQKDKYPAQLSGGQQQRVAIARALAMEP 155
Cdd:PLN03211 146 TQDDILYPHLTVRETLVFCsllrlPKSLTKQEKILvAESVISELgLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 156 KVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEmgfarkAADRVIFMADGAIV 215
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ------PSSRVYQMFDSVLV 279
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-170 |
1.05e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 72.66 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVegrplpaeGKELaalrsDVGM 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI--------GETV-----KLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSF-NLFAHKTILQNVTlAPTKVRKKNKADAEKRAleLLERVGI-ASQKDKYPAQLSGGQQQRVAIARALAMEPKVML 159
Cdd:TIGR03719 390 VDQSRdALDPNKTVWEEIS-GGLDIIKLGKREIPSRA--YVGRFNFkGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
170
....*....|.
gi 917391194 160 FDEPTSALDPE 170
Cdd:TIGR03719 467 LDEPTNDLDVE 477
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
15-213 |
1.33e-14 |
|
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: 70.36 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 15 HVLKDIDLEVPAGQVVVVLGPSGSGKSTLC-RTI-----------------NRLEPIDSGEI-SVEGRPlPA---EGKEL 72
Cdd:cd03270 9 HNLKNVDVDIPRNKLVVITGVSGSGKSSLAfDTIyaegqrryveslsayarQFLGQMDKPDVdSIEGLS-PAiaiDQKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 73 A-ALRSDVGMVFQSFN----LFAHKTIlqnvtlaptkvrkknkadaeKRALELLERVGIASQK-DKYPAQLSGGQQQRVA 146
Cdd:cd03270 88 SrNPRSTVGTVTEIYDylrlLFARVGI--------------------RERLGFLVDVGLGYLTlSRSAPTLSGGEAQRIR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 147 IARALAMEPKVML--FDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARkAADRVIFMADGA 213
Cdd:cd03270 148 LATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIR-AADHVIDIGPGA 215
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-217 |
1.94e-14 |
|
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: 72.16 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 19 DIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPID-SGEISVEGRPLPAEgKELAALRSDVGMVFQSFNLFAHKTIL-- 95
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIR-NPAQAIRAGIAMVPEDRKRHGIVPILgv 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 -QNVTLAP-TKVRKKNKADAEKRALELLERVGIASQKDKYP----AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
Cdd:TIGR02633 357 gKNITLSVlKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 917391194 170 EMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVED 217
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
15-207 |
2.90e-14 |
|
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: 69.95 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 15 HVLKDIDLEVPAGQVVVVLGPSGSGKSTLcrtINR-LEP-IDSGEISVEGRPLPAEGKELAALRSDVGMVFQS------- 85
Cdd:cd03271 9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSL---INDtLYPaLARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSpigrtpr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 86 ---------F----NLFA---HKTILQNVTLAptkVRKKNKADAE-------------------KRALELLERVGIASQK 130
Cdd:cd03271 86 snpatytgvFdeirELFCevcKGKRYNRETLE---VRYKGKSIADvldmtveealeffenipkiARKLQTLCDVGLGYIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 131 DKYPA-QLSGGQQQRVAIARALAME---PKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFArKAADRV 206
Cdd:cd03271 163 LGQPAtTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVI-KCADWI 241
|
.
gi 917391194 207 I 207
Cdd:cd03271 242 I 242
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
17-207 |
4.97e-14 |
|
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: 69.36 E-value: 4.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAG-----QVVVVLGPSGSGKSTLCRTI-NRLEPiDSGEISVEGRPLPAEGKELAAlrsDVGMVFQSFnlfa 90
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLaGVLKP-DEGDIEIELDTVSYKPQYIKA---DYEGTVRDL---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 91 hktiLQNVTlaptkvrkKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE 170
Cdd:cd03237 82 ----LSSIT--------KDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 917391194 171 ---MVNEVLDVMVSLAKEgmTMLVVTHEMGFARKAADRVI 207
Cdd:cd03237 150 qrlMASKVIRRFAENNEK--TAFVVEHDIIMIDYLADRLI 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-214 |
6.26e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 19 DIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEP-IDSGEISVEGRPL----PAEgkelaALRSDVGMVFQS---FNLFA 90
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVkirnPQQ-----AIAQGIAMVPEDrkrDGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 91 HKTILQNVTLAP----TKVRKKNKADAEKRALELLERVGI-ASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTS 165
Cdd:PRK13549 355 VMGVGKNITLAAldrfTGGSRIDDAAELKTILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 917391194 166 ALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAI 214
Cdd:PRK13549 435 GIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-196 |
1.34e-13 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 68.16 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 22 LEVPA-GQVVVVLGPSGSGKSTLCRTI---------NRLEPIDSGEISVEGRplpaeGKEL----AALRSDVGMVfqsfn 87
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILagklkpnlgKFDDPPDWDEILDEFR-----GSELqnyfTKLLEGDVKV----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 88 lfAHKTilQNVTLAPTKVRKK-----NKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDE 162
Cdd:cd03236 90 --IVKP--QYVDLIPKAVKGKvgellKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190
....*....|....*....|....*....|....
