|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-242 |
1.70e-159 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 441.36 E-value: 1.70e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasySRKDVHKLRQ 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD---SKKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:COG1126 78 KVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIK 240
Cdd:COG1126 158 MLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLS 237
|
..
gi 489248201 241 QV 242
Cdd:COG1126 238 KV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-217 |
2.54e-127 |
|
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: 359.15 E-value: 2.54e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasySRKDVHKLRQQ 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD---DKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03262 78 VGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-239 |
9.01e-119 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 339.47 E-value: 9.01e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIG----------DAKLNAASy 70
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGgeeirlkpdrDGELVPAD- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 71 sRKDVHKLRQQTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGI 150
Cdd:COG4598 87 -RRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 151 ARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245
|
....*....
gi 489248201 231 QNERTKKFI 239
Cdd:COG4598 246 KSERLRQFL 254
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-241 |
7.45e-110 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 316.31 E-value: 7.45e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAA---SYSRKDVHK 77
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 78 LRQQTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKK 237
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
....
gi 489248201 238 FIKQ 241
Cdd:PRK11264 243 FLEK 246
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-242 |
9.30e-102 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 295.46 E-value: 9.30e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasySRKDVHKLRQ 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND---PKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIK 240
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQ 237
|
..
gi 489248201 241 QV 242
Cdd:PRK09493 238 HV 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-247 |
1.11e-98 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 291.21 E-value: 1.11e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAF----KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasYSRKDVH 76
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTA--LSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 KLRQQTAMVFQNYNLFKNKTALQNVTEALITAqKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSRTVAENVALPLEIA-GVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERT 235
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELT 237
|
250
....*....|..
gi 489248201 236 KKFIKQVGEPAE 247
Cdd:COG1135 238 RRFLPTVLNDEL 249
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-231 |
1.34e-87 |
|
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: 259.44 E-value: 1.34e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKD----LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaaSYSRKDVH 76
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLT--LLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 KLRQQTAMVFQNYNLFKNKTALQNVTEALITAqKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSRTVFENVALPLEIA-GVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-239 |
1.76e-85 |
|
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: 254.13 E-value: 1.76e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsySRKDVHKLRQ 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGL--SEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPqNERTKKFI 239
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-240 |
3.27e-84 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 251.09 E-value: 3.27e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLN-AASYSRKDVHKLRQ 80
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfSQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTpEELFDNPQNERTKKFIK 240
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHYLS 241
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-239 |
2.15e-82 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 250.40 E-value: 2.15e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnaasysrKDVHKL-- 78
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG----------RDVTGLpp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 79 -RQQTAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:COG3842 75 eKRNVGMVFQDYALFPHLTVAENVAFGL-RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTH--EMAFAreVADKVIFMADGRIIEQGTPEELFDNPQNER 234
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHdqEEALA--LADRIAVMNDGRIEQVGTPEEIYERPATRF 231
|
....*
gi 489248201 235 TKKFI 239
Cdd:COG3842 232 VADFI 236
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-220 |
3.39e-81 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 242.64 E-value: 3.39e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKD----LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDVH 76
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI--SSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 KLRQQT-AMVFQNYNLFKNKTALQNVTEALItAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALA 155
Cdd:COG1136 82 RLRRRHiGFVFQFFNLLPELTALENVALPLL-LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFArEVADKVIFMADGRIIEQ 220
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVTHDPELA-ARADRVIRLRDGRIVSD 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-237 |
1.44e-79 |
|
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: 247.89 E-value: 1.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAF-----KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDV 75
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDL--TKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 76 HKLRQQTAMVFQNYN--LFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL-EHKADSYPITMSGGQQQRIGIAR 152
Cdd:COG1123 338 RELRRRVQMVFQDPYssLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELgLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
....*.
gi 489248201 232 NERTKK 237
Cdd:COG1123 498 HPYTRA 503
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-239 |
1.94e-79 |
|
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: 239.12 E-value: 1.94e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAS-YSRK-DVHKLR 79
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDiYDKKiDVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNYNLFkNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL----EHKADSYPITMSGGQQQRIGIARALA 155
Cdd:TIGR00972 82 RRVGMVFQKPNPF-PMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKqTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERT 235
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRT 239
|
....
gi 489248201 236 KKFI 239
Cdd:TIGR00972 240 EDYI 243
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-240 |
7.94e-79 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 237.60 E-value: 7.94e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLN-AASYSRKDVHKLRQ 80
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfSKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTpEELFDNPQNERTKKFIK 240
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNYLS 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-217 |
2.05e-78 |
|
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: 235.46 E-value: 2.05e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKD----LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDvHK 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELA-AF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 78 LRQQTAMVFQNYNLFKNKTALQNVTEALItAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:cd03255 80 RRRHIGFVFQSFNLLPDLTALENVELPLL-LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREvADKVIFMADGRI 217
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-226 |
4.82e-78 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 235.72 E-value: 4.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFK-DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASysRKDVHKLR 79
Cdd:COG3638 2 MLELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALR--GRALRRLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNYNLFKNKTALQNV-------TEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIAR 152
Cdd:COG3638 80 RRIGMIFQQFNLVPRLSVLTNVlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-248 |
1.34e-77 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 237.78 E-value: 1.34e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAF----KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDVH 76
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL--TALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 KLRQQTAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:PRK11153 79 KARRQIGMIFQHFNLLSSRTVFDNVALPL-ELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERT 235
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLT 237
|
250
....*....|....*.
gi 489248201 236 KKFIK---QVGEPAEL 248
Cdd:PRK11153 238 REFIQstlHLDLPEDY 253
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-239 |
2.93e-77 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 236.97 E-value: 2.93e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasYSRKDVHKLRqq 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL----FTNLPPRERR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 162 LLDEPTSALD----PELVAGVLQVIKSIaekQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKK 237
Cdd:COG1118 156 LLDEPFGALDakvrKELRRWLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVAR 232
|
..
gi 489248201 238 FI 239
Cdd:COG1118 233 FL 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-240 |
3.27e-76 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 231.40 E-value: 3.27e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAS--------YSRK 73
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRdkdgqlkvADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 74 DVHKLRQQTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKA-DSYPITMSGGQQQRIGIAR 152
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQN 232
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
....*...
gi 489248201 233 ERTKKFIK 240
Cdd:PRK10619 246 PRLQQFLK 253
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-231 |
8.25e-76 |
|
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: 229.31 E-value: 8.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDVHKLRQQ 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDI--SGLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF--DNPQ 231
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPL 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-219 |
5.80e-73 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 221.85 E-value: 5.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFK-DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASysRKDVHKLR 79
Cdd:COG2884 1 MIRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLK--RREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNYNLFKNKTALQNVTEALItAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPH 159
Cdd:COG2884 79 RRIGVVFQDFRLLPDRTVYENVALPLR-VTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIE 219
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-219 |
1.38e-72 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 222.27 E-value: 1.38e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAF----KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnaasysrKDVH 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----------KPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 KLRQQTAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:COG1116 77 GPGPDRGVVFQEPALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 157 DPHAILLDEPTSALDpELVAGVLQ--VIKSIAEKQTTMIIVTH---EMAFareVADKVIFMAD--GRIIE 219
Cdd:COG1116 156 DPEVLLMDEPFGALD-ALTRERLQdeLLRLWQETGKTVLFVTHdvdEAVF---LADRVVVLSArpGRIVE 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-246 |
1.58e-72 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 224.95 E-value: 1.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklrq 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNI----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 qtAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:COG3839 78 --AMVFQSYALYPHMTVYENIAFPL-KLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHE----MAFarevADKVIFMADGRIIEQGTPEELFDNPQNERT 235
Cdd:COG3839 155 FLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEELYDRPANLFV 230
|
250
....*....|.
gi 489248201 236 KKFIkqvGEPA 246
Cdd:COG3839 231 AGFI---GSPP 238
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-226 |
2.54e-72 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 220.71 E-value: 2.54e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasysRKDVHKLRQQ 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV------ARDPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLFKNKTALQNVtEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENL-RFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-221 |
1.46e-71 |
|
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: 217.77 E-value: 1.46e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklrqq 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 tAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03259 75 -GMVFQDYALFPHLTVAENIAFGL-KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-226 |
1.64e-71 |
|
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: 218.20 E-value: 1.64e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLL-----ERPDDGIIEIGDAKLNAasySRKDVH 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYD---LDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 KLRQQTAMVFQNYNLFkNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL--EHKADSYPITMSGGQQQRIGIARAL 154
Cdd:cd03260 78 ELRRRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489248201 155 AVDPHAILLDEPTSALDPELVAGVLQVIKSIAeKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELK-KEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-239 |
2.18e-71 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 219.14 E-value: 2.18e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLL--ERPD---DGIIEIGDAKLNAASYsrkDVH 76
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIYDPDV---DVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 KLRQQTAMVFQNYNLFkNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL----EHKADSYPITMSGGQQQRIGIAR 152
Cdd:COG1117 89 ELRRRVGMVFQKPNPF-PKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 153 ALAVDPHAILLDEPTSALDPelVAGvLQVIKSIAE--KQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDP--IST-AKIEELILElkKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNP 244
|
....*....
gi 489248201 231 QNERTKKFI 239
Cdd:COG1117 245 KDKRTEDYI 253
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-231 |
3.70e-71 |
|
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: 217.59 E-value: 3.70e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKD-LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasysRKDVHKLRQ 80
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT-----KKNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYN--LFkNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:COG1122 76 KVGLVFQNPDdqLF-APTVEEDVAFGP-ENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-216 |
3.86e-71 |
|
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: 215.51 E-value: 3.86e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysRKDVHKLRQQ 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL---EDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLFKNKTALQNVTEALitaqkkpkkeaeqigmdllrqvglehkadsypitmSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03229 78 IGMVFQDFALFPHLTVLENIALGL-----------------------------------SGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGR 216
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-226 |
6.38e-71 |
|
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: 217.44 E-value: 6.38e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLT-VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaaSYSRKDVHKLRQ 80
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDIN--KLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNV-------TEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARA 153
Cdd:cd03256 79 QIGMIFQQFNLIERLSVLENVlsgrlgrRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 154 LAVDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-240 |
6.60e-67 |
|
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: 207.35 E-value: 6.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAF----KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVH 76
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV-----TRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 KLRQQTAMVFQNY--NLFKNKTALQNVTEALiTAQKKPKKEaEQIGmDLLRQVGL-EHKADSYPITMSGGQQQRIGIARA 153
Cdd:COG1124 76 AFRRRVQMVFQDPyaSLHPRHTVDRILAEPL-RIHGLPDRE-ERIA-ELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 154 LAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQN 232
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
....*...
gi 489248201 233 ERTKKFIK 240
Cdd:COG1124 233 PYTRELLA 240
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-220 |
7.83e-67 |
|
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: 206.17 E-value: 7.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKD----LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdvhk 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 78 lrqqtAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:cd03293 76 -----GYVFQQDALLPWLTVLDNVALGL-ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 158 PHAILLDEPTSALDpELVAGVLQ--VIKSIAEKQTTMIIVTHEMAFAREVADKVIFMA--DGRIIEQ 220
Cdd:cd03293 150 PDVLLLDEPFSALD-ALTREQLQeeLLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSarPGRIVAE 215
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-228 |
1.89e-66 |
|
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: 206.00 E-value: 1.89e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAF-KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASysRKDVHKLR 79
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLR--GKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNYNLFKNKTALQNVTEALITAQKKPK-------KEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIAR 152
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVLHGRLGYKPTWRsllgrfsEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFD 228
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINkEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-242 |
3.44e-66 |
|
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: 206.34 E-value: 3.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASysRKDVHKLRQQT-AMVFQNYNLFKNKTAL 98
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMS--RKELRELRRKKiSMVFQSFALLPHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 99 QNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPeLVAGV 178
Cdd:cd03294 121 ENVAFGL-EVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP-LIRRE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 179 LQ--VIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIKQV 242
Cdd:cd03294 199 MQdeLLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGV 264
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-239 |
1.16e-65 |
|
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: 203.72 E-value: 1.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKlrQQ 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-----TDVPVQE--RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLFKNKTALQNVTEALIT---AQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVAFGLRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDP----ELVAGVLQVIKsiaEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNER 234
Cdd:cd03296 156 KVLLLDEPFGALDAkvrkELRRWLRRLHD---ELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
....*
gi 489248201 235 TKKFI 239
Cdd:cd03296 233 VYSFL 237
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-239 |
1.31e-65 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 205.71 E-value: 1.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTV-LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKLR 79
Cdd:COG1125 1 MIEFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDI-----RDLDPVELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNYNLFKNKTALQNVteALI-TAQKKPKKEAEQIGMDLLRQVGLEHK--ADSYPITMSGGQQQRIGIARALAV 156
Cdd:COG1125 76 RRIGYVIQQIGLFPHMTVAENI--ATVpRLLGWDKERIRARVDELLELVGLDPEeyRDRYPHELSGGQQQRVGVARALAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 157 DPHAILLDEPTSALDPeLVAGVLQV-IKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNER 234
Cdd:COG1125 154 DPPILLMDEPFGALDP-ITREQLQDeLLRLqRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDF 232
|
....*
gi 489248201 235 TKKFI 239
Cdd:COG1125 233 VADFV 237
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-221 |
1.56e-65 |
|
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: 203.12 E-value: 1.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKD----LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVh 76
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 kLRQQTAMVFQNYNLFKN--KTALQNVTEALITAQKKPKKEAEQ-IGMDLLRQVGL-EHKADSYPITMSGGQQQRIGIAR 152
Cdd:cd03257 80 -RRKEIQMVFQDPMSSLNprMTIGEQIAEPLRIHGKLSKKEARKeAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-231 |
2.45e-64 |
|
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: 202.98 E-value: 2.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFK----DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRC-LNLLERP--DDGIIEIGDAKLnaASYSRK 73
Cdd:COG0444 1 LLEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAiLGLLPPPgiTSGEILFDGEDL--LKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 74 DVHKLR-QQTAMVFQN-YnlfknkTAL-------QNVTEALITAQKKPKKEAEQIGMDLLRQVGL---EHKADSYPITMS 141
Cdd:COG0444 79 ELRKIRgREIQMIFQDpM------TSLnpvmtvgDQIAEPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 142 GGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQ 220
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEE 232
|
250
....*....|.
gi 489248201 221 GTPEELFDNPQ 231
Cdd:COG0444 233 GPVEELFENPR 243
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-228 |
5.94e-63 |
|
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: 197.19 E-value: 5.94e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDvhkLRQ 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL--ASLSRRE---LAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVteAL-----ITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALA 155
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRELV--ALgryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFD 228
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-231 |
1.57e-61 |
|
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: 193.04 E-value: 1.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKL-RQ 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-----TGLPPHEIaRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVTEALITAQK---------KPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIA 151
Cdd:cd03219 76 GIGRTFQIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 152 RALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
17-242 |
4.61e-61 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 196.86 E-value: 4.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAklNAASYSRKDVHKLRQQT-AMVFQNYNLFKNK 95
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGE--DITKLSKKELRELRRKKmSMVFQHFALLPHR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 TALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDP--- 172
Cdd:COG4175 121 TVLENVAFGL-EIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlir 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 173 -----ELVAgvLQviksiAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIKQV 242
Cdd:COG4175 200 remqdELLE--LQ-----AKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDV 267
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-239 |
4.91e-60 |
|
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: 189.37 E-value: 4.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnaasysrKDVHKL--- 78
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG----------KDITNLpph 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 79 RQQTAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03300 71 KRPVNTVFQNYALFPHLTVFENIAFGL-RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKK 237
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVAD 229
|
..
gi 489248201 238 FI 239
Cdd:cd03300 230 FI 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-231 |
5.15e-60 |
|
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: 189.86 E-value: 5.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKL-R 79
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-----TGLPPHRIaR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNYNLFKNKTALQNV--------TEALITA------QKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQ 145
Cdd:COG0411 79 LGIARTFQNPRLFPELTVLENVlvaaharlGRGLLAAllrlprARREEREARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 146 QRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPE 224
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
....*..
gi 489248201 225 ELFDNPQ 231
Cdd:COG0411 239 EVRADPR 245
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-216 |
7.68e-60 |
|
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: 188.06 E-value: 7.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 3 QVRHIRKAFKDLT--VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasysrKDVHKLRQ 80
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK-----LSLKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYN--LFKNktalqNVTEALITA---QKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALA 155
Cdd:cd03225 76 KVGLVFQNPDdqFFGP-----TVEEEVAFGlenLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGR 216
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-231 |
3.03e-59 |
|
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: 195.12 E-value: 3.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAF--KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLErPDDGIIEiGDAKLNAASYSRKDVHKL 78
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRIS-GEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 79 RQQTAMVFQNY-NLFKNKTALQNVTEALItAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:COG1123 82 GRRIGMVFQDPmTQLNPVTVGDQIAEALE-NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-242 |
3.29e-59 |
|
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: 191.02 E-value: 3.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklrqq 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDY------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 tAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:TIGR03265 79 -GIVFQSYALFPNLTVADNIAYGL-KNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIK 240
Cdd:TIGR03265 157 LLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG 236
|
..
gi 489248201 241 QV 242
Cdd:TIGR03265 237 EV 238
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-217 |
7.66e-59 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 185.40 E-value: 7.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIeigdaKLNAASYSRKDVHKLRQQ 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEI-----YLDGKPLSAMPPPEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLFKNkTALQNVTEALITAQKKPKKEAEQigmDLLRQVGLEHKADSYPIT-MSGGQQQRIGIARALAVDPHA 160
Cdd:COG4619 76 VAYVPQEPALWGG-TVRDNLPFPFQLRERKFDRERAL---ELLERLGLPPDILDKPVErLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKS-IAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-244 |
1.06e-57 |
|
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: 183.52 E-value: 1.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAklnaasYSRKDVHKLRQ 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE------DVRKEPREARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVtEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:COG4555 75 QIGVLPDERGLYDRLTVRENI-RYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKK-FI 239
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDaFV 233
|
....*
gi 489248201 240 KQVGE 244
Cdd:COG4555 234 ALIGS 238
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-241 |
1.00e-56 |
|
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: 180.96 E-value: 1.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLT-VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaklNAASYSRKDVHKLRQ 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFI-----DGEDIREQDPVELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVTeALITAQKKPKKEAEQIGMDLLRQVGLE--HKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03295 76 KIGYVIQQIGLFPHMTVEENIA-LVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKK 237
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAE 234
|
....
gi 489248201 238 FIKQ 241
Cdd:cd03295 235 FVGA 238
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-216 |
3.43e-56 |
|
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: 178.60 E-value: 3.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFK-DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaaSYSRKDVHKLR 79
Cdd:TIGR02673 1 MIEFHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVN--RLRGRQLPLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPH 159
Cdd:TIGR02673 79 RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVG-AALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGR 216
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-241 |
7.75e-56 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 178.41 E-value: 7.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVldGIDLEIKSGEVTAIIGPSGSGKSTLlrcLNLL---ERPDDGIIEIGDAKLNAASYSRKDVhk 77
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTL---LNLIagfLPPDSGRILWNGQDLTALPPAERPV-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 78 lrqqtAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIgMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALaVD 157
Cdd:COG3840 74 -----SMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQV-EQALERVGLAGLLDRLPGQLSGGQRQRVALARCL-VR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 158 PHAI-LLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERT 235
Cdd:COG3840 147 KRPIlLLDEPFSALDPALRQEMLDLVDELCrERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
....*.
gi 489248201 236 KKFIKQ 241
Cdd:COG3840 227 AAYLGI 232
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-225 |
1.37e-55 |
|
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: 178.01 E-value: 1.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKD----LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasYSRKDVH 76
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA--LDEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 KLR-QQTAMVFQNYNLFKNKTALQNVteaLITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALA 155
Cdd:COG4181 86 RLRaRHVGFVFQSFQLLPTLTALENV---MLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489248201 156 VDPhAILL-DEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEE 225
Cdd:COG4181 163 TEP-AILFaDEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-231 |
1.58e-55 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 180.70 E-value: 1.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAF---------KDLTV--LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgDAKlNAASY 70
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILF-DGQ-DITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 71 SRKDVHKLRQQTAMVFQN-Y-NLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL--EHkADSYPITMSGGQQQ 146
Cdd:COG4608 86 SGRELRPLRRRMQMVFQDpYaSLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrpEH-ADRYPHEFSGGQRQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 147 RIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEE 225
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLqDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDE 244
|
....*.
gi 489248201 226 LFDNPQ 231
Cdd:COG4608 245 LYARPL 250
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-231 |
4.49e-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 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: 178.03 E-value: 4.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasYSRKDVHKLRQQTAMVFQN--YNLF 92
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITA--KKKKKLKDLRKKVGLVFQFpeHQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 KNkTALQNVtealitA-----QKKPKKEAEQIGMDLLRQVGLEHK-ADSYPITMSGGQQQRIGIARALAVDPHAILLDEP 166
Cdd:TIGR04521 97 EE-TVYKDI------AfgpknLGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 167 TSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:TIGR04521 170 TAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-212 |
4.81e-54 |
|
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: 173.19 E-value: 4.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 4 VRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgDAKLNAASYSRKDVHKLRQQTA 83
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYL-NGQETPPLNSKKASKFRREKLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 84 MVFQNYNLFKNKTALQNVTEALItAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILL 163
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGLK-YKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489248201 164 DEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFArEVADKVIFM 212
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-217 |
8.81e-54 |
|
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: 171.04 E-value: 8.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasysRKDVHKLRQQ 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI------KKEPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLFKNKTALQNvtealitaqkkpkkeaeqigmdllrqvglehkadsypITMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03230 75 IGYLPEEPSLYENLTVREN-------------------------------------LKLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
20-242 |
1.47e-53 |
|
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: 176.58 E-value: 1.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEI-GDAKLNAASYSRKDVHklRQQTAMVFQNYNLFKNKTAL 98
Cdd:TIGR01186 12 ADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIdGENIMKQSPVELREVR--RKKIGMVFQQFALFPHMTIL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 99 QNvTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPeLVAGV 178
Cdd:TIGR01186 90 QN-TSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDP-LIRDS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 179 LQ--VIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIKQV 242
Cdd:TIGR01186 168 MQdeLKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-239 |
1.92e-53 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 176.68 E-value: 1.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVHklrqq 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVN----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 taMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:PRK09452 90 --TVFQSYALFPHMTVFENVAFGL-RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIaEKQT--TMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFI 239
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKAL-QRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFI 245
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-242 |
2.09e-53 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 176.04 E-value: 2.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIeigdaKLNAASYSRkdVHKLRQQ 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI-----RFHGTDVSR--LHARDRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLFKNKTALQNVTEAL--ITAQKKPKKEA-EQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:PRK10851 76 VGFVFQHYALFRHMTVFDNIAFGLtvLPRRERPNAAAiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPelvagvlQVIKSI--------AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:PRK10851 156 QILLLDEPFGALDA-------QVRKELrrwlrqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
250
....*....|..