gi 917391194 163 PTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEM 196
Cdd:cd03236 166 PSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-215 |
1.64e-13 |
|
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: 66.90 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTI-NRLEPIDS--GEISVEGRPlpaeGKELAA-LRSDVGMVFQSFNLFAHK 92
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVSveGDIHYNGIP----YKEFAEkYPGEIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 93 TILQnvTLaptkvrkknkadaeKRALELlervgiasQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMV 172
Cdd:cd03233 99 TVRE--TL--------------DFALRC--------KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 917391194 173 NEVLDVMVSLAKE-GMTMLVVTHEMG------FarkaaDRVIFMADGAIV 215
Cdd:cd03233 155 LEILKCIRTMADVlKTTTFVSLYQASdeiydlF-----DKVLVLYEGRQI 199
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-241 |
1.93e-13 |
|
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: 67.96 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTI-NRLEPiDSGEISVEGRplpaegkelaalrsdvgMVFQS-FNLFAHKT 93
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLIlGELEP-SEGKIKHSGR-----------------ISFSSqFSWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 94 ILQNVTLAPTKVRKKNKADAekRALELLERVGIASQKDKYP-----AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
Cdd:cd03291 114 IKENIIFGVSYDEYRYKSVV--KACQLEEDITKFPEKDNTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 169 PEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKaADRVIFMADGAivedtdpdSF----FDNPQSERArDFLGKILG 241
Cdd:cd03291 192 VFTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGS--------SYfygtFSELQSLRP-DFSSKLMG 258
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
17-207 |
3.14e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQ-----VVVVLGPSGSGKSTLCRTIN-RLEPiDSGEISVEGR----PlpaegkelAALRSDVGMVFQSF 86
Cdd:PRK13409 350 LGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAgVLKP-DEGEVDPELKisykP--------QYIKPDYDGTVEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 87 nLFAHKTILQNVTLAPtkvrkknkadaekralELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSA 166
Cdd:PRK13409 421 -LRSITDDLGSSYYKS----------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 917391194 167 LDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVI 207
Cdd:PRK13409 484 LDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLM 525
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-207 |
3.37e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.44 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 11 FGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEgrplpaegKEL--AALRSD-----VGMVF 83
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE--------QDLivARLQQDpprnvEGTVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 84 ---------QSFNLFAHKTILQNVTLAPT--------KVRKK----NKADAEKRALELLERVGIASqkDKYPAQLSGGQQ 142
Cdd:PRK11147 85 dfvaegieeQAEYLKRYHDISHLVETDPSeknlnelaKLQEQldhhNLWQLENRINEVLAQLGLDP--DAALSSLSGGWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917391194 143 QRVAIARALAMEPKVMLFDEPTSALDPEMVnEVLDVMVsLAKEGmTMLVVTHEMGFARKAADRVI 207
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETI-EWLEGFL-KTFQG-SIIFISHDRSFIRNMATRIV 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-169 |
4.34e-13 |
|
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: 68.40 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDsGEISVEGrpLPAEGKELAALRSDVGMVFQSFNLFAhKTIL 95
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDG--VSWNSVTLQTWRKAFGVIPQKVFIFS-GTFR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNvtLAPtkvrKKNKADAEkrALELLERVGIASQKDKYPAQ-----------LSGGQQQRVAIARALAMEPKVMLFDEPT 164
Cdd:TIGR01271 1310 KN--LDP----YEQWSDEE--IWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
....*
gi 917391194 165 SALDP 169
Cdd:TIGR01271 1382 AHLDP 1386
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
13-194 |
6.35e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.64 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 13 DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLP-AEGKELAALRSDVGmvfqsfNLFAH 91
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATrGDRSRFMAYLGHLP------GLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 92 KTILQNVT-LAPTKVRKKNKADAEKRALellerVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE 170
Cdd:PRK13543 97 LSTLENLHfLCGLHGRRAKQMPGSALAI-----VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
170 180
....*....|....*....|....
gi 917391194 171 MVNEVLDVMVSLAKEGMTMLVVTH 194
Cdd:PRK13543 172 GITLVNRMISAHLRGGGAALVTTH 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-241 |
6.81e-13 |
|
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: 67.63 E-value: 6.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTI-NRLEPIDsGEISVEGRplpaegkelaalrsdvgMVFQS-FNLFAHKT 93
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMImGELEPSE-GKIKHSGR-----------------ISFSPqTSWIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 94 ILQNVTLAPTkvRKKNKADAEKRALELLERVGIASQKDKYP-----AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
Cdd:TIGR01271 503 IKDNIIFGLS--YDEYRYTSVIKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 169 PEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKaADRVIFMADGAivedtdpdSFFDNPQSE---RARDFLGKILG 241
Cdd:TIGR01271 581 VVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEGV--------CYFYGTFSElqaKRPDFSSLLLG 647
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1-207 |
7.54e-13 |
|
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: 67.35 E-value: 7.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHfgdlhVLKDIDLEVPAGQVVVVLGPSGSGKSTLC---------RTINRLEPIDSGEISVEG--------- 62
Cdd:TIGR00630 613 FLTLKGAREN-----NLKNITVSIPLGLFTCITGVSGSGKSTLIndtlypalaNRLNGAKTVPGRYTSIEGlehldkvih 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 63 ------------------------RPLPAEGKELAALRSDVGMVfqSFNL--------FAHKTI------LQNV------ 98
Cdd:TIGR00630 688 idqspigrtprsnpatytgvfdeiRELFAETPEAKVRGYTPGRF--SFNVkggrceacQGDGVIkiemhfLPDVyvpcev 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 99 ---------TLAptkVRKKNKADAE-------------------KRALELLERVGIASQKDKYPA-QLSGGQQQRVAIAR 149
Cdd:TIGR00630 766 ckgkrynreTLE---VKYKGKNIADvldmtveeayeffeavpsiSRKLQTLCDVGLGYIRLGQPAtTLSGGEAQRIKLAK 842
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917391194 150 AL---AMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFArKAADRVI 207
Cdd:TIGR00630 843 ELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVI-KTADYII 902
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-207 |
2.19e-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: 65.96 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 6 DVQKHFGDLHvlkdidLEVPAGQ-----VVVVLGPSGSGKSTLCRTI-NRLEPiDSGEISVEGR----P--LPAEGKEL- 72
Cdd:COG1245 346 DLTKSYGGFS------LEVEGGEiregeVLGIVGPNGIGKTTFAKILaGVLKP-DEGEVDEDLKisykPqyISPDYDGTv 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 73 -AALRSDVGMVFQSfnlfahkTILQNvtlaptkvrkknkadaekralELLERVGIASQKDKYPAQLSGGQQQRVAIARAL 151
Cdd:COG1245 419 eEFLRSANTDDFGS-------SYYKT---------------------EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACL 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 152 AMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKE-GMTMLVVTHEMGFARKAADRVI 207
Cdd:COG1245 471 SRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-220 |
2.49e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.12 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGkeLAALRSDVGMVFQSFNLFAhKTIL 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG--LHDLRFKITIIPQDPVLFS-GSLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNvtLAPTKvrkkNKADAEK-RALELLERVG-IASQKDKYPAQ-------LSGGQQQRVAIARALAMEPKVMLFDEPTSA 166
Cdd:TIGR00957 1378 MN--LDPFS----QYSDEEVwWALELAHLKTfVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 917391194 167 LDPEMVNeVLDVMVSLAKEGMTMLVVTHEMGFARKAAdRVIFMADGAIVEDTDP 220
Cdd:TIGR00957 1452 VDLETDN-LIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAP 1503
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-227 |
2.70e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEgrplpaegkelaalRSDVGMVFQSFNLFAhkTIL 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE--------------RSIAYVPQQAWIMNA--TVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNVtLAPTKVRKKNKADAeKRALELLERV-----GIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE 170
Cdd:PTZ00243 739 GNI-LFFDEEDAARLADA-VRVSQLEADLaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 171 MVNEVLDVMVSLAKEGMTMLVVTHEMGFARKaADRVIFMADGAIVEDTDPDSFFDNP 227
Cdd:PTZ00243 817 VGERVVEECFLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-170 |
3.31e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.53 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVegrplpaeGKELaalrsDVGM 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI--------GETV-----KLAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 VFQSF-NLFAHKTILQNVT--LAPTKVRKK-------------NKADAEKralelleRVGiasqkdkypaQLSGGQQQRV 145
Cdd:PRK11819 392 VDQSRdALDPNKTVWEEISggLDIIKVGNReipsrayvgrfnfKGGDQQK-------KVG----------VLSGGERNRL 454
|
170 180
....*....|....*....|....*
gi 917391194 146 AIARALAMEPKVMLFDEPTSALDPE 170
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-172 |
3.59e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.34 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 15 HVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTInrlEPIDSgEISVEGRPLPAegkelaalrSDVGMVFQSFNLFAHKTI 94
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM---AGVDK-DFNGEARPQPG---------IKVGYLPQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 95 LQNVTLAPTKVRKKNKA-----------DAEKRAL-----------------ELLERVGIASQKDKYP------AQLSGG 140
Cdd:TIGR03719 86 RENVEEGVAEIKDALDRfneisakyaepDADFDKLaaeqaelqeiidaadawDLDSQLEIAMDALRCPpwdadvTKLSGG 165
|
170 180 190
....*....|....*....|....*....|..
gi 917391194 141 QQQRVAIARALAMEPKVMLFDEPTSALDPEMV 172
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESV 197
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-194 |
5.33e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 63.66 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLE--PIDSGEISVEGRPLPAEGKELAAlRSD 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRA-GEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQ---SFNLFAHKTILQNVTLAPTKVRKKNKADAEKRALELLERVGIAsqkdKYPAQL---------SGGQQQRVA 146
Cdd:PRK09580 80 IFMAFQypvEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALL----KMPEDLltrsvnvgfSGGEKKRND 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 917391194 147 IARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTH 194
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
16-196 |
5.58e-12 |
|
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: 63.72 E-value: 5.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDsGEISVEGrpLPAEGKELAALRSDVGMVFQSFNLFAhKTIL 95
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDG--VSWNSVPLQKWRKAFGVIPQKVFIFS-GTFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNvtLAPtkvrkkNKADAEKRALELLERVGIASQKDKYPAQL-----------SGGQQQRVAIARALAMEPKVMLFDEPT 164
Cdd:cd03289 95 KN--LDP------YGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190
....*....|....*....|....*....|..
gi 917391194 165 SALDPeMVNEVLDVMVSLAKEGMTMLVVTHEM 196
Cdd:cd03289 167 AHLDP-ITYQVIRKTLKQAFADCTVILSEHRI 197
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
6-212 |
5.75e-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: 62.65 E-value: 5.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 6 DVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTI-NRLEP-IDSGEISVEGRPLPAEgkelaaLRSDVGMVF 83
Cdd:cd03232 12 TVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAgVITGEILINGRPLDKN------FQRSTGYVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 84 QsfnlfahktilQNVTLAPTKVRKKNKADAEKRALELLERvgiasqkdkypaqlsggqqQRVAIARALAMEPKVMLFDEP 163
Cdd:cd03232 86 Q-----------QDVHSPNLTVREALRFSALLRGLSVEQR-------------------KRLTIGVELAAKPSILFLDEP 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 917391194 164 TSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMG---FARkaADRVIFMADG 212
Cdd:cd03232 136 TSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSasiFEK--FDRLLLLKRG 185
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-214 |
6.12e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.76 E-value: 6.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpAEgkelAALRSDVG- 80
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM-AD----ARHRRAVCp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 ----M-------------VF---QSF-NLFAHktilqnvtlaptkvrkkNKADAEKRALELLERVGIASQKDKyPA-QLS 138
Cdd:NF033858 77 riayMpqglgknlyptlsVFenlDFFgRLFGQ-----------------DAAERRRRIDELLRATGLAPFADR-PAgKLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 139 GGQQQRVAIARALAMEPKVMLFDEPTSALDP-------EMVNEVLDvmvslAKEGMTMLVVTHEM----GFarkaaDRVI 207
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEPTTGVDPlsrrqfwELIDRIRA-----ERPGMSVLVATAYMeeaeRF-----DWLV 208
|
....*..