gi 489248201 231 QNERTKKFIKQV 242
Cdd:PRK10851 229 ATRFVLEFMGEV 240
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-221 |
2.53e-53 |
|
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: 171.28 E-value: 2.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklrqq 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 tAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03301 75 -AMVFQNYALYPHMTVYDNIAFGL-KLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-239 |
1.41e-52 |
|
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: 170.21 E-value: 1.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLtVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIeigdaKLNAasysrKDVHKL--- 78
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI-----LLNG-----KDITNLppe 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 79 RQQTAMVFQNYNLFKNKTALQNVTEALITaQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIAYGLKK-RKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKK 237
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAE 228
|
..
gi 489248201 238 FI 239
Cdd:cd03299 229 FL 230
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-235 |
4.81e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 169.11 E-value: 4.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnaasysrKDVHKLRQ 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----------KPPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLfkNK----TALQNVTEALITAQ---KKPKKEAEQIGMDLLRQVGLEHKADSyPI-TMSGGQQQRIGIAR 152
Cdd:COG1121 76 RIGYVPQRAEV--DWdfpiTVRDVVLMGRYGRRglfRRPSRADREAVDEALERVGLEDLADR-PIgELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMaDGRIIEQGTPEELFDNPQN 232
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENL 231
|
...
gi 489248201 233 ERT 235
Cdd:COG1121 232 SRA 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-230 |
8.80e-52 |
|
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: 171.82 E-value: 8.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRhIRKAFKDLTvLDgIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKL--NAASYSRKdVHKL 78
Cdd:COG4148 2 MLEVD-FRLRRGGFT-LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLP-PHRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 79 RqqTAMVFQNYNLFKNKTALQNvteaLITAQKKPKKEAEQIGMD-LLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:COG4148 78 R--IGYVFQEARLFPHLSVRGN----LLYGRKRAPRAERRISFDeVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-227 |
2.61e-51 |
|
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: 167.99 E-value: 2.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDakLNAASysRKDVHKLRQQTAMVFQN-YNLFKN 94
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLD--EENLWEIRKKVGMVFQNpDNQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 KT-------ALQNvtealitaQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:TIGR04520 93 ATveddvafGLEN--------LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEAT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 168 SALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELF 227
Cdd:TIGR04520 165 SMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIF 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-226 |
6.49e-51 |
|
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: 176.18 E-value: 6.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLT--VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDakLNAASYSRKDvhkLR 79
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG--IDLRQIDPAS---LR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNYNLFkNKTALQNVTEAlitaqkKPKKEAEQIgMDLLRQVGLEHKADSYP-----------ITMSGGQQQRI 148
Cdd:COG2274 549 RQIGVVLQDVFLF-SGTIRENITLG------DPDATDEEI-IEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 149 GIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAeKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEEL 226
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-216 |
7.34e-51 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 163.18 E-value: 7.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 3 QVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKLRQQT 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI-----AKLPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 83 AMVFQnynlfknktalqnvtealitaqkkpkkeaeqigmdllrqvglehkadsypitMSGGQQQRIGIARALAVDPHAIL 162
Cdd:cd00267 76 GYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489248201 163 LDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGR 216
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-221 |
1.03e-50 |
|
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: 163.76 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 3 QVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDvhkLRQQT 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL--ASLSPKE---LARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 83 AMVFQnynlfknktalqnvtealitaqkkpkkeaeqigmdLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAIL 162
Cdd:cd03214 76 AYVPQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 163 LDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-217 |
1.54e-50 |
|
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: 164.50 E-value: 1.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaaSYSRKDVHKLRQQTAMVFQNYNLF 92
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGRAIPYLRRKIGVVFQDFRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 KNKTALQNVTEALITAQKKPKKEAEQIgMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDP 172
Cdd:cd03292 91 PDRNVYENVAFALEVTGVPPREIRKRV-PAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489248201 173 ELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:cd03292 170 DTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-226 |
4.66e-50 |
|
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: 171.87 E-value: 4.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAF--KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLrclNLLER---PDDGIIEIGDAKLnaASYSRKDvh 76
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLL---ALLLRfldPQSGSITLGGVDL--RDLDEDD-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 kLRQQTAMVFQNYNLFkNKTALQNVTEAlitaqkKPKKEAEQIgMDLLRQVGLEHKADSYP-----------ITMSGGQQ 145
Cdd:COG4987 407 -LRRRIAVVPQRPHLF-DTTLRENLRLA------RPDATDEEL-WAALERVGLGDWLAALPdgldtwlgeggRRLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 146 QRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMAfAREVADKVIFMADGRIIEQGTPEE 225
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV-LLITHRLA-GLERMDRILVLEDGRIVEQGTHEE 555
|
.
gi 489248201 226 L 226
Cdd:COG4987 556 L 556
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-225 |
5.43e-50 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 164.13 E-value: 5.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDVHK--- 77
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL--AAWSPWELARrra 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 78 -LRQQTAMVFQnynlFknkTALQNVteAL-ITAQKKPKKEAEQIGMDLLRQVGLEHKAD-SYPiTMSGGQQQRIGIARAL 154
Cdd:COG4559 79 vLPQHSSLAFP----F---TVEEVV--ALgRAPHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 155 A-------VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEE 225
Cdd:COG4559 149 AqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-239 |
1.14e-49 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 163.16 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLN-LLERPDDGIIEiGDAKLNAASYSRKDVHKLRQ 80
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNrLIELYPEARVS-GEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVTEAL-ITAQKKPKKEAEQIGMDLLRQVGL----EHKADSYPITMSGGQQQRIGIARALA 155
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLkLNRLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIaEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERT 235
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
....
gi 489248201 236 KKFI 239
Cdd:PRK14247 242 EKYV 245
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-216 |
1.29e-48 |
|
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: 159.91 E-value: 1.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAF-------KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEI--GDAKLNAASYS 71
Cdd:COG4778 4 LLEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 72 RKDVHKLRQQT-AMVFQNYNLFKNKTALQNVTEALItAQKKPKKEAEQIGMDLLRQVGL-EHKADSYPITMSGGQQQRIG 149
Cdd:COG4778 84 PREILALRRRTiGYVSQFLRVIPRVSALDVVAEPLL-ERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 150 IARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGR 216
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-226 |
1.65e-48 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 168.03 E-value: 1.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLrclNLLER---PDDGIIEIGDakLNAASYSRKDvhkLRQQTAMVFQNYNLF 92
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLV---NLLLRfydPTSGRILIDG--VDIRDLTLES---LRRQIGVVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 kNKTALQNVTEAlitaqkKPKKEAEQIgMDLLRQVGLEHKADSYP-----------ITMSGGQQQRIGIARALAVDPHAI 161
Cdd:COG1132 427 -SGTIRENIRYG------RPDATDEEV-EEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPIL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAeKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEEL 226
Cdd:COG1132 499 ILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEEL 561
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-226 |
2.23e-48 |
|
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: 167.63 E-value: 2.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkDVHKLRQQTAMVFQNYNLFKN 94
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL-----DPASWRRQIAWVPQNPYLFAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 kTALQNVTEAlitaqkKPKKEAEQIgMDLLRQVGLEHKADSYP-----------ITMSGGQQQRIGIARALAVDPHAILL 163
Cdd:COG4988 426 -TIRENLRLG------RPDASDEEL-EAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLL 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 164 DEPTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREvADKVIFMADGRIIEQGTPEEL 226
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRRLAKGRTV-ILITHRLALLAQ-ADRILVLDDGRIVEQGTHEEL 558
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-246 |
3.42e-47 |
|
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: 163.70 E-value: 3.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 8 RKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRC-LNLLerPDDGIIEIGDAKLNAasYSRKDVHKLRQQTAMVF 86
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLAlLRLI--PSEGEIRFDGQDLDG--LSRRALRPLRRRMQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 87 QN-YN-LFKNKTALQNVTEALITAQKKPKKEA-EQIGMDLLRQVGLEHKA-DSYPITMSGGQQQRIGIARALAVDPHAIL 162
Cdd:COG4172 369 QDpFGsLSPRMTVGQIIAEGLRVHGPGLSAAErRARVAEALEEVGLDPAArHRYPHEFSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 163 LDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIKQ 241
Cdd:COG4172 449 LDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAA 528
|
....*
gi 489248201 242 VGEPA 246
Cdd:COG4172 529 APLLE 533
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-239 |
5.20e-47 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 156.47 E-value: 5.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNlleRPDDGIIEI---GDAKLNAAS-YS-RKDV 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSIN---RMNDLNPEVtitGSIVYNGHNiYSpRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 76 HKLRQQTAMVFQNYNLFKnKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL-----EHKADSyPITMSGGQQQRIGI 150
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIwdevkDRLHDS-ALGLSGGQQQRVCI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 151 ARALAVDPHAILLDEPTSALDPeLVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDP-ISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
....*....
gi 489248201 231 QNERTKKFI 239
Cdd:PRK14239 239 KHKETEDYI 247
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-221 |
8.73e-47 |
|
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: 154.76 E-value: 8.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRhIRKAFKDLTvLDgIDLEIkSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasySRKDVHKLRQ 80
Cdd:cd03297 1 MLCVD-IEKRLPDFT-LK-IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD---SRKKINLPPQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 Q--TAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQigmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03297 74 QrkIGLVFQQYALFPHLNVRENLAFGLKRKRNREDRISVD---ELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03297 151 ELLLLDEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-242 |
9.46e-47 |
|
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: 158.04 E-value: 9.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 32 IIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVHklrqqtaMVFQNYNLFKNKTALQNVTEALiTAQKK 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHIN-------MVFQSYALFPHMTVEENVAFGL-KMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 112 PKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEK-QT 190
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489248201 191 TMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIKQV 242
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-239 |
2.34e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 155.64 E-value: 2.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 10 AFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAS-YSRKDVHKLRQQTAMVFQN 88
Cdd:PRK14271 30 GFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSiFNYRDVLEFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 89 YNLFKnKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL----EHKADSYPITMSGGQQQRIGIARALAVDPHAILLD 164
Cdd:PRK14271 110 PNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 165 EPTSALDPELVAGVLQVIKSIAEKqTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFI 239
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-216 |
5.30e-46 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 151.38 E-value: 5.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAF--KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkDVHKLR 79
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL-----DLESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNYNLFkNKTALQNVtealitaqkkpkkeaeqigmdllrqvglehkadsypitMSGGQQQRIGIARALAVDPH 159
Cdd:cd03228 76 KNIAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREvADKVIFMADGR 216
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTV-IVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-226 |
6.11e-46 |
|
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: 155.24 E-value: 6.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 9 KAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaklnaASYS-RKDVHKLRQQTAMVFQ 87
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARV-------AGYDvVREPRKVRRSIGIVPQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 88 NYNLFKNKTALQNVtEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:TIGR01188 74 YASVDEDLTGRENL-EMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPT 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 168 SALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:TIGR01188 153 TGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-239 |
6.38e-46 |
|
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: 160.24 E-value: 6.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKD----LTVLDGIDLEIKSGEVTAIIGPSGSGKS-TLLRCLNLLerPDDGIIEIGDAKLNAASYSRKDV 75
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLL--PDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 76 HKLRQ----QTAMVFQNynlfkNKTAL-------QNVTEALITAQKKPKKEAEQIGMDLLRQVGL---EHKADSYPITMS 141
Cdd:COG4172 84 RELRRirgnRIAMIFQE-----PMTSLnplhtigKQIAEVLRLHRGLSGAAARARALELLERVGIpdpERRLDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 142 GGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQ 220
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
250
....*....|....*....
gi 489248201 221 GTPEELFDNPQNERTKKFI 239
Cdd:COG4172 239 GPTAELFAAPQHPYTRKLL 257
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-234 |
9.93e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 154.08 E-value: 9.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLT-VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaaSYSRKDVHKLR 79
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI---KYDKKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNYN--LFKnKTALQNVTEALITAqKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:PRK13639 78 KTVGIVFQNPDdqLFA-PTVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNER 234
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-226 |
1.90e-45 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 151.50 E-value: 1.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDL--TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnaasYS-RKDVHKL 78
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING-------YSiRTDRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 79 RQQTAMVFQNYNLFKNKTALQNVteaLITAQKK--PKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHL---RFYARLKglPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAeKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-225 |
2.05e-45 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 152.62 E-value: 2.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDVHK--- 77
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPL--ADWSPAELARrra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 78 -LRQQTAMVFQnynlFknkTALQNVTEALITAQKkPKKEAEQIGMDLLRQVGLEHKAD-SYPiTMSGGQQQRIGIARALA 155
Cdd:PRK13548 80 vLPQHSSLSFP----F---TVEEVVAMGRAPHGL-SRAEDDALVAAALAQVDLAHLAGrDYP-QLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 156 ------VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEE 225
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERgLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-245 |
4.40e-45 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 152.48 E-value: 4.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLT--VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASysrkdVHKLR 79
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET-----VWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNY-NLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:PRK13635 81 RQVGMVFQNPdNQFVGATVQDDVAFGL-ENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQT-TMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELF---------- 227
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFksghmlqeig 238
|
250
....*....|....*....
gi 489248201 228 -DNPQNERTKKFIKQVGEP 245
Cdd:PRK13635 239 lDVPFSVKLKELLKRNGIL 257
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-221 |
5.90e-45 |
|
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: 149.95 E-value: 5.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 21 DLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklrqqtAMVFQNYNLFKNKTALQN 100
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPV-------SMLFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 101 VTEAL-----ITAQKKPKKEAeqigmdLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELV 175
Cdd:cd03298 91 VGLGLspglkLTAEDRQAIEV------ALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489248201 176 AGVLQ-VIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03298 165 AEMLDlVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-239 |
7.77e-45 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 151.15 E-value: 7.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLN-LLERPDDGIIEiGDAKLNAASYSRKDVH--KL 78
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrLLELNEEARVE-GEVRLFGRNIYSPDVDpiEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 79 RQQTAMVFQNYNLFKNKTALQNVTEAL-ITAQKKPKKEAEQIGMDLLRQVGL----EHKADSYPITMSGGQQQRIGIARA 153
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIGVkLNGLVKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 154 LAVDPHAILLDEPTSALDPELVAGVLQVIKSIaEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNE 233
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHE 242
|
....*.
gi 489248201 234 RTKKFI 239
Cdd:PRK14267 243 LTEKYV 248
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-236 |
8.66e-45 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 152.81 E-value: 8.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdAKLNAASYSRKDVHKLRQQTAMVFQN-Y-NLFKN 94
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYY--QGQDLLKADPEAQKLLRQKIQIVFQNpYgSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 KTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL--EHkADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDP 172
Cdd:PRK11308 109 KKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrpEH-YDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 173 ELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTK 236
Cdd:PRK11308 188 SVQAQVLNLMMDLqQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQ 252
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
8-231 |
1.39e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 151.33 E-value: 1.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 8 RKAFKDltvldgIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnAASYSRKDVHKLRQQTAMVFQ 87
Cdd:PRK13634 20 RRALYD------VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVI-TAGKKNKKLKPLRKKVGIVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 88 --NYNLFKNktalqnvtealiTAQKK----------PKKEAEQIGMDLLRQVGLEHKA-DSYPITMSGGQQQRIGIARAL 154
Cdd:PRK13634 93 fpEHQLFEE------------TVEKDicfgpmnfgvSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 155 AVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-229 |
1.81e-44 |
|
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: 149.12 E-value: 1.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKL-NAASYSRkdvhkLRQ 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItGLPPHER-----ARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTalqnVTEALITAQKKPKKEAEQIGMD-------LLRQVgLEHKADsypiTMSGGQQQRIGIARA 153
Cdd:cd03224 76 GIGYVPEGRRIFPELT----VEENLLLGAYARRRAKRKARLErvyelfpRLKER-RKQLAG----TLSGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 154 LAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDN 229
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-230 |
2.33e-44 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 152.57 E-value: 2.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklrqq 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDI------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 tAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:PRK11432 81 -CMVFQSYALFPHMSLGENVGYGL-KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-239 |
3.66e-44 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 149.60 E-value: 3.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKD---------LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSR 72
Cdd:COG4167 5 LEVRNLSKTFKYrtglfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 73 KDVHkLRqqtaMVFQNYNlfknkTAL---QNVTEAL-----ITAQKKPKKEAEQIgMDLLRQVGL--EHkADSYPITMSG 142
Cdd:COG4167 85 RCKH-IR----MIFQDPN-----TSLnprLNIGQILeeplrLNTDLTAEEREERI-FATLRLVGLlpEH-ANFYPHMLSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 143 GQQQRIGIARALAVDPHAILLDEPTSALDPELVAgvlQVIKSIAEKQTTM----IIVTHEMAFAREVADKVIFMADGRII 218
Cdd:COG4167 153 GQKQRVALARALILQPKIIIADEALAALDMSVRS---QIINLMLELQEKLgisyIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
250 260
....*....|....*....|.
gi 489248201 219 EQGTPEELFDNPQNERTKKFI 239
Cdd:COG4167 230 EYGKTAEVFANPQHEVTKRLI 250
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-239 |
6.77e-44 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 148.65 E-value: 6.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKL-NAASYSRK-DVHKLR 79
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFfNQNIYERRvNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNYNLFKnKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL----EHKADSYPITMSGGQQQRIGIARALA 155
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMAD-----GRIIEQGTPEELFDN 229
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNS 246
|
250
....*....|
gi 489248201 230 PQNERTKKFI 239
Cdd:PRK14258 247 PHDSRTREYV 256
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-168 |
1.49e-43 |
|
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: 144.33 E-value: 1.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasysRKDVHKLRQQTAMVFQNYNLFKNKT 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-----DDERKSLRKEIGYVFQDPQLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 97 ALQNVTEAL-ITAQKKPKKEAEQIgmDLLRQVGLEHKAD----SYPITMSGGQQQRIGIARALAVDPHAILLDEPTS 168
Cdd:pfam00005 76 VRENLRLGLlLKGLSKREKDARAE--EALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-226 |
3.39e-43 |
|
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: 145.59 E-value: 3.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGiieigdaKLNAASYS-RKDVHKLRQ 80
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG-------RATVAGHDvVREPREVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVteaLITA--QKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03265 74 RIGIVFQDLSVDDELTGWENL---YIHArlYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-217 |
1.34e-42 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 145.21 E-value: 1.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 4 VRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkdvhklRQQTA 83
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA----------REDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 84 MVFQNYNLFKNKTALQNVTEALitaQKKPKKEAEQIgmdlLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILL 163
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLGL---KGQWRDAALQA----LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 164 DEPTSALDPELVAGVLQVIKSIAEKQT-TMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-220 |
2.04e-42 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 145.00 E-value: 2.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAF----KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdvh 76
Cdd:COG4525 3 MLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 klrqqtAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:COG4525 79 ------GVVFQKDALLPWLNVLDNVAFGL-RLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 157 DPHAILLDEPTSALDP-------ELvagVLQViksIAEKQTTMIIVTHEMAFAREVADKVIFMAD--GRIIEQ 220
Cdd:COG4525 152 DPRFLLMDEPFGALDAltreqmqEL---LLDV---WQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVER 218
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-217 |
2.31e-42 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 143.32 E-value: 2.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLT----VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVH 76
Cdd:NF038007 1 MLNMQNAEKCYITKTiktkVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 KlRQQTAMVFQNYNLFKNKTALQNVTEALITaQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:NF038007 81 R-RELIGYIFQSFNLIPHLSIFDNVALPLKY-RGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAfAREVADKVIFMADGRI 217
Cdd:NF038007 159 NPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
9-230 |
4.37e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 145.76 E-value: 4.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 9 KAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSR-----------KDVHK 77
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHelitnpyskkiKNFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 78 LRQQTAMVFQ--NYNLFKNkTALQNVTEALItAQKKPKKEAEQIGMDLLRQVGLEHK-ADSYPITMSGGQQQRIGIARAL 154
Cdd:PRK13631 114 LRRRVSMVFQfpEYQLFKD-TIEKDIMFGPV-ALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 155 AVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-205 |
5.18e-42 |
|
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: 142.23 E-value: 5.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasysRKDVHKLRQ 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI------RDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVteALITAQKKPKKEAEQIgMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:COG4133 76 RLAYLGHADGLKPELTVRENL--RFWAALYGLRADREAI-DEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTH---EMAFAREV 205
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqplELAAARVL 200
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-243 |
1.56e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 143.40 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKD--LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDD---GIIEIGDAKLNAasysrKDVH 76
Cdd:PRK13640 6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTA-----KTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 KLRQQTAMVFQNY-NLFKNKTALQNVTEALITAQKkPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALA 155
Cdd:PRK13640 81 DIREKVGIVFQNPdNQFVGATVGDDVAFGLENRAV-PRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFArEVADKVIFMADGRIIEQGTPEELFDNPQner 234
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE--- 235
|
....*....
gi 489248201 235 tkkFIKQVG 243
Cdd:PRK13640 236 ---MLKEIG 241
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-226 |
3.78e-41 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 141.37 E-value: 3.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDakLNAASYSRKDVHK--- 77
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDG--LDVATTPSRELAKrla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 78 -LRQqtamvfqnynlfknktalQNVTEALIT------------AQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQ 144
Cdd:COG4604 79 iLRQ------------------ENHINSRLTvrelvafgrfpySKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 145 QQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTP 223
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTP 220
|
...
gi 489248201 224 EEL 226
Cdd:COG4604 221 EEI 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-218 |
4.47e-41 |
|
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: 138.33 E-value: 4.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSrkdvHKLRQQ 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR----DARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQnynlfknktalqnvtealitaqkkpkkeaeqigmdllrqvglehkadsypitMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03216 77 IAMVYQ----------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRII 218
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-226 |
7.08e-41 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 141.78 E-value: 7.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasysRKDVHKL-- 78
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-----PEDRRRIgy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 79 ----RqqtamvfqnyNLFKNKTalqnVTEALI-TAQKK--PKKEAEQIGMDLLRQVGLEHKADSyPI-TMSGGQQQRIGI 150
Cdd:COG4152 76 lpeeR----------GLYPKMK----VGEQLVyLARLKglSKAEAKRRADEWLERLGLGDRANK-KVeELSKGNQQKVQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 151 ARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-225 |
7.53e-41 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 147.95 E-value: 7.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAF----KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdAKLNAASYSRKDVH 76
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRV--AGQDVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 KLRQQT-AMVFQNYNLFKNKTALQNVTEALITAqKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALA 155
Cdd:PRK10535 82 QLRREHfGFIFQRYHLLSHLTAAQNVEVPAVYA-GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEE 225
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQE 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-231 |
7.58e-41 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 140.16 E-value: 7.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnaasysrKDVHKL-- 78
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG----------EDITHLpm 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 79 ----RQ------QTAMVFqnynlfKNKTALQNVtEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRI 148
Cdd:COG1137 73 hkraRLgigylpQEASIF------RKLTVEDNI-LAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 149 GIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEmafARE---VADKVIFMADGRIIEQGTPEE 225
Cdd:COG1137 146 EIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHN---VREtlgICDRAYIISEGKVLAEGTPEE 222
|
....*.