gi 917391194 208 FMADGAI 214
Cdd:NF033858 209 AMDAGRV 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-213 |
1.64e-11 |
|
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: 63.88 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 24 VPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEgkeLAALRSDVGMVFQSFNLFAHKTILQNVTLApT 103
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN---ISDVHQNMGYCPQFDAIDDLLTGREHLYLY-A 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 104 KVRKKNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLA 183
Cdd:TIGR01257 2038 RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII 2117
|
170 180 190
....*....|....*....|....*....|
gi 917391194 184 KEGMTMLVVTHEMGFARKAADRVIFMADGA 213
Cdd:TIGR01257 2118 REGRAVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
54-208 |
1.79e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.51 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 54 DSGEISVEGrpLPAEGKELAALRSDVGMVFQSFNLFaHKTILQNVTLAPTKVRKKNKADAEKRAL--ELLErvGIASQKD 131
Cdd:PTZ00265 1275 NSGKILLDG--VDICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAAidEFIE--SLPNKYD 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 132 K----YPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLA-KEGMTMLVVTHEMGFARKAADRV 206
Cdd:PTZ00265 1350 TnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASIKRSDKIV 1429
|
..
gi 917391194 207 IF 208
Cdd:PTZ00265 1430 VF 1431
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-233 |
3.44e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.69 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGkeLAALRSDVGMVFQSFNLFAhKTIL 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG--LTDLRRVLSIIPQSPVLFS-GTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNVTlaptKVRKKNKADAekraLELLERVGIASQKDKYPAQL-----------SGGQQQRVAIARALAMEPKVMLFDEPT 164
Cdd:PLN03232 1328 FNID----PFSEHNDADL----WEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 165 SALDPEmVNEVLDVMVSLAKEGMTMLVVTHEMGFARKaADRVIFMADGAIVEDTDPDSFFDNPQSERAR 233
Cdd:PLN03232 1400 ASVDVR-TDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFR 1466
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-212 |
3.47e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.82 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 6 DVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTI-NRLEP--IDSGEISVEGRPLPAEGKelaalRSdVGMV 82
Cdd:TIGR00956 768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERVTTgvITGGDRLVNGRPLDSSFQ-----RS-IGYV 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 83 FQSFNLFAHKTILQNVTLA-----PTKVRKKNKADAEKRALELLER-------VGIASQKdkypaqLSGGQQQRVAIARA 150
Cdd:TIGR00956 842 QQQDLHLPTSTVRESLRFSaylrqPKSVSKSEKMEYVEEVIKLLEMesyadavVGVPGEG------LNVEQRKRLTIGVE 915
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 151 LAMEPKVMLF-DEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHE---MGFArkAADRVIFMADG 212
Cdd:TIGR00956 916 LVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsaILFE--EFDRLLLLQKG 979
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-202 |
4.80e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFG---DLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPlPAEGKELAALRSD 78
Cdd:PTZ00265 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH-NLKDINLKWWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 79 VGMVFQSFNLFAHkTILQNV--TLAPTK------------------------------------------------VRKK 108
Cdd:PTZ00265 462 IGVVSQDPLLFSN-SIKNNIkySLYSLKdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsnelieMRKN 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 109 NKADAEKRALELLERVGI----ASQKDKY-------PAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLD 177
Cdd:PTZ00265 541 YQTIKDSEVVDVSKKVLIhdfvSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250 260
....*....|....*....|....*.
gi 917391194 178 VMVSL-AKEGMTMLVVTHEMGFARKA 202
Cdd:PTZ00265 621 TINNLkGNENRITIIIAHRLSTIRYA 646
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
11-195 |
7.70e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.58 E-value: 7.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 11 FGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPaegKELAALRSDVGMVfqsfnlfA 90
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK---KDLCTYQKQLCFV-------G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 91 HKT-ILQNVTLaptkvRKKNKAD--AEKRALELLERVGIASQKD--KYP-AQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
Cdd:PRK13540 81 HRSgINPYLTL-----RENCLYDihFSPGAVGITELCRLFSLEHliDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|.