gi 489248201 226 LFDNPQ 231
Cdd:COG1137 223 ILNNPL 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-221 |
8.09e-41 |
|
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: 139.27 E-value: 8.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnaaSYSRKDVHKLRQQ 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG------KSYQKNIEALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVfQNYNLFKNKTALQNVtEALITAQKKPKKEAEQIgmdlLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03268 75 GALI-EAPGFYPNLTARENL-RLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-242 |
8.26e-41 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 144.41 E-value: 8.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 22 LEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDakLNAASYSRKDVHKLR-QQTAMVFQNYNLFKNKTALQN 100
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKISDAELREVRrKKIAMVFQSFALMPHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 101 VTEALITAqKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPeLVAGVLQ 180
Cdd:PRK10070 127 TAFGMELA-GINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP-LIRTEMQ 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 181 --VIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIKQV 242
Cdd:PRK10070 205 deLVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-230 |
1.22e-40 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 139.60 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKlRQQ 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-----TKLPMHK-RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVF--QNYNLFKNKTALQNVTEALITaQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPH 159
Cdd:cd03218 75 LGIGYlpQEASIFRKLTVEENILAVLEI-RGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEmafARE---VADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHN---VREtlsITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-221 |
1.24e-40 |
|
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: 138.82 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 11 FKDLTV-------LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnaasysrKDVHKLRQQTA 83
Cdd:cd03235 2 VEDLTVsygghpvLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG----------KPLEKERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 84 MVFQNYNLFKNK--TALQNVTEAL---ITAQKKPKKEAEQIGMDLLRQVGLEHKADsYPI-TMSGGQQQRIGIARALAVD 157
Cdd:cd03235 72 YVPQRRSIDRDFpiSVRDVVLMGLyghKGLFRRLSKADKAKVDEALERVGLSELAD-RQIgELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMaDGRIIEQG 221
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
17-239 |
1.62e-40 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 140.30 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLErpD-------DGIIEIGDAKLNAasySRKDVHKLRQQTAMVFQNY 89
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLN--DlipgfrvEGKVTFHGKNLYA---PDVDPVEVRRRIGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 90 NLFKnKTALQNVTEAlitaqkkPKKEAEQIGMD-----LLRQVGL----EHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:PRK14243 101 NPFP-KSIYDNIAYG-------ARINGYKGDMDelverSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEkQTTMIIVTHEMAFAREVADKVIFMA---------DGRIIEQGTPEELFDNPQ 231
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSPQ 251
|
....*...
gi 489248201 232 NERTKKFI 239
Cdd:PRK14243 252 QQATRDYV 259
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-239 |
2.87e-40 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 142.09 E-value: 2.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasysrkDVHKLRQQ 81
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-------DVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLFKNKTALQNVTEALITAQKKpKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAK-KEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 162 LLDEPTSALDPEL-VAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFI 239
Cdd:PRK11000 156 LLDEPLSNLDAALrVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFI 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-229 |
3.15e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 140.61 E-value: 3.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFK-----DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIE--IGDAKLNAASYSR-- 72
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNKKKTKEKek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 73 ---------------KDVHKLRQQTAMVFQ--NYNLFKnktalQNVTEALITAQKK---PKKEAEQIGMDLLRQVGL-EH 131
Cdd:PRK13651 83 vleklviqktrfkkiKKIKEIRRRVGVVFQfaEYQLFE-----QTIEKDIIFGPVSmgvSKEEAKKRAAKYIELVGLdES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 132 KADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIF 211
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIF 237
|
250
....*....|....*...
gi 489248201 212 MADGRIIEQGTPEELFDN 229
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSD 255
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
6.78e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 138.59 E-value: 6.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIrkAFK----DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasysRKDVH 76
Cdd:PRK13632 7 MIKVENV--SFSypnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS-----KENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 KLRQQTAMVFQNY-NLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALA 155
Cdd:PRK13632 80 EIRKKIGIIFQNPdNQFIGATVEDDIAFGL-ENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQT-TMIIVTHEMafaREV--ADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDM---DEAilADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-239 |
9.67e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 137.87 E-value: 9.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLN-LLERPDDGIIEIGDAKLNAASYSRKDVHKLRQQTAMVFQNYNL 91
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrLIEIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 92 FKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL----EHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489248201 168 SALDPELVAGVLQVIKSIaEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFI 239
Cdd:PRK14246 182 SMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-247 |
1.12e-39 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 137.84 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLL----ERPDDGIIEIGDAKLNAASYSRkDVH 76
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRTVQREGRLAR-DIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 KLRQQTAMVFQNYNLFKNKTALQNV-------TEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIG 149
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVligalgsTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 150 IARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVT-HEMAFAREVADKVIFMADGRIIEQGTPEElFD 228
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDGSSQQ-FD 241
|
250
....*....|....*....
gi 489248201 229 NPQNERTKKFIKQVGEPAE 247
Cdd:PRK09984 242 NERFDHLYRSINRVEENAK 260
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-227 |
1.48e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 138.37 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASySRKDVHKLRQQTAMVFQ--NYNLFKN 94
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKT-KDKYIRPVRKRIGMVFQfpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 ktalqNVTEALITAQKK---PKKEAEQIGMDLLRQVGLEHKA-DSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSAL 170
Cdd:PRK13646 102 -----TVEREIIFGPKNfkmNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 171 DPELVAGVLQVIKSIAEKQT-TMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF 227
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENkTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-226 |
1.91e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 142.46 E-value: 1.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYsrKDVHKLRq 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSP--RDAQAAG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 qTAMVFQNYNLFKNKTALQNV------TEALITAQKKPKKEAEQigmdLLRQVGLEHKADSyPI-TMSGGQQQRIGIARA 153
Cdd:COG1129 81 -IAIIHQELNLVPNLSVAENIflgrepRRGGLIDWRAMRRRARE----LLARLGLDIDPDT-PVgDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 154 LAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-218 |
3.33e-39 |
|
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: 135.08 E-value: 3.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkdvhKLRQQTAMVFQN--YNLF 92
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK--------ERRKSIGYVMQDvdYQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 KNktalqNVTEALITAQKKPKKEAEQIGmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDP 172
Cdd:cd03226 86 TD-----SVREELLLGLKELDAGNEQAE-TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489248201 173 ELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRII 218
Cdd:cd03226 160 KNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
3.36e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 137.29 E-value: 3.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLT-VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasYSRKDVHKLR 79
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID---YSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQ--NYNLFkNKTALQNVTEALITAQKkPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:PRK13636 82 ESVGMVFQdpDNQLF-SASVYQDVSFGAVNLKL-PEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF 227
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-227 |
4.31e-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: 135.98 E-value: 4.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGI-IEIGDAKLNAAsysrkDVHKLR 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGE-----DVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMV---FQNYNlfknkTALQNVTEALITA-------QKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIG 149
Cdd:COG1119 78 KRIGLVspaLQLRF-----PRDETVLDVVLSGffdsiglYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 150 IARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF 227
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAaEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-202 |
4.80e-39 |
|
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: 134.09 E-value: 4.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasYSRKDVHKLRQQTAMVFQNYN--LFK 93
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLD---YSRKGLLERRQRVGLVFQDPDdqLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 94 nKTALQNVTEALITAQKKPKkEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPE 173
Cdd:TIGR01166 84 -ADVDQDVAFGPLNLGLSEA-EVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180
....*....|....*....|....*....
gi 489248201 174 LVAGVLQVIKSIAEKQTTMIIVTHEMAFA 202
Cdd:TIGR01166 162 GREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-231 |
6.73e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 136.50 E-value: 6.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASySRKDVHKLRQQTAMVFQ--NYNLFKN 94
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPET-GNKNLKKLRKKVSLVFQfpEAQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 kTALQNVtealitaQKKPK------KEAEQIGMDLLRQVGL-EHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:PRK13641 102 -TVLKDV-------EFGPKnfgfseDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 168 SALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-242 |
9.89e-39 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 138.43 E-value: 9.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasysrkDVHKLRQ 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-------HVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:PRK11607 92 PINMMFQSYALFPHMTVEQNIAFGL-KQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGV-LQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFI 239
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
|
...
gi 489248201 240 KQV 242
Cdd:PRK11607 251 GSV 253
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-226 |
1.03e-38 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 134.32 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 21 DLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklrqqtAMVFQNYNLFKNKTALQN 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPV-------SMLFQENNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 101 VTEAL-----ITAQKKPKKEaeqigmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELV 175
Cdd:PRK10771 92 IGLGLnpglkLNAAQREKLH------AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489248201 176 AGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK10771 166 QEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-221 |
1.79e-38 |
|
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: 133.45 E-value: 1.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 21 DLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklrqqtAMVFQNYNLFKNKTALQN 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPV-------SMLFQENNLFAHLTVRQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 101 VTEALITAQKKPKKEAEQIgMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQ 180
Cdd:TIGR01277 91 IGLGLHPGLKLNAEQQEKV-VDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489248201 181 VIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:TIGR01277 170 LVKQLCsERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-217 |
1.83e-38 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 133.46 E-value: 1.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAF-KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDVHKLR 79
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDI--TRLKNREVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMdLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPH 159
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSA-ALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-235 |
2.20e-38 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 134.28 E-value: 2.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEI-----GDAKLNAASYSRKDv 75
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdgQLRDLYALSEAERR- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 76 HKLRQQTAMVFQN--YNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLE-HKADSYPITMSGGQQQRIGIAR 152
Cdd:PRK11701 85 RLLRTEWGFVHQHprDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKS-IAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQ 244
|
....
gi 489248201 232 NERT 235
Cdd:PRK11701 245 HPYT 248
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-231 |
3.39e-38 |
|
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: 133.18 E-value: 3.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKL-R 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI-----TGLPPHRIaR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNYNLFKNKTalqnVTEALITAQKkPKKEAEQIGMDLLRQVGLehkadsYPI----------TMSGGQQQRIG 149
Cdd:COG0410 78 LGIGYVPEGRRIFPSLT----VEENLLLGAY-ARRDRAEVRADLERVYEL------FPRlkerrrqragTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 150 IARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDN 229
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLAD 226
|
..
gi 489248201 230 PQ 231
Cdd:COG0410 227 PE 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-227 |
4.23e-38 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 133.78 E-value: 4.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKD---------LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYS 71
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDL--YQLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 72 RKDVHKLRQQTAMVFQN-YNLFK-NKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHK-ADSYPITMSGGQQQRI 148
Cdd:TIGR02769 80 RKQRRAFRRDVQLVFQDsPSAVNpRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEdADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 149 GIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF 227
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLL 239
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-227 |
5.86e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 134.09 E-value: 5.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASySRKDVHKLRQQTAMVFQ--NYNLFKnKTA 97
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS-KQKEIKPVRKKVGVVFQfpESQLFE-ETV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 98 LQNVTealITAQK--KPKKEAEQIGMDLLRQVGLEHKA-DSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPEL 174
Cdd:PRK13643 103 LKDVA---FGPQNfgIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489248201 175 VAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF 227
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-226 |
8.49e-38 |
|
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: 132.35 E-value: 8.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKD-LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKLRQ 80
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI-----REVTLDSLRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFkNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSY----PITMSGGQQQRIGIARALAV 156
Cdd:cd03253 76 AIGVVPQDTVLF-NDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIvgerGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMafaREV--ADKVIFMADGRIIEQGTPEEL 226
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTT-IVIAHRL---STIvnADKIIVLKDGRIVERGTHEEL 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-239 |
9.90e-38 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 132.97 E-value: 9.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEI-GDaklNAASYSRKDVHKLR 79
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGE---NIPAMSRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPH 159
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 160 AILLDEPTSALDPeLVAGVLqvIKSIAEKQ----TTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPqNERT 235
Cdd:PRK11831 164 LIMFDEPFVGQDP-ITMGVL--VKLISELNsalgVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRV 239
|
....
gi 489248201 236 KKFI 239
Cdd:PRK11831 240 RQFL 243
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-227 |
1.55e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 132.95 E-value: 1.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASySRKDVHKLRQQTAMVFQ--NYNLFKn 94
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTS-KNKDIKQIRKKVGLVFQfpESQLFE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 KTALQNVTealITAQK--KPKKEAEQIGMDLLRQVGL-EHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD 171
Cdd:PRK13649 101 ETVLKDVA---FGPQNfgVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 172 PELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF 227
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-219 |
1.68e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 132.50 E-value: 1.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 14 LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDVHKLRQQTAMVFQNYNLFK 93
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL--AKLNRAQRKAFRRDIQMVFQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 94 N--KTALQNVTEAL--ITAQKKPKKEAEQigMDLLRQVGL--EHkADSYPITMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:PRK10419 103 NprKTVREIIREPLrhLLSLDKAERLARA--SEMLRAVDLddSV-LDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489248201 168 SALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIE 219
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFgTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-225 |
3.90e-37 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 136.31 E-value: 3.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsySRKDVHKLRq 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIR--SPRDAIALG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 qTAMVFQNYNLFKNKTALQNV---TEALITAQKKPKKEAEQIgMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:COG3845 82 -IGMVHQHFMLVPNLTVAENIvlgLEPTKGGRLDRKAARARI-RELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEE 225
Cdd:COG3845 160 ARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-221 |
4.04e-37 |
|
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: 129.80 E-value: 4.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLT----VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdAKLNAAsysrKDVH 76
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV--DGFDVV----KEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 KLRQQTAMVFQNYNLFKNKTALQNVteaLITAQKKPKKEAEQIGM--DLLRQVGLEHKADSYPITMSGGQQQRIGIARAL 154
Cdd:cd03266 75 EARRRLGFVSDSTGLYDRLTARENL---EYFAGLYGLKGDELTARleELADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 155 AVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-215 |
6.49e-37 |
|
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: 129.89 E-value: 6.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdvhklrqqtAMVFQNYNLFKNKT 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR----------MVVFQNYSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 97 ALQNVTEALITAQKK-PKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPeLV 175
Cdd:TIGR01184 71 VRENIALAVDRVLPDlSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA-LT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489248201 176 AGVLQ--VIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADG 215
Cdd:TIGR01184 150 RGNLQeeLMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-221 |
6.58e-37 |
|
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: 129.32 E-value: 6.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdvhklrqq 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLFKNKTalqnVTEALI-TAQKK--PKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03269 72 IGYLPEERGLYPKMK----VIDQLVyLAQLKglKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-230 |
1.02e-36 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 132.66 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFK-DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklr 79
Cdd:PRK11650 3 GLKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDI---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 qqtAMVFQNYNLFKNKTALQNVTEALITAqKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPH 159
Cdd:PRK11650 79 ---AMVFQNYALYPHMSVRENMAYGLKIR-GMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 160 AILLDEPTSALDPEL-VAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRiIEQ-GTPEELFDNP 230
Cdd:PRK11650 155 VFLFDEPLSNLDAKLrVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV-AEQiGTPVEVYEKP 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-230 |
1.08e-36 |
|
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: 132.54 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasySRKDV----HKLRqqTAMVFQNYNLFKNK 95
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD---SRKGIflppEKRR--IGYVFQEARLFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 TALQNvteaLITAQKKPKKEAEQIGMD-LLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPEL 174
Cdd:TIGR02142 91 SVRGN----LRYGMKRARPSERRISFErVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 175 VAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:TIGR02142 167 KYEILPYLERLhAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-229 |
1.92e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 130.17 E-value: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklRQQTAMVFQ--NYNLFKN 94
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDI---RKKVGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 KTA------LQNVTEALITAQKKPKKEAEQIGMDLlrqvglEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTS 168
Cdd:PRK13637 100 TIEkdiafgPINLGLSEEEIENRVKRAMNIVGLDY------EDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489248201 169 ALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDN 229
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-228 |
2.56e-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: 2.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaaSYSRKdvhKLRQQTAMVFQNYNLFkNK 95
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR--DISRK---SLRSMIGVVLQDTFLF-SG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 TALQNVTEA-LITAQKKPKKEAEQIGMDLL---RQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD 171
Cdd:cd03254 92 TIMENIRLGrPNATDEEVIEAAKEAGAHDFimkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 172 PELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFD 228
Cdd:cd03254 172 TETEKLIQEALEKLMKGRTS-IIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
13-226 |
2.68e-36 |
|
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: 128.43 E-value: 2.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTllrCLNLLER---PDDGIIEIGDAKLNaasysRKDVHKLRQQTAMVFQNY 89
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERfydPTSGEILLDGVDIR-----DLNLRWLRSQIGLVSQEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 90 NLFkNKTALQNVtealitAQKKPKKEAEQIgMDLLRQ-------VGLEHKADS----YPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03249 87 VLF-DGTIAENI------RYGKPDATDEEV-EEAAKKanihdfiMSLPDGYDTlvgeRGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREvADKVIFMADGRIIEQGTPEEL 226
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTT-IVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDEL 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
12-245 |
2.99e-36 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 130.60 E-value: 2.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 12 KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL-NLLERPDDGIIEIGDAKLNAasySRKDVHKLRQQTAMVFQN-- 88
Cdd:PRK15079 32 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIiGLVKATDGEVAWLGKDLLGM---KDDEWRAVRSDIQMIFQDpl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 89 YNLFKNKTALQNVTEALITAQKK-PKKEAEQIGMDLLRQVGL-EHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEP 166
Cdd:PRK15079 109 ASLNPRMTIGEIIAEPLRTYHPKlSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 167 TSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIKQVGEP 245
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVPIP 268
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-222 |
4.29e-36 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 127.62 E-value: 4.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKdvHKLR-QQTAMVFQNYNLFKN 94
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAK--AELRnQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 KTALQNVTEALITAQKKPKkEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPEL 174
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPA-EINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489248201 175 VAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVaDKVIFMADGRIIEQGT 222
Cdd:PRK11629 181 ADSIFQLLGELNRLQgTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELS 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-231 |
1.37e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 127.56 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasysrKDVHKLRQQTAMVFQN-YNLFKNK 95
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD-----DNFEKLRKHIGIVFQNpDNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 TALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELV 175
Cdd:PRK13648 100 IVKYDVAFGL-ENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 176 AGVLQVIKSI-AEKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:PRK13648 179 QNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
13-227 |
1.44e-35 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 132.90 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkDVHKLRQQTAMVFQNYNLF 92
Cdd:TIGR02204 352 DQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQL-----DPAELRARMALVPQDPVLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 KNkTALQNV-------TEALITAQKKPKKEAEQIGmdllrqvGLEHKADSY----PITMSGGQQQRIGIARALAVDPHAI 161
Cdd:TIGR02204 427 AA-SVMENIrygrpdaTDEEVEAAARAAHAHEFIS-------ALPEGYDTYlgerGVTLSGGQRQRIAIARAILKDAPIL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIvTHEMAFAREvADKVIFMADGRIIEQGTPEELF 227
Cdd:TIGR02204 499 LLDEATSALDAESEQLVQQALETLMKGRTTLII-AHRLATVLK-ADRIVVMDQGRIVAQGTHAELI 562
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-226 |
1.72e-35 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 132.64 E-value: 1.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLrclNLLER---PDDGIIEIGDAKLNAasYSRKDvhkLRQQTAMVFQNYNLF 92
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLL---QLLTRawdPQQGEILLNGQPIAD--YSEAA---LRQAISVVSQRVHLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 kNKTALQNVTEAlitaqkKPKKEAEQIgMDLLRQVGLEHKADSYP----------ITMSGGQQQRIGIARALAVDPHAIL 162
Cdd:PRK11160 427 -SATLRDNLLLA------APNASDEAL-IEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 163 LDEPTSALDPELVAGVLQVIKSIAeKQTTMIIVTHEMaFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK11160 499 LDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-245 |
2.82e-35 |
|
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: 131.46 E-value: 2.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLE--RPDDGII--------------------- 58
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 59 -------EIGDAKLNAASYSRKDVHKLRQQTAMVFQ-NYNLFKNKTALQNVTEALITAQKkPKKEAEQIGMDLLRQVGLE 130
Cdd:TIGR03269 81 pcpvcggTLEPEEVDFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGY-EGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 131 HKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPE---LVAGVLqvIKSIAEKQTTMIIVTHEMAFAREVAD 207
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtakLVHNAL--EEAVKASGISMVLTSHWPEVIEDLSD 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 489248201 208 KVIFMADGRIIEQGTPEELfdnpqnerTKKFIKQVGEP 245
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEV--------VAVFMEGVSEV 267
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-221 |
3.22e-35 |
|
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: 124.61 E-value: 3.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGeVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasysRKDVHKLRQQ 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV------LKQPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLFKNKTALQNVtEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03264 74 IGYLPQEFGVYPNFTVREFL-DYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELGEDRIV-ILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-228 |
3.24e-35 |
|
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: 125.42 E-value: 3.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLrclNLLER---PDDGIIEIGDakLNAASYSRKDvhkLRQQTAMVFQNYNLF 92
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLV---NLIPRfydVDSGRILIDG--HDVRDYTLAS---LRRQIGLVSQDVFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 kNKTALQNVtealitAQKKPKKEAEQIgMDLLRQVGLEHKADSYP-----------ITMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03251 89 -NDTVAENI------AYGRPGATREEV-EEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFD 228
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTT-FVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-217 |
3.48e-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: 123.48 E-value: 3.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaaSYSRKDvhkLRQQTAMVFQNYNLFKNk 95
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS--QWDPNE---LGDHVGYLPQDDELFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 TALQNVtealitaqkkpkkeaeqigmdllrqvglehkadsypitMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELV 175
Cdd:cd03246 91 SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489248201 176 AGVLQVIKSIAEKQTTMIIVTHEMAFAREvADKVIFMADGRI 217
Cdd:cd03246 133 RALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-246 |
4.23e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 126.36 E-value: 4.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDG--IIEIGDAKLnaasysRKDVHKLRQQTAMVFQNYNlf 92
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGkvYVDGLDTSD------EENLWDIRNKAGMVFQNPD-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 kNKTALQNVTEALITAQKKPKKEAEQIGM---DLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSA 169
Cdd:PRK13633 96 -NQIVATIVEEDVAFGPENLGIPPEEIRErvdESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 170 LDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFdnPQNERTKKF---IKQVGEP 245
Cdd:PRK13633 175 LDPSGRREVVNTIKELNKKYgITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF--KEVEMMKKIgldVPQVTEL 251
|
.
gi 489248201 246 A 246
Cdd:PRK13633 252 A 252
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-225 |
7.85e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 123.75 E-value: 7.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLrcLNLLERPDDGIIEIGDAKLNAASYSRKDVHklRQ 80
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLL--AAIAGTLSPAFSASGEVLLNGRRLTALPAE--QR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVTEALitAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:COG4136 77 RIGILFQDDLLFPHLSVGENLAFAL--PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 161 ILLDEPTSALDPELVAGVLQ-VIKSIAEKQTTMIIVTHEMAFARevadkvifmADGRIIEQGTPEE 225
Cdd:COG4136 155 LLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEEDAP---------AAGRVLDLGNWQH 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-226 |
1.83e-34 |
|
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: 129.15 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIE--IGDAKLNAASYSRKDVHKLRQQTAMVFQNYNLFKN 94
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEWVDMTKPGPDGRGRAKRYIGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 KTALQNVTEALitAQKKPKKEAEQIGMDLLRQVGLEHKA-----DSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSA 169
Cdd:TIGR03269 380 RTVLDNLTEAI--GLELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 170 LDPELVAGVLQVI-KSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:TIGR03269 458 MDPITKVDVTHSIlKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-212 |
3.17e-34 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 128.56 E-value: 3.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkDVHKLRQQTAMVFQNYNLFkNK 95
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA-----DADSWRDQIAWVPQHPFLF-AG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 TALQNVTEALITAQKKPKKEA-EQIGMDLLRQV---GLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD 171
Cdd:TIGR02857 411 TIAENIRLARPDASDAEIREAlERAGLDEFVAAlpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489248201 172 PELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREvADKVIFM 212
Cdd:TIGR02857 491 AETEAEVLEALRALAQGRTV-LLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-227 |
5.73e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 123.30 E-value: 5.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLT---VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHK 77
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL-----TEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 78 LRQQTAMVFQNY-NLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:PRK13650 79 IRHKIGMVFQNPdNQFVGATVEDDVAFGL-ENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMafaREVA--DKVIFMADGRIIEQGTPEELF 227
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDL---DEVAlsDRVLVMKNGQVESTSTPRELF 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
13-229 |
5.85e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 123.58 E-value: 5.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVHKLRQQTAMVFQ--NYN 90
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 91 LFKNkTALQNVTEALITAQKKpKKEAEQIGMDLLRQVGL-EHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSA 169
Cdd:PRK13645 103 LFQE-TIEKDIAFGPVNLGEN-KQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 170 LDPELVAGVLQVIKSIAEKQTTMII-VTHEMAFAREVADKVIFMADGRIIEQGTPEELFDN 229
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIImVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-228 |
6.28e-34 |
|
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: 128.30 E-value: 6.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAF--KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLrclNLLER---PDDGIIEIGDAKLnaASYSRKDvh 76
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLV---NLIPRfyePDSGQILLDGHDL--ADYTLAS-- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 kLRQQTAMVFQNYNLFkNKTALQNVT-EALITAQKKPKKEAEQIG--MDLLRQV--GLEHKADSYPITMSGGQQQRIGIA 151
Cdd:TIGR02203 404 -LRRQVALVSQDVVLF-NDTIANNIAyGRTEQADRAEIERALAAAyaQDFVDKLplGLDTPIGENGVLLSGGQRQRLAIA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 152 RALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIvTHEMAfAREVADKVIFMADGRIIEQGTPEELFD 228
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVI-AHRLS-TIEKADRIVVMDDGRIVERGTHNELLA 556
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-228 |
1.46e-33 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 121.44 E-value: 1.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkDVHKLRQQTAMVFQNYNLFkNK 95
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA-----DPAWLRRQVGVVLQENVLF-NR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 TALQNVTEALITAQKKPKKEAEQIG--MDLLRQV--GLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD 171
Cdd:cd03252 91 SIRDNIALADPGMSMERVIEAAKLAgaHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 172 PELVAGVLQVIKSIAEKQtTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFD 228
Cdd:cd03252 171 YESEHAIMRNMHDICAGR-TVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-228 |
2.25e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 121.77 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLT-VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasysrKDVHKLRQ 80
Cdd:PRK13647 5 IEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA-----ENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYN--LFKNkTALQNVTEALITaQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:PRK13647 80 KVGLVFQDPDdqVFSS-TVWDDVAFGPVN-MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFD 228
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-230 |
2.93e-33 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 120.87 E-value: 2.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIeigdaKLNAASYSRKDVHKL-R 79
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI-----LLRGQHIEGLPGHQIaR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNYNLFKNKTALQNvteaLITAQ-------------KKPK-KEAEQIGMDL----LRQVGLEHKADSYPITMS 141
Cdd:PRK11300 80 MGVVRTFQHVRLFREMTVIEN----LLVAQhqqlktglfsgllKTPAfRRAESEALDRaatwLERVGLLEHANRQAGNLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 142 GGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQ 220
Cdd:PRK11300 156 YGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN 235
|
250
....*....|
gi 489248201 221 GTPEELFDNP 230
Cdd:PRK11300 236 GTPEEIRNNP 245
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-230 |
4.64e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 120.86 E-value: 4.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLT-VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdAKLNAASYSRkdVHKLR 79
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV--SGIDTGDFSK--LQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQN-YNLFKNKTALQNVT---EALITAQKKPKKEAEQIgmdlLRQVGLEHKADSYPITMSGGQQQRIGIARALA 155
Cdd:PRK13644 77 KLVGIVFQNpETQFVGRTVEEDLAfgpENLCLPPIEIRKRVDRA----LAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAfAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-242 |
6.55e-33 |
|
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: 119.94 E-value: 6.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEI---GDAKLNAASYSRKDVHK 77
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAELELYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 78 L-RQQTAMVFQNY--NLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLE-HKADSYPITMSGGQQQRIGIARA 153
Cdd:TIGR02323 83 LmRTEWGFVHQNPrdGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQIARN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 154 LAVDPHAILLDEPTSALDPELVAGVLQVIKS-IAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQN 232
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLDVSVQARLLDLLRGlVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQH 242
|
250
....*....|
gi 489248201 233 ERTKKFIKQV 242
Cdd:TIGR02323 243 PYTQLLVSSI 252
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-236 |
8.71e-33 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 119.80 E-value: 8.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAfKDLTVLDGIDLEIKSGEVTAIIGPSGSGKStlLRCLNLLERPDDGIIEIG-----DAKLNAASysrkdvh 76
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAgrvllDGKPVAPC------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 KLRQQT-AMVFQN----YNLFKNKTAlqnvtEALITAQKKPKKEAEQIGMDLLRQVGLEHKA---DSYPITMSGGQQQRI 148
Cdd:PRK10418 75 ALRGRKiATIMQNprsaFNPLHTMHT-----HARETCLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 149 GIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTT-MIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF 227
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
....*....
gi 489248201 228 DNPQNERTK 236
Cdd:PRK10418 230 NAPKHAVTR 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-239 |
9.58e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 124.43 E-value: 9.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 15 TVLDGIDLEIKSGEVTAIIGPSGSGKST----LLRCLNllerpDDGIIEIGDAKLNaaSYSRKDVHKLRQQTAMVFQNYN 90
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLH--NLNRRQLLPVRHRIQVVFQDPN 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 91 LFKNK--TALQNVTEALITAQKK-PKKEAEQIGMDLLRQVGLEhkADS---YPITMSGGQQQRIGIARALAVDPHAILLD 164
Cdd:PRK15134 373 SSLNPrlNVLQIIEEGLRVHQPTlSAAQREQQVIAVMEEVGLD--PETrhrYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 165 EPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFI 239
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-228 |
3.12e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 119.52 E-value: 3.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASysrkdvHKLRQQ 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA------RHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLFKNKTALQNVteaLITAQ--KKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPH 159
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENL---LVFGRyfGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFD 228
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-242 |
4.45e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 117.81 E-value: 4.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKdvhKLRQ 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI--SMLSSR---QLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQnynlfknktalQNVTEALITAQK--------------KPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQ 146
Cdd:PRK11231 77 RLALLPQ-----------HHLTPEGITVRElvaygrspwlslwgRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 147 RIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
250
....*....|....*.
gi 489248201 227 FdnpqnerTKKFIKQV 242
Cdd:PRK11231 226 M-------TPGLLRTV 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
8-221 |
5.72e-32 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 116.99 E-value: 5.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 8 RKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLrclNLLE-RPDDGIIEIGDAKLNAASYSRkdvHKLRQQTAMVF 86
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLL---DAISgRVEGGGTTSGQILFNGQPRKP---DQFQKCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 87 QNYNLFKNKTALQNVTEALI------TAQKKPKKEAEQIGmdlLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:cd03234 88 QDDILLPGLTVRETLTYTAIlrlprkSSDAIRKKRVEDVL---LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEM---AFarEVADKVIFMADGRIIEQG 221
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPrsdLF--RLFDRILLLSSGEIVYSG 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-221 |
9.26e-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: 116.15 E-value: 9.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAklnaaSYSRKDVHKLRQQTAMVFQNYNLFK-- 93
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT-----DIRQLDPADLRRNIGYVPQDVTLFYgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 94 ---NKT-ALQNVTEALIT-----------AQKKPKkeaeqiGMDLlrQVGlEHKADsypitMSGGQQQRIGIARALAVDP 158
Cdd:cd03245 94 lrdNITlGAPLADDERILraaelagvtdfVNKHPN------GLDL--QIG-ERGRG-----LSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEkQTTMIIVTHEMAFArEVADKVIFMADGRIIEQG 221
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
17-247 |
1.11e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 118.69 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKS-TLLRCLNLLERPddgiieiGDAKLNAASYSRKDVHKL----RQQ-----TAMVF 86
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP-------GRVMAEKLEFNGQDLQRIsekeRRNlvgaeVAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 87 QN--YNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL---EHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:PRK11022 96 QDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQT-TMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIK 240
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLR 255
|
....*..
gi 489248201 241 QVGEPAE 247
Cdd:PRK11022 256 ALPEFAQ 262
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-226 |
1.65e-31 |
|
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: 115.70 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 3 QVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNA-ASYSRkdvhkLRQQ 81
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKlPPHER-----ARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLFKNKTALQNVtealitaqkkpkkeaeQIGMDLLRQVGLEHKADSY---PITM----------SGGQQQRI 148
Cdd:TIGR03410 77 IAYVPQGREIFPRLTVEENL----------------LTGLAALPRRSRKIPDEIYelfPVLKemlgrrggdlSGGQQQQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 149 GIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:TIGR03410 141 AIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRaEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-219 |
4.58e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 115.18 E-value: 4.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdvhklrq 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 qtAMVFQNYNLFKNKTALQNVTEALITAqKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:PRK11248 73 --GVVFQNEGLLPWRNVQDNVAFGLQLA-GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 161 ILLDEPTSALDP----ELVAGVLQVIKSIAeKQTTMIivTHEMAFAREVADKVIFMA--DGRIIE 219
Cdd:PRK11248 150 LLLDEPFGALDAftreQMQTLLLKLWQETG-KQVLLI--THDIEEAVFMATELVLLSpgPGRVVE 211
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-226 |
5.48e-31 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 120.07 E-value: 5.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLlrcLNLLER---PDDGIIEIgDAkLNAASYSRKdvhKLRQQTAMVFQNYNLFk 93
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRvfdPQSGRILI-DG-TDIRTVTRA---SLRRNIAVVFQDAGLF- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 94 NKTALQN------------VTEALITAQ------KKPKKEAEQIGmdllrQVGLEhkadsypitMSGGQQQRIGIARALA 155
Cdd:PRK13657 422 NRSIEDNirvgrpdatdeeMRAAAERAQahdfieRKPDGYDTVVG-----ERGRQ---------LSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIvTHEMAFAREvADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMKGRTTFII-AHRLSTVRN-ADRILVFDNGRVVESGSFDEL 556
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
16-226 |
6.00e-31 |
|
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: 120.23 E-value: 6.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkDVHKLRQQTAMVFQNYNLFkNK 95
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIA-----DPAWLRRQMGVVLQENVLF-SR 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 TALQNVT--------EALITAQKKPKKEAEQIGmdlLRQvGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:TIGR01846 546 SIRDNIAlcnpgapfEHVIHAAKLAGAHDFISE---LPQ-GYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEAT 621
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 168 SALDPELVAGVLQVIKSIAeKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEEL 226
Cdd:TIGR01846 622 SALDYESEALIMRNMREIC-RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEEL 678
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
16-228 |
8.16e-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: 119.97 E-value: 8.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDakLNAASYSRKDvhkLRQQTAMVFQNYNLFkNK 95
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDG--VDIRQIDPAD---LRRNIGYVPQDPRLF-YG 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 TALQNVT--------EALITAqkkpkkeAEQIGM-DLLRQ--VGLEHkadsyPIT-----MSGGQQQRIGIARALAVDPH 159
Cdd:TIGR03375 554 TLRDNIAlgapyaddEEILRA-------AELAGVtEFVRRhpDGLDM-----QIGergrsLSGGQRQAVALARALLRDPP 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQtTMIIVTHEMAFArEVADKVIFMADGRIIEQGTPEELFD 228
Cdd:TIGR03375 622 ILLLDEPTSAMDNRSEERFKDRLKRWLAGK-TLVLVTHRTSLL-DLVDRIIVMDNGRIVADGPKDQVLE 688
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-221 |
1.19e-30 |
|
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: 112.26 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 12 KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNllERPDDGIIEiGDAKLNAASYSRKdvhKLRQQTAMVFQNYNL 91
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA--GRRTGLGVS-GEVLINGRPLDKR---SFRKIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 92 FKNKTalqnVTEAL-ITAQkkpkkeaeqigmdlLRQVglehkadsypitmSGGQQQRIGIARALAVDPHAILLDEPTSAL 170
Cdd:cd03213 94 HPTLT----VRETLmFAAK--------------LRGL-------------SGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489248201 171 DPELVAGVLQVIKSIAEKQTTMIIVTHE-MAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03213 143 DSSSALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-221 |
1.28e-30 |
|
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: 112.02 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAF--KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRclnLLER---PDDGIIEIGDAKLNAASYSrkdvh 76
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQ---LLTGdlkPQQGEITLDGVPVSDLEKA----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 kLRQQTAMVFQNYNLFkNKTALQNVTEALitaqkkpkkeaeqigmdllrqvglehkadsypitmSGGQQQRIGIARALAV 156
Cdd:cd03247 73 -LSSLISVLNQRPYLF-DTTLRNNLGRRF-----------------------------------SGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAEKQtTMIIVTHEMAfAREVADKVIFMADGRIIEQG 221
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK-TLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-229 |
1.43e-30 |
|
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: 113.26 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIeigdaKLNAASYSRKDVHKLrqq 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEI-----IFDGHPWTRKDLHKI--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 tAMVFQNYNLFKNKTALQNVtEALITAQKKPKKEAEQIgmdlLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:TIGR03740 73 -GSLIESPPLYENLTARENL-KVHTTLLGLPDSRIDEV----LNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTP------EELFDN 229
Cdd:TIGR03740 147 ILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKInksenlEKLFVE 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-230 |
2.19e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 116.48 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGD---AKLNAASYSRKdVHK 77
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvEALSARAASRR-VAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 78 LRQQTAMVFQnynlFKNKTALQnVTEALITAQKKPKKEAEQIGMD-LLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:PRK09536 82 VPQDTSLSFE----FDVRQVVE-MGRTPHRSRFDTWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-230 |
2.97e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 118.29 E-value: 2.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTllrCLNLLER---PDDGIIEIGDAKLnaasySRKDVHKLRQQTAMVFQNY 89
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNlyqPTGGQVLLDGVPL-----VQYDHHYLHRQVALVGQEP 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 90 NLFkNKTALQNVTEALitaQKKPKKE----AEQIGMDLLRQvGLEHKADS----YPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:TIGR00958 565 VLF-SGSVRENIAYGL---TDTPDEEimaaAKAANAHDFIM-EFPNGYDTevgeKGSQLSGGQKQRIAIARALVRKPRVL 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 162 LLDEPTSALDPElVAGVLQVIKSIAEKqtTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:TIGR00958 640 ILDEATSALDAE-CEQLLQESRSRASR--TVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-234 |
3.84e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 112.68 E-value: 3.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 9 KAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGD---AKLNAASYSRKDVHKLRQQtAMV 85
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDediSLLPLHARARRGIGYLPQE-ASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 86 FQNYNLFKNKTALQNVTEALITAQKKPKKEaeqigmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDE 165
Cdd:PRK10895 90 FRRLSVYDNLMAVLQIRDDLSAEQREDRAN------ELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 166 PTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNER 234
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-225 |
4.58e-30 |
|
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: 117.16 E-value: 4.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDVHK----LRQQTAM----VFQ 87
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL--SQWDREELGRhigyLPQDVELfdgtIAE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 88 NYNLFKNKTAlQNVTEALITA------QKKPKKEAEQIGMDLLRqvglehkadsypitMSGGQQQRIGIARALAVDPHAI 161
Cdd:COG4618 425 NIARFGDADP-EKVVAAAKLAgvhemiLRLPDGYDTRIGEGGAR--------------LSGGQRQRIGLARALYGDPRLV 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAfAREVADKVIFMADGRIIEQGTPEE 225
Cdd:COG4618 490 VLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
5.29e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 112.97 E-value: 5.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFK-DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaklNAASYSRKDVHKLR 79
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLI-----RGEPITKENIREVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNYN--LFkNKTALQNVTEALITAQKKPKKEAEQIGmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:PRK13652 78 KFVGLVFQNPDdqIF-SPTVEQDIAFGPINLGLDEETVAHRVS-SALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-226 |
1.23e-29 |
|
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: 116.46 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRclnLLER---PDDGIIEIGDAKLnaasysrKDV--HKLRQQTAMVFQNY 89
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLAR---LLFRfydVTSGRILIDGQDI-------RDVtqASLRAAIGIVPQDT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 90 NLFkNKTALQNV-------TEALITAQKKpkkeAEQIGmDLLRQV--GLEhkadsypiTM--------SGGQQQRIGIAR 152
Cdd:COG5265 442 VLF-NDTIAYNIaygrpdaSEEEVEAAAR----AAQIH-DFIESLpdGYD--------TRvgerglklSGGEKQRVAIAR 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMII------VTHemafarevADKVIFMADGRIIEQGTPEEL 226
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIahrlstIVD--------ADEILVLEAGRIVERGTHAEL 579
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-227 |
1.34e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 112.02 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 11 FKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasYSRKDVHKLRQQTAMVFQN-- 88
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD---YSKRGLLALRQQVATVFQDpe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 89 ----YNLFKNKTA--LQN--VTEALITaqkKPKKEAeqigMDLLRQVGLEHKadsyPIT-MSGGQQQRIGIARALAVDPH 159
Cdd:PRK13638 88 qqifYTDIDSDIAfsLRNlgVPEAEIT---RRVDEA----LTLVDAQHFRHQ----PIQcLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF 227
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-226 |
1.98e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 115.71 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 12 KDLTVL--DG------IDLEIKSGEVTAIIGPSGSGKSTLLrclNLLE--RPDDGIIEIGDAKLNAAsysrkDVHKLRQQ 81
Cdd:PRK11174 353 EDLEILspDGktlagpLNFTLPAGQRIALVGPSGAGKTSLL---NALLgfLPYQGSLKINGIELREL-----DPESWRKH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLFKNkTALQNVTEAlitaqkKPKKEAEQIgMDLLRQV-----------GLEHKADSYPITMSGGQQQRIGI 150
Cdd:PRK11174 425 LSWVGQNPQLPHG-TLRDNVLLG------NPDASDEQL-QQALENAwvseflpllpqGLDTPIGDQAAGLSVGQAQRLAL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 151 ARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREVaDKVIFMADGRIIEQGTPEEL 226
Cdd:PRK11174 497 ARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTT-LMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAEL 570
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-228 |
2.10e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 113.00 E-value: 2.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdvhklRQQ 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA------RAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLFKNKTALQNVteaLITAQ--KKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPH 159
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENL---LVFGRyfGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFD 228
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-248 |
2.84e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 114.80 E-value: 2.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFK----DLTVLDGIDLEIKSGEVTAIIGPSGSGKS-TLLRCLNLLERPDdGIIEIGDAKLNAASYSRKDV 75
Cdd:PRK15134 5 LLAIENLSVAFRqqqtVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPP-VVYPSGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 76 HKLRQ----QTAMVFQNYNLFKNktALQNVTEAL---ITAQKKPKKEAEQIGM-DLLRQVGLEHKA---DSYPITMSGGQ 144
Cdd:PRK15134 84 QTLRGvrgnKIAMIFQEPMVSLN--PLHTLEKQLyevLSLHRGMRREAARGEIlNCLDRVGIRQAAkrlTDYPHQLSGGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 145 QQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTP 223
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRA 241
|
250 260
....*....|....*....|....*..
gi 489248201 224 EELFDNPQNERTKKFI--KQVGEPAEL 248
Cdd:PRK15134 242 ATLFSAPTHPYTQKLLnsEPSGDPVPL 268
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-242 |
4.55e-29 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 114.76 E-value: 4.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPddGIIEIGDAKLNAasySRKDVHKLRQQTAMVFQNYNLFKN 94
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLLNG---MPIDAKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 KTALqnvtEALI-TAQKK-----PKKEAEQIGMDLLRQVGLEHKADS---YPITM---SGGQQQRIGIARALAVDPHAIL 162
Cdd:TIGR00955 114 LTVR----EHLMfQAHLRmprrvTKKEKRERVDEVLQALGLRKCANTrigVPGRVkglSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 163 LDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHE-MAFAREVADKVIFMADGRIIEQGTPEEL---FDN-----PQNE 233
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAvpfFSDlghpcPENY 269
|
....*....
gi 489248201 234 RTKKFIKQV 242
Cdd:TIGR00955 270 NPADFYVQV 278
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-230 |
6.02e-29 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 111.35 E-value: 6.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFK----DLTVLDGIDLEIKSGEVTAIIGPSGSGKS-TLLRCLNLLERpdDGIIEiGDAKLNAA---SYSR 72
Cdd:PRK09473 12 LLDVKDLRVTFStpdgDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAA--NGRIG-GSATFNGReilNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 73 KDVHKLR-QQTAMVFQNynlfkNKTAL-------QNVTEALITAQKKPKKEA--EQIGM-DLLRQVGLEHKADSYPITMS 141
Cdd:PRK09473 89 KELNKLRaEQISMIFQD-----PMTSLnpymrvgEQLMEVLMLHKGMSKAEAfeESVRMlDAVKMPEARKRMKMYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 142 GGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQ 220
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 243
|
250
....*....|
gi 489248201 221 GTPEELFDNP 230
Cdd:PRK09473 244 GNARDVFYQP 253
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-239 |
1.77e-28 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 108.72 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVL---------DGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYS 71
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWfrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 72 RKDvhklrQQTAMVFQNynlfkNKTAL---QNVTEAL-----ITAQKKPKKEAEQIgMDLLRQVGL--EHkADSYPITMS 141
Cdd:PRK15112 84 YRS-----QRIRMIFQD-----PSTSLnprQRISQILdfplrLNTDLEPEQREKQI-IETLRQVGLlpDH-ASYYPHMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 142 GGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIEQ 220
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
250
....*....|....*....
gi 489248201 221 GTPEELFDNPQNERTKKFI 239
Cdd:PRK15112 232 GSTADVLASPLHELTKRLI 250
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-218 |
2.19e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 108.25 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTV-----LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDV 75
Cdd:COG1101 1 MLELKNLSKTFNPGTVnekraLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-----TKLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 76 HKLRQQTAMVFQN------YNLfknkTALQNvteaLITAQKKPKKEAEQIGM---------DLLRQV--GLEHKADSyPI 138
Cdd:COG1101 76 YKRAKYIGRVFQDpmmgtaPSM----TIEEN----LALAYRRGKRRGLRRGLtkkrrelfrELLATLglGLENRLDT-KV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 139 -TMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGR 216
Cdd:COG1101 147 gLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
..