gi 917391194 165 SALDPEMVNEVLDVMVSLAKEGMTMLVVTHE 195
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-216 |
1.22e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLpAEGKELAALRSDVGMVFQ---SFNLFAHKT 93
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI-NNHNANEAINHGFALVTEerrSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 94 ILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQKDKYPAQ------LSGGQQQRVAIARALAMEPKVMLFDEPTSAL 167
Cdd:PRK10982 343 IGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 917391194 168 DPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADG---AIVE 216
Cdd:PRK10982 423 DVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGlvaGIVD 474
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-215 |
1.69e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.29 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 2 IVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRT-INRLEPiDSGEISVegrplpAEGKELAALRSDVG 80
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTlVGELEP-DSGTVKW------SENANIGYYAQDHA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQsfnlfahktilQNVTLAPTKVRKKNKADAEKRALELLERVgIASQKD--KYPAQLSGGQQQRVAIARALAMEPKVM 158
Cdd:PRK15064 393 YDFE-----------NDLTLFDWMSQWRQEGDDEQAVRGTLGRL-LFSQDDikKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 917391194 159 LFDEPTSALDPEMVnEVLDvmVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIV 215
Cdd:PRK15064 461 VMDEPTNHMDMESI-ESLN--MALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-216 |
3.05e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.50 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRlEP---IDSGEISVEGRPLPAEGKElaaLRS 77
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPaykILEGDILFKGESILDLEPE---ERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 78 DVGmVFQSFNLFAHKTILQN---VTLAPTKVRKKNKaDAEKRALELLErvgIASQKDKY----PAQL--------SGGQQ 142
Cdd:CHL00131 83 HLG-IFLAFQYPIEIPGVSNadfLRLAYNSKRKFQG-LPELDPLEFLE---IINEKLKLvgmdPSFLsrnvnegfSGGEK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 143 QRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHemgFARK----AADRVIFMADGAIVE 216
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRLldyiKPDYVHVMQNGKIIK 232
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
16-224 |
8.99e-10 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 57.23 E-value: 8.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEG---RPLPaegkeLAALRSDVGMVFQSFNLFAhK 92
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidiSKLP-----LHTLRSRLSIILQDPILFS-G 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 93 TILQNvtLAPtkvrkkNKADAEKRALELLERVGIASQKDKYPAQL-----------SGGQQQRVAIARALAMEPKVMLFD 161
Cdd:cd03288 110 SIRFN--LDP------ECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917391194 162 EPTSALDpeMVNE-VLDVMVSLAKEGMTMLVVTHEMGfARKAADRVIFMADGAIVEDTDPDSFF 224
Cdd:cd03288 182 EATASID--MATEnILQKVVMTAFADRTVVTIAHRVS-TILDADLVLVLSRGILVECDTPENLL 242
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-172 |
2.07e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 12 GDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEIsvegrpLPAEGKElaalrsdVGMVFQSFNLFAH 91
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA------RPAPGIK-------VGYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 92 KTILQNVTLAPTKVRKK-------NKADAEKRAL--ELLERVG-------------IASQ------------KDKYPAQL 137
Cdd:PRK11819 85 KTVRENVEEGVAEVKAAldrfneiYAAYAEPDADfdALAAEQGelqeiidaadawdLDSQleiamdalrcppWDAKVTKL 164
|
170 180 190
....*....|....*....|....*....|....*
gi 917391194 138 SGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMV 172
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV 199
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-192 |
5.46e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 21 DLEVPAGQVVVVLGPSGSGKSTLCRTInrlepidSGEISvegrplPAEGKELAALRSDVGMVFQSFNLFAHKTILQNVT- 99
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARAL-------AGELP------LLSGERQSQFSHITRLSFEQLQKLVSDEWQRNNTd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 100 -LAPTK------VRK--KNKADAEKRALELLERVGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE 170
Cdd:PRK10938 90 mLSPGEddtgrtTAEiiQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180
....*....|....*....|..
gi 917391194 171 MVNEVLDVMVSLAKEGMTMLVV 192
Cdd:PRK10938 170 SRQQLAELLASLHQSGITLVLV 191
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-229 |
7.03e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.90 E-value: 7.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGRPLPAEGkeLAALRSDVGMVFQSFNLFAhKTIL 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG--LMDLRKVLGIIPQAPVLFS-GTVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 96 QNvtLAPtkVRKKNKADAekraLELLER-----------VGIASQKDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
Cdd:PLN03130 1331 FN--LDP--FNEHNDADL----WESLERahlkdvirrnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 165 SALDPEMvnevlDVMV--SLAKE--GMTMLVVTHEMGFARKaADRVIFMADGAIVEDTDPDSFFDNPQS 229
Cdd:PLN03130 1403 AAVDVRT-----DALIqkTIREEfkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEGS 1465
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-208 |
7.17e-09 |
|
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: 53.15 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 27 GQVVVVLGPSGSGKSTLCRTI-NRLEPIDSGEISVEGRPLPAEGKELAALRSDVGmvfqsfnlfahktilqnvtlaptkv 105
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLLLIIVGG------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 106 rkknkadaekralellervgiasqkdkYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLD------VM 179
Cdd:smart00382 57 ---------------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLL 109
|
170 180
....*....|....*....|....*....
gi 917391194 180 VSLAKEGMTMLVVTHEMGFARKAADRVIF 208
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-215 |
7.27e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 7.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 15 HVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTI-------NRlepidSGEISVEGRPLP------AEGKELAALRSDVgm 81
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrsygrNI-----SGTVFKDGKEVDvstvsdAIDAGLAYVTEDR-- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 82 vfQSFNLFAHKTILQNVTLAP-TKVRKKNKADAEKR---ALELLERVGI-ASQKDKYPAQLSGGQQQRVAIARALAMEPK 156
Cdd:NF040905 347 --KGYGLNLIDDIKRNITLANlGKVSRRGVIDENEEikvAEEYRKKMNIkTPSVFQKVGNLSGGNQQKVVLSKWLFTDPD 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 917391194 157 VMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIV 215
Cdd:NF040905 425 VLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-236 |
1.19e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 16 VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTI----NRLEPIDSGEISVEGRPlPAEGKElaALRSDVGMVFQSFNLFAH 91
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGIT-PEEIKK--HYRGDVVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 92 KTILQNVTLAPTKVRKKNKAD-------AEKRALELLERVGIASQKD-----KYPAQLSGGQQQRVAIARALAMEPKVML 159
Cdd:TIGR00956 153 LTVGETLDFAARCKTPQNRPDgvsreeyAKHIADVYMATYGLSHTRNtkvgnDFVRGVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 160 FDEPTSALDP----EMVNeVLDVMVSLAKegMTMLVVTHEMG-FARKAADRVIFMADGAIVEDTDPD---SFFDN----- 226
Cdd:TIGR00956 233 WDNATRGLDSatalEFIR-ALKTSANILD--TTPLVAIYQCSqDAYELFDKVIVLYEGYQIYFGPADkakQYFEKmgfkc 309
|
250
....*....|
gi 917391194 227 PQSERARDFL 236
Cdd:TIGR00956 310 PDRQTTADFL 319
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
15-207 |
1.31e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.83 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 15 HVLKDIDLEVPAGQVVVVLGPSGSGKS-----TLCRTINRL-----EP---IDSGEIS--VE-GRPLPAEGKELAALR-- 76
Cdd:PRK00635 609 HNLKDLTISLPLGRLTVVTGVSGSGKSslindTLVPAVEEFieqgfCSnlsIQWGAISrlVHiTRDLPGRSQRSIPLTyi 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 77 ---SDVGMVFQ---------------SFNL----------FAHKTILQNVTLAPT-------------KVRKKNK--AD- 112
Cdd:PRK00635 689 kafDDLRELFAeqprskrlgltkshfSFNTplgacaecqgLGSITTTDNRTSIPCpsclgkrflpqvlEVRYKGKniADi 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 113 -------AEK---------RALELLERVGIasqkDKYP-----AQLSGGQQQRVAIARAL---AMEPKVMLFDEPTSALD 168
Cdd:PRK00635 769 lemtayeAEKffldepsihEKIHALCSLGL----DYLPlgrplSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLH 844
|
250 260 270
....*....|....*....|....*....|....*....
gi 917391194 169 PEMVNEVLDVMVSLAKEGMTMLVVTHEMGFArKAADRVI 207
Cdd:PRK00635 845 THDIKALIYVLQSLTHQGHTVVIIEHNMHVV-KVADYVL 882
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
15-203 |
1.35e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 52.75 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 15 HVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTInrlepidsgeisvegrplpaegkelaalrsdvgmvfqSFNLFAHKti 94
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAI-------------------------------------GLALGGAQ-- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 95 lqnvtlAPTKVRKKNKADAEKrALELLERVGIASQkdkypaqLSGGQQQRVAIARALAMEPK----VMLFDEPTSALDPE 170
Cdd:cd03227 50 ------SATRRRSGVKAGCIV-AAVSAELIFTRLQ-------LSGGEKELSALALILALASLkprpLYILDEIDRGLDPR 115
|
170 180 190
....*....|....*....|....*....|...
gi 917391194 171 MVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAA 203
Cdd:cd03227 116 DGQALAEAILEHLVKGAQVIVITHLPELAELAD 148
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-221 |
1.74e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTI-NRLEPIdSGEISVegrplpAEGKELAALRSDv 79
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLaGELAPV-SGEIGL------AKGIKLGYFAQH- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 80 gmvfQSFNLFAHKTILQNVT-LAPTkvrkknkaDAEKRALELLErvGIASQKDKYP---AQLSGGQQQRVAIARALAMEP 155
Cdd:PRK10636 384 ----QLEFLRADESPLQHLArLAPQ--------ELEQKLRDYLG--GFGFQGDKVTeetRRFSGGEKARLVLALIVWQRP 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917391194 156 KVMLFDEPTSALDPEMVNEVLDVMVSLakEGmTMLVVTHEMGFARKAADRVIFMADGAiVEDTDPD 221
Cdd:PRK10636 450 NLLLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLLRSTTDDLYLVHDGK-VEPFDGD 511
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
6-207 |
2.50e-08 |
|
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: 52.19 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 6 DVQKHFGDLHVLKDIDlEVPAGQVVVVLGPSGSGKSTLCRTInrlepidsgeisvEGRPLPAEGK-ELAALRsdvgmvfq 84
Cdd:cd03222 5 DCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKIL-------------AGQLIPNGDNdEWDGIT-------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 85 sfnlfahktilqnVTLAPTKVrkknkadaekralellervgiasqkdkypaQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
Cdd:cd03222 63 -------------PVYKPQYI------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPS 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 917391194 165 SALDPEMVNEVLDVMVSLAKEGM-TMLVVTHEMGFARKAADRVI 207
Cdd:cd03222 100 AYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIH 143
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
113-198 |
4.22e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 113 AEKRALELLERVGIASQ-KDKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpemVNEVLDVMVSLAKEGMTMLV 191
Cdd:PLN03073 320 AEARAASILAGLSFTPEmQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIV 396
|
....*..
gi 917391194 192 VTHEMGF 198
Cdd:PLN03073 397 VSHAREF 403
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
15-43 |
1.09e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 51.95 E-value: 1.09e-07
10 20
....*....|....*....|....*....
gi 917391194 15 HVLKDIDLEVPAGQVVVVLGPSGSGKSTL 43
Cdd:COG0178 14 HNLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-233 |
1.81e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.75 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 135 AQLSGGQQQRVAIARALAMEPK--VMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFArKAADRVIFMADG 212
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIIDIGPG 553
|
90 100
....*....|....*....|....*..
gi 917391194 213 A------IVEDTDPDSFFDNPQSERAR 233
Cdd:PRK00635 554 AgifggeVLFNGSPREFLAKSDSLTAK 580
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
12-226 |
2.04e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.04 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 12 GDLH-VLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTInrlepidsgeisvEGRPLPAEGKelAALRSDVGMVFQSFNLFA 90
Cdd:PRK13545 34 GEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLI-------------AGVTMPNKGT--VDIKGSAALIAISSGLNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 91 HKTILQNVTLAP--TKVRKKNKADAEKRALELLERVGIASQKDKypaQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
Cdd:PRK13545 99 QLTGIENIELKGlmMGLTKEKIKEIIPEIIEFADIGKFIYQPVK---TYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 169 PEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDSFFDN 226
Cdd:PRK13545 176 QTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
15-207 |
3.79e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.41 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 15 HVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTI------NRLEpidsgeisvEGRPLPAEGKELAALR--SDVGMVFQS- 85
Cdd:COG0178 619 NNLKNVDVEIPLGVLTCVTGVSGSGKSTLVNDIlypalaRKLN---------GAKEKPGPHDSIEGLEhiDKVIDIDQSp 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 86 ---------------F----NLFAhKTILQ------------NV------------------------------------ 98
Cdd:COG0178 690 igrtprsnpatytgvFdpirELFA-QTPEAkargykpgrfsfNVkggrceacqgdgvikiemhflpdvyvpcevckgkry 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 99 ---TLApTKVRKKNKAD---------AE--------KRALELLERVGIAsqkdkY-----PA-QLSGGQQQRVAIARALA 152
Cdd:COG0178 769 nreTLE-VKYKGKNIADvldmtveeaLEffenipkiARKLQTLQDVGLG-----YiklgqPAtTLSGGEAQRVKLASELS 842
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 153 MEPK---VMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFArKAADRVI 207
Cdd:COG0178 843 KRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVI-KTADWII 899
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
15-43 |
1.09e-06 |
|
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: 49.24 E-value: 1.09e-06
10 20
....*....|....*....|....*....