gi 489248201 217 II 218
Cdd:COG1101 227 II 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-210 |
2.56e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 106.16 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 10 AFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVHK-----LRQQTAM 84
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDslpltVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 85 -VFQNYNLFKNKTAL--QNVTEALitaqkkpkkeaEQIGMDLL--RQVGlehkadsypiTMSGGQQQRIGIARALAVDPH 159
Cdd:NF040873 81 gRWARRGLWRRLTRDdrAAVDDAL-----------ERVGLADLagRQLG----------ELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREvADKVI 210
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCV 189
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-220 |
2.72e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 107.17 E-value: 2.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAF----KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLerpDDGiiEIGDAKLNAASYSRKDVH 76
Cdd:PRK10584 6 IVEVHHLKKSVgqgeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGL---DDG--SSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 ---KLR-QQTAMVFQNYNLFKNKTALQNVT-EALITAQKKpkKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIA 151
Cdd:PRK10584 81 araKLRaKHVGFVFQSFMLIPTLNALENVElPALLRGESS--RQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 152 RALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREvADKVIFMADGRIIEQ 220
Cdd:PRK10584 159 RAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-219 |
4.96e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.31 E-value: 4.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaKLNAASYSrkdvhklrQ 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE-TVKIGYFD--------Q 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAmvfqnyNLFKNKTALQNVTEAlitAQKKPKKEAEQI-------GMDLLRQVGlehkadsypiTMSGGQQQRIGIARA 153
Cdd:COG0488 386 HQE------ELDPDKTVLDELRDG---APGGTEQEVRGYlgrflfsGDDAFKPVG----------VLSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 154 LAVDPHAILLDEPTSALDPElvagVLQVIKS-IAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIE 219
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIE----TLEALEEaLDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-232 |
6.44e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.49 E-value: 6.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasysrKDVHKLRQQTAMVFQNY-NL 91
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA-----ENVWNLRRKIGMVFQNPdNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 92 FKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD 171
Cdd:PRK13642 94 FVGATVEDDVAFGM-ENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489248201 172 PELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFDNPQN 232
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
15-226 |
1.41e-27 |
|
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: 110.13 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaaSYSRKDVHK----LRQQTAM----VF 86
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK--QWDRETFGKhigyLPQDVELfpgtVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 87 QNYNLFKNKTALQNVTEALITAQKKpkkeaEQIgmdllrqVGLEHKADSY----PITMSGGQQQRIGIARALAVDPHAIL 162
Cdd:TIGR01842 410 ENIARFGENADPEKIIEAAKLAGVH-----ELI-------LRLPDGYDTVigpgGATLSGGQRQRIALARALYGDPKLVV 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 163 LDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAfAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEV 540
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-229 |
3.08e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 108.98 E-value: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdVHKLrq 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK--AHQL-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEqigmdLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:PRK15439 87 GIYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQ-----LLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDN 229
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-226 |
1.18e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 103.91 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaaSYSRKDVHKlrqQTAMVFQNYNLFKN 94
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ--HYASKEVAR---RIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 KTALQNVTEALITAQ---KKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD 171
Cdd:PRK10253 96 ITVQELVARGRYPHQplfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 172 PELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK10253 176 ISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-226 |
2.77e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 106.64 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAF--KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLrclNLLERPDDgiIEIGDAKLNAASYSRKDVHKLR 79
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIA---NLLTRFYD--IDEGEILLDGHDLRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTAMVFQNYNLFkNKTALQNVTEAlitaqKKPKKEAEQI--------GMDLLRQvgLEHKADSY----PITMSGGQQQR 147
Cdd:PRK11176 417 NQVALVSQNVHLF-NDTIANNIAYA-----RTEQYSREQIeeaarmayAMDFINK--MDNGLDTVigenGVLLSGGQRQR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 148 IGIARALAVDPHAILLDEPTSALDPElVAGVLQVIKSIAEKQTTMIIVTHEMAfAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTE-SERAIQAALDELQKNRTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAEL 565
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-242 |
4.38e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 106.09 E-value: 4.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKD----LTVLDGIDLEIKSGEVTAIIGPSGSGKS----TLLRCLN-----------LLERPDDGIIEIG 61
Cdd:PRK10261 12 VLAVENLNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEqagglvqcdkmLLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 62 DaklnaasYSRKDVHKLR-QQTAMVFQNYNLFKNK--TALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL-EHKA--DS 135
Cdd:PRK10261 92 E-------QSAAQMRHVRgADMAMIFQEPMTSLNPvfTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIpEAQTilSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 136 YPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKsIAEKQTTM--IIVTHEMAFAREVADKVIFMA 213
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIK-VLQKEMSMgvIFITHDMGVVAEIADRVLVMY 243
|
250 260
....*....|....*....|....*....
gi 489248201 214 DGRIIEQGTPEELFDNPQNERTKKFIKQV 242
Cdd:PRK10261 244 QGEAVETGSVEQIFHAPQHPYTRALLAAV 272
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-228 |
5.27e-26 |
|
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: 105.98 E-value: 5.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEigdakLNAASYSRKDVHKLRQQTAMVFQNYNLF--- 92
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIL-----LNGFSLKDIDRHTLRQFINYLPQEPYIFsgs 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 ---------KNKTALQNVTEALITAQKKpkKEAEQIgmdllrQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILL 163
Cdd:TIGR01193 564 ilenlllgaKENVSQDEIWAACEIAEIK--DDIENM------PLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLIL 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 164 DEPTSALDPELVAGVLQVIKSIAEKqtTMIIVTHEMAFAREVaDKVIFMADGRIIEQGTPEELFD 228
Cdd:TIGR01193 636 DESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLD 697
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-217 |
6.24e-26 |
|
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: 101.01 E-value: 6.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTllrCLNLLER---PDDGIIEIGDAKLNAasYSRKDVHKlrqQTAMVFQNY 89
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENfyqPQGGQVLLDGKPISQ--YEHKYLHS---KVSLVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 90 NLFkNKTALQNVTEALITAQKKPKKEAEQI----GMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDE 165
Cdd:cd03248 98 VLF-ARSLQDNIAYGLQSCSFECVKEAAQKahahSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489248201 166 PTSALDPELVAGVLQVIKSIAEKQTTMIIvTHEMAFArEVADKVIFMADGRI 217
Cdd:cd03248 177 ATSALDAESEQQVQQALYDWPERRTVLVI-AHRLSTV-ERADQILVLDGGRI 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-216 |
8.03e-26 |
|
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: 98.29 E-value: 8.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGdaklnaasySRKDVHKLRQq 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------STVKIGYFEQ- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 tamvfqnynlfknktalqnvtealitaqkkpkkeaeqigmdllrqvglehkadsypitMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03221 71 ----------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 162 LLDEPTSALDPElvaGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGR 216
Cdd:cd03221 93 LLDEPTNHLDLE---SIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-197 |
8.54e-26 |
|
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: 105.14 E-value: 8.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIeigdaKLNAASYSRKDVHKLRQQTAMVFQNYNLFkNK 95
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV-----TLDGVPVSSLDQDEVRRRVSVCAQDAHLF-DT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 TALQNVteaLITAQKKPKKEAeqigMDLLRQVGLEHKADSYP-----------ITMSGGQQQRIGIARALAVDPHAILLD 164
Cdd:TIGR02868 424 TVRENL---RLARPDATDEEL----WAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|...
gi 489248201 165 EPTSALDPELVAGVLQVIKSiAEKQTTMIIVTH 197
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-225 |
1.15e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.54 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFK----------------------DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGII 58
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrrrtrreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 59 EIgdaklnaasysRKDVhklrqqTAMV-----FQNyNLfknkTALQNVTeaLI-TAQKKPKKEAEQigmdLLRQV----G 128
Cdd:COG1134 84 EV-----------NGRV------SALLelgagFHP-EL----TGRENIY--LNgRLLGLSRKEIDE----KFDEIvefaE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 129 LEHKADSyPI-TMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVAD 207
Cdd:COG1134 136 LGDFIDQ-PVkTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCD 214
|
250
....*....|....*...
gi 489248201 208 KVIFMADGRIIEQGTPEE 225
Cdd:COG1134 215 RAIWLEKGRLVMDGDPEE 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-242 |
1.89e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 104.55 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 12 KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdVHKLRQQTAMVFQN--Y 89
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGK--LQALRRDIQFIFQDpyA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 90 NLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL--EHkADSYPITMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:PRK10261 413 SLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlpEH-AWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 168 SALDPELVAgvlQVIKSIAEKQTTM----IIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIKQV 242
Cdd:PRK10261 492 SALDVSIRG---QIINLLLDLQRDFgiayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
12-224 |
3.24e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 99.37 E-value: 3.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 12 KDLTV-------LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLnlLERPDDGIIEiGDAKLNAASYSRKDVHKlRQQT-- 82
Cdd:COG0396 4 KNLHVsvegkeiLKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MGHPKYEVTS-GSILLDGEDILELSPDE-RARAgi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 83 AMVFQ---------NYNLFKnkTALQNVTEALITAQ---KKPKKEAEQIGMD---LLRQV--GLehkadsypitmSGGQQ 145
Cdd:COG0396 80 FLAFQypveipgvsVSNFLR--TALNARRGEELSAReflKLLKEKMKELGLDedfLDRYVneGF-----------SGGEK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 146 QRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREV-ADKVIFMADGRIIEQGTPE 224
Cdd:COG0396 147 KRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIkPDFVHVLVDGRIVKSGGKE 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-218 |
6.97e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.45 E-value: 6.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 4 VRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaklnaasysRKDVhklrqQTA 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-----------PKGL-----RIG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 84 MVFQNYNLFKNKTALQNVTEAL--ITAQKKPKKEAEQ----IGMDLLRQVGLEHK---ADSY------------------ 136
Cdd:COG0488 65 YLPQEPPLDDDLTVLDTVLDGDaeLRALEAELEELEAklaePDEDLERLAELQEEfeaLGGWeaearaeeilsglgfpee 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 137 ----PI-TMSGGQQQRIGIARALAVDPHAILLDEPTSALDpelvagvlqvIKSIA--EK-----QTTMIIVTHEMAFARE 204
Cdd:COG0488 145 dldrPVsELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----------LESIEwlEEflknyPGTVLVVSHDRYFLDR 214
|
250
....*....|....
gi 489248201 205 VADKVIFMADGRII 218
Cdd:COG0488 215 VATRILELDRGKLT 228
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
11-223 |
7.96e-25 |
|
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: 97.95 E-value: 7.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 11 FKDLT---------VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKLRQQ 81
Cdd:cd03244 5 FKNVSlryrpnlppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI-----SKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLF-----KNKTALQNVTE-----ALITAQKKPKKEAEQIGMDLLRQVGLEHkadsypitMSGGQQQRIGIA 151
Cdd:cd03244 80 ISIIPQDPVLFsgtirSNLDPFGEYSDeelwqALERVGLKEFVESLPGGLDTVVEEGGEN--------LSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 152 RALAVDPHAILLDEPTSALDPELVAGVLQVIKSiAEKQTTMIIVTHE----MAFarevaDKVIFMADGRIIEQGTP 223
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRldtiIDS-----DRILVLDKGRVVEFDSP 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
10-197 |
1.20e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.81 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 10 AFKDLTV--------LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLL--------ERPDDGiieigdaklnaasysrk 73
Cdd:COG4178 364 ALEDLTLrtpdgrplLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwpygsgriARPAGA----------------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 74 dvhklrqqtAMVF---QNYnlfknktaLQNVT--EALI---TAQKKPKKEAEQIgmdlLRQVGLEHKADSY------PIT 139
Cdd:COG4178 427 ---------RVLFlpqRPY--------LPLGTlrEALLypaTAEAFSDAELREA----LEAVGLGHLAERLdeeadwDQV 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 140 MSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSiAEKQTTMIIVTH 197
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-231 |
3.92e-24 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 98.79 E-value: 3.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasySRKDV----HKLRqqTAMVFQNYNLFKNK 95
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFD---AEKGIclppEKRR--IGYVFQDARLFPHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 TALQNVTEALitaQKKPKKEAEQIgMDLLrqvGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD-P-- 172
Cdd:PRK11144 92 KVRGNLRYGM---AKSMVAQFDKI-VALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPrk 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 173 -ELvagvLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:PRK11144 165 rEL----LPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-216 |
1.98e-23 |
|
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: 93.69 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLnllerpddgiieIGDAKLNAASYSrkdVHKlrqQTAMVFQNYNLFkNK 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL------------LGELEKLSGSVS---VPG---SIAYVSQEPWIQ-NG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 TALQNVT----------EALITA-------QKKPKKEAEQIGmdllrQVGlehkadsypITMSGGQQQRIGIARALAVDP 158
Cdd:cd03250 81 TIRENILfgkpfdeeryEKVIKAcalepdlEILPDGDLTEIG-----EKG---------INLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 159 HAILLDEPTSALDPELVAGVLQ-VIKSIAEKQTTMIIVTHEMAFAREvADKVIFMADGR 216
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-232 |
5.90e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 93.75 E-value: 5.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL-NLLerPDDGIIEIGDAKLNAASYSRKDVHK--LRQQT----AM-VFQN 88
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLL--PGQGEILLNGRPLSDWSAAELARHRayLSQQQsppfAMpVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 89 YNLFKNKTALQNVTEALItaqkkpkkeaeqigMDLLRQVGLEHKADSyPIT-MSGGQQQRIGIARAL-----AVDPHA-- 160
Cdd:COG4138 90 LALHQPAGASSEAVEQLL--------------AQLAEALGLEDKLSR-PLTqLSGGEWQRVRLAAVLlqvwpTINPEGql 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDnPQN 232
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT-PEN 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-215 |
7.05e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.78 E-value: 7.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaklNAASYSRKDvHKLRQ 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI-----NNINYNKLD-HKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 Q--TAMVFQNYNLFKNKTALQNV------TEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIAR 152
Cdd:PRK09700 79 QlgIGIIYQELSVIDELTVLENLyigrhlTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADG 215
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-197 |
1.11e-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: 91.65 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 14 LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDV-HKLRQQTAMvfqnynlf 92
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENiLYLGHLPGL-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 KNK-TALQNVT---EALITAQKKPKkeaeqigmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTS 168
Cdd:TIGR01189 85 KPElSALENLHfwaAIHGGAQRTIE--------DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*....
gi 489248201 169 ALDPELVAGVLQVIKSIAEKQTTMIIVTH 197
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-218 |
1.34e-22 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 96.05 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLeRPD---DGIIEIGDAKLNAASYSRKDvhk 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASNIRDTE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 78 lRQQTAMVFQNYNLFKNKTALQNV---TEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPIT-MSGGQQQRIGIARA 153
Cdd:TIGR02633 77 -RAGIVIIHQELTLVPELSVAENIflgNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 154 LAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRII 218
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-224 |
2.34e-21 |
|
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: 88.35 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL--NLLERPDDGIIEIGDAKLNAAS-YSRKdvhkl 78
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPpEERA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 79 RQQTAMVFQNynlfknKTALQNVTEalitaqkkpkkeaeqigMDLLRQVGLehkadsypiTMSGGQQQRIGIARALAVDP 158
Cdd:cd03217 76 RLGIFLAFQY------PPEIPGVKN-----------------ADFLRYVNE---------GFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTH-EMAFAREVADKVIFMADGRIIEQGTPE 224
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-218 |
2.66e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 92.30 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLeRPD---DGIIEIGDAKLNAASYsrKDVHk 77
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNI--RDTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 78 lRQQTAMVFQNYNLFKNKTALQNV------TEALITAQKKPKKEAEQigmdLLRQVGLEHKADSYPITMSGGQQQRIGIA 151
Cdd:PRK13549 81 -RAGIAIIHQELALVKELSVLENIflgneiTPGGIMDYDAMYLRAQK----LLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 152 RALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRII 218
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-221 |
2.91e-21 |
|
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: 88.36 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 12 KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaklnaasysrkdvhkLRQQTAMVFQNYNL 91
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-----------------RGRVSSLLGLGGGF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 92 FKNKTALQNVT-EALI---TAQKKPKKEAE-----QIGMDLLRQVGlehkadsypiTMSGGQQQRIGIARALAVDPHAIL 162
Cdd:cd03220 96 NPELTGRENIYlNGRLlglSRKEIDEKIDEiiefsELGDFIDLPVK----------TYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 163 LDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-223 |
3.16e-21 |
|
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: 92.38 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasysrkDVHKLRQQTAMVFQNYNLFKNKT 96
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET------NLDAVRQSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 97 ALQNVteaLITAQKKPKKEAE-QIGMD-LLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPEL 174
Cdd:TIGR01257 1020 VAEHI---LFYAQLKGRSWEEaQLEMEaMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489248201 175 VAGVLQVIKSIAEKQtTMIIVTHEMAFAREVADKVIFMADGRIIEQGTP 223
Cdd:TIGR01257 1097 RRSIWDLLLKYRSGR-TIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-226 |
3.40e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.46 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGD---AKLNAASYSRKdVHKLRQQTAmvfqnynl 91
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqplESWSSKAFARK-VAYLPQQLP-------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 92 fknktALQNVT-EALITAQKKP-------------KKEAEQIGMdllrqVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:PRK10575 96 -----AAEGMTvRELVAIGRYPwhgalgrfgaadrEKVEEAISL-----VGLKPLAHRLVDSLSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-230 |
1.42e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 90.16 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLrclNLLERPDDgiIEIGDAKLNAASYSRKDVHKLRQQ 81
Cdd:PRK10789 316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLL---SLIQRHFD--VSEGDIRFHDIPLTKLQLDSWRSR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYNLFKNKTAlQNVtealitAQKKPKKEAEQIGM---------DLLR-QVGLEHKADSYPITMSGGQQQRIGIA 151
Cdd:PRK10789 391 LAVVSQTPFLFSDTVA-NNI------ALGRPDATQQEIEHvarlasvhdDILRlPQGYDTEVGERGVMLSGGQKQRISIA 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 152 RALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQtTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:PRK10789 464 RALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGR-TVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-238 |
1.53e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 87.57 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL--NLLE-RPDDGIIEIGDAKLNAASYSRKDVHK 77
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGgGAPRGARVTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 78 LRQQTAMVFQnynlfKNKTALQNVTEALITAQKKPkkEAEQIGMDLLRQVGLE----HKADSYPI------TMSGGQQQR 147
Cdd:PRK13547 81 LARLRAVLPQ-----AAQPAFAFSAREIVLLGRYP--HARRAGALTHRDGEIAwqalALAGATALvgrdvtTLSGGELAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 148 IGIARALA---------VDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:PRK13547 154 VQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLArDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
250 260
....*....|....*....|.
gi 489248201 218 IEQGTPEELFDNPQNERTKKF 238
Cdd:PRK13547 234 VAHGAPADVLTPAHIARCYGF 254
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-221 |
1.61e-20 |
|
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: 87.00 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 4 VRHI-RKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnAASYSRKDVHkLRQQT 82
Cdd:cd03267 23 LKSLfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRKKF-LRRIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 83 AMVFQNYNLFKNKTALQnvTEALITA--QKKPKKEAEQIG--MDLLRqvgLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03267 98 VVFGQKTQLWWDLPVID--SFYLLAAiyDLPPARFKKRLDelSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-249 |
3.07e-20 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 89.02 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 5 RHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSrkdvHKLRQQTAM 84
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSK----EALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 85 VFQNYNLFKNKTALQNV------TEALITAQKKPKKEAEQIGMDLLRQVGLEHKAdsypITMSGGQQQRIGIARALAVDP 158
Cdd:PRK10982 78 VHQELNLVLQRSVMDNMwlgrypTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKV----ATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELfDNPQ------- 231
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL-TMDKiiammvg 232
|
250
....*....|....*...
gi 489248201 232 NERTKKFIKQVGEPAELV 249
Cdd:PRK10982 233 RSLTQRFPDKENKPGEVI 250
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-217 |
4.29e-20 |
|
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: 84.41 E-value: 4.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 12 KDLTV---LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaklNAASYSRKDVHKLRQQtAMVFqn 88
Cdd:cd03215 8 RGLSVkgaVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITL-----DGKPVTRRSPRDAIRA-GIAY-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 89 ynlfknktalqnVTEalitaqkKPKKEAEQIGMDLLRQVGLehkadsyPITMSGGQQQRIGIARALAVDPHAILLDEPTS 168
Cdd:cd03215 80 ------------VPE-------DRKREGLVLDLSVAENIAL-------SSLLSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489248201 169 ALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:cd03215 134 GVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-187 |
7.56e-20 |
|
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: 83.83 E-value: 7.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 12 KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNllERPDDGIIEiGDAKLNAasysRKDVHKLRQQTAMVFQNYNL 91
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAGVIT-GEILING----RPLDKNFQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 92 FKNKTalqnVTEAL-ITAqkkpkkeaeqigmdLLRQVGLEHKadsypitmsggqqQRIGIARALAVDPHAILLDEPTSAL 170
Cdd:cd03232 91 SPNLT----VREALrFSA--------------LLRGLSVEQR-------------KRLTIGVELAAKPSILFLDEPTSGL 139
|
170
....*....|....*..
gi 489248201 171 DPELVAGVLQVIKSIAE 187
Cdd:cd03232 140 DSQAAYNIVRFLKKLAD 156
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-210 |
7.97e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.77 E-value: 7.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdvhkLRQ 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI-----YRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFkNKTALQNVteaLITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPIT-MSGGQQQRIGIARALAVDPH 159
Cdd:PRK10247 82 QVSYCAQTPTLF-GDTVYDNL---IFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEmafAREV--ADKVI 210
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHD---KDEInhADKVI 208
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-229 |
1.86e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.16 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKdvhkLRQ 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI----MRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQvgLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDN 229
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-197 |
2.58e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 83.47 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL--NLLERPDDGIIEIGDAKLNaasysrkdvhklrqqtamvfqnynlf 92
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFG-------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 KNKTALQNVtealitAQKKPKKEAeqigMDLLRQVGLehkADSY-----PITMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:COG2401 98 REASLIDAI------GRKGDFKDA----VELLNAVGL---SDAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|...
gi 489248201 168 SALDPEL---VAGVLQviKSIAEKQTTMIIVTH 197
Cdd:COG2401 165 SHLDRQTakrVARNLQ--KLARRAGITLVVATH 195
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-197 |
8.67e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 8.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYsRKDVHKLRQQTAMvfqnynlf 92
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV-AEACHYLGHRNAM-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 knKTALqNVTEALITAQKKPKKEAEQIgMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDP 172
Cdd:PRK13539 85 --KPAL-TVAENLEFWAAFLGGEELDI-AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180
....*....|....*....|....*
gi 489248201 173 ELVAGVLQVIKSIAEKQTTMIIVTH 197
Cdd:PRK13539 161 AAVALFAELIRAHLAQGGIVIAATH 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-235 |
9.49e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.60 E-value: 9.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRK-------------AFKDL--------TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIE 59
Cdd:COG4586 1 IIEVENLSKtyrvyekepglkgALKGLfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 60 IgdaklnaASYS-RKDVHKLRQQTAMVF-------------QNYNLFKnktALQNVtealitaqkkPKKEAEQIgMDLLR 125
Cdd:COG4586 81 V-------LGYVpFKRRKEFARRIGVVFgqrsqlwwdlpaiDSFRLLK---AIYRI----------PDAEYKKR-LDELV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 126 QV-GLEHKADSyPI-TMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFA 202
Cdd:COG4586 140 ELlDLGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDI 218
|
250 260 270
....*....|....*....|....*....|...
gi 489248201 203 REVADKVIFMADGRIIEQGTPEELFDNPQNERT 235
Cdd:COG4586 219 EALCDRVIVIDHGRIIYDGSLEELKERFGPYKT 251
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-215 |
1.55e-18 |
|
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: 81.22 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVHKlRQQTAMVFQNYNLF 92
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRN-RYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 kNKTALQNVTEALITAQKKPKKEAE----QIGMDLLrQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTS 168
Cdd:cd03290 92 -NATVEENITFGSPFNKQRYKAVTDacslQPDIDLL-PFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489248201 169 ALDPELVAGVLQ--VIKSIAEKQTTMIIVTHEMAFAREvADKVIFMADG 215
Cdd:cd03290 170 ALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-227 |
2.02e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 84.00 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAF-KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSrkdvhKLRQ 80
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS-----VLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQN-----YNLFKNKTALQNVTEALITAqkkpKKEAEQIGmDLLRQV--GLEHKADSYPITMSGGQQQRIGIARA 153
Cdd:PRK10790 416 GVAMVQQDpvvlaDTFLANVTLGRDISEEQVWQ----ALETVQLA-ELARSLpdGLYTPLGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 154 LAVDPHAILLDEPTSALDpelvAGVLQVIK---SIAEKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELF 227
Cdd:PRK10790 491 LVQTPQILILDEATANID----SGTEQAIQqalAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-243 |
2.70e-18 |
|
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: 80.92 E-value: 2.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 23 EIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaKLNAASYSRKDVhklrqqtamvfqnynlfknkTALQNVT 102
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI---ELDTVSYKPQYI--------------------KADYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 103 -EALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQV 181
Cdd:cd03237 78 vRDLLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 182 IKSIAEK-QTTMIIVTHEMAFAREVADKVIFMaDGRIIEQGTPeelfDNPQNERT--KKFIKQVG 243
Cdd:cd03237 158 IRRFAENnEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGVA----NPPQSLRSgmNRFLKNLD 217
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-240 |
3.40e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 82.26 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRC-LNLLerPDDGII-----EIGDAKLNAASYS-RKDVhkLRQQTAMVFQN 88
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAiCGIT--KDNWHVtadrfRWNGIDLLKLSPReRRKI--IGREIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 89 YN--LFKNKTALQNVTEALITAQKKPK-----KEAEQIGMDLLRQVGL-EHKA--DSYPITMSGGQQQRIGIARALAVDP 158
Cdd:COG4170 98 PSscLDPSAKIGDQLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIkDHKDimNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKK 237
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQLQgTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKA 257
|
...
gi 489248201 238 FIK 240
Cdd:COG4170 258 LLR 260
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-202 |
3.91e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.85 E-value: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 18 DGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIeigdaklnaaSYSRKDVHKLRQQtamvFqNYNLF----- 92
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV----------LWQGEPIRRQRDE----Y-HQDLLylghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 ---KNK-TALQNvteaLITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARaLAVDPHAI-LLDEPT 167
Cdd:PRK13538 83 pgiKTElTALEN----LRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALAR-LWLTRAPLwILDEPF 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 489248201 168 SALDpelVAGVLQVIKSIAE--KQTTMIIVT--HEMAFA 202
Cdd:PRK13538 158 TAID---KQGVARLEALLAQhaEQGGMVILTthQDLPVA 193
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
12-224 |
1.13e-17 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 79.23 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 12 KDLTV-------LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLnlLERPD----DGIIEIGDAKLNAAS---YSRKDVHk 77
Cdd:TIGR01978 4 KDLHVsvedkeiLKGVNLTVKKGEIHAIMGPNGSGKSTLSKTI--AGHPSyevtSGTILFKGQDLLELEpdeRARAGLF- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 78 lrqqtaMVFQN-------YNLFKNKTALQNVTEAlitAQKKPKKEAE-----QIGMDLLRQVGlEHKADSYPITMSGGQQ 145
Cdd:TIGR01978 81 ------LAFQYpeeipgvSNLEFLRSALNARRSA---RGEEPLDLLDfekllKEKLALLDMDE-EFLNRSVNEGFSGGEK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 146 QRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVA-DKVIFMADGRIIEQGTPE 224
Cdd:TIGR01978 151 KRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKpDYVHVLLDGRIVKSGDVE 230
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-219 |
1.29e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.50 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 5 RHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASysrkDVHKLRQQTAM 84
Cdd:PRK11288 8 DGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAS----TTAALAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 85 VFQNYNLFKNKTALQNV------TEALITAQKKPKKEA----EQIGMDLLRQVGLEHkadsypitMSGGQQQRIGIARAL 154
Cdd:PRK11288 84 IYQELHLVPEMTVAENLylgqlpHKGGIVNRRLLNYEAreqlEHLGVDIDPDTPLKY--------LSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 155 AVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIE 219
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-225 |
1.41e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.21 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 23 EIKSGEVTAIIGPSGSGKSTLLRCL-NLLerPDDGIIEIGDAKLNAASYSRKDVHK--LRQQ----TAM-VFQNYNLFK- 93
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMaGLL--PGSGSIQFAGQPLEAWSAAELARHRayLSQQqtppFAMpVFQYLTLHQp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 94 NKTALQNVTEALitaqkkpkkeaeqigMDLLRQVGLEHKADSYPITMSGGQQQRIGIARAL-----AVDPHA--ILLDEP 166
Cdd:PRK03695 96 DKTRTEAVASAL---------------NEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAGqlLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 167 TSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEE 225
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-226 |
5.22e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.68 E-value: 5.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 12 KDLTV---LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSrkdvHKLRQQTAMVFQN 88
Cdd:COG1129 260 EGLSVggvVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPR----DAIRAGIAYVPED 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 89 ---YNLFKNKTALQNVTealITAQKK--------PKKEAEQIGmDLLRQVGLehKADS--YPI-TMSGGQQQRIGIARAL 154
Cdd:COG1129 336 rkgEGLVLDLSIRENIT---LASLDRlsrgglldRRRERALAE-EYIKRLRI--KTPSpeQPVgNLSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 155 AVDPHAILLDEPTSALDpelV---AGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:COG1129 410 ATDPKVLILDEPTRGID---VgakAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-244 |
6.87e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 79.63 E-value: 6.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLrclnllerpddgiieigDAKLNAASYSRKDVHKLRQQTAMVFQNYNLFkNKT 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLI-----------------SAMLGELSHAETSSVVIRGSVAYVPQVSWIF-NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 97 ALQNVteaLITAQKKPKKEAEQIGMdllrqVGLEHKADSYP-----------ITMSGGQQQRIGIARALAVDPHAILLDE 165
Cdd:PLN03232 695 VRENI---LFGSDFESERYWRAIDV-----TALQHDLDLLPgrdlteigergVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 166 PTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVaDKVIFMADGRIIEQGTPEELFDNpqNERTKKFIKQVGE 244
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS--GSLFKKLMENAGK 842
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
9-221 |
1.01e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.15 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 9 KAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNllerpddGIIEIGDAKLNAASYSRKDVHKLRQQTAMVFQN 88
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALA-------GRIQGNNFTGTILANNRKPTKQILKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 89 YNLFKNKTalqnVTEALI--TAQKKPKKEAEQ----IGMDLLRQVGLEH-----KADSYPITMSGGQQQRIGIARALAVD 157
Cdd:PLN03211 149 DILYPHLT----VRETLVfcSLLRLPKSLTKQekilVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLIN 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHE-MAFAREVADKVIFMADGRIIEQG 221
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-229 |
1.13e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 79.01 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLnLLERP--DDGIIEIgdaklnaasysrkdvhklRQQTAMVFQNYNLFkN 94
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAM-LGELPprSDASVVI------------------RGTVAYVPQVSWIF-N 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 KTALQNVteaLITAQKKPKKEAEQIgmdllRQVGLEHKADSYP-----------ITMSGGQQQRIGIARALAVDPHAILL 163
Cdd:PLN03130 693 ATVRDNI---LFGSPFDPERYERAI-----DVTALQHDLDLLPggdlteigergVNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 164 DEPTSALDPELVAGVLQviKSIAE--KQTTMIIVTHEMAFAREVaDKVIFMADGRIIEQGTPEELFDN 229
Cdd:PLN03130 765 DDPLSALDAHVGRQVFD--KCIKDelRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-197 |
1.17e-16 |
|
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: 75.61 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 14 LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYS-RKDVHKLRQQTAM-----VFQ 87
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIkttlsVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 88 NYNLFKNKTALQNVTEALITaqkkpkkeaeqigMDLlrqVGLEHKADSYpitMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:cd03231 93 NLRFWHADHSDEQVEEALAR-------------VGL---NGFEDRPVAQ---LSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|
gi 489248201 168 SALDPELVAGVLQVIKSIAEKQTTMIIVTH 197
Cdd:cd03231 154 TALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-228 |
2.26e-16 |
|
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: 78.06 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLnlLERPDdgiieigdaKLNAASYSRKDVHKLRQQTAMvfQNYNLFKN-- 94
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMD---------KVEGHVHMKGSVAYVPQQAWI--QNDSLRENil 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 ------KTALQNVTEA---LITAQKKPKKEAEQIGmdllrqvglehkadSYPITMSGGQQQRIGIARALAVDPHAILLDE 165
Cdd:TIGR00957 721 fgkalnEKYYQQVLEAcalLPDLEILPSGDRTEIG--------------EKGVNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 166 PTSALDP-------ELVAGVLQVIKSiaekqTTMIIVTHEMAFAREVaDKVIFMADGRIIEQGTPEELFD 228
Cdd:TIGR00957 787 PLSAVDAhvgkhifEHVIGPEGVLKN-----KTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-215 |
3.24e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 77.84 E-value: 3.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNllERPDDGIIEIGDAKLNA----ASYSR-------KDVHkLRQQ 81
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGrpldSSFQRsigyvqqQDLH-LPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TamvfqnynlfknktalqnVTEALITA------QKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGG----QQQRIGIA 151
Cdd:TIGR00956 852 T------------------VRESLRFSaylrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIG 913
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 152 RALAVDPHAIL-LDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHE-MAFAREVADKVIFMADG 215
Cdd:TIGR00956 914 VELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpSAILFEEFDRLLLLQKG 979
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-223 |
4.66e-16 |
|
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: 74.37 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKLRQQTAMVFQNYNLFKNk 95
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI-----STIPLEDLRSSLTIIPQDPTLFSG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 talqnvtealiTAQKKPKKEAEQIGMDLLRQVGLEHKADSypitMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELV 175
Cdd:cd03369 97 -----------TIRSNLDPFDEYSDEEIYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489248201 176 AGVLQVIKSiAEKQTTMIIVTHEMafaREVA--DKVIFMADGRIIEQGTP 223
Cdd:cd03369 162 ALIQKTIRE-EFTNSTILTIAHRL---RTIIdyDKILVMDAGEVKEYDHP 207
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
7-221 |
5.18e-16 |
|
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: 73.84 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 7 IRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLeRPDDGIIEiGDAKLNAASYsRKDVHKLRQQTAMVF 86
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-TEGNVSVE-GDIHYNGIPY-KEFAEKYPGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 87 QNYNLFKNKTalqnVTEALITAqkkpkkeAEQIGMDLLRQVglehkadsypitmSGGQQQRIGIARALAVDPHAILLDEP 166
Cdd:cd03233 90 EEDVHFPTLT----VRETLDFA-------LRCKGNEFVRGI-------------SGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 167 TSALDPELVAGVLQVIKSIA--EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMAdvLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-224 |
5.19e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 75.06 E-value: 5.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRClnLLERPDDGIIEiGDAKLNAASYSRKDVHKLRQ 80
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKV--IAGHPAYKILE-GDILFKGESILDLEPEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTA-MVFQN---YNLFKNKTALQNVTEALITAQKKPKKEA---EQIGMDLLRQVGLEHKADSYPIT--MSGGQQQRIGIA 151
Cdd:CHL00131 84 LGIfLAFQYpieIPGVSNADFLRLAYNSKRKFQGLPELDPlefLEIINEKLKLVGMDPSFLSRNVNegFSGGEKKRNEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 152 RALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHemaFARE----VADKVIFMADGRIIEQGTPE 224
Cdd:CHL00131 164 QMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRLldyiKPDYVHVMQNGKIIKTGDAE 237
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-217 |
1.09e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYsrkdvhKLRQQTAMVF-----QNYNLFKN 94
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST------AQRLARGLVYlpedrQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 KTALQNVTeALITAQK----KPKKEA---EQigmdLLRQVGLEHKADSYPI-TMSGGQQQRIGIARALAVDPHAILLDEP 166
Cdd:PRK15439 356 APLAWNVC-ALTHNRRgfwiKPARENavlER----YRRALNIKFNHAEQAArTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489248201 167 TSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-226 |
2.18e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.04 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEigdaklnaasYSRKDVH---- 76
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIL----------YLGKEVTfngp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 KLRQQT--AMVFQNYNLFKNKTALQNV------TEALITAQ-KKPKKEAEQigmdLLRQVGLEHKADSYPITMSGGQQQR 147
Cdd:PRK10762 74 KSSQEAgiGIIHQELNLIPQLTIAENIflgrefVNRFGRIDwKKMYAEADK----LLARLNLRFSSDKLVGELSIGEQQM 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 148 IGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK10762 150 VEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
7-210 |
3.90e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.07 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 7 IRKAFKD--LTVLDGidlEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgDAKLnaaSYsrkdvhK---LRQQ 81
Cdd:PRK13409 346 LTKKLGDfsLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELKI---SY------KpqyIKPD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 82 TAMVFQNYnlfknktaLQNVTEALITAQKKPkkeaeqigmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:PRK13409 413 YDGTVEDL--------LRSITDDLGSSYYKS---------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLY 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAE-KQTTMIIVTHEMAFAREVADKVI 210
Cdd:PRK13409 476 LLDEPSAHLDVEQRLAVAKAIRRIAEeREATALVVDHDIYMIDYISDRLM 525
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-197 |
7.35e-15 |
|
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: 69.88 E-value: 7.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNllerpddGIIEIGDAKLNaaSYSRKDVHKLRQQTAMVFQNynlfkn 94
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALA-------GLWPWGSGRIG--MPEGEDLLFLPQRPYLPLGT------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 ktalqnvtealitaqkkpkkeaeqigmdlLRQVGLehkadsYP--ITMSGGQQQRIGIARALAVDPHAILLDEPTSALDP 172
Cdd:cd03223 80 -----------------------------LREQLI------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180
....*....|....*....|....*
gi 489248201 173 ELVAGVLQVIKsiaEKQTTMIIVTH 197
Cdd:cd03223 125 ESEDRLYQLLK---ELGITVISVGH 146
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-226 |
7.69e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 72.85 E-value: 7.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLErPDDGIieiGDAKLNAASYSRKDVHK-LRQ 80
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G-PDAGR---RPWRF*TWCANRRALRRtIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQigmdLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:NF000106 90 HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADE----LLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:NF000106 166 LYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-219 |
8.06e-15 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 73.29 E-value: 8.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdvhkLRQQTAMVFQNYNLFKNktalq 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREA-----YRQLFSAVFSDFHLFDR----- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 100 nvteaLITAQKKPkkEAEQIgMDLLRQVGLEHK---ADSYPIT--MSGGQQQRIGIARALAVDPHAILLDEPTSALDP-- 172
Cdd:COG4615 421 -----LLGLDGEA--DPARA-RELLERLELDHKvsvEDGRFSTtdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPef 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489248201 173 ------ELvagvLQVIKsiaEKQTTMIIVTH-EMAFarEVADKVIFMADGRIIE 219
Cdd:COG4615 493 rrvfytEL----LPELK---ARGKTVIAISHdDRYF--DLADRVLKMDYGKLVE 537
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-234 |
1.29e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkdvhkLRQQ-TAMVFQNYNLFK 93
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA---------LQKNlVAYVPQSEEVDW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 94 NKTALqnVTEALITAQ-------KKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEP 166
Cdd:PRK15056 92 SFPVL--VEDVVMMGRyghmgwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 167 TSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIfMADGRIIEQGTPEELFDNPQNER 234
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTFTAENLEL 236
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-219 |
1.34e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.51 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 5 RHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL-----------------------NLLERPDDGIIEIg 61
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvyphgsyegeilfdgevcrfkDIRDSEALGIVII- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 62 daklnaasysrkdvHklrQQTAMVFQ---NYNLF-KNKTAlqnvTEALITAQKKPKKEAEqigmdLLRQVGLEHKADSyP 137
Cdd:NF040905 84 --------------H---QELALIPYlsiAENIFlGNERA----KRGVIDWNETNRRARE-----LLAKVGLDESPDT-L 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 138 ITMSG-GQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGR 216
Cdd:NF040905 137 VTDIGvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
...
gi 489248201 217 IIE 219
Cdd:NF040905 217 TIE 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-231 |
1.49e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.89 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLrcLNLLErpddgIIEI--GDAKLNAASYSRKDVHKLRQQTAMVFQNYNLFk 93
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLL--LTFMR-----MVEVcgGEIRVNGREIGAYGLRELRRQFSMIPQDPVLF- 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 94 NKTALQNVTEALITAQKKPKKEAEQIGmdLLRQVGLEHKA-DSYPI----TMSGGQQQRIGIARA-LAVDPHAILLDEPT 167
Cdd:PTZ00243 1397 DGTVRQNVDPFLEASSAEVWAALELVG--LRERVASESEGiDSRVLeggsNYSVGQRQLMCMARAlLKKGSGFILMDEAT 1474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 168 SALDPELVAGVLQVIKSiAEKQTTMIIVTHEMafaREVA--DKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:PTZ00243 1475 ANIDPALDRQIQATVMS-AFSAYTVITIAHRL---HTVAqyDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-173 |
2.30e-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: 71.89 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDA-KLNAASYSRKDvhklrq 80
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvKLAYVDQSRDA------ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 qtamvfqnynLFKNKTALQNVTEalitaqkkpkkeaeqiGMDLLRQVGLEHKADSY-------------PI-TMSGGQQQ 146
Cdd:TIGR03719 397 ----------LDPNKTVWEEISG----------------GLDIIKLGKREIPSRAYvgrfnfkgsdqqkKVgQLSGGERN 450
|
170 180
....*....|....*....|....*..
gi 489248201 147 RIGIARALAVDPHAILLDEPTSALDPE 173
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
16-240 |
3.17e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 70.99 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKStllrclnLLERPDDGIIEiGDAKLNAASYSRKDVHKLR-----------QQTAM 84
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKS-------LIAKAICGVTK-DNWRVTADRMRFDDIDLLRlsprerrklvgHNVSM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 85 VFQNYNLFKNKTalQNVTEALITA-----------QKKPKKEAEQIgmDLLRQVGL-EHKA--DSYPITMSGGQQQRIGI 150
Cdd:PRK15093 94 IFQEPQSCLDPS--ERVGRQLMQNipgwtykgrwwQRFGWRKRRAI--ELLHRVGIkDHKDamRSFPYELTEGECQKVMI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 151 ARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDN 229
Cdd:PRK15093 170 AIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNnTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTT 249
|
250
....*....|.
gi 489248201 230 PQNERTKKFIK 240
Cdd:PRK15093 250 PHHPYTQALIR 260
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
11-240 |
4.55e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.60 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 11 FKDLTvldgidLEIKSGEVTAIIGPSGSGKSTLLrclNLLER----PDDGIIEIGDAKLNAASYSRKDVHKLRQQTAMV- 85
Cdd:PTZ00265 1184 YKDLT------FSCDSKKTTAIVGETGSGKSTVM---SLLMRfydlKNDHHIVFKNEHTNDMTNEQDYQGDEEQNVGMKn 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 86 ------------FQNYNLFKNKTA------------LQNVTEALITAQKKP-----------KKEAEQIGMDLLRQV--- 127
Cdd:PTZ00265 1255 vnefsltkeggsGEDSTVFKNSGKilldgvdicdynLKDLRNLFSIVSQEPmlfnmsiyeniKFGKEDATREDVKRAckf 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 128 --------GLEHKADS----YPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDP---ELVAGVLQVIKSIAEKqtTM 192
Cdd:PTZ00265 1335 aaidefieSLPNKYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADK--TI 1412
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 489248201 193 IIVTHEMAFAREVADKVIFMADGR----IIEQGTPEELFdNPQNERTKKFIK 240
Cdd:PTZ00265 1413 ITIAHRIASIKRSDKIVVFNNPDRtgsfVQAHGTHEELL-SVQDGVYKKYVK 1463
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-200 |
5.16e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.97 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 25 KSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEigdaklNAASYsrKDVHKLRQQTAMvfQNYnlfknktaLQNVTEA 104
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD------EEPSW--DEVLKRFRGTEL--QDY--------FKKLANG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 105 LITAQKKPK-----------------KEAEQIGM--DLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDE 165
Cdd:COG1245 159 EIKVAHKPQyvdlipkvfkgtvrellEKVDERGKldELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....*
gi 489248201 166 PTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMA 200
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLA 273
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-221 |
7.64e-14 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 69.05 E-value: 7.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL------------------NLLE-----RPDDGI 57
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagredyevtggtvefkgkDLLElspedRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 58 -------IEI-GDAKLNAASYSRKDVHKLRQQTAM-VFQNYNLFKNKTALQNVTEALITaqkkpkkeaeqigmdllRQVG 128
Cdd:PRK09580 81 fmafqypVEIpGVSNQFFLQTALNAVRSYRGQEPLdRFDFQDLMEEKIALLKMPEDLLT-----------------RSVN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 129 lehkadsypITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVA-D 207
Cdd:PRK09580 144 ---------VGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpD 214
|
250
....*....|....