gi 917391194 15 HVLKDIDLEVPAGQVVVVLGPSGSGKSTL 43
Cdd:TIGR00630 10 HNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
15-43 |
1.44e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.53 E-value: 1.44e-06
10 20
....*....|....*....|....*....
gi 917391194 15 HVLKDIDLEVPAGQVVVVLGPSGSGKSTL 43
Cdd:PRK00349 14 HNLKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
113-198 |
3.12e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 113 AEKRALELLERVGIASQKDKYP-AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVmvsLAKEGMTMLV 191
Cdd:PRK15064 131 AEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDV---LNERNSTMII 207
|
....*..
gi 917391194 192 VTHEMGF 198
Cdd:PRK15064 208 ISHDRHF 214
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
11-207 |
3.50e-06 |
|
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: 46.45 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 11 FGDLHVLKDIDLEVPagqVVVVLGPSGSGKSTLcrtinrlepIDSGEISVEGRpLPAEGKELAALRSdvgmvfqsfnLFA 90
Cdd:cd03240 9 IRSFHERSEIEFFSP---LTLIVGQNGAGKTTI---------IEALKYALTGE-LPPNSKGGAHDPK----------LIR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 91 HKTILQNVTLApTKVRKKNKADAEkRALELLERVGIASQKD------KYPAQLSGGQQQ------RVAIARALAMEPKVM 158
Cdd:cd03240 66 EGEVRAQVKLA-FENANGKKYTIT-RSLAILENVIFCHQGEsnwpllDMRGRCSGGEKVlasliiRLALAETFGSNCGIL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 917391194 159 LFDEPTSALDPEMVNEVL-DVMVSLAKEG-MTMLVVTHEMGFARkAADRVI 207
Cdd:cd03240 144 ALDEPTTNLDEENIEESLaEIIEERKSQKnFQLIVITHDEELVD-AADHIY 193
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
17-43 |
3.58e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 47.37 E-value: 3.58e-06
10 20
....*....|....*....|....*..
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTL 43
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTL 651
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
9-194 |
1.82e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 9 KHFGDLHVLKDIDLEvpaGQVVVVLGPSGSGKSTLCRTI---------------NRLEPIDSGEISVE------------ 61
Cdd:COG0419 8 ENFRSYRDTETIDFD---DGLNLIVGPNGAGKSTILEAIryalygkarsrsklrSDLINVGSEEASVElefehggkryri 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 62 -------GRPLPAEGKELAAlrsdvgMVFQSFNLFAHKTILQNVTLAPTKVRKKNKADAEKRAL--ELLERVgiasQKDK 132
Cdd:COG0419 85 errqgefAEFLEAKPSERKE------ALKRLLGLEIYEELKERLKELEEALESALEELAELQKLkqEILAQL----SGLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 917391194 133 YPAQLSGGQQQRVAIARALAmepkvMLFDepTSALDPEMVNEVLDVMVSLAkegmtmlVVTH 194
Cdd:COG0419 155 PIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
26-59 |
2.73e-05 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 43.54 E-value: 2.73e-05
10 20 30
....*....|....*....|....*....|....*..
gi 917391194 26 AGQVVVVLGPSGSGKSTLcrtINRLEPIDS---GEIS 59
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTL---LNALLPELVlatGEIS 117
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-229 |
7.03e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 137 LSGGQQQRVAIARALAME-PKVM-LFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGfARKAADRVIFMADGA- 213
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED-TIRAADYVIDIGPGAg 567
|
90 100
....*....|....*....|.
gi 917391194 214 -----IVEDTDPDSFFDNPQS 229
Cdd:TIGR00630 568 ehggeVVASGTPEEILANPDS 588
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
26-59 |
7.54e-05 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 42.88 E-value: 7.54e-05
10 20 30
....*....|....*....|....*....|....*..
gi 917391194 26 AGQVVVVLGPSGSGKSTLcrtINRLEP---IDSGEIS 59
Cdd:PRK00098 163 AGKVTVLAGQSGVGKSTL---LNALAPdleLKTGEIS 196
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
134-194 |
8.52e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.76 E-value: 8.52e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917391194 134 PAQLSGGQQQ---RVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTH 194
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-231 |
2.29e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 1 MIVLRDVQKHFGDLHVLKDIDLEVPAGQVVVVLGPSGSGKSTLCRTINRLEPIDSGEISVEGR-PLPAEGKELAALRS-- 77
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPALPQpa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 78 -----DVGMVFQSFNLFAHKTILQNVTLAPTKVRKKNKA-DA---EKRALELLERVGIASQKDKYPAQ-LSGGQQQRVAI 147
Cdd:PRK10636 81 leyviDGDREYRQLEAQLHDANERNDGHAIATIHGKLDAiDAwtiRSRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 148 ARALAMEPKVMLFDEPTSALDpemvnevLDVMVSLAK-----EGmTMLVVTHEMGFARKAADRVIFMADGAIVEDTDPDS 222
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLD-------LDAVIWLEKwlksyQG-TLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYS 232
|
....*....