gi 489248201 208 KVIFMADGRIIEQG 221
Cdd:PRK09580 215 YVHVLYQGRIVKSG 228
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
11-221 |
1.05e-13 |
|
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: 66.96 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 11 FKDLTV--LDGIDLEIKSGEVTAIIGPSGSGKSTLLRclnllerpdDGIIEIGDAKLNAA--SYSRkdvhklrQQTAMVF 86
Cdd:cd03238 3 VSGANVhnLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLISFlpKFSR-------NKLIFID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 87 QnynlfknktaLQNVTEalitaqkkpkkeaeqIGMDLLRqvgLEHKADsypiTMSGGQQQRIGIARALAVDPHAIL--LD 164
Cdd:cd03238 67 Q----------LQFLID---------------VGLGYLT---LGQKLS----TLSGGELQRVKLASELFSEPPGTLfiLD 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 165 EPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREvADKVIFMA------DGRIIEQG 221
Cdd:cd03238 115 EPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGpgsgksGGKVVFSG 176
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
7-210 |
1.10e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.81 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 7 IRKAFKD--LTVLDGidlEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEiGDAKLnaaSYSRKDVhklrqqtam 84
Cdd:COG1245 347 LTKSYGGfsLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKI---SYKPQYI--------- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 85 vfqnynlfknkTALQNVT-EALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILL 163
Cdd:COG1245 411 -----------SPDYDGTvEEFLRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489248201 164 DEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVI 210
Cdd:COG1245 480 DEPSAHLDVEQRLAVAKAIRRFAENRgKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-219 |
1.46e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.62 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkDVHKLRQQTAMVFQNYNLFknktalq 99
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE-----QPEDYRKLFSAVFTDFHLF------- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 100 nvtEALITAQKKPKKEAeqIGMDLLRQVGLEHKADS-----YPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPEL 174
Cdd:PRK10522 410 ---DQLLGPEGKPANPA--LVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489248201 175 VAGVLQV-IKSIAEKQTTMIIVTHEMAFArEVADKVIFMADGRIIE 219
Cdd:PRK10522 485 RREFYQVlLPLLQEMGKTIFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-231 |
1.74e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.83 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEigdaklnaasysrkDVHKLRq 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------------RNGKLR- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 qTAMVFQNYNLfkNKTALQNVTEALitaQKKPKKEAEQIgMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:PRK09544 69 -IGYVPQKLYL--DTTLPLTVNRFL---RLRPGTKKEDI-LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 161 ILLDEPTSALDpelVAGVLQVIKSIAEKQTTM----IIVTHEMAFAREVADKVIFMaDGRIIEQGTPEELFDNPQ 231
Cdd:PRK09544 142 LVLDEPTQGVD---VNGQVALYDLIDQLRRELdcavLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE 212
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-229 |
2.82e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.00 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDakLNAASYSRKDVHK---LRQQTAMVFQN---Y 89
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG--CDISKFGLMDLRKvlgIIPQAPVLFSGtvrF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 90 NL--FkNKTALQNVTEALITAQKKpkkeaeqigmDLLRQ--VGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDE 165
Cdd:PLN03130 1332 NLdpF-NEHNDADLWESLERAHLK----------DVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 166 PTSALDPELVAgVLQviKSIAE--KQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFDN 229
Cdd:PLN03130 1401 ATAAVDVRTDA-LIQ--KTIREefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-226 |
5.68e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.74 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 14 LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsySRKDVHKL--------RQQTAMV 85
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGL--SPRERRRLgvayipedRLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 86 fQNYNLFKNkTALQNVTEALITA-----QKKPKKEAEQI--GMDlLRQVGLEHKADSypitMSGGQQQRIGIARALAVDP 158
Cdd:COG3845 349 -PDMSVAEN-LILGRYRRPPFSRggfldRKAIRAFAEELieEFD-VRTPGPDTPARS----LSGGNQQKVILARELSRDP 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRII-----EQGTPEEL 226
Cdd:COG3845 422 KLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVgevpaAEATREEI 494
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-226 |
1.81e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.58 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNllerpDDGIIEIGDAKLNAASY--SRKDVHklrqqtamvfQNYNLFKN 94
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLT-----GDTTVTSGDATVAGKSIltNISDVH----------QNMGYCPQ 2019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 KTALQNvteaLITAQKK----------PKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLD 164
Cdd:TIGR01257 2020 FDAIDD----LLTGREHlylyarlrgvPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLD 2095
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489248201 165 EPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:TIGR01257 2096 EPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
17-223 |
2.60e-12 |
|
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: 64.56 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLL---------RCLNL-LERPDDGIIEIGDAKL-----------------NAAS 69
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLkKEQPGNHDRIEGLEHIdkvividqspigrtprsNPAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 70 YSrKDVHKLRQqtamVF------QNYN------LFKNKTALQ----NVTEALITAQKKPKKEAEqigMDLLRQVGLEHKA 133
Cdd:cd03271 91 YT-GVFDEIRE----LFcevckgKRYNretlevRYKGKSIADvldmTVEEALEFFENIPKIARK---LQTLCDVGLGYIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 134 DSYPI-TMSGGQQQRIGIARALA-VDPHAIL--LDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAReVADKV 209
Cdd:cd03271 163 LGQPAtTLSGGEAQRIKLAKELSkRSTGKTLyiLDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CADWI 241
|
250 260
....*....|....*....|
gi 489248201 210 IFM------ADGRIIEQGTP 223
Cdd:cd03271 242 IDLgpeggdGGGQVVASGTP 261
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-225 |
3.55e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.30 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL-NLLErPDDGIIEIGDaklNAasysrkDVHKLRQ 80
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLvGELE-PDSGTVKWSE---NA------NIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQN-YNLFK----------NKTALQNVTEALITAQKKPKKEAEQIgmdllrqvglehkadsypitmSGGQQQRIG 149
Cdd:PRK15064 390 DHAYDFENdLTLFDwmsqwrqegdDEQAVRGTLGRLLFSQDDIKKSVKVL---------------------SGGEKGRML 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 150 IARALAVDPHAILLDEPTSALDPElvagvlqVIKSIA---EK-QTTMIIVTHEMAFAREVADKVIFMADGRIIE-QGTPE 224
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEPTNHMDME-------SIESLNmalEKyEGTLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYE 521
|
.
gi 489248201 225 E 225
Cdd:PRK15064 522 E 522
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-242 |
3.78e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.77 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAklNAASYSRKDvhkLRQQTAMVFQNYNLFKNK 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDC--DVAKFGLTD---LRRVLSIIPQSPVLFSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 TALQ----------NVTEALITAQKKPKKEAEQIGMDLLRQVGLEhkadsypiTMSGGQQQRIGIARALAVDPHAILLDE 165
Cdd:PLN03232 1326 VRFNidpfsehndaDLWEALERAHIKDVIDRNPFGLDAEVSEGGE--------NFSVGQRQLLSLARALLRRSKILVLDE 1397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 166 PTSALDPELVAGVLQVIKSiAEKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFDNpqneRTKKFIKQV 242
Cdd:PLN03232 1398 ATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSR----DTSAFFRMV 1468
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-210 |
4.13e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 10 AFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEI-GD-----------------------AKL 65
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDlivarlqqdpprnvegtvydfvaEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 66 NAASYSRKDVHKLRQQTAMVFQNYNLfkNKTA-LQNVTEALITAQKKPKkeaeqIgMDLLRQVGLEhkADSYPITMSGGQ 144
Cdd:PRK11147 92 EEQAEYLKRYHDISHLVETDPSEKNL--NELAkLQEQLDHHNLWQLENR-----I-NEVLAQLGLD--PDAALSSLSGGW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 145 QQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIaekQTTMIIVTHEMAFAREVADKVI 210
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF---QGSIIFISHDRSFIRNMATRIV 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-203 |
4.22e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAF---KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDA-------------KL 65
Cdd:PTZ00265 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrsKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 66 NAAS------------------YSRKDVHKLRQQT------------------AMVFQNYNLFKNKTAlqnvTEALITAQ 109
Cdd:PTZ00265 463 GVVSqdpllfsnsiknnikyslYSLKDLEALSNYYnedgndsqenknkrnscrAKCAGDLNDMSNTTD----SNELIEMR 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 110 KKPKKEAEQIGMDLLRQVGLEHKADSYP-----------ITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGV 178
Cdd:PTZ00265 539 KNYQTIKDSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260
....*....|....*....|....*.
gi 489248201 179 LQVIKSIAEKQTTM-IIVTHEMAFAR 203
Cdd:PTZ00265 619 QKTINNLKGNENRItIIIAHRLSTIR 644
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-173 |
4.36e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.14 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGD-AKLNAASYSRKdvhklrq 80
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGEtVKLAYVDQSRD------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 qtamvfqnyNLFKNKTALQNVTEalitaqkkpkkeaeqiGMDLLRQVGLEHKADSY-------------PI-TMSGGQQQ 146
Cdd:PRK11819 398 ---------ALDPNKTVWEEISG----------------GLDIIKVGNREIPSRAYvgrfnfkggdqqkKVgVLSGGERN 452
|
170 180
....*....|....*....|....*..
gi 489248201 147 RIGIARALAVDPHAILLDEPTSALDPE 173
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-206 |
7.26e-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: 64.57 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLE-------RPDDGiIEIG----DAKLNAASYSRKDVHKLRQQTAM 84
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDkdfngeaRPQPG-IKVGylpqEPQLDPTKTVRENVEEGVAEIKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 85 VFQNYNLFKNKTALQNVT-EALITAQKKPKKEAE-QIGMDLLRQvgLEHKADSY-------PIT-MSGGQQQRIGIARAL 154
Cdd:TIGR03719 99 ALDRFNEISAKYAEPDADfDKLAAEQAELQEIIDaADAWDLDSQ--LEIAMDALrcppwdaDVTkLSGGERRRVALCRLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489248201 155 AVDPHAILLDEPTSALDPELVAGVLQVIKsiaEKQTTMIIVTHEMAFAREVA 206
Cdd:TIGR03719 177 LSKPDMLLLDEPTNHLDAESVAWLERHLQ---EYPGTVVAVTHDRYFLDNVA 225
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
13-197 |
9.96e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.56 E-value: 9.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgDAKLNAASYSRKDVHKLRQQTAmvfqnynLF 92
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATRGDRSRFMAYLGHLPG-------LK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 KNKTALQNVTEALITAQKKPKkeaeQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARaLAVDPHAI-LLDEPTSALD 171
Cdd:PRK13543 95 ADLSTLENLHFLCGLHGRRAK----QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLD 169
|
170 180
....*....|....*....|....*.
gi 489248201 172 PELVAGVLQVIKSIAEKQTTMIIVTH 197
Cdd:PRK13543 170 LEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-200 |
1.16e-11 |
|
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: 62.77 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 25 KSGEVTAIIGPSGSGKSTLLRCL------NL---LERPD-DGIIEI--GDAKLNAASYSRKDVHKLRQQTAMVFQNYNLF 92
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILagklkpNLgkfDDPPDwDEILDEfrGSELQNYFTKLLEGDVKVIVKPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 KNKtalqnVTEALITAQKKPKKEaeqigmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDP 172
Cdd:cd03236 104 KGK-----VGELLKKKDERGKLD------ELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*...
gi 489248201 173 ELVAGVLQVIKSIAEKQTTMIIVTHEMA 200
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-200 |
1.24e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 24 IKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEigdaklnaASYSRKDVHKLRQQTAMvfQNYnlfknktaLQNVTE 103
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYE--------EEPSWDEVLKRFRGTEL--QNY--------FKKLYN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 104 ALITAQKKPK-----------------KEAEQIGM--DLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLD 164
Cdd:PRK13409 158 GEIKVVHKPQyvdlipkvfkgkvrellKKVDERGKldEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*.
gi 489248201 165 EPTSALDPELVAGVLQVIKSIAEKQtTMIIVTHEMA 200
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAEGK-YVLVVEHDLA 272
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
7-247 |
2.41e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.20 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 7 IRKAFKD-----LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL--NLlerpdDGIIEIGDAKLNAASYSRKDVHK-L 78
Cdd:TIGR00956 62 FRKLKKFrdtktFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasNT-----DGFHIGVEGVITYDGITPEEIKKhY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 79 RQQTAMVFQNYNLFKNKTalqnVTEALITAQKKpkKEAEQIGMDLLRQVGLEHKADSYPIT------------------M 140
Cdd:TIGR00956 137 RGDVVYNAETDVHFPHLT----VGETLDFAARC--KTPQNRPDGVSREEYAKHIADVYMATyglshtrntkvgndfvrgV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 141 SGGQQQRIGIARALAVDPHAILLDEPTSALDPelvAGVLQVIKSIAE-----KQTTMIIVTHEMAFAREVADKVIFMADG 215
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDS---ATALEFIRALKTsanilDTTPLVAIYQCSQDAYELFDKVIVLYEG 287
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489248201 216 RIIEQGTPEEL--------FDNPQNERTKKFIKQVGEPAE 247
Cdd:TIGR00956 288 YQIYFGPADKAkqyfekmgFKCPDRQTTADFLTSLTSPAE 327
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-217 |
2.53e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.26 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNllerpddGIIEIGDAKLNAAsysrKDVHKLRQQ----TAMVFQNYNL 91
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLL-------SQFEISEGRVWAE----RSIAYVPQQawimNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 92 FKNKTAlqnvtEALITAQKKPKKEAEqigmdlLRQV--GLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSA 169
Cdd:PTZ00243 744 FDEEDA-----ARLADAVRVSQLEAD------LAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489248201 170 LDPELVAGVLQ--VIKSIAEKqtTMIIVTHEM-AFARevADKVIFMADGRI 217
Cdd:PTZ00243 813 LDAHVGERVVEecFLGALAGK--TRVLATHQVhVVPR--ADYVVALGDGRV 859
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
121-226 |
4.65e-11 |
|
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: 62.34 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 121 MDLLRQVGLEHKADSYPI-TMSGGQQQRIGIARAL---AVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVT 196
Cdd:TIGR00630 810 LQTLCDVGLGYIRLGQPAtTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIE 889
|
90 100 110
....*....|....*....|....*....|....*.
gi 489248201 197 HEMAFAReVADKVIFM------ADGRIIEQGTPEEL 226
Cdd:TIGR00630 890 HNLDVIK-TADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
17-212 |
5.33e-11 |
|
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: 59.30 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLlerpddgiieigdaklnaasysrkdvhklrqqtAMVFQNYNLFKNKT 96
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAIGL---------------------------------ALGGAQSATRRRSG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 97 ALQNVTEALItaqkkpkkEAEQIGMDllrqvglehkadsypITMSGGQQQRIGIARALAVDPHA----ILLDEPTSALDP 172
Cdd:cd03227 58 VKAGCIVAAV--------SAELIFTR---------------LQLSGGEKELSALALILALASLKprplYILDEIDRGLDP 114
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489248201 173 ELVAGVLQVIKSIAEKQTTMIIVTHEMAFArEVADKVIFM 212
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIVITHLPELA-ELADKLIHI 153
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
23-210 |
6.48e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 59.51 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 23 EIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaklnaasysrkdvhklrqqtamvfqnynlfknktalqnvt 102
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW------------------------------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 103 eALITAQKKPKKeaeqigmdllrqvglehkadsypITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVI 182
Cdd:cd03222 59 -DGITPVYKPQY-----------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
170 180
....*....|....*....|....*....
gi 489248201 183 KSIAEK-QTTMIIVTHEMAFAREVADKVI 210
Cdd:cd03222 115 RRLSEEgKKTALVVEHDLAVLDYLSDRIH 143
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-226 |
7.33e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.68 E-value: 7.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIE-----IGDAKLNAASYSR---- 72
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdMADARHRRAVCPRiaym 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 73 -----KDVHklrqQTAMVFQNYNLFknktalqnvteALITAQKKPKKEAeQIGmDLLRQVGLEHKADSYPITMSGGQQQR 147
Cdd:NF033858 82 pqglgKNLY----PTLSVFENLDFF-----------GRLFGQDAAERRR-RID-ELLRATGLAPFADRPAGKLSGGMKQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 148 IGIARALAVDPHAILLDEPTSALDP-------ELvagvlqvIKSIAEKQTTM--IIVThemAFAREVA--DKVIFMADGR 216
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPTTGVDPlsrrqfwEL-------IDRIRAERPGMsvLVAT---AYMEEAErfDWLVAMDAGR 214
|
250
....*....|
gi 489248201 217 IIEQGTPEEL 226
Cdd:NF033858 215 VLATGTPAEL 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
16-227 |
1.27e-10 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 59.92 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTL-LRCLNLLERPDDGIIeigdakLNAASYSRKDVHKLRQQTAMVFQNYNLF-- 92
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFDGKIV------IDGIDISKLPLHTLRSRLSIILQDPILFsg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 --------KNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHkadsypitMSGGQQQRIGIARALAVDPHAILLD 164
Cdd:cd03288 110 sirfnldpECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGEN--------FSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 165 EPTSALDPElVAGVLQVIKSIAEKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELF 227
Cdd:cd03288 182 EATASIDMA-TENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-217 |
1.87e-10 |
|
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: 60.22 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL-NLLERPDDGIIEIGDAKLNaasySRKDVHKLRQQTAMVFQN---YNLF 92
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVD----IRNPAQAIRAGIAMVPEDrkrHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 KNKTALQNVTEALI---TAQKKPKKEAEQIGMDL-LRQVGLEHKADSYPIT-MSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:TIGR02633 352 PILGVGKNITLSVLksfCFKMRIDAAAELQIIGSaIQRLKVKTASPFLPIGrLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489248201 168 SALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-234 |
3.66e-10 |
|
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: 58.71 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEigdaKLNAASYSrkdvhklrQQTAMVFQNynlfknk 95
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK----HSGRISFS--------SQFSWIMPG------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 TALQNVTEALITAQKKPKK--EAEQIGMDLLRqvgLEHKaDSYP-----ITMSGGQQQRIGIARALAVDPHAILLDEPTS 168
Cdd:cd03291 113 TIKENIIFGVSYDEYRYKSvvKACQLEEDITK---FPEK-DNTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 169 ALDPELVAGVLQ--VIKSIAEKqtTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELfdnpQNER 234
Cdd:cd03291 189 YLDVFTEKEIFEscVCKLMANK--TRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSEL----QSLR 249
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-226 |
4.92e-10 |
|
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: 59.57 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDakLNAASYSrkdVHKLRQQTAMVFQNYNLFKNK 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--LNIAKIG---LHDLRFKITIIPQDPVLFSGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 TAL----------QNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHkadsypitMSGGQQQRIGIARALAVDPHAILLDE 165
Cdd:TIGR00957 1376 LRMnldpfsqysdEEVWWALELAHLKTFVSALPDKLDHECAEGGEN--------LSVGQRQLVCLARALLRKTKILVLDE 1447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 166 PTSALDPELVAGVLQVIKSIAEKQTTMIIvTHE----MAFARevadkVIFMADGRIIEQGTPEEL 226
Cdd:TIGR00957 1448 ATAAVDLETDNLIQSTIRTQFEDCTVLTI-AHRlntiMDYTR-----VIVLDKGEVAEFGAPSNL 1506
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
29-210 |
8.87e-10 |
|
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: 56.85 E-value: 8.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 29 VTAIIGPSGSGKSTLLRCLNLL---ERPDDGIIEIGDAKLNAASYSRKDVH---KLRQQTAM-VFQNYNLFKNktalqnv 101
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKYAltgELPPNSKGGAHDPKLIREGEVRAQVKlafENANGKKYtITRSLAILEN------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 102 teALITAQkkpkkeaEQIGMDLLRQVGlehkadsypiTMSGGQQQ------RIGIARALAVDPHAILLDEPTSALDPELV 175
Cdd:cd03240 97 --VIFCHQ-------GESNWPLLDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENI 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 489248201 176 AGVL-QVIKSI-AEKQTTMIIVTHEMAFaREVADKVI 210
Cdd:cd03240 158 EESLaEIIEERkSQKNFQLIVITHDEEL-VDAADHIY 193
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-198 |
1.19e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasysRKDVHKLRQ 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI------KKDLCTYQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVTEALITAqkkpkkeAEQIGMD-LLRQVGLEHKADsYPI-TMSGGQQQRIGIARALAVDP 158
Cdd:PRK13540 75 QLCFVGHRSGINPYLTLRENCLYDIHFS-------PGAVGITeLCRLFSLEHLID-YPCgLLSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHE 198
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-234 |
1.27e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.38 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEigdaKLNAASYSrkdvhklrQQTAMVFQNynlfknk 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK----HSGRISFS--------PQTSWIMPG------- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 TALQNVTEALITAQKKPKK--EAEQIGMDLlrqvGLEHKADSYP-----ITMSGGQQQRIGIARALAVDPHAILLDEPTS 168
Cdd:TIGR01271 502 TIKDNIIFGLSYDEYRYTSviKACQLEEDI----ALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 169 ALDPELVAGVLQ--VIKSIAEKqtTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELfdnpQNER 234
Cdd:TIGR01271 578 HLDVVTEKEIFEscLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL----QAKR 638
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2-243 |
2.28e-09 |
|
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: 56.93 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKaFKDLTvldgIDLeikSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGI-IEIGDAklnaasYSRKDVHKLRQ 80
Cdd:COG3593 6 IKIKNFRS-IKDLS----IEL---SDDLTVLVGENNSGKSSILEALRLLLGPSSSRkFDEEDF------YLGDDPDLPEI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNY-----NLFKNKTALQNVTEALITAQKKPKKEAEQI-------------------------GMDLLRQVGLE 130
Cdd:COG3593 72 EIELTFGSLlsrllRLLLKEEDKEELEEALEELNEELKEALKALnellseylkelldgldlelelsldeLEDLLKSLSLR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 131 -HKADSYPITMSG-GQQQRIGIA--RALA-----VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAF 201
Cdd:COG3593 152 iEDGKELPLDRLGsGFQRLILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHL 231
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489248201 202 AREV-ADKVIFMADGRIIEQGTpeELFDNPQNERtKKFIKQVG 243
Cdd:COG3593 232 LSEVpLENIRRLRRDSGGTTST--KLIDLDDEDL-RKLLRYLG 271
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-219 |
2.82e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.72 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 12 KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERpddgiIEIGDAKLNAASYS-RKDVHKLRQQTAMVFQNY- 89
Cdd:PRK09700 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK-----RAGGEIRLNGKDISpRSPLDAVKKGMAYITESRr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 90 --NLFKNKTALQNVTEAL------------ITAQKKPKKEAEQIGMDLLRQVgleHKADSYPITMSGGQQQRIGIARALA 155
Cdd:PRK09700 349 dnGFFPNFSIAQNMAISRslkdggykgamgLFHEVDEQRTAENQRELLALKC---HSVNQNITELSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIE 219
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
9-198 |
3.02e-09 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 56.21 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 9 KAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLL-------ERPDDGIIE-------------------IGD 62
Cdd:COG1106 11 RSFKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEALYFLrnlvlnsSQPGDKLVEpflldsesknepsefeilfLLD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 63 AKLNAA--SYSRKDVHK--------LRQQTAMVFQN-YNLFKNKTALQNVTEALITAQKKPKKEAEQIgMDLLRQVGLE- 130
Cdd:COG1106 91 GVRYEYgfELDKERIISewlyflstAAQLNVPLLSPlYDWFDNNISLDTSSDGLTLLLKEDESLKEEL-LELLKIADPGi 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 131 ---------------------HKADSYPIT---MSGGQQQRIGIARALA---VDPHAILLDEPTSALDPELVAGVLQVIK 183
Cdd:COG1106 170 edieveeeeiedlverklifkHKGGNVPLPlseESDGTKRLLALAGALLdalAKGGVLLIDEIEASLHPSLLRKLLKLFL 249
|
250
....*....|....*.
gi 489248201 184 SIAEKQTT-MIIVTHE 198
Cdd:COG1106 250 DLANKNNAqLIFTTHS 265
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
140-226 |
3.81e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.55 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 140 MSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI-- 217
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRIsg 475
|
90
....*....|..
gi 489248201 218 ---IEQGTPEEL 226
Cdd:PRK10762 476 eftREQATQEKL 487
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-226 |
6.76e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 6.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLN-LLERPDdgiieiGDAKLNAASYSRKDVhKLRQ 80
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTgLLPASE------GEAWLFGQPVDAGDI-ATRR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 81 QTAMVFQNYNLFKNKTALQNVteaLITAQ--KKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:NF033858 340 RVGYMSQAFSLYGELTVRQNL---ELHARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKP 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 159 HAILLDEPTSALDPelVA--GVLQVIKSIA-EKQTTMIIVTHEMAFArEVADKVIFMADGRIIEQGTPEEL 226
Cdd:NF033858 417 ELLILDEPTSGVDP--VArdMFWRLLIELSrEDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAAL 484
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-218 |
7.19e-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: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 26 SGEVTAIIGPSGSGKSTLLRCL-NLLERPDDGIIEIGDAKLnaasysrkdvhklrqqtamvfqnynlfknktalqnvtea 104
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDI--------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 105 litaqkkpkkeaeqigMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQ---- 180
Cdd:smart00382 42 ----------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleel 105
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489248201 181 --VIKSIAEKQTTMIIVTHEMAFAREVAdkVIFMADGRII 218
Cdd:smart00382 106 rlLLLLKSEKNLTVILTTNDEKDLGPAL--LRRRFDRRIV 143
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-241 |
9.13e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 55.61 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 139 TMSGGQQQRIGIARALAVDPHAI--LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHE---MAFAREVAD----KV 209
Cdd:PRK00635 476 TLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLADRIIDigpgAG 555
|
90 100 110
....*....|....*....|....*....|..
gi 489248201 210 IFmaDGRIIEQGTPEElFDNPQNERTKKFIKQ 241
Cdd:PRK00635 556 IF--GGEVLFNGSPRE-FLAKSDSLTAKYLRQ 584
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-217 |
1.28e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.92 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasysRKDVHKLRQ---------------QTAM 84
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI----RSPRDAIRAgimlcpedrkaegiiPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 85 VFQNYNLFKNKtalQNVTEALITAQKKPKKEAEQigmdLLRQVGLEHKADSYPI-TMSGGQQQRIGIARALAVDPHAILL 163
Cdd:PRK11288 348 VADNINISARR---HHLRAGCLINNRWEAENADR----FIRSLNIKTPSREQLImNLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489248201 164 DEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
2-197 |
1.29e-08 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 54.23 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRkAFKDLTvldgIDLEIKSGeVTAIIGPSGSGKSTLLRCLNL-LERPDDGIIEIGDAKLN------------AA 68
Cdd:COG3950 6 LTIENFR-GFEDLE----IDFDNPPR-LTVLVGENGSGKTTLLEAIALaLSGLLSRLDDVKFRKLLirngefgdsaklIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 69 SYS--R-------KDVHKLRQQTAMVFQNY-NLFKNKTALQNVTEALITAQKKPKKEAE--------------------- 117
Cdd:COG3950 80 YYGtsRllldgplKKLERLKEEYFSRLDGYdSLLDEDSNLREFLEWLREYLEDLENKLSdeldekleavrealnkllpdf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 118 ---QIGMDLLRQVGLEHKADSYPIT-MSGGQQQRIGIA-----RALAVDPHA---------ILLDEPTSALDPELVAGVL 179
Cdd:COG3950 160 kdiRIDRDPGRLVILDKNGEELPLNqLSDGERSLLALVgdlarRLAELNPALenplegegiVLIDEIDLHLHPKWQRRIL 239
|
250
....*....|....*...
gi 489248201 180 QVIKSIAEKqTTMIIVTH 197
Cdd:COG3950 240 PDLRKIFPN-IQFIVTTH 256
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
139-217 |
1.56e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 1.56e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 139 TMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-217 |
2.33e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRC------------LNLLERPDDGIIEIGDAKLNAAs 69
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndLTLFGRRRGSGETIWDIKKHIG- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 70 YSRKDVHkLRQQTAMVFQNYNL---FKNKTALQNVTEALitaQKKPKKEAEQIGMDllrqvglEHKADSYPITMSGGQQQ 146
Cdd:PRK10938 340 YVSSSLH-LDYRVSTSVRNVILsgfFDSIGIYQAVSDRQ---QKLAQQWLDILGID-------KRTADAPFHSLSWGQQR 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 147 RIGIARALAVDPHAILLDEPTSALDP---ELVAGVLQVIksIAEKQTTMIIVTHEMAFARE-VADKVIFMADGRI 217
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVL--ISEGETQLLFVSHHAEDAPAcITHRLEFVPDGDI 481
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-229 |
2.86e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.74 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEI-GDAKLNAASYSRKDvhKLRQQTAMVFQNYNLFKNK 95
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGSAALIAISSGLNG--QLTGIENIELKGLMMGLTK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 96 TALQNVTEALItaqkkpkkEAEQIGMDLLRQVGlehkadsypiTMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELV 175
Cdd:PRK13545 118 EKIKEIIPEII--------EFADIGKFIYQPVK----------TYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489248201 176 AGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDN 229
Cdd:PRK13545 180 KKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-215 |
3.08e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.08 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 14 LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLnlLERPDDGIIEiGDAKLnaASYSRKdvhklrQQTAMVFQNYNLFK 93
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVL--AGRKTGGYIE-GDIRI--SGFPKK------QETFARISGYCEQN 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 94 NKTALQ-NVTEALITAQ--KKPKKEAEQIGMDLLRQV----GLEHKADS---YP-IT-MSGGQQQRIGIARALAVDPHAI 161
Cdd:PLN03140 962 DIHSPQvTVRESLIYSAflRLPKEVSKEEKMMFVDEVmelvELDNLKDAivgLPgVTgLSTEQRKRLTIAVELVANPSII 1041
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAF-AREVADKVIFMADG 215
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKRG 1096
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-217 |
3.34e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGdAKLNAASYsrkDVHKLrqqtamvfqnyNLF 92
Cdd:PRK11147 331 GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-TKLEVAYF---DQHRA-----------ELD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 93 KNKTALQNVTEAlitaqkkpKKEAEQIGMDllRQV------GLEH-KADSYPI-TMSGGQQQRIGIARALAVDPHAILLD 164
Cdd:PRK11147 396 PEKTVMDNLAEG--------KQEVMVNGRP--RHVlgylqdFLFHpKRAMTPVkALSGGERNRLLLARLFLKPSNLLILD 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 165 EPTSALDPElvagVLQVIKS-IAEKQTTMIIVTHEMAFA-REVADKVIFMADGRI 217
Cdd:PRK11147 466 EPTNDLDVE----TLELLEElLDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGKI 516
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
11-217 |
3.85e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 11 FKDLTVldGIDLEIKsgevTAIIGPSGSGKSTLLRCLNLLERPDDGIIeIGDAKLNAASYSRKDVHKLRQQTAMVFQNYN 90
Cdd:PLN03073 525 FKNLNF--GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKVRMAVFSQHHVDGLDLSSNPLLYMMR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 91 LFKNktalqnVTEALITAQkkpkkeaeqigmdlLRQVGLEHKADSYPI-TMSGGQQQRIGIARALAVDPHAILLDEPTSA 169
Cdd:PLN03073 598 CFPG------VPEQKLRAH--------------LGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNH 657
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489248201 170 LDPELVAGVLQvikSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:PLN03073 658 LDLDAVEALIQ---GLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-226 |
1.39e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 21 DLEIKSGEVTAIIGPSGSGKSTLLRCLNllerpDDGIIEIGDAKLNAASYSRKDVHKLRQQTAMVFQnynlfKNKTALQN 100
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALA-----GELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQ-----RNNTDMLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 101 VTE---ALITAQ------KKPKKEAEqigmdLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD 171
Cdd:PRK10938 93 PGEddtGRTTAEiiqdevKDPARCEQ-----LAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 172 PELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK10938 168 VASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
139-236 |
1.55e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 139 TMSGGQQQRIGIARALAVDPHAILLDEPTSALDpelVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRII 218
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLV 420
|
90
....*....|....*...
gi 489248201 219 EQGTPEELFDNPQNERTK 236
Cdd:PLN03073 421 TYKGDYDTFERTREEQLK 438
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-221 |
1.97e-07 |
|
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: 50.33 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTLL---------------------RCLNLLERPD-DGI------IEIgDAKLNAa 68
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDvDSIeglspaIAI-DQKTTS- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 69 sysrkdvHKLRQQTAMVFQNYNLFKNKTALQNVTEALitaqkkpkkeaeqigmDLLRQVGLEHKADSYPI-TMSGGQQQR 147
Cdd:cd03270 89 -------RNPRSTVGTVTEIYDYLRLLFARVGIRERL----------------GFLVDVGLGYLTLSRSApTLSGGEAQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 148 IGIARALAVDPHAIL--LDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREvADKVIFMA------DGRIIE 219
Cdd:cd03270 146 IRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVIDIGpgagvhGGEIVA 224
|
..
gi 489248201 220 QG 221
Cdd:cd03270 225 QG 226
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
115-241 |
2.21e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.37 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 115 EAEQIGMD---------LLRQVGLEHKADSYPI-TMSGGQQQRIGIA-RALAVDPHAIL--LDEPTSALDPELVAGVLQV 181
Cdd:PRK00635 775 EAEKFFLDepsihekihALCSLGLDYLPLGRPLsSLSGGEIQRLKLAyELLAPSKKPTLyvLDEPTTGLHTHDIKALIYV 854
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 182 IKSIAEKQTTMIIVTHEMAFAReVADKVIFMA------DGRIIEQGTPEELF--DNPQNERTKKFIKQ 241
Cdd:PRK00635 855 LQSLTHQGHTVVIIEHNMHVVK-VADYVLELGpeggnlGGYLLASCSPEELIhlHTPTAKALRPYLSS 921
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
121-247 |
2.89e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.80 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 121 MDLLRQVGLehkadSYpI-------TMSGGQQQRIGIARALA--VDPHAI-LLDEPTSALDPELVAGVLQVIKSIAEKQT 190
Cdd:COG0178 807 LQTLQDVGL-----GY-IklgqpatTLSGGEAQRVKLASELSkrSTGKTLyILDEPTTGLHFHDIRKLLEVLHRLVDKGN 880
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 191 TMIIVTHEMAFAReVADKVIfmaD---------GRIIEQGTPEELFDNPQNErTKKFIKQVGEPAE 247
Cdd:COG0178 881 TVVVIEHNLDVIK-TADWII---DlgpeggdggGEIVAEGTPEEVAKVKASY-TGRYLKEYLEAAR 941
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-206 |
4.55e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 1 MIQVRhirKAF-KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGiieigDAKLnAASYSrkdVHKLR 79
Cdd:PRK11819 9 MNRVS---KVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-----EARP-APGIK---VGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 80 QQTamvfqnyNLFKNKTALQNVTEALitAQKKPK-KEAEQIG---------MDLL--RQVGLEHKADSY----------- 136
Cdd:PRK11819 77 QEP-------QLDPEKTVRENVEEGV--AEVKAAlDRFNEIYaayaepdadFDALaaEQGELQEIIDAAdawdldsqlei 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 137 ------------PIT-MSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGvLQviKSIAEKQTTMIIVTHEMAFAR 203
Cdd:PRK11819 148 amdalrcppwdaKVTkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAW-LE--QFLHDYPGTVVAVTHDRYFLD 224
|
...
gi 489248201 204 EVA 206
Cdd:PRK11819 225 NVA 227
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-197 |
4.96e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.85 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRkAFKDLTVldgIDLEiksGEVTAIIGPSGSGKSTLLRCLNL-------------------------------- 49
Cdd:COG0419 5 LRLENFR-SYRDTET---IDFD---DGLNLIVGPNGAGKSTILEAIRYalygkarsrsklrsdlinvgseeasvelefeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 50 ------LERPDDGIIEIgdakLNAASYSRKDVhkLRQqtamVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDL 123
Cdd:COG0419 78 ggkryrIERRQGEFAEF----LEAKPSERKEA--LKR----LLGLEIYEELKERLKELEEAL-ESALEELAELQKLKQEI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 124 LRQV-GLEHKAdsypiTMSGGQQQRIGIARALavdphAILLDepTSALDPELVAGVLQVIKSIAekqttmiIVTH 197
Cdd:COG0419 147 LAQLsGLDPIE-----TLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
121-242 |
6.15e-07 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 50.07 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 121 MDLLRQVGLehkadSY------PITMSGGQQQRIGIARALA---------VdphailLDEPTSALDPELVAGVLQVIKSI 185
Cdd:PRK00349 811 LQTLVDVGL-----GYiklgqpATTLSGGEAQRVKLAKELSkrstgktlyI------LDEPTTGLHFEDIRKLLEVLHRL 879
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 186 AEKQTTMIIVTHEMafarevaDkVIFMAD-------------GRIIEQGTPEELFDNPqNERTKKFIKQV 242
Cdd:PRK00349 880 VDKGNTVVVIEHNL-------D-VIKTADwiidlgpeggdggGEIVATGTPEEVAKVE-ASYTGRYLKPV 940
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-242 |
8.11e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.84 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 14 LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLrcLNLLERPDDGIIEIGDAKLN------------AASYSRKDVH----- 76
Cdd:PLN03140 178 LTILKDASGIIKPSRMTLLLGPPSSGKTTLL--LALAGKLDPSLKVSGEITYNgyrlnefvprktSAYISQNDVHvgvmt 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 77 ------------------------KLRQQTAMVF--QNYNLFKNKTALQNVTEALITaqkkpKKEAEQIGMDLLRQ--VG 128
Cdd:PLN03140 256 vketldfsarcqgvgtrydllselARREKDAGIFpeAEVDLFMKATAMEGVKSSLIT-----DYTLKILGLDICKDtiVG 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 129 lehkaDSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAE--KQTTMIIVTHEMAFAREVA 206
Cdd:PLN03140 331 -----DEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHltEATVLMSLLQPAPETFDLF 405
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489248201 207 DKVIFMADGRIIEQGTPE---ELFDN-----PQNERTKKFIKQV 242
Cdd:PLN03140 406 DDIILLSEGQIVYQGPRDhilEFFEScgfkcPERKGTADFLQEV 449
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-247 |
9.67e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.52 E-value: 9.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDdgiieiGDAKLNAASYSRKDVHKLRQQTAMVFQNYNLFKN 94
Cdd:TIGR01271 1233 AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE------GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSG 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 kTALQNVTEALITAQKKPKKEAEQIGM-DLLRQV--GLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD 171
Cdd:TIGR01271 1307 -TFRKNLDPYEQWSDEEIWKVAEEVGLkSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 172 PElvagVLQVIKSIAeKQT----TMIIVTHEMAFAREVadKVIFMADGRIIEQgtpeelFDNPQ---NERTkkFIKQVGE 244
Cdd:TIGR01271 1386 PV----TLQIIRKTL-KQSfsncTVILSEHRVEALLEC--QQFLVIEGSSVKQ------YDSIQkllNETS--LFKQAMS 1450
|
...
gi 489248201 245 PAE 247
Cdd:TIGR01271 1451 AAD 1453
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
15-172 |
1.55e-06 |
|
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: 47.93 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDdgiieiGDAKLNAASYSRKDVHKLRQQTAMVFQNYNLFKN 94
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE------GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 kTALQNVTEALITAQKKPKKEAEqigmdllrQVGLEHKADSYP-----------ITMSGGQQQRIGIARALAVDPHAILL 163
Cdd:cd03289 92 -TFRKNLDPYGKWSDEEIWKVAE--------EVGLKSVIEQFPgqldfvlvdggCVLSHGHKQLMCLARSVLSKAKILLL 162
|
....*....
gi 489248201 164 DEPTSALDP 172
Cdd:cd03289 163 DEPSAHLDP 171
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
140-217 |
2.43e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 2.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 140 MSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-197 |
4.46e-06 |
|
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: 47.44 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 23 EIKSGEVTAIIGPSGSGKSTLLRCLN--------LLERPDDGIIEIgdakLNAASYsrKDVHKLRQQTAMVFQNYNLFKN 94
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFY----VPQRPY--MTLGTLRDQIIYPDSSEDMKRR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 95 KTALQNVTEALitaqkkpkkEAEQIGMDLLRQVGLEHKADsYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPEL 174
Cdd:TIGR00954 548 GLSDKDLEQIL---------DNVQLTHILEREGGWSAVQD-WMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617
|
170 180
....*....|....*....|...
gi 489248201 175 VAGVLQVIKsiaEKQTTMIIVTH 197
Cdd:TIGR00954 618 EGYMYRLCR---EFGITLFSVSH 637
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
124-231 |
5.17e-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: 47.32 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 124 LRQVGLEHKADSYPI-TMSGGQQQRIGIARALAVDPHAIL--LDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMA 200
Cdd:TIGR00630 472 LIDVGLDYLSLSRAAgTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED 551
|
90 100 110
....*....|....*....|....*....|....*..
gi 489248201 201 FAREvADKVIFMA------DGRIIEQGTPEELFDNPQ 231
Cdd:TIGR00630 552 TIRA-ADYVIDIGpgagehGGEVVASGTPEEILANPD 587
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
98-197 |
9.05e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 45.84 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 98 LQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPIT---MSGGQQQRIGIARALAVDPHA---ILLDEPTSALD 171
Cdd:pfam13304 192 LKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPafeLSDGTKRLLALLAALLSALPKgglLLIDEPESGLH 271
|
90 100
....*....|....*....|....*.
gi 489248201 172 PELVAGVLQVIKSIAEKQTTMIIVTH 197
Cdd:pfam13304 272 PKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
18-69 |
9.59e-06 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 42.20 E-value: 9.59e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 489248201 18 DGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDdgiieiGDAKLNAAS 69
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPA------KRARFNKAA 58
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
123-229 |
7.29e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 123 LLRQVGLEHKADSYPIT-MSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIaekQTTMIIVTHEMAF 201
Cdd:PRK10636 132 LLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY---QGTLILISHDRDF 208
|
90 100
....*....|....*....|....*...
gi 489248201 202 AREVADKVIFmadgriIEQGTPEELFDN 229
Cdd:PRK10636 209 LDPIVDKIIH------IEQQSLFEYTGN 230
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
12-240 |
8.56e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.88 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 12 KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIE-IGDAKLNAAsysrkdvhklrqqtamvfqNYN 90
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDrNGEVSVIAI-------------------SAG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 91 LFKNKTALQNVTEALITAQKKPKkEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSAL 170
Cdd:PRK13546 96 LSGQLTGIENIEFKMLCMGFKRK-EIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 171 DPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFdnPQNErtkKFIK 240
Cdd:PRK13546 175 DQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL--PKYE---AFLN 239
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
1-50 |
8.58e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.00 E-value: 8.58e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 489248201 1 MIQVRHIR--KAFKDLTVldgiDLeiksGEVTAIIGPSGSGKSTLLRCLNLL 50
Cdd:COG4637 1 MITRIRIKnfKSLRDLEL----PL----GPLTVLIGANGSGKSNLLDALRFL 44
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
29-62 |
1.53e-04 |
|
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: 41.99 E-value: 1.53e-04
10 20 30
....*....|....*....|....*....|....
gi 489248201 29 VTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGD 62
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTD 34
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
147-214 |
2.64e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 2.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 147 RIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKsiaEKQTTMIIVTHEMAFAREVADKvifMAD 214
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLN---ERNSTMIIISHDRHFLNSVCTH---MAD 224
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
94-215 |
4.53e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 94 NKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLehkadSYPI------TMSGGQQQRIGIARALAVDPHAI--LLDE 165
Cdd:PRK00635 1341 DVTFLKKFLLTIHDDEEPSIIQDLLNRLTFIDKVGL-----SYITlgqeqdTLSDGEHYRLHLAKKISSNLTDIiyLLED 1415
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489248201 166 PTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREVADKVIFMADG 215
Cdd:PRK00635 1416 PLSGLHPQDAPTLLQLIKELVTNNNT-VIATDRSGSLAEHADHLIHLGPG 1464
|
|
| Rad50_Sulf |
NF041034 |
DNA double-strand break repair ATPase Rad50; |
147-223 |
9.96e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 468963 [Multi-domain] Cd Length: 872 Bit Score: 40.08 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 147 RIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFaREVADKVIFM---ADGRIIEQGTP 223
Cdd:NF041034 793 RLAIAKSLMDEIGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIVVTHDEEL-KEISDYIISVekkGDSSKVKVGSY 871
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
17-43 |
1.30e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 1.30e-03
10 20
....*....|....*....|....*..
gi 489248201 17 LDGIDLEIKSGEVTAIIGPSGSGKSTL 43
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
29-173 |
3.87e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 37.16 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 29 VTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLN--AASYSRKDVHKLRQQTAM-VFQNYNLFknkTALQNVTEAL 105
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINniAKPYCTYIGHNLGLKLEMtVFENLKFW---SEIYNSAETL 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 106 ITAQKKPKKEaeqigmDLLrqvglehkaDSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPE 173
Cdd:PRK13541 105 YAAIHYFKLH------DLL---------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
7-56 |
4.17e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 38.25 E-value: 4.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 489248201 7 IRKAFKDLTVLDGIDLEIKsgeVTAIIGPSGSGKSTLLR--CLNLLERPDDG 56
Cdd:COG5635 163 LLERIESLKRLELLEAKKK---RLLILGEPGSGKTTLLRylALELAERYLDA 211
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
18-74 |
4.19e-03 |
|
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: 37.38 E-value: 4.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 18 DGIDlEIK---SGEVTAIIGPSGSGKSTLlrcLNLLerpddgiieIGDAKLNAASYSRKD 74
Cdd:cd01854 74 EGLD-ELRellKGKTSVLVGQSGVGKSTL---LNAL---------LPELVLATGEISEKL 120
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
29-60 |
6.64e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 35.78 E-value: 6.64e-03
10 20 30
....*....|....*....|....*....|...
gi 489248201 29 VTAIIGPSGSGKSTLLRCL-NLLERPDDGIIEI 60
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLlEQLPEVRDSVVFV 39
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
2-138 |
9.95e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 35.93 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 2 IQVRHIRKaFKDLTvldgIDLeikSGEVTAIIGPSGSGKSTLLRCLNL--------LERPDDGIIEIGDAKLNaasysrk 73
Cdd:pfam13476 1 LTIENFRS-FRDQT----IDF---SKGLTLITGPNGSGKTTILDAIKLalygktsrLKRKSGGGFVKGDIRIG------- 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 74 DVHKLRQQTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPI 138
Cdd:pfam13476 66 LEGKGKAYVEITFENNDGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKII 130
|
|
|