gi 917391194 223 FFDNPQSER 231
Cdd:PRK10636 233 SFEVQRATR 241
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
137-214 |
4.28e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 4.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917391194 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVsLAKEGMTMlvVTHEMGFARKAADRVIFMADGAI 214
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV-LFQGGVLM--VSHDEHLISGSVDELWVVSEGKV 702
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
26-59 |
4.39e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.83 E-value: 4.39e-04
10 20 30
....*....|....*....|....*....|....*..
gi 917391194 26 AGQVVVVLGPSGSGKSTLcrtINRLEP---IDSGEIS 59
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTL---LNALLPeldLRTGEIS 138
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-242 |
5.16e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 40.37 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 17 LKDIDLEVPAGQVVVVlGPSGSGKSTLCRTINRL-----------------EPIDSGEISVE-------GRPLPAEGKE- 71
Cdd:COG3593 14 IKDLSIELSDDLTVLV-GENNSGKSSILEALRLLlgpsssrkfdeedfylgDDPDLPEIEIEltfgsllSRLLRLLLKEe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 72 --------LAALRSDVGMVFQSFNLFAHKTILQNVTLAPTKVRKKNKadaEKRALELLERVGIASQKDKYPAQLSGGQQQ 143
Cdd:COG3593 93 dkeeleeaLEELNEELKEALKALNELLSEYLKELLDGLDLELELSLD---ELEDLLKSLSLRIEDGKELPLDRLGSGFQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 144 RVAIARALAM-------EPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHEMGFARKA-ADRVIFMADGAiv 215
Cdd:COG3593 170 LILLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVpLENIRRLRRDS-- 247
|
250 260
....*....|....*....|....*..
gi 917391194 216 EDTDPDSFFDNPQSEraRDFLGKILGH 242
Cdd:COG3593 248 GGTTSTKLIDLDDED--LRKLLRYLGV 272
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
29-61 |
6.83e-04 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 39.01 E-value: 6.83e-04
10 20 30
....*....|....*....|....*....|....*.
gi 917391194 29 VVVVLGPSGSGKSTLCRTINR---LEPIDSGEISVE 61
Cdd:cd02020 1 IIAIDGPAGSGKSTVAKLLAKklgLPYLDTGGIRTE 36
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-195 |
9.96e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.21 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 14 LHVLKDIDLEVPAGQVVVVLGPSGSGKSTLC------RTINRLEpidsGEISVEGRPLPAEG-------KELAALRSDVG 80
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMdvlagrKTGGYIE----GDIRISGFPKKQETfarisgyCEQNDIHSPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 81 MVFQSFnlfahktILQNVTLAPTKVRKKNKADAEKRALELLERVGIASQKDKYPA--QLSGGQQQRVAIARALAMEPKVM 158
Cdd:PLN03140 969 TVRESL-------IYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSII 1041
|
170 180 190
....*....|....*....|....*....|....*..
gi 917391194 159 LFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTHE 195
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
27-122 |
3.14e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 38.56 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 27 GQVVVVLGPSGSGKSTLCR-----TINRLEPIDSGEISVEGRPlPAEGKELAALRSDvgmvFQSFNLFAHKTILQNVTLA 101
Cdd:COG4694 24 KKLNLIYGENGSGKSTLSRilrslELGDTSSEVIAEFEIEAGG-SAPNPSVRVFNRD----FVEENLRSGEEIKGIFTLG 98
|
90 100
....*....|....*....|.
gi 917391194 102 PTKVRKKNKADAEKRALELLE 122
Cdd:COG4694 99 EENIELEEEIEELEKEIEDLK 119
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
17-45 |
3.46e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 38.25 E-value: 3.46e-03
10 20
....*....|....*....|....*....
gi 917391194 17 LKDIDLEVPAGQVVVVLGPSGSGKSTLCR 45
Cdd:COG5635 170 LKRLELLEAKKKRLLILGEPGSGKTTLLR 198
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
27-45 |
4.57e-03 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 36.97 E-value: 4.57e-03
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
131-194 |
6.39e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 36.77 E-value: 6.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917391194 131 DKYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEMVNEVLDVMVSLAKEGMTMLVVTH 194
Cdd:PRK13541 118 DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
29-90 |
8.73e-03 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 35.94 E-value: 8.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917391194 29 VVVVLGPSGSGKSTLCRTINR---LEPIDSGEISvegrplpaegKELAALRsdvGMVFQSFNLFA 90
Cdd:PRK04182 2 IITISGPPGSGKTTVARLLAEklgLKHVSAGEIF----------RELAKER---GMSLEEFNKYA 53
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
129-195 |
8.86e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 36.94 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917391194 129 QKDKY---PAQLSGGQQQ------RVAIARALA--------MEPkvMLFDEPTSALDPEMVNEVLDVMVSLAKEGM-TML 190
Cdd:PRK02224 771 QKDGEplePEQLSGGERAlfnlslRCAIYRLLAegiegdapLPP--LILDEPTVFLDSGHVSQLVDLVESMRRLGVeQIV 848
|
....*
gi 917391194 191 VVTHE 195
Cdd:PRK02224 849 VVSHD 853
|
|
| GPN3 |
cd17872 |
GPN-loop GTPase 3; GPN-loop GTPase 3 (GPN3) is a small GTPase that is required for nuclear ... |
27-47 |
9.44e-03 |
|
GPN-loop GTPase 3; GPN-loop GTPase 3 (GPN3) is a small GTPase that is required for nuclear targeting of RNA polymerase II. It forms heterodimers with GPN1.
Pssm-ID: 349781 [Multi-domain] Cd Length: 196 Bit Score: 35.97 E-value: 9.44e-03
|
| |
